|
Name |
Accession |
Description |
Interval |
E-value |
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
56-632 |
0e+00 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 552.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 56 LLITGTVAAVIHGAGFPLLAIVLGGMTTVFLRAQNSdfvvgvdnvnpeglvpisldefnSEVVKYCIYYLVLGVLMFFTS 135
Cdd:COG1132 22 LLILALLLLLLSALLELLLPLLLGRIIDALLAGGDL-----------------------SALLLLLLLLLGLALLRALLS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 136 YVQIACFESYAERLVHKLRQNYLKAILRQQIQWFDKQQTGNLTARLTDDLERVREGLGDKFALLVQMFAAFLAGYGVGFF 215
Cdd:COG1132 79 YLQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 216 YSWSMTLVMMGFAPLIVLSGAKMSKSMATRTRVEQETYAVAGAIAEETFSSIRTVHSLNGHKRELDRFYNALEVGRQTGI 295
Cdd:COG1132 159 IDWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 296 VKYCYMGIGVGFSNLCMYSSYALAFWYGSTLIINDpTFDRGLIFTVFFAVLSGSTSLGGALPHLASFGTARGAASTVLRV 375
Cdd:COG1132 239 RAARLSALFFPLMELLGNLGLALVLLVGGLLVLSG-SLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFEL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 376 INSHPKIdPYSLEGILVDNMKGDISFKDVHFRYPSRKDihVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTK 455
Cdd:COG1132 318 LDEPPEI-PDPPGAVPLPPVRGEIEFENVSFSYPGDRP--VLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTS 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 456 GRVLIDGVDLREVNVHSLREQIGIVSQEPVLFDGTIYENIKMGNEHATHDQVVEACKMANANDFIKRLPDGYGTRVGEKG 535
Cdd:COG1132 395 GRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERG 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 536 VQLSGGQKQRIAIARALVKNPKILLLDEATSALDTEAEREVQGALDQAQAGRTTIIVAHRLSTIRNVDRIFVFKAGNIVE 615
Cdd:COG1132 475 VNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVE 554
|
570
....*....|....*..
gi 124244275 616 SGSHEELMSKQGIFYDM 632
Cdd:COG1132 555 QGTHEELLARGGLYARL 571
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
56-1262 |
1.58e-167 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 537.69 E-value: 1.58e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 56 LLITGTVAAVIHGAGFPLLAIVLGgmttVFLRAQNsdfvVGvDNVNPeglvpisldefnsevvkyCIYYLVL-GVLMFFT 134
Cdd:PTZ00265 61 LLGVSFVCATISGGTLPFFVSVFG----VIMKNMN----LG-ENVND------------------IIFSLVLiGIFQFIL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 135 SYVQIACFESYAERLVHKLRQNYLKAILRQQIQWFDKQQTGNLTARLTDDLERVREGLGDKFALLVQMFAAFLAGYGVGF 214
Cdd:PTZ00265 114 SFISSFCMDVVTTKILKTLKLEFLKSVFYQDGQFHDNNPGSKLTSDLDFYLEQVNAGIGTKFITIFTYASAFLGLYIWSL 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 215 FYSWSMTLVMMGFAPLIVLSGAKMSKSMATRTRVEQETYAVAGAIAEETFSSIRTVHSLNGHKRELDRFyNALEVGRQTG 294
Cdd:PTZ00265 194 FKNARLTLCITCVFPLIYICGVICNKKVKINKKTSLLYNNNTMSIIEEALVGIRTVVSYCGEKTILKKF-NLSEKLYSKY 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 295 IVKYCYM-GIGVGFSNLCMYSSYALAFWYGSTLIINDPT-------FDRGLIFTVFFAVLSGSTSLGGALPHLASFGTAR 366
Cdd:PTZ00265 273 ILKANFMeSLHIGMINGFILASYAFGFWYGTRIIISDLSnqqpnndFHGGSVISILLGVLISMFMLTIILPNITEYMKSL 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 367 GAASTVLRVINSHPKIDPYSlEGILVDNMKgDISFKDVHFRYPSRKDIHVLKGISLELKAGDKIALVGSSGCGKSTIVNL 446
Cdd:PTZ00265 353 EATNSLYEIINRKPLVENND-DGKKLKDIK-KIQFKNVRFHYDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKL 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 447 LQRFYDPTKGRVLI-DGVDLREVNVHSLREQIGIVSQEPVLFDGTIYENIKMG----------------NEHATHD---- 505
Cdd:PTZ00265 431 IERLYDPTEGDIIInDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKYSlyslkdlealsnyyneDGNDSQEnknk 510
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 506 -------------------------------------QVVEACKMANANDFIKRLPDGYGTRVGEKGVQLSGGQKQRIAI 548
Cdd:PTZ00265 511 rnscrakcagdlndmsnttdsneliemrknyqtikdsEVVDVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISI 590
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 549 ARALVKNPKILLLDEATSALDTEAEREVQGALD--QAQAGRTTIIVAHRLSTIRNVDRIFVF------------------ 608
Cdd:PTZ00265 591 ARAIIRNPKILILDEATSSLDNKSEYLVQKTINnlKGNENRITIIIAHRLSTIRYANTIFVLsnrergstvdvdiigedp 670
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 609 -------------------------KAGN----IVESGSHEELM-SKQGIFYDM-TQAQVVRQQQQEAGKDIEDTISESA 657
Cdd:PTZ00265 671 tkdnkennnknnkddnnnnnnnnnnKINNagsyIIEQGTHDALMkNKNGIYYTMiNNQKVSSKKSSNNDNDKDSDMKSSA 750
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 658 HSHLSRKSSTRSAISIATSIHQLAEEVEECKAPPTS---------------MFK---------------IFKFNGDKVGW 707
Cdd:PTZ00265 751 YKDSERGYDPDEMNGNSKHENESASNKKSCKMSDENasennaggklpflrnLFKrkpkapnnlrivyreIFSYKKDVTII 830
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 708 FiggiFGAFIFGSVTPVFALVYAE----IFNVYSLPADQMQANVYfwcgmFVLMGITFFVGFFTSANCLGRCGESL--TM 781
Cdd:PTZ00265 831 A----LSILVAGGLYPVFALLYAKyvstLFDFANLEANSNKYSLY-----ILVIAIAMFISETLKNYYNNVIGEKVekTM 901
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 782 KLRFeaFKNLLRQDIAFYDDLRHGTGKLCTRFATDAPNVRYVFTRLPVVLAS-IVTICGALGIGFYYGWQLALILVvmvp 860
Cdd:PTZ00265 902 KRRL--FENILYQEISFFDQDKHAPGLLSAHINRDVHLLKTGLVNNIVIFTHfIVLFLVSMVMSFYFCPIVAAVLT---- 975
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 861 llvmGGYFeMQMRF---------GKQIRDTQLLEEAGKVASQAVEHIRTVHSLNRQEQFH--FTYCEY-LREPFNTNLKH 928
Cdd:PTZ00265 976 ----GTYF-IFMRVfairarltaNKDVEKKEINQPGTVFAYNSDDEIFKDPSFLIQEAFYnmNTVIIYgLEDYFCNLIEK 1050
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 929 AHTY------------GAVFAFSQSLIFFMYAAAFYLGSIFVNQQAMQPIDVYRVFFAISFCGQMIGNTTSFIPDVVKAR 996
Cdd:PTZ00265 1051 AIDYsnkgqkrktlvnSMLWGFSQSAQLFINSFAYWFGSFLIRRGTILVDDFMKSLFTFLFTGSYAGKLMSLKGDSENAK 1130
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 997 LAASLLFYLIEHPTPIDSLSDSGI----VKPITGNISIRNVFFNYPTRKDTKVLQGFTLDIKAGKTVALVGHSGCGKSTI 1072
Cdd:PTZ00265 1131 LSFEKYYPLIIRKSNIDVRDNGGIriknKNDIKGKIEIMDVNFRYISRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTV 1210
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1073 MGLLERFYN------------------------------------------------------QDKGMIMIDGDNIRNLN 1098
Cdd:PTZ00265 1211 MSLLMRFYDlkndhhivfknehtndmtneqdyqgdeeqnvgmknvnefsltkeggsgedstvfKNSGKILLDGVDICDYN 1290
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1099 ISSLREQVCIVSQEPTLFDCTIGENICYGtNRNVTYQEIVEAAKMANIHNFILGLPDGYDTHVGEKGTQLSGGQKQRIAI 1178
Cdd:PTZ00265 1291 LKDLRNLFSIVSQEPMLFNMSIYENIKFG-KEDATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAI 1369
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1179 ARALVRSPSVLLLDEATSALDTESEKIVQEAL--DAAKQGRTCLVIAHRLSTIQNSDVIAIVSE----GKIVE-KGTHDE 1251
Cdd:PTZ00265 1370 ARALLREPKILLLDEATSSLDSNSEKLIEKTIvdIKDKADKTIITIAHRIASIKRSDKIVVFNNpdrtGSFVQaHGTHEE 1449
|
1450
....*....|..
gi 124244275 1252 LIRKSE-IYQKF 1262
Cdd:PTZ00265 1450 LLSVQDgVYKKY 1461
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
688-1266 |
2.98e-164 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 502.00 E-value: 2.98e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 688 KAPPTSMFKIFKFNGDKVGWFIGGIFGAFIFGSVTPVFALVYAEIFNVYSLPADQMQanVYFWCGMFVLMGITFFVGFFT 767
Cdd:COG1132 3 KSPRKLLRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGGDLSA--LLLLLLLLLGLALLRALLSYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 768 SANCLGRCGESLTMKLRFEAFKNLLRQDIAFYDdlRHGTGKLCTRFATDAPNVRYVFTR-LPVVLASIVTICGALGIGFY 846
Cdd:COG1132 81 QRYLLARLAQRVVADLRRDLFEHLLRLPLSFFD--RRRTGDLLSRLTNDVDAVEQFLAHgLPQLVRSVVTLIGALVVLFV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 847 YGWQLALILVVMVPLLVMGGYFeMQMRFGKQIRDTQllEEAGKVASQAVEH---IRTVHSLNRQEQFHFTYCEYLREPFN 923
Cdd:COG1132 159 IDWRLALIVLLVLPLLLLVLRL-FGRRLRKLFRRVQ--EALAELNGRLQESlsgIRVVKAFGREERELERFREANEELRR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 924 TNLKHAHTYGAVFAFSQSLIFFMYAAAFYLGSIFVNQQAMQPIDVYRVFFAISFCGQMIGNTTSFIPDVVKARLAASLLF 1003
Cdd:COG1132 236 ANLRAARLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIF 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1004 YLIEHPTPIDSLSDSGIVKPITGNISIRNVFFNYPtrKDTKVLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQD 1083
Cdd:COG1132 316 ELLDEPPEIPDPPGAVPLPPVRGEIEFENVSFSYP--GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPT 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1084 KGMIMIDGDNIRNLNISSLREQVCIVSQEPTLFDCTIGENICYGtNRNVTYQEIVEAAKMANIHNFILGLPDGYDTHVGE 1163
Cdd:COG1132 394 SGRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYG-RPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGE 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1164 KGTQLSGGQKQRIAIARALVRSPSVLLLDEATSALDTESEKIVQEALDAAKQGRTCLVIAHRLSTIQNSDVIAIVSEGKI 1243
Cdd:COG1132 473 RGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRI 552
|
570 580
....*....|....*....|...
gi 124244275 1244 VEKGTHDELIRKSEIYQKFCETQ 1266
Cdd:COG1132 553 VEQGTHEELLARGGLYARLYRLQ 575
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
125-632 |
4.30e-145 |
|
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: 456.22 E-value: 4.30e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 125 LVLGVLMFFTSYVQIACFESYAERLVHKLRQNYLKAILRQQIQWFDKQQTGNLTARLTDdLERVREGLGDKFA-LLVQMF 203
Cdd:COG2274 203 LLALLFEGLLRLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRFRD-VESIREFLTGSLLtALLDLL 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 204 AAFLAGyGVGFFYSWSMTLVMMGFAPLIVLSGAKMSKSMATRTRVEQETYAVAGAIAEETFSSIRTVHSLNGHKRELDR- 282
Cdd:COG2274 282 FVLIFL-IVLFFYSPPLALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRFRRRw 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 283 ---FYNALEVGRQTGIVkycyMGIGVGFSNLCMYSSYALAFWYGSTLIINDPtfdrgliFTV--FFA-------VLSGST 350
Cdd:COG2274 361 enlLAKYLNARFKLRRL----SNLLSTLSGLLQQLATVALLWLGAYLVIDGQ-------LTLgqLIAfnilsgrFLAPVA 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 351 SLGGalpHLASFGTARGAASTVLRVINSHPKIDPySLEGILVDNMKGDISFKDVHFRYPSRkDIHVLKGISLELKAGDKI 430
Cdd:COG2274 430 QLIG---LLQRFQDAKIALERLDDILDLPPEREE-GRSKLSLPRLKGDIELENVSFRYPGD-SPPVLDNISLTIKPGERV 504
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 431 ALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDLREVNVHSLREQIGIVSQEPVLFDGTIYENIKMGNEHATHDQVVEA 510
Cdd:COG2274 505 AIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPDATDEEIIEA 584
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 511 CKMANANDFIKRLPDGYGTRVGEKGVQLSGGQKQRIAIARALVKNPKILLLDEATSALDTEAEREVQGALDQAQAGRTTI 590
Cdd:COG2274 585 ARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVI 664
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 124244275 591 IVAHRLSTIRNVDRIFVFKAGNIVESGSHEELMSKQGIFYDM 632
Cdd:COG2274 665 IIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLARKGLYAEL 706
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
399-632 |
6.34e-140 |
|
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: 424.64 E-value: 6.34e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 399 ISFKDVHFRYPSRKDIHVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDLREVNVHSLREQIG 478
Cdd:cd03249 1 IEFKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 479 IVSQEPVLFDGTIYENIKMGNEHATHDQVVEACKMANANDFIKRLPDGYGTRVGEKGVQLSGGQKQRIAIARALVKNPKI 558
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKI 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124244275 559 LLLDEATSALDTEAEREVQGALDQAQAGRTTIIVAHRLSTIRNVDRIFVFKAGNIVESGSHEELMSKQGIFYDM 632
Cdd:cd03249 161 LLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKL 234
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
1028-1266 |
3.30e-138 |
|
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: 420.02 E-value: 3.30e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1028 ISIRNVFFNYPTRKDTKVLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGMIMIDGDNIRNLNISSLREQVC 1107
Cdd:cd03249 1 IEFKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1108 IVSQEPTLFDCTIGENICYGTNrNVTYQEIVEAAKMANIHNFILGLPDGYDTHVGEKGTQLSGGQKQRIAIARALVRSPS 1187
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYGKP-DATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPK 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124244275 1188 VLLLDEATSALDTESEKIVQEALDAAKQGRTCLVIAHRLSTIQNSDVIAIVSEGKIVEKGTHDELIRKSEIYQKFCETQ 1266
Cdd:cd03249 160 ILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKAQ 238
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
67-632 |
3.44e-125 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 403.33 E-value: 3.44e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 67 HGAGFPLLAI-VLGGMTTVFLRAQNSDFVVGvdnvnpeglvPISLDEFNSEVVKYCIYYLVLGVLMFFtsyvQIACFESY 145
Cdd:TIGR00958 163 LISAFVFLTLsSLGEMFIPFYTGRVIDTLGG----------DKGPPALASAIFFMCLLSIASSVSAGL----RGGSFNYT 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 146 AERLVHKLRQNYLKAILRQQIQWFDKQQTGNLTARLTDDLERVREGLGDKFALLVQMFAAFLAGYGVGFFYSWSMTLVMM 225
Cdd:TIGR00958 229 MARINLRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLVMLLGLLGFMLWLSPRLTMVTL 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 226 GFAPLIVLSGAKMSK---SMATRTrveQETYAVAGAIAEETFSSIRTVHSLNGHKRELDRFYNALE----VGRQTGIVKY 298
Cdd:TIGR00958 309 INLPLVFLAEKVFGKryqLLSEEL---QEAVAKANQVAEEALSGMRTVRSFAAEEGEASRFKEALEetlqLNKRKALAYA 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 299 CYMGIgvgfSNLCMYSSYALAFWYGSTLIInDPTFDRGLIFTVFFAVLSgstsLGGALPHLASFGT----ARGAASTVLR 374
Cdd:TIGR00958 386 GYLWT----TSVLGMLIQVLVLYYGGQLVL-TGKVSSGNLVSFLLYQEQ----LGEAVRVLSYVYSgmmqAVGASEKVFE 456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 375 VINSHPKIdpySLEGILV-DNMKGDISFKDVHFRYPSRKDIHVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDP 453
Cdd:TIGR00958 457 YLDRKPNI---PLTGTLApLNLEGLIEFQDVSFSYPNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQP 533
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 454 TKGRVLIDGVDLREVNVHSLREQIGIVSQEPVLFDGTIYENIKMGNEHATHDQVVEACKMANANDFIKRLPDGYGTRVGE 533
Cdd:TIGR00958 534 TGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGE 613
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 534 KGVQLSGGQKQRIAIARALVKNPKILLLDEATSALDTEAEREVQGalDQAQAGRTTIIVAHRLSTIRNVDRIFVFKAGNI 613
Cdd:TIGR00958 614 KGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQE--SRSRASRTVLLIAHRLSTVERADQILVLKKGSV 691
|
570
....*....|....*....
gi 124244275 614 VESGSHEELMSKQGIFYDM 632
Cdd:TIGR00958 692 VEMGTHKQLMEDQGCYKHL 710
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
691-1266 |
1.09e-123 |
|
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: 399.21 E-value: 1.09e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 691 PTSMFKIFKFNGDKVGWFIGGIFG-------AFIFGSVTPVFALVYAeIF--NVYS--LPADQMQANVYFWCGMFVLMGI 759
Cdd:COG2274 130 PTPEFDKRGEKPFGLRWFLRLLRRyrrlllqVLLASLLINLLALATP-LFtqVVIDrvLPNQDLSTLWVLAIGLLLALLF 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 760 TFFVGFFtSANCLGRCGESLTMKLRFEAFKNLLRQDIAFYDdlRHGTGKLCTRFaTDAPNVRYVFT-RLPVVLASIVTIC 838
Cdd:COG2274 209 EGLLRLL-RSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFE--SRSVGDLASRF-RDVESIREFLTgSLLTALLDLLFVL 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 839 GALGIGFYYGWQLALILVVMVPLLVMGGYFemqmrFGKQIRDT--QLLEEAGKVASQAVE---HIRTVHSLNRQEQFHFT 913
Cdd:COG2274 285 IFLIVLFFYSPPLALVVLLLIPLYVLLGLL-----FQPRLRRLsrEESEASAKRQSLLVEtlrGIETIKALGAESRFRRR 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 914 YCEYLREPFNTNLKHAHTYGAVFAFSQSLIFFMYAAAFYLGSIFVNQQAM---QpidvyrvFFAI-SFCGQMIG---NTT 986
Cdd:COG2274 360 WENLLAKYLNARFKLRRLSNLLSTLSGLLQQLATVALLWLGAYLVIDGQLtlgQ-------LIAFnILSGRFLApvaQLI 432
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 987 SFIPDVVKARLAASLLFYLIEHPTPIDSLSDSGIVKPITGNISIRNVFFNYPTRkDTKVLQGFTLDIKAGKTVALVGHSG 1066
Cdd:COG2274 433 GLLQRFQDAKIALERLDDILDLPPEREEGRSKLSLPRLKGDIELENVSFRYPGD-SPPVLDNISLTIKPGERVAIVGRSG 511
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1067 CGKSTIMGLLERFYNQDKGMIMIDGDNIRNLNISSLREQVCIVSQEPTLFDCTIGENICYGtNRNVTYQEIVEAAKMANI 1146
Cdd:COG2274 512 SGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLG-DPDATDEEIIEAARLAGL 590
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1147 HNFILGLPDGYDTHVGEKGTQLSGGQKQRIAIARALVRSPSVLLLDEATSALDTESEKIVQEALDAAKQGRTCLVIAHRL 1226
Cdd:COG2274 591 HDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRL 670
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 124244275 1227 STIQNSDVIAIVSEGKIVEKGTHDELIRKSEIYQKFCETQ 1266
Cdd:COG2274 671 STIRLADRIIVLDKGRIVEDGTHEELLARKGLYAELVQQQ 710
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
69-629 |
7.71e-123 |
|
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: 392.53 E-value: 7.71e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 69 AGFPLLAIVLGGMTTVFLRaqnsdfvVGVDNVNPEGLVPISLDEFNSevvkYCIYYLVLGVLMFFTSYVQIACFESYAER 148
Cdd:TIGR02204 20 VLAALVALLITAAATLSLP-------YAVRLMIDHGFSKDSSGLLNR----YFAFLLVVALVLALGTAARFYLVTWLGER 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 149 LVHKLRQNYLKAILRQQIQWFDKQQTGNLTARLTDDLERVREGLGDKFALLVQMFAAFLAGYGVGFFYSWSMTLVMMGFA 228
Cdd:TIGR02204 89 VVADIRRAVFAHLISLSPSFFDKNRSGEVVSRLTTDTTLLQSVIGSSLSMALRNALMCIGGLIMMFITSPKLTSLVLLAV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 229 PLIVLSGAKMSKSMATRTRVEQETYAVAGAIAEETFSSIRTVHSLNGHKRELDRFYNALEVGRQTGIVKYCYMGIGVGFS 308
Cdd:TIGR02204 169 PLVLLPILLFGRRVRKLSRESQDRIADAGSYAGETLGAIRTVQAFGHEDAERSRFGGAVEKAYEAARQRIRTRALLTAIV 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 309 NLCMYSSYALAFWYGSTLIINDPTFDRGLIFTVFFAVLSGStSLGGALPHLASFGTARGAASTVLRVINSHPKIDPYSLE 388
Cdd:TIGR02204 249 IVLVFGAIVGVLWVGAHDVIAGKMSAGTLGQFVFYAVMVAG-SIGTLSEVWGELQRAAGAAERLIELLQAEPDIKAPAHP 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 389 GILVDNMKGDISFKDVHFRYPSRKDIHVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDLREV 468
Cdd:TIGR02204 328 KTLPVPLRGEIEFEQVNFAYPARPDQPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDLRQL 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 469 NVHSLREQIGIVSQEPVLFDGTIYENIKMGNEHATHDQVVEACKMANANDFIKRLPDGYGTRVGEKGVQLSGGQKQRIAI 548
Cdd:TIGR02204 408 DPAELRARMALVPQDPVLFAASVMENIRYGRPDATDEEVEAAARAAHAHEFISALPEGYDTYLGERGVTLSGGQRQRIAI 487
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 549 ARALVKNPKILLLDEATSALDTEAEREVQGALDQAQAGRTTIIVAHRLSTIRNVDRIFVFKAGNIVESGSHEELMSKQGI 628
Cdd:TIGR02204 488 ARAILKDAPILLLDEATSALDAESEQLVQQALETLMKGRTTLIIAHRLATVLKADRIVVMDQGRIVAQGTHAELIAKGGL 567
|
.
gi 124244275 629 F 629
Cdd:TIGR02204 568 Y 568
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
399-632 |
2.60e-117 |
|
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: 364.63 E-value: 2.60e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 399 ISFKDVHFRYPSrKDIHVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDLREVNVHSLREQIG 478
Cdd:cd03251 1 VEFKNVTFRYPG-DGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 479 IVSQEPVLFDGTIYENIKMGNEHATHDQVVEACKMANANDFIKRLPDGYGTRVGEKGVQLSGGQKQRIAIARALVKNPKI 558
Cdd:cd03251 80 LVSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124244275 559 LLLDEATSALDTEAEREVQGALDQAQAGRTTIIVAHRLSTIRNVDRIFVFKAGNIVESGSHEELMSKQGIFYDM 632
Cdd:cd03251 160 LILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKL 233
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
125-629 |
3.62e-117 |
|
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: 377.13 E-value: 3.62e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 125 LVLGVLMFFTSYvqiaCFESYAERLVHKLRQNYLKAILRQQIQWFDKQQTGNLTARLTDDLERVREGLGDKFALLVQMFA 204
Cdd:TIGR02203 65 VLRGICSFVSTY----LLSWVSNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLVRETL 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 205 AFLAGYGVGFFYSWSMTLVMMGFAPLIVLSGAKMSKSMATRTRVEQETYAVAGAIAEETFSSIRTVHSLNGHKRELDRFY 284
Cdd:TIGR02203 141 TVIGLFIVLLYYSWQLTLIVVVMLPVLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFD 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 285 NALEVGRQTGIVKYCYMGIGVGFSNLCMYSsyALAFwygstliindptfdrgLIFTVFFAVLSGSTSLGG---------- 354
Cdd:TIGR02203 221 AVSNRNRRLAMKMTSAGSISSPITQLIASL--ALAV----------------VLFIALFQAQAGSLTAGDftafitamia 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 355 ---ALPHLAS----FGTARGAASTVLRVINSHPKIDPYSLEgilVDNMKGDISFKDVHFRYPSRkDIHVLKGISLELKAG 427
Cdd:TIGR02203 283 lirPLKSLTNvnapMQRGLAAAESLFTLLDSPPEKDTGTRA---IERARGDVEFRNVTFRYPGR-DRPALDSISLVIEPG 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 428 DKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDLREVNVHSLREQIGIVSQEPVLFDGTIYENIKMGN-EHATHDQ 506
Cdd:TIGR02203 359 ETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRtEQADRAE 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 507 VVEACKMANANDFIKRLPDGYGTRVGEKGVQLSGGQKQRIAIARALVKNPKILLLDEATSALDTEAEREVQGALDQAQAG 586
Cdd:TIGR02203 439 IERALAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQG 518
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 124244275 587 RTTIIVAHRLSTIRNVDRIFVFKAGNIVESGSHEELMSKQGIF 629
Cdd:TIGR02203 519 RTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHNELLARNGLY 561
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
702-1266 |
1.62e-114 |
|
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: 370.18 E-value: 1.62e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 702 GDKVGWFIGGIFGAFIFGSVTPVFALVYAEIFNvyslPADQMQANVYFWCGMFVLMGI---TFFVGFFTSanclgRCGES 778
Cdd:TIGR02204 18 GRVLAALVALLITAAATLSLPYAVRLMIDHGFS----KDSSGLLNRYFAFLLVVALVLalgTAARFYLVT-----WLGER 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 779 LTMKLRFEAFKNLLRQDIAFYDDLRhgTGKLCTRFATDAPNVRYVF-TRLPVVLASIVTICGALGIGFYYGWQLALILVV 857
Cdd:TIGR02204 89 VVADIRRAVFAHLISLSPSFFDKNR--SGEVVSRLTTDTTLLQSVIgSSLSMALRNALMCIGGLIMMFITSPKLTSLVLL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 858 MVPLlVMGGYFEMQMRFGKQIRDTQ-LLEEAGKVASQAVEHIRTVHSLNRQEQFHFTYCEYLREPFNTNLKHAHTYGAVF 936
Cdd:TIGR02204 167 AVPL-VLLPILLFGRRVRKLSRESQdRIADAGSYAGETLGAIRTVQAFGHEDAERSRFGGAVEKAYEAARQRIRTRALLT 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 937 AFSQSLIFFMYAAAFYLGSIFVNQQAMQPIDVYR-VFFAIsFCGQMIGNTTSFIPDVVKARLAASLLFYLI-EHPTPIDS 1014
Cdd:TIGR02204 246 AIVIVLVFGAIVGVLWVGAHDVIAGKMSAGTLGQfVFYAV-MVAGSIGTLSEVWGELQRAAGAAERLIELLqAEPDIKAP 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1015 LSDSGIVKPITGNISIRNVFFNYPTRKDTKVLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGMIMIDGDNI 1094
Cdd:TIGR02204 325 AHPKTLPVPLRGEIEFEQVNFAYPARPDQPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDL 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1095 RNLNISSLREQVCIVSQEPTLFDCTIGENICYGtNRNVTYQEIVEAAKMANIHNFILGLPDGYDTHVGEKGTQLSGGQKQ 1174
Cdd:TIGR02204 405 RQLDPAELRARMALVPQDPVLFAASVMENIRYG-RPDATDEEVEAAARAAHAHEFISALPEGYDTYLGERGVTLSGGQRQ 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1175 RIAIARALVRSPSVLLLDEATSALDTESEKIVQEALDAAKQGRTCLVIAHRLSTIQNSDVIAIVSEGKIVEKGTHDELIR 1254
Cdd:TIGR02204 484 RIAIARAILKDAPILLLDEATSALDAESEQLVQQALETLMKGRTTLIIAHRLATVLKADRIVVMDQGRIVAQGTHAELIA 563
|
570
....*....|..
gi 124244275 1255 KSEIYQKFCETQ 1266
Cdd:TIGR02204 564 KGGLYARLARLQ 575
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
397-632 |
2.77e-114 |
|
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: 370.30 E-value: 2.77e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 397 GDISFKDVHFRYPSRKDIhvLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDLREVNVHSLREQ 476
Cdd:COG5265 356 GEVRFENVSFGYDPERPI--LKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAA 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 477 IGIVSQEPVLFDGTIYENIKMGNEHATHDQVVEACKMANANDFIKRLPDGYGTRVGEKGVQLSGGQKQRIAIARALVKNP 556
Cdd:COG5265 434 IGIVPQDTVLFNDTIAYNIAYGRPDASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNP 513
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 124244275 557 KILLLDEATSALDTEAEREVQGALDQAQAGRTTIIVAHRLSTIRNVDRIFVFKAGNIVESGSHEELMSKQGIFYDM 632
Cdd:COG5265 514 PILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLYAQM 589
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
669-1259 |
3.14e-114 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 373.67 E-value: 3.14e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 669 SAISIATSIHQLAEEVEECKAPPtsMFKIFKFNGDKVGWFIGGIFGAFIFgSVTPVF-----ALVYAEIFNVYSLPAdqM 743
Cdd:TIGR00958 126 AVLSSAGASEKEAEQGQSETADL--LFRLLGLSGRDWPWLISAFVFLTLS-SLGEMFipfytGRVIDTLGGDKGPPA--L 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 744 QANVYFwcgmfvlMGITFFVGFFtSANCLGRC----GESLTMKLRFEAFKNLLRQDIAFYDDlrHGTGKLCTRFATDAPN 819
Cdd:TIGR00958 201 ASAIFF-------MCLLSIASSV-SAGLRGGSfnytMARINLRIREDLFRSLLRQDLGFFDE--NKTGELTSRLSSDTQT 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 820 V-RYVFTRLPVVLASIVTICGALGIGFYYGWQLALILVVMVPLLvmggyFEMQMRFGKQIR----DTQ-LLEEAGKVASQ 893
Cdd:TIGR00958 271 MsRSLSLNVNVLLRNLVMLLGLLGFMLWLSPRLTMVTLINLPLV-----FLAEKVFGKRYQllseELQeAVAKANQVAEE 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 894 AVEHIRTVHSLNRQEQFHFTYCEYLREPFNTNLKHAHTYGAVFAFSQSLIFFMYAAAFYLGSIFVNQQAMQPIDVyrvff 973
Cdd:TIGR00958 346 ALSGMRTVRSFAAEEGEASRFKEALEETLQLNKRKALAYAGYLWTTSVLGMLIQVLVLYYGGQLVLTGKVSSGNL----- 420
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 974 aISFC------GQMIGNTTSFIPDVVKARLAASLLFYLIEHpTPidSLSDSGIVKP--ITGNISIRNVFFNYPTRKDTKV 1045
Cdd:TIGR00958 421 -VSFLlyqeqlGEAVRVLSYVYSGMMQAVGASEKVFEYLDR-KP--NIPLTGTLAPlnLEGLIEFQDVSFSYPNRPDVPV 496
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1046 LQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGMIMIDGDNIRNLNISSLREQVCIVSQEPTLFDCTIGENIC 1125
Cdd:TIGR00958 497 LKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIA 576
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1126 YGTNRnVTYQEIVEAAKMANIHNFILGLPDGYDTHVGEKGTQLSGGQKQRIAIARALVRSPSVLLLDEATSALDTESEKI 1205
Cdd:TIGR00958 577 YGLTD-TPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQL 655
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 124244275 1206 VQEalDAAKQGRTCLVIAHRLSTIQNSDVIAIVSEGKIVEKGTHDELIRKSEIY 1259
Cdd:TIGR00958 656 LQE--SRSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQGCY 707
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
399-632 |
1.17e-113 |
|
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: 354.61 E-value: 1.17e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 399 ISFKDVHFRY-PSRKdihVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDLREVNVHSLREQI 477
Cdd:cd03253 1 IEFENVTFAYdPGRP---VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 478 GIVSQEPVLFDGTIYENIKMGNEHATHDQVVEACKMANANDFIKRLPDGYGTRVGEKGVQLSGGQKQRIAIARALVKNPK 557
Cdd:cd03253 78 GVVPQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 124244275 558 ILLLDEATSALDTEAEREVQGALDQAQAGRTTIIVAHRLSTIRNVDRIFVFKAGNIVESGSHEELMSKQGIFYDM 632
Cdd:cd03253 158 ILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEM 232
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
708-1259 |
4.97e-113 |
|
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: 365.96 E-value: 4.97e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 708 FIGGIFGAFIFGSVTPVFALVYAEIFNVYSLPADqmqANVYFW-----CGMFVLMGITFFVGFFtsanCLGRCGESLTMK 782
Cdd:TIGR02203 16 LVLAGVAMILVAATESTLAALLKPLLDDGFGGRD---RSVLWWvplvvIGLAVLRGICSFVSTY----LLSWVSNKVVRD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 783 LRFEAFKNLLRQDIAFYDdlRHGTGKLCTRFATDAPNVRYVFTR-LPVVLASIVTICGALGIGFYYGWQLALILVVMVPL 861
Cdd:TIGR02203 89 IRVRMFEKLLGLPVSFFD--RQPTGTLLSRITFDSEQVASAATDaFIVLVRETLTVIGLFIVLLYYSWQLTLIVVVMLPV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 862 LVmggyFEMQM---RFGKQIRDTQ-LLEEAGKVASQAVEHIRTVHSLNRQEQfhftycEYLREPFNTN------LKHAHT 931
Cdd:TIGR02203 167 LS----ILMRRvskRLRRISKEIQnSMGQVTTVAEETLQGYRVVKLFGGQAY------ETRRFDAVSNrnrrlaMKMTSA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 932 YGAVFAFSQSLIFFMYAAAFYLGSIFVNQQAMQPIDVYRVFFAISFCGQMIGNTTSFIPDVVKARLAASLLFYLIEHPTP 1011
Cdd:TIGR02203 237 GSISSPITQLIASLALAVVLFIALFQAQAGSLTAGDFTAFITAMIALIRPLKSLTNVNAPMQRGLAAAESLFTLLDSPPE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1012 IDslsDSGIVKP-ITGNISIRNVFFNYPTRkDTKVLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGMIMID 1090
Cdd:TIGR02203 317 KD---TGTRAIErARGDVEFRNVTFRYPGR-DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLD 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1091 GDNIRNLNISSLREQVCIVSQEPTLFDCTIGENICYGTNRNVTYQEIVEAAKMANIHNFILGLPDGYDTHVGEKGTQLSG 1170
Cdd:TIGR02203 393 GHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRTEQADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSG 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1171 GQKQRIAIARALVRSPSVLLLDEATSALDTESEKIVQEALDAAKQGRTCLVIAHRLSTIQNSDVIAIVSEGKIVEKGTHD 1250
Cdd:TIGR02203 473 GQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHN 552
|
....*....
gi 124244275 1251 ELIRKSEIY 1259
Cdd:TIGR02203 553 ELLARNGLY 561
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
125-627 |
1.95e-112 |
|
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: 364.08 E-value: 1.95e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 125 LVLGVLMFFTSYVQIACFESYAERLVHKLRQNYLKAILRQQIQWFDKQQTGNLTARLTDDLErvreGLGDKFAL-LVQMF 203
Cdd:COG4988 65 LAVLLLRALLAWLRERAAFRAAARVKRRLRRRLLEKLLALGPAWLRGKSTGELATLLTEGVE----ALDGYFARyLPQLF 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 204 AAFLAG---YGVGFFYSWSMTLVMMGFAPLIVLSGAKMSKSMATRTRVEQETYAVAGAIAEETFSSIRTVHSLNGHKREL 280
Cdd:COG4988 141 LAALVPlliLVAVFPLDWLSGLILLVTAPLIPLFMILVGKGAAKASRRQWRALARLSGHFLDRLRGLTTLKLFGRAKAEA 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 281 DRFYNALEVGRQTgivkycYMGI-GVGFSnlcmySSYAL-AFWYGSTLIIndptfdrglIFTVFFAVLSGSTSLGGAL-- 356
Cdd:COG4988 221 ERIAEASEDFRKR------TMKVlRVAFL-----SSAVLeFFASLSIALV---------AVYIGFRLLGGSLTLFAALfv 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 357 ---------PhLASFGT-------ARGAASTVLRVINSHPKIDPYSlEGILVDNMKGDISFKDVHFRYPSRKdiHVLKGI 420
Cdd:COG4988 281 lllapefflP-LRDLGSfyharanGIAAAEKIFALLDAPEPAAPAG-TAPLPAAGPPSIELEDVSFSYPGGR--PALDGL 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 421 SLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDLREVNVHSLREQIGIVSQEPVLFDGTIYENIKMGNE 500
Cdd:COG4988 357 SLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRP 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 501 HATHDQVVEACKMANANDFIKRLPDGYGTRVGEKGVQLSGGQKQRIAIARALVKNPKILLLDEATSALDTEAEREVQGAL 580
Cdd:COG4988 437 DASDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQAL 516
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 124244275 581 DQAQAGRTTIIVAHRLSTIRNVDRIFVFKAGNIVESGSHEELMSKQG 627
Cdd:COG4988 517 RRLAKGRTVILITHRLALLAQADRILVLDDGRIVEQGTHEELLAKNG 563
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
698-1012 |
1.60e-110 |
|
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: 349.44 E-value: 1.60e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 698 FKFNGDKVGWFIGGIFGAFIFGSVTPVFALVYAEIFNVYSLP-ADQMQANVYFWCGMFVLMGITFFVGFFTSANCLGRCG 776
Cdd:cd18578 1 LKLNKPEWPLLLLGLIGAIIAGAVFPVFAILFSKLISVFSLPdDDELRSEANFWALMFLVLAIVAGIAYFLQGYLFGIAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 777 ESLTMKLRFEAFKNLLRQDIAFYDDLRHGTGKLCTRFATDAPNVRYVF-TRLPVVLASIVTICGALGIGFYYGWQLALIL 855
Cdd:cd18578 81 ERLTRRLRKLAFRAILRQDIAWFDDPENSTGALTSRLSTDASDVRGLVgDRLGLILQAIVTLVAGLIIAFVYGWKLALVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 856 VVMVPLLVMGGYFEMQMRFGKQIRDTQLLEEAGKVASQAVEHIRTVHSLNRQEQFHFTYCEYLREPFNTNLKHAHTYGAV 935
Cdd:cd18578 161 LATVPLLLLAGYLRMRLLSGFEEKNKKAYEESSKIASEAVSNIRTVASLTLEDYFLEKYEEALEEPLKKGLRRALISGLG 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 124244275 936 FAFSQSLIFFMYAAAFYLGSIFVNQQAMQPIDVYRVFFAISFCGQMIGNTTSFIPDVVKARLAASLLFYLIEHPTPI 1012
Cdd:cd18578 241 FGLSQSLTFFAYALAFWYGGRLVANGEYTFEQFFIVFMALIFGAQSAGQAFSFAPDIAKAKAAAARIFRLLDRKPEI 317
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
57-372 |
1.21e-109 |
|
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: 346.38 E-value: 1.21e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 57 LITGTVAAVIHGAGFPLLAIVLGGMTTVFlraqnSDFVVGvdnvnpeglvPISLDEFNSEVVKYCIYYLVLGVLMFFTSY 136
Cdd:cd18577 1 LIIGLLAAIAAGAALPLMTIVFGDLFDAF-----TDFGSG----------ESSPDEFLDDVNKYALYFVYLGIGSFVLSY 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 137 VQIACFESYAERLVHKLRQNYLKAILRQQIQWFDKQQTGNLTARLTDDLERVREGLGDKFALLVQMFAAFLAGYGVGFFY 216
Cdd:cd18577 66 IQTACWTITGERQARRIRKRYLKALLRQDIAWFDKNGAGELTSRLTSDTNLIQDGIGEKLGLLIQSLSTFIAGFIIAFIY 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 217 SWSMTLVMMGFAPLIVLSGAKMSKSMATRTRVEQETYAVAGAIAEETFSSIRTVHSLNGHKRELDRFYNALEVGRQTGIV 296
Cdd:cd18577 146 SWKLTLVLLATLPLIAIVGGIMGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKALEKARKAGIK 225
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 124244275 297 KYCYMGIGVGFSNLCMYSSYALAFWYGSTLIINDPTfDRGLIFTVFFAVLSGSTSLGGALPHLASFGTARGAASTV 372
Cdd:cd18577 226 KGLVSGLGLGLLFFIIFAMYALAFWYGSRLVRDGEI-SPGDVLTVFFAVLIGAFSLGQIAPNLQAFAKARAAAAKI 300
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
125-629 |
4.22e-106 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 347.39 E-value: 4.22e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 125 LVLGVLMF---FTSYVQIACFESYAERLVHKLRQNYLKAILRQQIQWFDKQQTGNLTARLTDDLERV------------R 189
Cdd:PRK11176 69 LVVIGLMIlrgITSFISSYCISWVSGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVassssgalitvvR 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 190 EGlgdkfALLVQMFAaflagygVGFFYSWSMTLVMMGFAPLIVLSGAKMSKSMATRTRVEQETYAVAGAIAEETFSSIRT 269
Cdd:PRK11176 149 EG-----ASIIGLFI-------MMFYYSWQLSLILIVIAPIVSIAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKE 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 270 VHSLNGHKRELDRFYNALEVGRQTGIvkycYMGIGVGFSN--LCMYSSYALAF-WYGSTLIINDPTFDRGLIFTVF---F 343
Cdd:PRK11176 217 VLIFGGQEVETKRFDKVSNRMRQQGM----KMVSASSISDpiIQLIASLALAFvLYAASFPSVMDTLTAGTITVVFssmI 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 344 AVLSGSTSLGGALphlASFGTARGAASTVLRVINSHPKIDPYSLEgilVDNMKGDISFKDVHFRYPSrKDIHVLKGISLE 423
Cdd:PRK11176 293 ALMRPLKSLTNVN---AQFQRGMAACQTLFAILDLEQEKDEGKRV---IERAKGDIEFRNVTFTYPG-KEVPALRNINFK 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 424 LKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDLREVNVHSLREQIGIVSQEPVLFDGTIYENIKMG-NEHA 502
Cdd:PRK11176 366 IPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYArTEQY 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 503 THDQVVEACKMANANDFIKRLPDGYGTRVGEKGVQLSGGQKQRIAIARALVKNPKILLLDEATSALDTEAEREVQGALDQ 582
Cdd:PRK11176 446 SREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDE 525
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 124244275 583 AQAGRTTIIVAHRLSTIRNVDRIFVFKAGNIVESGSHEELMSKQGIF 629
Cdd:PRK11176 526 LQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQNGVY 572
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
397-627 |
8.39e-106 |
|
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: 333.42 E-value: 8.39e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 397 GDISFKDVHFRYpsRKDIHVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDLREVNVHSLREQ 476
Cdd:cd03254 1 GEIEFENVNFSY--DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 477 IGIVSQEPVLFDGTIYENIKMGNEHATHDQVVEACKMANANDFIKRLPDGYGTRVGEKGVQLSGGQKQRIAIARALVKNP 556
Cdd:cd03254 79 IGVVLQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 124244275 557 KILLLDEATSALDTEAEREVQGALDQAQAGRTTIIVAHRLSTIRNVDRIFVFKAGNIVESGSHEELMSKQG 627
Cdd:cd03254 159 KILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
1028-1263 |
4.06e-103 |
|
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: 326.11 E-value: 4.06e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1028 ISIRNVFFNYPtRKDTKVLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGMIMIDGDNIRNLNISSLREQVC 1107
Cdd:cd03251 1 VEFKNVTFRYP-GDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1108 IVSQEPTLFDCTIGENICYGTnRNVTYQEIVEAAKMANIHNFILGLPDGYDTHVGEKGTQLSGGQKQRIAIARALVRSPS 1187
Cdd:cd03251 80 LVSQDVFLFNDTVAENIAYGR-PGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 124244275 1188 VLLLDEATSALDTESEKIVQEALDAAKQGRTCLVIAHRLSTIQNSDVIAIVSEGKIVEKGTHDELIRKSEIYQKFC 1263
Cdd:cd03251 159 ILILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKLH 234
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
752-1259 |
2.86e-102 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 336.99 E-value: 2.86e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 752 GMFVLMGITFFVgfftSANCLGRCGESLTMKLRFEAFKNLLRQDIAFYDdlRHGTGKLCTRFATDAPNVRYVFTRlpvVL 831
Cdd:PRK11176 73 GLMILRGITSFI----SSYCISWVSGKVVMTMRRRLFGHMMGMPVSFFD--KQSTGTLLSRITYDSEQVASSSSG---AL 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 832 ASIV----TICGALGIGFYYGWQLALILVVMVPLlVMGGYFEMQMRF---GKQIRDT---------QLLEEAGKVAS--- 892
Cdd:PRK11176 144 ITVVregaSIIGLFIMMFYYSWQLSLILIVIAPI-VSIAIRVVSKRFrniSKNMQNTmgqvttsaeQMLKGHKEVLIfgg 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 893 QAVEHIRTVHSLN--RQEQFHFTYCEYLREPFntnlkhahtygAVFAFSQSLIFFMYAAAFylGSIFVNQQAMQPIDVYR 970
Cdd:PRK11176 223 QEVETKRFDKVSNrmRQQGMKMVSASSISDPI-----------IQLIASLALAFVLYAASF--PSVMDTLTAGTITVVFS 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 971 VFFAISFCGQMIGNTTSfipDVVKARLAASLLFYLIEhptpIDSLSDSGI--VKPITGNISIRNVFFNYPTrKDTKVLQG 1048
Cdd:PRK11176 290 SMIALMRPLKSLTNVNA---QFQRGMAACQTLFAILD----LEQEKDEGKrvIERAKGDIEFRNVTFTYPG-KEVPALRN 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1049 FTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGMIMIDGDNIRNLNISSLREQVCIVSQEPTLFDCTIGENICYGT 1128
Cdd:PRK11176 362 INFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYAR 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1129 NRNVTYQEIVEAAKMANIHNFILGLPDGYDTHVGEKGTQLSGGQKQRIAIARALVRSPSVLLLDEATSALDTESEKIVQE 1208
Cdd:PRK11176 442 TEQYSREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQA 521
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 124244275 1209 ALDAAKQGRTCLVIAHRLSTIQNSDVIAIVSEGKIVEKGTHDELIRKSEIY 1259
Cdd:PRK11176 522 ALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQNGVY 572
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
145-632 |
9.75e-102 |
|
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: 335.20 E-value: 9.75e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 145 YAERLV-H--------KLRQNYLKAILRQQIQWFDKQQTGNLTARLTDDLERVreglgDKFAL--LVQMFAAFLAGYGVG 213
Cdd:COG4987 73 YLERLVsHdatlrllaDLRVRLYRRLEPLAPAGLARLRSGDLLNRLVADVDAL-----DNLYLrvLLPLLVALLVILAAV 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 214 F---FYSWSMTLVMMGF-------APLIVLSGAKMSKSMATRTRVEQETYAVAG--AIAEetfssIRTVHSLNGHKRELD 281
Cdd:COG4987 148 AflaFFSPALALVLALGlllagllLPLLAARLGRRAGRRLAAARAALRARLTDLlqGAAE-----LAAYGALDRALARLD 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 282 RF---YNALEvGRQTGIVkycymGIGVGFSNLCMYSSYALAFWYGSTLIiNDPTFDRGLIFTVFFAVLS---GSTSLGGA 355
Cdd:COG4987 223 AAearLAAAQ-RRLARLS-----ALAQALLQLAAGLAVVAVLWLAAPLV-AAGALSGPLLALLVLAALAlfeALAPLPAA 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 356 LPHLasfGTARGAASTVLRVINSHPKI-DPyslEGILVDNMKGDISFKDVHFRYPSRKDIhVLKGISLELKAGDKIALVG 434
Cdd:COG4987 296 AQHL---GRVRAAARRLNELLDAPPAVtEP---AEPAPAPGGPSLELEDVSFRYPGAGRP-VLDGLSLTLPPGERVAIVG 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 435 SSGCGKSTIVNLLQRFYDPTKGRVLIDGVDLREVNVHSLREQIGIVSQEPVLFDGTIYENIKMGNEHATHDQVVEACKMA 514
Cdd:COG4987 369 PSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPDATDEELWAALERV 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 515 NANDFIKRLPDGYGTRVGEKGVQLSGGQKQRIAIARALVKNPKILLLDEATSALDTEAEREVQGALDQAQAGRTTIIVAH 594
Cdd:COG4987 449 GLGDWLAALPDGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITH 528
|
490 500 510
....*....|....*....|....*....|....*...
gi 124244275 595 RLSTIRNVDRIFVFKAGNIVESGSHEELMSKQGIFYDM 632
Cdd:COG4987 529 RLAGLERMDRILVLEDGRIVEQGTHEELLAQNGRYRQL 566
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
1028-1266 |
1.21e-98 |
|
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: 314.17 E-value: 1.21e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1028 ISIRNVFFNYPTRKdtKVLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGMIMIDGDNIRNLNISSLREQVC 1107
Cdd:cd03253 1 IEFENVTFAYDPGR--PVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1108 IVSQEPTLFDCTIGENICYGtNRNVTYQEIVEAAKMANIHNFILGLPDGYDTHVGEKGTQLSGGQKQRIAIARALVRSPS 1187
Cdd:cd03253 79 VVPQDTVLFNDTIGYNIRYG-RPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124244275 1188 VLLLDEATSALDTESEKIVQEALDAAKQGRTCLVIAHRLSTIQNSDVIAIVSEGKIVEKGTHDELIRKSEIYQKFCETQ 1266
Cdd:cd03253 158 ILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMWKAQ 236
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
146-632 |
3.35e-97 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 323.07 E-value: 3.35e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 146 AERLVHKLRQ----NYLKAILRQQIQWFDKQQTGNLTA---RLTDDLERV-----REGLGDKFALLVQMfaaflagyGVG 213
Cdd:PRK13657 80 ADRLAHRRRLavltEYFERIIQLPLAWHSQRGSGRALHtllRGTDALFGLwlefmREHLATLVALVVLL--------PLA 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 214 FFYSWSMTLVMMGFAPLIVLSGA-KMSKSMATRTRVEQETYAVAgAIAEETFSSIRTVHSLN---GHKRELDRFYNALEV 289
Cdd:PRK13657 152 LFMNWRLSLVLVVLGIVYTLITTlVMRKTKDGQAAVEEHYHDLF-AHVSDAIGNVSVVQSYNrieAETQALRDIADNLLA 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 290 GrQTGIVkycymgigvgfsnlcmySSYALAfwygSTLIINDPTFDRGLIFTV-FFAVLSGSTSLG-------------GA 355
Cdd:PRK13657 231 A-QMPVL-----------------SWWALA----SVLNRAASTITMLAILVLgAALVQKGQLRVGevvafvgfatlliGR 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 356 LPHLASFgtargaastVLRVINSHPKI-DPYSLE-----------GILVDNMKGDISFKDVHFRYPSRKdiHVLKGISLE 423
Cdd:PRK13657 289 LDQVVAF---------INQVFMAAPKLeEFFEVEdavpdvrdppgAIDLGRVKGAVEFDDVSFSYDNSR--QGVEDVSFE 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 424 LKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDLREVNVHSLREQIGIVSQEPVLFDGTIYENIKMGNEHAT 503
Cdd:PRK13657 358 AKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRPDAT 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 504 HDQVVEACKMANANDFIKRLPDGYGTRVGEKGVQLSGGQKQRIAIARALVKNPKILLLDEATSALDTEAEREVQGALDQA 583
Cdd:PRK13657 438 DEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDEL 517
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 124244275 584 QAGRTTIIVAHRLSTIRNVDRIFVFKAGNIVESGSHEELMSKQGIFYDM 632
Cdd:PRK13657 518 MKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVARGGRFAAL 566
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
1026-1255 |
4.51e-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: 309.54 E-value: 4.51e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1026 GNISIRNVFFNYptRKDTKVLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGMIMIDGDNIRNLNISSLREQ 1105
Cdd:cd03254 1 GEIEFENVNFSY--DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1106 VCIVSQEPTLFDCTIGENICYGTNRNvTYQEIVEAAKMANIHNFILGLPDGYDTHVGEKGTQLSGGQKQRIAIARALVRS 1185
Cdd:cd03254 79 IGVVLQDTFLFSGTIMENIRLGRPNA-TDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRD 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1186 PSVLLLDEATSALDTESEKIVQEALDAAKQGRTCLVIAHRLSTIQNSDVIAIVSEGKIVEKGTHDELIRK 1255
Cdd:cd03254 158 PKILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAK 227
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
125-632 |
2.30e-94 |
|
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: 318.61 E-value: 2.30e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 125 LVLGVLMFFTSYVQIACFESYAERLVHKLRQNYLKAILRQQIQWFDKQQTGNLTARLTDdLERVREGL-GDKFALLVQMF 203
Cdd:TIGR01846 186 LAVAIFEPALGGLRTYLFAHLTSRIDVELGARLYRHLLGLPLGYFESRRVGDTVARVRE-LEQIRNFLtGSALTVVLDLL 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 204 AAFLAgYGVGFFYSWSMTLVMMGFAPLIVLSGAKMSKSMatRTRVEQ--ETYAVAGAIAEETFSSIRTV-------HSLN 274
Cdd:TIGR01846 265 FVVVF-LAVMFFYSPTLTGVVIGSLVCYALLSVFVGPIL--RKRVEDkfERSAAATSFLVESVTGIETIkatatepQFQN 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 275 GHKRELDRFYNALEVGRQTGIvkycymgIGVGFSNLCMYSSYALAFWYGSTLIINDPTFDRGLiftVFFAVLSGSTSlgG 354
Cdd:TIGR01846 342 RWDRQLAAYVAASFRVTNLGN-------IAGQAIELIQKLTFAILLWFGAHLVIGGALSPGQL---VAFNMLAGRVT--Q 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 355 ALPHLAS----FGTARGAASTVLRVINsHPKiDPYSLEGILVDNMKGDISFKDVHFRYpsRKDI-HVLKGISLELKAGDK 429
Cdd:TIGR01846 410 PVLRLAQlwqdFQQTGIALERLGDILN-SPT-EPRSAGLAALPELRGAITFENIRFRY--APDSpEVLSNLNLDIKPGEF 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 430 IALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDLREVNVHSLREQIGIVSQEPVLFDGTIYENIKMGNEHATHDQVVE 509
Cdd:TIGR01846 486 IGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAWLRRQMGVVLQENVLFSRSIRDNIALCNPGAPFEHVIH 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 510 ACKMANANDFIKRLPDGYGTRVGEKGVQLSGGQKQRIAIARALVKNPKILLLDEATSALDTEAEREVQGALDQAQAGRTT 589
Cdd:TIGR01846 566 AAKLAGAHDFISELPQGYNTEVGEKGANLSGGQRQRIAIARALVGNPRILIFDEATSALDYESEALIMRNMREICRGRTV 645
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 124244275 590 IIVAHRLSTIRNVDRIFVFKAGNIVESGSHEELMSKQGIFYDM 632
Cdd:TIGR01846 646 IIIAHRLSTVRACDRIIVLEKGQIAESGRHEELLALQGLYARL 688
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
1026-1259 |
6.02e-94 |
|
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: 314.84 E-value: 6.02e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1026 GNISIRNVFFNY-PTRKdtkVLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGMIMIDGDNIRNLNISSLRE 1104
Cdd:COG5265 356 GEVRFENVSFGYdPERP---ILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRA 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1105 QVCIVSQEPTLFDCTIGENICYGtNRNVTYQEIVEAAKMANIHNFILGLPDGYDTHVGEKGTQLSGGQKQRIAIARALVR 1184
Cdd:COG5265 433 AIGIVPQDTVLFNDTIAYNIAYG-RPDASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLK 511
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 124244275 1185 SPSVLLLDEATSALDTESEKIVQEALDAAKQGRTCLVIAHRLSTIQNSDVIAIVSEGKIVEKGTHDELIRKSEIY 1259
Cdd:COG5265 512 NPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLY 586
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
399-630 |
3.26e-90 |
|
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: 290.93 E-value: 3.26e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 399 ISFKDVHFRYpsRKD-IHVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDLREVNVHSLREQI 477
Cdd:cd03252 1 ITFEHVRFRY--KPDgPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 478 GIVSQEPVLFDGTIYENIKMGNEHATHDQVVEACKMANANDFIKRLPDGYGTRVGEKGVQLSGGQKQRIAIARALVKNPK 557
Cdd:cd03252 79 GVVLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 124244275 558 ILLLDEATSALDTEAEREVQGALDQAQAGRTTIIVAHRLSTIRNVDRIFVFKAGNIVESGSHEELMSKQGIFY 630
Cdd:cd03252 159 ILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYA 231
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
998-1255 |
2.71e-86 |
|
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: 292.05 E-value: 2.71e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 998 AASLLFYLIEHPTPIDSLSDSGIVKPITGNISIRNVFFNYPTRKdtKVLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLE 1077
Cdd:COG4988 307 AAEKIFALLDAPEPAAPAGTAPLPAAGPPSIELEDVSFSYPGGR--PALDGLSLTIPPGERVALVGPSGAGKSTLLNLLL 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1078 RFYNQDKGMIMIDGDNIRNLNISSLREQVCIVSQEPTLFDCTIGENICYGtNRNVTYQEIVEAAKMANIHNFILGLPDGY 1157
Cdd:COG4988 385 GFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLG-RPDASDEELEAALEAAGLDEFVAALPDGL 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1158 DTHVGEKGTQLSGGQKQRIAIARALVRSPSVLLLDEATSALDTESEKIVQEALDAAKQGRTCLVIAHRLSTIQNSDVIAI 1237
Cdd:COG4988 464 DTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQADRILV 543
|
250
....*....|....*...
gi 124244275 1238 VSEGKIVEKGTHDELIRK 1255
Cdd:COG4988 544 LDDGRIVEQGTHEELLAK 561
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
399-611 |
3.12e-85 |
|
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: 274.65 E-value: 3.12e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 399 ISFKDVHFRYPSRKDiHVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDLREVNVHSLREQIG 478
Cdd:cd03228 1 IEFKNVSFSYPGRPK-PVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 479 IVSQEPVLFDGTIYENIkmgnehathdqvveackmanandfikrlpdgygtrvgekgvqLSGGQKQRIAIARALVKNPKI 558
Cdd:cd03228 80 YVPQDPFLFSGTIRENI------------------------------------------LSGGQRQRIAIARALLRDPPI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 124244275 559 LLLDEATSALDTEAEREVQGALDQAQAGRTTIIVAHRLSTIRNVDRIFVFKAG 611
Cdd:cd03228 118 LILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDG 170
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
779-1264 |
2.97e-83 |
|
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: 283.58 E-value: 2.97e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 779 LTMKLRFEAFKNLLRQDIAFydDLRHGTGKLCTRFATDAPNVRYVFTRL--PVVLASIVTICGALGIGFYYgWQLALILV 856
Cdd:COG4987 86 LLADLRVRLYRRLEPLAPAG--LARLRSGDLLNRLVADVDALDNLYLRVllPLLVALLVILAAVAFLAFFS-PALALVLA 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 857 VM-------VPLLVMggyfemqmRFGKQIrDTQLLEEAGKVASQAVEHI-------------RTVHSLNRQEQfhftycE 916
Cdd:COG4987 163 LGlllagllLPLLAA--------RLGRRA-GRRLAAARAALRARLTDLLqgaaelaaygaldRALARLDAAEA------R 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 917 YLREpfntNLKHAHTYGAVFAFSQSLIFFMYAAAFYLGSIFVNQQAMQPIDVYRVFFAI--SFcgqmigNTTSFIPDVV- 993
Cdd:COG4987 228 LAAA----QRRLARLSALAQALLQLAAGLAVVAVLWLAAPLVAAGALSGPLLALLVLAAlaLF------EALAPLPAAAq 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 994 ---KARLAASLLFYLIEHPTPIdSLSDSGIVKPITGNISIRNVFFNYPTRkDTKVLQGFTLDIKAGKTVALVGHSGCGKS 1070
Cdd:COG4987 298 hlgRVRAAARRLNELLDAPPAV-TEPAEPAPAPGGPSLELEDVSFRYPGA-GRPVLDGLSLTLPPGERVAIVGPSGSGKS 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1071 TIMGLLERFYNQDKGMIMIDGDNIRNLNISSLREQVCIVSQEPTLFDCTIGENICYGtNRNVTYQEIVEAAKMANIHNFI 1150
Cdd:COG4987 376 TLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLA-RPDATDEELWAALERVGLGDWL 454
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1151 LGLPDGYDTHVGEKGTQLSGGQKQRIAIARALVRSPSVLLLDEATSALDTESEKIVQEALDAAKQGRTCLVIAHRLSTIQ 1230
Cdd:COG4987 455 AALPDGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLE 534
|
490 500 510
....*....|....*....|....*....|....
gi 124244275 1231 NSDVIAIVSEGKIVEKGTHDELIRKSEIYQKFCE 1264
Cdd:COG4987 535 RMDRILVLEDGRIVEQGTHEELLAQNGRYRQLYQ 568
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
831-1255 |
9.73e-82 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 279.92 E-value: 9.73e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 831 LASIVTICGALGIGFYYGWQLALILVVMVPLLVMGGYFEMQMRFGKQIRDTQLLEEAGKVASQAVEHIRTVHSLNRQEqf 910
Cdd:PRK13657 138 LATLVALVVLLPLALFMNWRLSLVLVVLGIVYTLITTLVMRKTKDGQAAVEEHYHDLFAHVSDAIGNVSVVQSYNRIE-- 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 911 hfTYCEYLREpFNTNLKHAHT-------YGAVFAFSQSLIFFMyaAAFYLGSIFVNQQAMQPIDVyrVFFaISFCGQMIG 983
Cdd:PRK13657 216 --AETQALRD-IADNLLAAQMpvlswwaLASVLNRAASTITML--AILVLGAALVQKGQLRVGEV--VAF-VGFATLLIG 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 984 ---NTTSFIPDVVKArlAASL-LFYLIEHPTP-IDSLSDSGIVKPITGNISIRNVFFNYPTRKdtKVLQGFTLDIKAGKT 1058
Cdd:PRK13657 288 rldQVVAFINQVFMA--APKLeEFFEVEDAVPdVRDPPGAIDLGRVKGAVEFDDVSFSYDNSR--QGVEDVSFEAKPGQT 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1059 VALVGHSGCGKSTIMGLLERFYNQDKGMIMIDGDNIRNLNISSLREQVCIVSQEPTLFDCTIGENICYGtNRNVTYQEIV 1138
Cdd:PRK13657 364 VAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVG-RPDATDEEMR 442
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1139 EAAKMANIHNFILGLPDGYDTHVGEKGTQLSGGQKQRIAIARALVRSPSVLLLDEATSALDTESEKIVQEALDAAKQGRT 1218
Cdd:PRK13657 443 AAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRT 522
|
410 420 430
....*....|....*....|....*....|....*..
gi 124244275 1219 CLVIAHRLSTIQNSDVIAIVSEGKIVEKGTHDELIRK 1255
Cdd:PRK13657 523 TFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVAR 559
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
393-613 |
6.68e-80 |
|
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: 262.02 E-value: 6.68e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 393 DNMKGDISFKDVHFRYPSRKDIHVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDLREVNVHS 472
Cdd:cd03248 6 DHLKGIVKFQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 473 LREQIGIVSQEPVLFDGTIYENIKMGNEHATHDQVVEACKMANANDFIKRLPDGYGTRVGEKGVQLSGGQKQRIAIARAL 552
Cdd:cd03248 86 LHSKVSLVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARAL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 124244275 553 VKNPKILLLDEATSALDTEAEREVQGALDQAQAGRTTIIVAHRLSTIRNVDRIFVFKAGNI 613
Cdd:cd03248 166 IRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
397-617 |
8.50e-80 |
|
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: 261.37 E-value: 8.50e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 397 GDISFKDVHFRYPSRKdIHVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDLREVNVHSLREQ 476
Cdd:cd03245 1 GRIEFRNVSFSYPNQE-IPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 477 IGIVSQEPVLFDGTIYENIKMGNEHATHDQVVEACKMANANDFIKRLPDGYGTRVGEKGVQLSGGQKQRIAIARALVKNP 556
Cdd:cd03245 80 IGYVPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 124244275 557 KILLLDEATSALDTEAEREVQGALDQAQAGRTTIIVAHRLSTIRNVDRIFVFKAGNIVESG 617
Cdd:cd03245 160 PILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
1026-1243 |
1.12e-79 |
|
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: 261.25 E-value: 1.12e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1026 GNISIRNVFFNYPTRKDTKVLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGMIMIDGDNIRNLNISSLREQ 1105
Cdd:cd03248 10 GIVKFQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1106 VCIVSQEPTLFDCTIGENICYGTnRNVTYQEIVEAAKMANIHNFILGLPDGYDTHVGEKGTQLSGGQKQRIAIARALVRS 1185
Cdd:cd03248 90 VSLVGQEPVLFARSLQDNIAYGL-QSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRN 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 124244275 1186 PSVLLLDEATSALDTESEKIVQEALDAAKQGRTCLVIAHRLSTIQNSDVIAIVSEGKI 1243
Cdd:cd03248 169 PQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
53-382 |
3.97e-79 |
|
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: 263.16 E-value: 3.97e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 53 DLLLLITGTVAAVIHGAGFPLLAIVLGGMTTVFlraqnsdfvvgvdnvnpeglVPISLDEFNSEVVKYCIYYLVLGVLMF 132
Cdd:cd18578 7 EWPLLLLGLIGAIIAGAVFPVFAILFSKLISVF--------------------SLPDDDELRSEANFWALMFLVLAIVAG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 133 FTSYVQIACFESYAERLVHKLRQNYLKAILRQQIQWFDKQQ--TGNLTARLTDDLERVREGLGDKFALLVQMFAAFLAGY 210
Cdd:cd18578 67 IAYFLQGYLFGIAGERLTRRLRKLAFRAILRQDIAWFDDPEnsTGALTSRLSTDASDVRGLVGDRLGLILQAIVTLVAGL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 211 GVGFFYSWSMTLVMMGFAPLIVLSGAKMSKSMATRTRVEQETYAVAGAIAEETFSSIRTVHSLNGHKRELDRFYNALEVG 290
Cdd:cd18578 147 IIAFVYGWKLALVGLATVPLLLLAGYLRMRLLSGFEEKNKKAYEESSKIASEAVSNIRTVASLTLEDYFLEKYEEALEEP 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 291 RQTGIVKYCYMGIGVGFSNLCMYSSYALAFWYGSTLIINDP-TFDRglIFTVFFAVLSGSTSLGGALPHLASFGTARGAA 369
Cdd:cd18578 227 LKKGLRRALISGLGFGLSQSLTFFAYALAFWYGGRLVANGEyTFEQ--FFIVFMALIFGAQSAGQAFSFAPDIAKAKAAA 304
|
330
....*....|...
gi 124244275 370 STVLRVINSHPKI 382
Cdd:cd18578 305 ARIFRLLDRKPEI 317
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
162-632 |
1.54e-76 |
|
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: 267.98 E-value: 1.54e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 162 LRQQIQWFDKQQTGNLTARlTDDLERVREGLGDKF--ALLVQMFAAFlaGYGVGFFYSWSMTLVMMGfapLIVLSGAKMS 239
Cdd:TIGR03797 220 LRLPVSFFRQYSTGDLASR-AMGISQIRRILSGSTltTLLSGIFALL--NLGLMFYYSWKLALVAVA---LALVAIAVTL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 240 KSMATRTRVEQETYAVAGAIAEETFSSIRTVHSLN---GHKRELDR----FYNALEVGRQTGIVKYCYMGIGVGFSNLCM 312
Cdd:TIGR03797 294 VLGLLQVRKERRLLELSGKISGLTVQLINGISKLRvagAENRAFARwaklFSRQRKLELSAQRIENLLTVFNAVLPVLTS 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 313 YSSYALAFWYGSTLIINDPTFdrgLIFTVFFAVLSGS-TSLGGALPHLASFGTARGAASTVLRVI--NSHPKIDPysleG 389
Cdd:TIGR03797 374 AALFAAAISLLGGAGLSLGSF---LAFNTAFGSFSGAvTQLSNTLISILAVIPLWERAKPILEALpeVDEAKTDP----G 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 390 ILvdnmKGDISFKDVHFRYpsRKD-IHVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDLREV 468
Cdd:TIGR03797 447 KL----SGAIEVDRVTFRY--RPDgPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGL 520
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 469 NVHSLREQIGIVSQEPVLFDGTIYENIkMGNEHATHDQVVEACKMANANDFIKRLPDGYGTRVGEKGVQLSGGQKQRIAI 548
Cdd:TIGR03797 521 DVQAVRRQLGVVLQNGRLMSGSIFENI-AGGAPLTLDEAWEAARMAGLAEDIRAMPMGMHTVISEGGGTLSGGQRQRLLI 599
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 549 ARALVKNPKILLLDEATSALDTEAEREVQGALDQAQAGRttIIVAHRLSTIRNVDRIFVFKAGNIVESGSHEELMSKQGI 628
Cdd:TIGR03797 600 ARALVRKPRILLFDEATSALDNRTQAIVSESLERLKVTR--IVIAHRLSTIRNADRIYVLDAGRVVQQGTYDELMAREGL 677
|
....
gi 124244275 629 FYDM 632
Cdd:TIGR03797 678 FAQL 681
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
146-632 |
1.96e-76 |
|
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: 264.83 E-value: 1.96e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 146 AERLVHKLRQNYLKA----ILRQQIQWFDKQQTGN---LTARLTDD-----LERVREGLGDKFALLVQMFAAFLAgygvg 213
Cdd:TIGR01192 80 ADRLAHGRRATLLTEafgrIISMPLSWHQQRGTSNalhTLLRATETlfglwLEFMRQHLATFVALFLLIPTAFAM----- 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 214 ffySWSMTLVMMGFAPL-IVLSGAKMSKSMATRTRVEQETYAVAGAIAEeTFSSIRTVHSLN---GHKRELDRFYNALeV 289
Cdd:TIGR01192 155 ---DWRLSIVLMVLGILyILIAKLVMQRTKNGQAAVEHHYHNVFKHVSD-SISNVSVVHSYNrieAETSALKQFTNNL-L 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 290 GRQTGIVKYcyMGIGVGFSNLCMYSSYALAFWYGSTLIINDPTFDRGLIFTVFFAVLsgstsLGGALPHLASFGTargaa 369
Cdd:TIGR01192 230 SAQYPVLDW--WALASGLNRMASTISMMCILVIGTVLVIKGELSVGEVIAFIGFANL-----LIGRLDQMSGFIT----- 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 370 stvlRVINSHPKI-DPYSLEGILVD-----------NMKGDISFKDVHFRYPSRKdiHVLKGISLELKAGDKIALVGSSG 437
Cdd:TIGR01192 298 ----QIFEARAKLeDFFDLEDSVFQreepadapelpNVKGAVEFRHITFEFANSS--QGVFDVSFEAKAGQTVAIVGPTG 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 438 CGKSTIVNLLQRFYDPTKGRVLIDGVDLREVNVHSLREQIGIVSQEPVLFDGTIYENIKMGNEHATHDQVVEACKMANAN 517
Cdd:TIGR01192 372 AGKTTLINLLQRVYDPTVGQILIDGIDINTVTRESLRKSIATVFQDAGLFNRSIRENIRLGREGATDEEVYEAAKAAAAH 451
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 518 DFIKRLPDGYGTRVGEKGVQLSGGQKQRIAIARALVKNPKILLLDEATSALDTEAEREVQGALDQAQAGRTTIIVAHRLS 597
Cdd:TIGR01192 452 DFILKRSNGYDTLVGERGNRLSGGERQRLAIARAILKNAPILVLDEATSALDVETEARVKNAIDALRKNRTTFIIAHRLS 531
|
490 500 510
....*....|....*....|....*....|....*
gi 124244275 598 TIRNVDRIFVFKAGNIVESGSHEELMSKQGIFYDM 632
Cdd:TIGR01192 532 TVRNADLVLFLDQGRLIEKGSFQELIQKDGRFYKL 566
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
1028-1266 |
8.96e-76 |
|
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: 250.87 E-value: 8.96e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1028 ISIRNVFFNYptRKDTK-VLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGMIMIDGDNIRNLNISSLREQV 1106
Cdd:cd03252 1 ITFEHVRFRY--KPDGPvILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1107 CIVSQEPTLFDCTIGENICYgTNRNVTYQEIVEAAKMANIHNFILGLPDGYDTHVGEKGTQLSGGQKQRIAIARALVRSP 1186
Cdd:cd03252 79 GVVLQENVLFNRSIRDNIAL-ADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1187 SVLLLDEATSALDTESEKIVQEALDAAKQGRTCLVIAHRLSTIQNSDVIAIVSEGKIVEKGTHDELIRKSEIYQKFCETQ 1266
Cdd:cd03252 158 RILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQLQ 237
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
57-372 |
1.68e-74 |
|
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: 250.27 E-value: 1.68e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 57 LITGTVAAVIHGAGFPLLAIVLGGMTTVFLRAQNSDFVVGVDNVNPEGLVPISLDEfnsEVVKYCIYYLVLGVLMFFTSY 136
Cdd:cd18558 1 MVVGILCAIIHGGLLPAFMVIFGDMTDSFTNGGMTNITGNSSGLNSSAGPFEKLEE---EMTLYAYYYLIIGAIVLITAY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 137 VQIACFESYAERLVHKLRQNYLKAILRQQIQWFDKQQTGNLTARLTDDLERVREGLGDKFALLVQMFAAFLAGYGVGFFY 216
Cdd:cd18558 78 IQGSFWGLAAGRQTKKIRYKFFHAIMRQEIGWFDVNDTGELNTRLADDVSKINEGIGDKIGVIFQNIATFGTGFIIGFIR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 217 SWSMTLVMMGFAPLIVLSGAKMSKSMATRTRVEQETYAVAGAIAEETFSSIRTVHSLNGHKRELDRFYNALEVGRQTGIV 296
Cdd:cd18558 158 GWKLTLVILAISPVLGLSAVVWAKILSGFTDKEKKAYAKAGAVAEEVLEAFRTVIAFGGQQKEETRYAQNLEIAKRNGIK 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 124244275 297 KYCYMGIGVGFSNLCMYSSYALAFWYGSTLIINDpTFDRGLIFTVFFAVLSGSTSLGGALPHLASFGTARGAASTV 372
Cdd:cd18558 238 KAITFNISMGAAFLLIYASYALAFWYGTYLVTQQ-EYSIGEVLTVFFSVLIGAFSAGQQVPSIEAFANARGAAYHI 312
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
356-1259 |
2.56e-74 |
|
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: 272.20 E-value: 2.56e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 356 LPHLASFGTARGAASTVLRVINSHPKIDPYSLEGILVDNMKGD-ISFKDVHFRYpSRKDIHVLKGISLELKAGDKIALVG 434
Cdd:TIGR00957 593 LPMVISSIVQASVSLKRLRIFLSHEELEPDSIERRTIKPGEGNsITVHNATFTW-ARDLPPTLNGITFSIPEGALVAVVG 671
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 435 SSGCGKSTIVNLLQRFYDPTKGRVLIDGvdlrevnvhslreQIGIVSQEPVLFDGTIYENIKMGN--EHATHDQVVEACK 512
Cdd:TIGR00957 672 QVGCGKSSLLSALLAEMDKVEGHVHMKG-------------SVAYVPQQAWIQNDSLRENILFGKalNEKYYQQVLEACA 738
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 513 MANAndfIKRLPDGYGTRVGEKGVQLSGGQKQRIAIARALVKNPKILLLDEATSALDTEAEREV-------QGALdqaqA 585
Cdd:TIGR00957 739 LLPD---LEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIfehvigpEGVL----K 811
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 586 GRTTIIVAHRLSTIRNVDRIFVFKAGNIVESGSHEELMSKQGIFYDM---------TQAQVVRQQQQEAGKD-----IED 651
Cdd:TIGR00957 812 NKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAFAEFlrtyapdeqQGHLEDSWTALVSGEGkeaklIEN 891
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 652 T--ISESAHSHLSRKSSTRSAISIATSIH-------QLAEEVEEC--------KAPPTSMFKIFKFNGDKVGWFIG--GI 712
Cdd:TIGR00957 892 GmlVTDVVGKQLQRQLSASSSDSGDQSRHhgssaelQKAEAKEETwklmeadkAQTGQVELSVYWDYMKAIGLFITflSI 971
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 713 FgAFIFGSVTPVFALVYAEIFNVYSLpADQMQANVYFWCGMFVLMGITFFVGFFTSANCLGRCGESLTMKLRFEAFKNLL 792
Cdd:TIGR00957 972 F-LFVCNHVSALASNYWLSLWTDDPM-VNGTQNNTSLRLSVYGALGILQGFAVFGYSMAVSIGGIQASRVLHQDLLHNKL 1049
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 793 RQDIAFYDdlRHGTGKLCTRFATDAPNVRYVFTrlPVVLASIVTICGALGIGFYYGWQLALILVVMVPLLVMggYFEMQM 872
Cdd:TIGR00957 1050 RSPMSFFE--RTPSGNLVNRFSKELDTVDSMIP--PVIKMFMGSLFNVIGALIVILLATPIAAVIIPPLGLL--YFFVQR 1123
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 873 RFGKQIRDTQLLEEAGKVA-----SQAVEHIRTVHSLNRQEQFhftyceYLREPFNTNLKHAHTYGAVFA---FSQSLIF 944
Cdd:TIGR00957 1124 FYVASSRQLKRLESVSRSPvyshfNETLLGVSVIRAFEEQERF------IHQSDLKVDENQKAYYPSIVAnrwLAVRLEC 1197
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 945 F-----MYAAAFYLgsifVNQQAMQPIDV-------YRVFFAISFCGQMIGNTTSFIPDVVKARLAASL---LFYLIEHP 1009
Cdd:TIGR00957 1198 VgncivLFAALFAV----ISRHSLSAGLVglsvsysLQVTFYLNWLVRMSSEMETNIVAVERLKEYSETekeAPWQIQET 1273
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1010 TPIDSLsdsgivkPITGNISIRNVFFNYptRKDTK-VLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGMIM 1088
Cdd:TIGR00957 1274 APPSGW-------PPRGRVEFRNYCLRY--REDLDlVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEII 1344
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1089 IDGDNIRNLNISSLREQVCIVSQEPTLFDCTIGENIcyGTNRNVTYQEIVEAAKMANIHNFILGLPDGYDTHVGEKGTQL 1168
Cdd:TIGR00957 1345 IDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNL--DPFSQYSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENL 1422
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1169 SGGQKQRIAIARALVRSPSVLLLDEATSALDTESEKIVQEALDAAKQGRTCLVIAHRLSTIQNSDVIAIVSEGKIVEKGT 1248
Cdd:TIGR00957 1423 SVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGA 1502
|
970
....*....|.
gi 124244275 1249 HDELIRKSEIY 1259
Cdd:TIGR00957 1503 PSNLLQQRGIF 1513
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
161-627 |
2.63e-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: 259.49 E-value: 2.63e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 161 ILRQQIQWFDKQQTGNLTARLTDDlERVREGLGDKFA-----LLVQMFAAFLAgygvgFFYSWSMTLVMMGFAPLIVLSG 235
Cdd:TIGR03796 237 ILRLPVRFFAQRHAGDIASRVQLN-DQVAEFLSGQLAttaldAVMLVFYALLM-----LLYDPVLTLIGIAFAAINVLAL 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 236 AKMSKSMATRTRVEQETYAVAGAIAeetFSSIRTVHSLNGHKRELDRF-----YNALEV-GRQTGIVKYCYMGIgvgFSN 309
Cdd:TIGR03796 311 QLVSRRRVDANRRLQQDAGKLTGVA---ISGLQSIETLKASGLESDFFsrwagYQAKLLnAQQELGVLTQILGV---LPT 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 310 LCMYSSYALAFWYGSTLIIN-DPTFDRGLIFTV----FFAVLSGSTSLGGALPHLASfgtargaasTVLRV--INSHPkI 382
Cdd:TIGR03796 385 LLTSLNSALILVVGGLRVMEgQLTIGMLVAFQSlmssFLEPVNNLVGFGGTLQELEG---------DLNRLddVLRNP-V 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 383 DPYSLEGILVD-------NMKGDISFKDVHFRYpSRKDIHVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTK 455
Cdd:TIGR03796 455 DPLLEEPEGSAatsepprRLSGYVELRNITFGY-SPLEPPLIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWS 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 456 GRVLIDGVDLREVNVHSLREQIGIVSQEPVLFDGTIYENIKMGNEHATHDQVVEACKMANANDFIKRLPDGYGTRVGEKG 535
Cdd:TIGR03796 534 GEILFDGIPREEIPREVLANSVAMVDQDIFLFEGTVRDNLTLWDPTIPDADLVRACKDAAIHDVITSRPGGYDAELAEGG 613
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 536 VQLSGGQKQRIAIARALVKNPKILLLDEATSALDTEAEREVQGALdqAQAGRTTIIVAHRLSTIRNVDRIFVFKAGNIVE 615
Cdd:TIGR03796 614 ANLSGGQRQRLEIARALVRNPSILILDEATSALDPETEKIIDDNL--RRRGCTCIIVAHRLSTIRDCDEIIVLERGKVVQ 691
|
490
....*....|..
gi 124244275 616 SGSHEELMSKQG 627
Cdd:TIGR03796 692 RGTHEELWAVGG 703
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
1028-1242 |
1.74e-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: 1.74e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1028 ISIRNVFFNYPTRkDTKVLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGMIMIDGDNIRNLNISSLREQVC 1107
Cdd:cd03228 1 IEFKNVSFSYPGR-PKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1108 IVSQEPTLFDCTIGENIcygtnrnvtyqeiveaakmanihnfilglpdgydthvgekgtqLSGGQKQRIAIARALVRSPS 1187
Cdd:cd03228 80 YVPQDPFLFSGTIRENI-------------------------------------------LSGGQRQRIAIARALLRDPP 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 124244275 1188 VLLLDEATSALDTESEKIVQEALDAAKQGRTCLVIAHRLSTIQNSDVIAIVSEGK 1242
Cdd:cd03228 117 ILILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
397-618 |
4.99e-72 |
|
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: 239.32 E-value: 4.99e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 397 GDISFKDVHFRYPSRKDIhVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDLREVNVHSLREQ 476
Cdd:cd03244 1 GDIEFKNVSLRYRPNLPP-VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 477 IGIVSQEPVLFDGTIYENIKMGNEHaTHDQVVEACKMANANDFIKRLPDGYGTRVGEKGVQLSGGQKQRIAIARALVKNP 556
Cdd:cd03244 80 ISIIPQDPVLFSGTIRSNLDPFGEY-SDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124244275 557 KILLLDEATSALDTEAEREVQGALDQAQAGRTTIIVAHRLSTIRNVDRIFVFKAGNIVESGS 618
Cdd:cd03244 159 KILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
1010-1266 |
1.19e-71 |
|
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: 254.28 E-value: 1.19e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1010 TPIDSLSDSGIVKP-ITGNISIRNVFFNYptRKDT-KVLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGMI 1087
Cdd:TIGR01846 437 SPTEPRSAGLAALPeLRGAITFENIRFRY--APDSpEVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQV 514
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1088 MIDGDNIRNLNISSLREQVCIVSQEPTLFDCTIGENICYGtNRNVTYQEIVEAAKMANIHNFILGLPDGYDTHVGEKGTQ 1167
Cdd:TIGR01846 515 LVDGVDLAIADPAWLRRQMGVVLQENVLFSRSIRDNIALC-NPGAPFEHVIHAAKLAGAHDFISELPQGYNTEVGEKGAN 593
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1168 LSGGQKQRIAIARALVRSPSVLLLDEATSALDTESEKIVQEALDAAKQGRTCLVIAHRLSTIQNSDVIAIVSEGKIVEKG 1247
Cdd:TIGR01846 594 LSGGQRQRIAIARALVGNPRILIFDEATSALDYESEALIMRNMREICRGRTVIIIAHRLSTVRACDRIIVLEKGQIAESG 673
|
250
....*....|....*....
gi 124244275 1248 THDELIRKSEIYQKFCETQ 1266
Cdd:TIGR01846 674 RHEELLALQGLYARLWQQQ 692
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
117-632 |
1.43e-70 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 247.70 E-value: 1.43e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 117 VVKYCIYYlVLGVLMFFTSYvqiacfesyaeRLVHKLRQNYLKAILRQQIQWFDKQQTGNLTARLTDDLERVREGLGDKF 196
Cdd:PRK10789 47 VVVYLLRY-VWRVLLFGASY-----------QLAVELREDFYRQLSRQHPEFYLRHRTGDLMARATNDVDRVVFAAGEGV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 197 ALLVQ---MFAAFLAGYGVGFfySWSMTLVMMGFAPLIVLSGAKMSKSMATRTRVEQETYAVAGAIAEETFSSIRTVHSL 273
Cdd:PRK10789 115 LTLVDslvMGCAVLIVMSTQI--SWQLTLLALLPMPVMAIMIKRYGDQLHERFKLAQAAFSSLNDRTQESLTSIRMIKAF 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 274 NGHKRELDRFYN-ALEVGRQTGIVK----------YcymgIGVGFSNLcmyssyaLAFWYGSTLIINdptfdrgliftvf 342
Cdd:PRK10789 193 GLEDRQSALFAAdAEDTGKKNMRVAridarfdptiY----IAIGMANL-------LAIGGGSWMVVN------------- 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 343 favlsGSTSLGgalpHLASFG-------------------TARGAA--STVLRVINSHPKIDPYSLEgilVDNMKGDISF 401
Cdd:PRK10789 249 -----GSLTLG----QLTSFVmylglmiwpmlalawmfniVERGSAaySRIRAMLAEAPVVKDGSEP---VPEGRGELDV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 402 KDVHFRYPsRKDIHVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDLREVNVHSLREQIGIVS 481
Cdd:PRK10789 317 NIRQFTYP-QTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVS 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 482 QEPVLFDGTIYENIKMGNEHATHDQVVEACKMANANDFIKRLPDGYGTRVGEKGVQLSGGQKQRIAIARALVKNPKILLL 561
Cdd:PRK10789 396 QTPFLFSDTVANNIALGRPDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILIL 475
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 124244275 562 DEATSALDTEAEREVQGALDQAQAGRTTIIVAHRLSTIRNVDRIFVFKAGNIVESGSHEELMSKQGIFYDM 632
Cdd:PRK10789 476 DDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSGWYRDM 546
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
778-1261 |
2.59e-69 |
|
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: 247.55 E-value: 2.59e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 778 SLTMKLRFeaFKNLLRQDIAFYDDlRHgTGKLCTRFATDAPNVRYVFTRLPVVLASIVTICGALGIGFYYGWQLALILVV 857
Cdd:TIGR03796 226 AVGMSARF--LWHILRLPVRFFAQ-RH-AGDIASRVQLNDQVAEFLSGQLATTALDAVMLVFYALLMLLYDPVLTLIGIA 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 858 MVPLLVMGGYFEMQMRFGKQIRdtqLLEEAGKVASQAVEHIRTVHSLNR---QEQFHFTYCEYLREPFNTNLKHAHTYGA 934
Cdd:TIGR03796 302 FAAINVLALQLVSRRRVDANRR---LQQDAGKLTGVAISGLQSIETLKAsglESDFFSRWAGYQAKLLNAQQELGVLTQI 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 935 VFAFSQSLIFFMYAAAFYLGSIFVNQQAMQpIDVYRVFFAI--SFCG---QMIGNTTSF---------IPDVVKARLAAs 1000
Cdd:TIGR03796 379 LGVLPTLLTSLNSALILVVGGLRVMEGQLT-IGMLVAFQSLmsSFLEpvnNLVGFGGTLqelegdlnrLDDVLRNPVDP- 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1001 llfyLIEHPTPIDSLSDSgiVKPITGNISIRNVFFNYpTRKDTKVLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFY 1080
Cdd:TIGR03796 457 ----LLEEPEGSAATSEP--PRRLSGYVELRNITFGY-SPLEPPLIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLY 529
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1081 NQDKGMIMIDGDNIRNLNISSLREQVCIVSQEPTLFDCTIGENIcygT--NRNVTYQEIVEAAKMANIHNFILGLPDGYD 1158
Cdd:TIGR03796 530 QPWSGEILFDGIPREEIPREVLANSVAMVDQDIFLFEGTVRDNL---TlwDPTIPDADLVRACKDAAIHDVITSRPGGYD 606
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1159 THVGEKGTQLSGGQKQRIAIARALVRSPSVLLLDEATSALDTESEKIVQEALdaAKQGRTCLVIAHRLSTIQNSDVIAIV 1238
Cdd:TIGR03796 607 AELAEGGANLSGGQRQRLEIARALVRNPSILILDEATSALDPETEKIIDDNL--RRRGCTCIIVAHRLSTIRDCDEIIVL 684
|
490 500
....*....|....*....|...
gi 124244275 1239 SEGKIVEKGTHDELIRKSEIYQK 1261
Cdd:TIGR03796 685 ERGKVVQRGTHEELWAVGGAYAR 707
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
396-625 |
1.38e-67 |
|
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: 238.88 E-value: 1.38e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 396 KGDISFKDVHFRYPSRKDiHVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDLREVNVHSLRE 475
Cdd:COG4618 328 KGRLSVENLTVVPPGSKR-PILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGR 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 476 QIGIVSQEPVLFDGTIYENI-KMGNehATHDQVVEACKMANANDFIKRLPDGYGTRVGEKGVQLSGGQKQRIAIARALVK 554
Cdd:COG4618 407 HIGYLPQDVELFDGTIAENIaRFGD--ADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYG 484
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124244275 555 NPKILLLDEATSALDTEAEREVQGALDQA-QAGRTTIIVAHRLSTIRNVDRIFVFKAGNIVESGSHEELMSK 625
Cdd:COG4618 485 DPRLVVLDEPNSNLDDEGEAALAAAIRALkARGATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
415-632 |
2.51e-67 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 238.59 E-value: 2.51e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 415 HVLKG-ISLELKAGDKIALVGSSGCGKSTIVNLLQRFYdPTKGRVLIDGVDLREVNVHSLREQIGIVSQEPVLFDGTIYE 493
Cdd:PRK11174 363 KTLAGpLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRD 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 494 NIKMGNEHATHDQVVEACKMANANDFIKRLPDGYGTRVGEKGVQLSGGQKQRIAIARALVKNPKILLLDEATSALDTEAE 573
Cdd:PRK11174 442 NVLLGNPDASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSE 521
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 124244275 574 REVQGALDQAQAGRTTIIVAHRLSTIRNVDRIFVFKAGNIVESGSHEELMSKQGIFYDM 632
Cdd:PRK11174 522 QLVMQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATL 580
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
74-607 |
2.54e-67 |
|
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: 237.18 E-value: 2.54e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 74 LAIVLGGMTTVFLRAQNSDFVVGVDNVNPEGLvpiSLDEFNSEVVKYCIYYLVLGVLMFFTSYVQIACfesyAERLVHKL 153
Cdd:TIGR02857 7 LLALLGVLGALLIIAQAWLLARVVDGLISAGE---PLAELLPALGALALVLLLRALLGWLQERAAARA----AAAVKSQL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 154 RQNYLKAILRQQIQWFDKQQTGNLTARLTDDLErvreGLGDKFAL-LVQMFAA------FLAgygVGFFYSWSMTLVMMG 226
Cdd:TIGR02857 80 RERLLEAVAALGPRWLQGRPSGELATLALEGVE----ALDGYFARyLPQLVLAvivplaILA---AVFPQDWISGLILLL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 227 FAPLIVLSGAKMSKSMATRTRVEQETYAVAGAIAEETFSSIRTVHSLNGHKRELDRFYNALEVGRQTGivkycyMGI-GV 305
Cdd:TIGR02857 153 TAPLIPIFMILIGWAAQAAARKQWAALSRLSGHFLDRLRGLPTLKLFGRAKAQAAAIRRSSEEYRERT------MRVlRI 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 306 GFsnlcmYSSYAL-----------AFWYGSTLIINDPTFDRGLIFTV----FFAVLSGStslgGALPHLASFGTArgAAS 370
Cdd:TIGR02857 227 AF-----LSSAVLelfatlsvalvAVYIGFRLLAGDLDLATGLFVLLlapeFYLPLRQL----GAQYHARADGVA--AAE 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 371 TVLRVINSHPKIDPYSLEgiLVDNMKGDISFKDVHFRYPSRKDihVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRF 450
Cdd:TIGR02857 296 ALFAVLDAAPRPLAGKAP--VTAAPASSLEFSGVSVAYPGRRP--ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGF 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 451 YDPTKGRVLIDGVDLREVNVHSLREQIGIVSQEPVLFDGTIYENIKMGNEHATHDQVVEACKMANANDFIKRLPDGYGTR 530
Cdd:TIGR02857 372 VDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLARPDASDAEIREALERAGLDEFVAALPQGLDTP 451
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 124244275 531 VGEKGVQLSGGQKQRIAIARALVKNPKILLLDEATSALDTEAEREVQGALDQAQAGRTTIIVAHRLSTIRNVDRIFV 607
Cdd:TIGR02857 452 IGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRIVV 528
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
337-630 |
6.79e-66 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 234.33 E-value: 6.79e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 337 LIFTVFFAVLSGSTSL---GGALPHLASFGTArgaASTVLRVINSHPKIDpYSLEGILVDNmKGDISFKDVHFRYPSRKD 413
Cdd:PRK11160 279 LIALFVFAALAAFEALmpvAGAFQHLGQVIAS---ARRINEITEQKPEVT-FPTTSTAAAD-QVSLTLNNVSFTYPDQPQ 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 414 iHVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDLREVNVHSLREQIGIVSQEPVLFDGTIYE 493
Cdd:PRK11160 354 -PVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRD 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 494 NIKMGNEHATHDQVVEACKMANANDFIKRlPDGYGTRVGEKGVQLSGGQKQRIAIARALVKNPKILLLDEATSALDTEAE 573
Cdd:PRK11160 433 NLLLAAPNASDEALIEVLQQVGLEKLLED-DKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETE 511
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 124244275 574 REVQGALDQAQAGRTTIIVAHRLSTIRNVDRIFVFKAGNIVESGSHEELMSKQGIFY 630
Cdd:PRK11160 512 RQILELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQGRYY 568
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
1026-1247 |
1.95e-65 |
|
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: 220.54 E-value: 1.95e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1026 GNISIRNVFFNYPTRKdTKVLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGMIMIDGDNIRNLNISSLREQ 1105
Cdd:cd03245 1 GRIEFRNVSFSYPNQE-IPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1106 VCIVSQEPTLFDCTIGENICYGtNRNVTYQEIVEAAKMANIHNFILGLPDGYDTHVGEKGTQLSGGQKQRIAIARALVRS 1185
Cdd:cd03245 80 IGYVPQDVTLFYGTLRDNITLG-APLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLND 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124244275 1186 PSVLLLDEATSALDTESEKIVQEALDAAKQGRTCLVIAHRLSTIQNSDVIAIVSEGKIVEKG 1247
Cdd:cd03245 159 PPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
756-1266 |
1.65e-64 |
|
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: 232.92 E-value: 1.65e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 756 LMGITFFVGFFTSANCLGRCGESLTMkLRFEAFKN----------LLRQDIAFYDdlRHGTGKLCTRfatdAPNVRYVFT 825
Cdd:TIGR03797 175 LVQIALALLAAAVGAAAFQLAQSLAV-LRLETRMDaslqaavwdrLLRLPVSFFR--QYSTGDLASR----AMGISQIRR 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 826 RLP-----VVLASIVTICgALGIGFYYGWQLALILVVM--VPLLVMGGYFEMQMRfgkqiRDTQLLEEAGKVASQAVEHI 898
Cdd:TIGR03797 248 ILSgstltTLLSGIFALL-NLGLMFYYSWKLALVAVALalVAIAVTLVLGLLQVR-----KERRLLELSGKISGLTVQLI 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 899 RTV-------------------HSLNRQEQFHFTYCEYLREPFNTNLKhAHTYGAVFAFsqsLIFFMYAAAFYLGSiFVN 959
Cdd:TIGR03797 322 NGIsklrvagaenrafarwaklFSRQRKLELSAQRIENLLTVFNAVLP-VLTSAALFAA---AISLLGGAGLSLGS-FLA 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 960 qqamqpidvyrvfFAISFcGQMIGNTTSFIPDVVKArLAASLLFyliEHPTPI-DSLSDSGIVKP----ITGNISIRNVF 1034
Cdd:TIGR03797 397 -------------FNTAF-GSFSGAVTQLSNTLISI-LAVIPLW---ERAKPIlEALPEVDEAKTdpgkLSGAIEVDRVT 458
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1035 FNYptRKDTK-VLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGMIMIDGDNIRNLNISSLREQVCIVSQEP 1113
Cdd:TIGR03797 459 FRY--RPDGPlILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLDVQAVRRQLGVVLQNG 536
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1114 TLFDCTIGENICyGTNRnVTYQEIVEAAKMANIHNFILGLPDGYDTHVGEKGTQLSGGQKQRIAIARALVRSPSVLLLDE 1193
Cdd:TIGR03797 537 RLMSGSIFENIA-GGAP-LTLDEAWEAARMAGLAEDIRAMPMGMHTVISEGGGTLSGGQRQRLLIARALVRKPRILLFDE 614
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 124244275 1194 ATSALDTESEKIVQEALDAAKQGRtcLVIAHRLSTIQNSDVIAIVSEGKIVEKGTHDELIRKSEIYQKFCETQ 1266
Cdd:TIGR03797 615 ATSALDNRTQAIVSESLERLKVTR--IVIAHRLSTIRNADRIYVLDAGRVVQQGTYDELMAREGLFAQLARRQ 685
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
708-1000 |
2.86e-61 |
|
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: 211.95 E-value: 2.86e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 708 FIGGIFGAFIFGSVTPVFALVYAEIFNVYS------LPADQMQANVYFWCGMFVLMGITFFVGFFTSANCLGRCGESLTM 781
Cdd:cd18577 1 LIIGLLAAIAAGAALPLMTIVFGDLFDAFTdfgsgeSSPDEFLDDVNKYALYFVYLGIGSFVLSYIQTACWTITGERQAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 782 KLRFEAFKNLLRQDIAFYDDlrHGTGKLCTRFATDAPNVRYVF-TRLPVVLASIVTICGALGIGFYYGWQLALILVVMVP 860
Cdd:cd18577 81 RIRKRYLKALLRQDIAWFDK--NGAGELTSRLTSDTNLIQDGIgEKLGLLIQSLSTFIAGFIIAFIYSWKLTLVLLATLP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 861 LLVMGGYFeMQMRFGKQIRDTQ-LLEEAGKVASQAVEHIRTVHSLNRQEQFHFTYCEYLREPFNTNLKHAHTYGAVFAFS 939
Cdd:cd18577 159 LIAIVGGI-MGKLLSKYTKKEQeAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKALEKARKAGIKKGLVSGLGLGLL 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 124244275 940 QSLIFFMYAAAFYLGSIFVNQQAMQPIDVYRVFFAISFCGQMIGNTTSFIPDVVKARLAAS 1000
Cdd:cd18577 238 FFIIFAMYALAFWYGSRLVRDGEISPGDVLTVFFAVLIGAFSLGQIAPNLQAFAKARAAAA 298
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
145-596 |
6.33e-61 |
|
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: 218.38 E-value: 6.33e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 145 YAERLV-H--------KLRQNYLKAILRQQIQWFDKQQTGNLTARLTDDLERVREGLgdkFALLVQMFAAFLAG---YGV 212
Cdd:TIGR02868 71 YLERLVgHdaalrslgALRVRVYERLARQALAGRRRLRRGDLLGRLGADVDALQDLY---VRVIVPAGVALVVGaaaVAA 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 213 GFFYSWSMTLVMM------GF-APLIVLSGAKMSKSMATRTRVE---QETYAVAGAiAEETFS--SIRTVHSLnghkREL 280
Cdd:TIGR02868 148 IAVLSVPAALILAaglllaGFvAPLVSLRAARAAEQALARLRGElaaQLTDALDGA-AELVASgaLPAALAQV----EEA 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 281 DRFYNALEVGRQTGivkycyMGIGVGFSNLCMYSSYALAFWYGSTLIIN---DPTFDRGLIFTVFfAVLSGSTSLGGALP 357
Cdd:TIGR02868 223 DRELTRAERRAAAA------TALGAALTLLAAGLAVLGALWAGGPAVADgrlAPVTLAVLVLLPL-AAFEAFAALPAAAQ 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 358 HLasfGTARGAASTVLRVIN--------SHPKIDPYSLEGIlvdnmkgDISFKDVHFRYPSrkDIHVLKGISLELKAGDK 429
Cdd:TIGR02868 296 QL---TRVRAAAERIVEVLDaagpvaegSAPAAGAVGLGKP-------TLELRDLSAGYPG--APPVLDGVSLDLPPGER 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 430 IALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDLREVNVHSLREQIGIVSQEPVLFDGTIYENIKMGNEHATHDQVVE 509
Cdd:TIGR02868 364 VAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPDATDEELWA 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 510 ACKMANANDFIKRLPDGYGTRVGEKGVQLSGGQKQRIAIARALVKNPKILLLDEATSALDTEAEREVQGALDQAQAGRTT 589
Cdd:TIGR02868 444 ALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTV 523
|
....*..
gi 124244275 590 IIVAHRL 596
Cdd:TIGR02868 524 VLITHHL 530
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
97-632 |
1.26e-60 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 219.20 E-value: 1.26e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 97 VDNVNPEGLVPISLdefnseVVKYCIYYLVLGVLMFFTSYVQIACFESYAERLVHKLRQNYLKAILRQQIQWFDKQQTGN 176
Cdd:PRK10790 50 IDNMVAKGNLPLGL------VAGLAAAYVGLQLLAAGLHYAQSLLFNRAAVGVVQQLRTDVMDAALRQPLSAFDTQPVGQ 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 177 LTARLTDDLERVREglgdkfaLLVQMFAAFLAGYG-VG------FFYSWSMTLVMMGFAP--LIVLS-GAKMSKSMATRT 246
Cdd:PRK10790 124 LISRVTNDTEVIRD-------LYVTVVATVLRSAAlIGamlvamFSLDWRMALVAIMIFPavLVVMViYQRYSTPIVRRV 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 247 RveqeTYAvagAIAEETFSSIRTVHSLNGHKRELDRF-----------YNA-LEVGRQTGIVKYCYMGIgvgFSNLCMyS 314
Cdd:PRK10790 197 R----AYL---ADINDGFNEVINGMSVIQQFRQQARFgermgeasrshYMArMQTLRLDGFLLRPLLSL---FSALIL-C 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 315 SYALAFWYGSTLIINdptfdrgliFTVFFAVLSGSTSLGGALPHLAS----FGTARGAASTVLRVINS---HPKIDPYSL 387
Cdd:PRK10790 266 GLLMLFGFSASGTIE---------VGVLYAFISYLGRLNEPLIELTTqqsmLQQAVVAGERVFELMDGprqQYGNDDRPL 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 388 EGilvdnmkGDISFKDVHFRYpsRKDIHVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDLRE 467
Cdd:PRK10790 337 QS-------GRIDIDNVSFAY--RDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSS 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 468 VNVHSLREQIGIVSQEPVLFDGTIYENIKMGnEHATHDQVVEACKMANANDFIKRLPDGYGTRVGEKGVQLSGGQKQRIA 547
Cdd:PRK10790 408 LSHSVLRQGVAMVQQDPVVLADTFLANVTLG-RDISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLA 486
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 548 IARALVKNPKILLLDEATSALDTEAEREVQGALDQAQAGRTTIIVAHRLSTIRNVDRIFVFKAGNIVESGSHEELMSKQG 627
Cdd:PRK10790 487 LARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQG 566
|
....*
gi 124244275 628 IFYDM 632
Cdd:PRK10790 567 RYWQM 571
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
135-632 |
2.65e-60 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 221.15 E-value: 2.65e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 135 SYVQIACFESYAERLVHKLRQNYLKAILRQQIQWFDKQQTGNLTARLTDdLERVREGLGDK-FALLVQMFAAFLAGYGVG 213
Cdd:TIGR01193 213 SYIQIFLLNVLGQRLSIDIILSYIKHLFELPMSFFSTRRTGEIVSRFTD-ASSIIDALASTiLSLFLDMWILVIVGLFLV 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 214 FFYS--WSMTLVMMGFAPLIVLSGAKMSKSMATRTrveQETYAVAGAIAEETFSSIRTVHSLNG-----HKRElDRFYNA 286
Cdd:TIGR01193 292 RQNMllFLLSLLSIPVYAVIIILFKRTFNKLNHDA---MQANAVLNSSIIEDLNGIETIKSLTSeaerySKID-SEFGDY 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 287 LEVGRQTGIVKYCYMGIGVGfSNLCMYssyALAFWYGSTLiindptfdrgliftvffaVLSGSTSLGgalpHLASFGTAR 366
Cdd:TIGR01193 368 LNKSFKYQKADQGQQAIKAV-TKLILN---VVILWTGAYL------------------VMRGKLTLG----QLITFNALL 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 367 GAASTVLR-VINSHPKIDPYSL------EGILVD-------------NMKGDISFKDVHFRYPSRKDIhvLKGISLELKA 426
Cdd:TIGR01193 422 SYFLTPLEnIINLQPKLQAARVannrlnEVYLVDsefinkkkrtelnNLNGDIVINDVSYSYGYGSNI--LSDISLTIKM 499
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 427 GDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDLREVNVHSLREQIGIVSQEPVLFDGTIYENIKMGN-EHATHD 505
Cdd:TIGR01193 500 NSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLGAkENVSQD 579
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 506 QVVEACKMANANDFIKRLPDGYGTRVGEKGVQLSGGQKQRIAIARALVKNPKILLLDEATSALDTEAEREVQGALDQAQA 585
Cdd:TIGR01193 580 EIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQD 659
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 124244275 586 gRTTIIVAHRLSTIRNVDRIFVFKAGNIVESGSHEELMSKQGIFYDM 632
Cdd:TIGR01193 660 -KTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYASL 705
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
962-1255 |
3.10e-60 |
|
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: 217.31 E-value: 3.10e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 962 AMQPIDvyrvffaisfcgQMIGNTTSFipdvVKARLA-ASLLFYLIEHPTPIDSLSdsgIVKPiTGNISIRNVFFNYPTR 1040
Cdd:COG4618 284 ALAPIE------------QAIGGWKQF----VSARQAyRRLNELLAAVPAEPERMP---LPRP-KGRLSVENLTVVPPGS 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1041 KDTkVLQGFTLDIKAGKTVALVGHSGCGKST----IMGLLErfynQDKGMIMIDGDNIRNLNISSLREQVCIVSQEPTLF 1116
Cdd:COG4618 344 KRP-ILRGVSFSLEPGEVLGVIGPSGSGKSTlarlLVGVWP----PTAGSVRLDGADLSQWDREELGRHIGYLPQDVELF 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1117 DCTIGENICygtnR--NVTYQEIVEAAKMANIHNFILGLPDGYDTHVGEKGTQLSGGQKQRIAIARALVRSPSVLLLDEA 1194
Cdd:COG4618 419 DGTIAENIA----RfgDADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEP 494
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124244275 1195 TSALDTESEKIVQEALDAAKQ-GRTCLVIAHRLSTIQNSDVIAIVSEGKIVEKGTHDELIRK 1255
Cdd:COG4618 495 NSNLDDEGEAALAAAIRALKArGATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
57-349 |
7.57e-60 |
|
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: 206.72 E-value: 7.57e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 57 LITGTVAAVIHGAGFPLLAIVLGGMTTVFLRAQNSDFVvgvdnvnpeglvpisldefnsEVVKYCIYYLVLGVLMFFTSY 136
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLPDGDPETQ---------------------ALNVYSLALLLLGLAQFILSF 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 137 VQIACFESYAERLVHKLRQNYLKAILRQQIQWFDKQQTGNLTARLTDDLERVREGLGDKFALLVQMFAAFLAGYGVGFFY 216
Cdd:pfam00664 60 LQSYLLNHTGERLSRRLRRKLFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYY 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 217 SWSMTLVMMGFAPLIVLSGAKMSKSMATRTRVEQETYAVAGAIAEETFSSIRTVHSLNGHKRELDRFYNALEVGRQTGIV 296
Cdd:pfam00664 140 GWKLTLVLLAVLPLYILVSAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIK 219
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 124244275 297 KYCYMGIGVGFSNLCMYSSYALAFWYGSTLII-NDPTFDRGLIFTVFFAVLSGS 349
Cdd:pfam00664 220 KAVANGLSFGITQFIGYLSYALALWFGAYLVIsGELSVGDLVAFLSLFAQLFGP 273
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
126-1255 |
2.73e-59 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 224.47 E-value: 2.73e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 126 VLGVLMFFTSYVQIACFESYAE---RLVHKLRQNYLKAILRQQIQWFDKQQ----TGNLTARLTDD---LERVREGL--- 192
Cdd:PLN03232 342 VYAFLIFFGVTFGVLCESQYFQnvgRVGFRLRSTLVAAIFHKSLRLTHEARknfaSGKVTNMITTDanaLQQIAEQLhgl 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 193 -GDKFALLVQMFAAFlAGYGVGFFYSWSMTLVMMGFAPLIVLSGAKMSKSMATRT--RVeqetyavagAIAEETFSSIRT 269
Cdd:PLN03232 422 wSAPFRIIVSMVLLY-QQLGVASLFGSLILFLLIPLQTLIVRKMRKLTKEGLQWTdkRV---------GIINEILASMDT 491
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 270 VHSLNGHKRELDRFYnalevgrqtgivkycymgiGVGFSNLCMYSSYALAFWYGSTLIINDPTFDRGLIFTVFfAVLSGS 349
Cdd:PLN03232 492 VKCYAWEKSFESRIQ-------------------GIRNEELSWFRKAQLLSAFNSFILNSIPVVVTLVSFGVF-VLLGGD 551
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 350 TSLGGALPHLASFGTARGAAST----VLRVIN---SHPKIDPYSL--EGILVDNMKGD-----ISFKDVHFRYPSRKDIH 415
Cdd:PLN03232 552 LTPARAFTSLSLFAVLRSPLNMlpnlLSQVVNanvSLQRIEELLLseERILAQNPPLQpgapaISIKNGYFSWDSKTSKP 631
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 416 VLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIdgvdlrevnvhsLREQIGIVSQEPVLFDGTIYENI 495
Cdd:PLN03232 632 TLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSSVV------------IRGSVAYVPQVSWIFNATVRENI 699
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 496 KMGN--EHATHDQVVEACKMANANDFikrLPDGYGTRVGEKGVQLSGGQKQRIAIARALVKNPKILLLDEATSALDTEAE 573
Cdd:PLN03232 700 LFGSdfESERYWRAIDVTALQHDLDL---LPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVA 776
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 574 REV-QGALDQAQAGRTTIIVAHRLSTIRNVDRIFVFKAGNIVESGSHEELmSKQGIFYDmtqaqvvrQQQQEAGKdIEDT 652
Cdd:PLN03232 777 HQVfDSCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAEL-SKSGSLFK--------KLMENAGK-MDAT 846
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 653 ISESAHS----HLSRKSSTRSAISIATSIHQLAE------EVEECKAPPTSMFKIFKFNgDKVG--WFIGGIFGAFIFGS 720
Cdd:PLN03232 847 QEVNTNDenilKLGPTVTIDVSERNLGSTKQGKRgrsvlvKQEERETGIISWNVLMRYN-KAVGglWVVMILLVCYLTTE 925
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 721 VTPVFALVYAEIFNvyslpaDQMQANVY---FWCGMFVLMGITFFVGFFTSANCLGRCGESLTMKLRFEAFKNLLRQDIA 797
Cdd:PLN03232 926 VLRVSSSTWLSIWT------DQSTPKSYspgFYIVVYALLGFGQVAVTFTNSFWLISSSLHAAKRLHDAMLNSILRAPML 999
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 798 FYDDlrHGTGKLCTRFATD-------APNVRYVFTRLPVVLASIVTICGALGigfyygwqlALILVVMVPLLVMggYFEM 870
Cdd:PLN03232 1000 FFHT--NPTGRVINRFSKDigdidrnVANLMNMFMNQLWQLLSTFALIGTVS---------TISLWAIMPLLIL--FYAA 1066
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 871 QMRFGKQIRDTQLLEEAGKV--------ASQAVEHIRTVHSLNRQEQFHftyCEYLREPFNTNLKHAHTYGAVFAFSQSL 942
Cdd:PLN03232 1067 YLYYQSTSREVRRLDSVTRSpiyaqfgeALNGLSSIRAYKAYDRMAKIN---GKSMDNNIRFTLANTSSNRWLTIRLETL 1143
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 943 ---IFFMYAAAFYLGSIFVNQQAMqpidvyrvfFAiSFCGQMIG---NTTSFIPDVVK-ARLAASLLFYLIEHPTPIDSL 1015
Cdd:PLN03232 1144 ggvMIWLTATFAVLRNGNAENQAG---------FA-STMGLLLSytlNITTLLSGVLRqASKAENSLNSVERVGNYIDLP 1213
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1016 SDS-GIVK--------PITGNISIRNVFFNYptRKD-TKVLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDKG 1085
Cdd:PLN03232 1214 SEAtAIIEnnrpvsgwPSRGSIKFEDVHLRY--RPGlPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKG 1291
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1086 MIMIDGDNIRNLNISSLREQVCIVSQEPTLFDCTIGENICYGTNRNVTyqEIVEAAKMANIHNFILGLPDGYDTHVGEKG 1165
Cdd:PLN03232 1292 RIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNIDPFSEHNDA--DLWEALERAHIKDVIDRNPFGLDAEVSEGG 1369
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1166 TQLSGGQKQRIAIARALVRSPSVLLLDEATSALDTESEKIVQEALDAAKQGRTCLVIAHRLSTIQNSDVIAIVSEGKIVE 1245
Cdd:PLN03232 1370 ENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLE 1449
|
1210
....*....|
gi 124244275 1246 KGTHDELIRK 1255
Cdd:PLN03232 1450 YDSPQELLSR 1459
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
995-1235 |
1.43e-58 |
|
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: 211.76 E-value: 1.43e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 995 ARLAASLLFYLIEHPTPIdSLSDSGIVKPITGNISIRNVFFNYPTRkdTKVLQGFTLDIKAGKTVALVGHSGCGKSTIMG 1074
Cdd:TIGR02857 290 GVAAAEALFAVLDAAPRP-LAGKAPVTAAPASSLEFSGVSVAYPGR--RPALRPVSFTVPPGERVALVGPSGAGKSTLLN 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1075 LLERFYNQDKGMIMIDGDNIRNLNISSLREQVCIVSQEPTLFDCTIGENICYGTnRNVTYQEIVEAAKMANIHNFILGLP 1154
Cdd:TIGR02857 367 LLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLAR-PDASDAEIREALERAGLDEFVAALP 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1155 DGYDTHVGEKGTQLSGGQKQRIAIARALVRSPSVLLLDEATSALDTESEKIVQEALDAAKQGRTCLVIAHRLSTIQNSDV 1234
Cdd:TIGR02857 446 QGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADR 525
|
.
gi 124244275 1235 I 1235
Cdd:TIGR02857 526 I 526
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
1026-1248 |
2.03e-58 |
|
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: 200.80 E-value: 2.03e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1026 GNISIRNVFFNYptRKDTK-VLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGMIMIDGDNIRNLNISSLRE 1104
Cdd:cd03244 1 GDIEFKNVSLRY--RPNLPpVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1105 QVCIVSQEPTLFDCTIGENIC-YGTnrnVTYQEIVEAAKMANIHNFILGLPDGYDTHVGEKGTQLSGGQKQRIAIARALV 1183
Cdd:cd03244 79 RISIIPQDPVLFSGTIRSNLDpFGE---YSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 124244275 1184 RSPSVLLLDEATSALDTESEKIVQEALDAAKQGRTCLVIAHRLSTIQNSDVIAIVSEGKIVEKGT 1248
Cdd:cd03244 156 RKSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
782-1260 |
1.73e-57 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 209.96 E-value: 1.73e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 782 KLRFEAFKNLLRQDIAFYDdlRHGTGKLCTRFATDAPNVR--YVfTRLPVVLASIVTIcGALGIG-FYYGWQLALILVVM 858
Cdd:PRK10790 99 QLRTDVMDAALRQPLSAFD--TQPVGQLISRVTNDTEVIRdlYV-TVVATVLRSAALI-GAMLVAmFSLDWRMALVAIMI 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 859 VP--LLVMGGY----------------------------------FEMQMRFGKQIRDtqlleeagkvASQAvehirtvH 902
Cdd:PRK10790 175 FPavLVVMVIYqrystpivrrvrayladindgfnevingmsviqqFRQQARFGERMGE----------ASRS-------H 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 903 SLNRQEQFHFTycEYLREPFNTNLKHAHTYGAV--FAFSQSLIF---FMYAAAFYLGSI------FVNQQAMqpidvyrv 971
Cdd:PRK10790 238 YMARMQTLRLD--GFLLRPLLSLFSALILCGLLmlFGFSASGTIevgVLYAFISYLGRLneplieLTTQQSM-------- 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 972 ffaisfcgqmignttsfipdVVKARLAASLLFYLIEHPTPiDSLSDSgivKPIT-GNISIRNVFFNYptRKDTKVLQGFT 1050
Cdd:PRK10790 308 --------------------LQQAVVAGERVFELMDGPRQ-QYGNDD---RPLQsGRIDIDNVSFAY--RDDNLVLQNIN 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1051 LDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGMIMIDGDNIRNLNISSLREQVCIVSQEPTLFDCTIGENICYGtnR 1130
Cdd:PRK10790 362 LSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLG--R 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1131 NVTYQEIVEAAKMANIHNFILGLPDGYDTHVGEKGTQLSGGQKQRIAIARALVRSPSVLLLDEATSALDTESEKIVQEAL 1210
Cdd:PRK10790 440 DISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQAL 519
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 124244275 1211 DAAKQGRTCLVIAHRLSTIQNSDVIAIVSEGKIVEKGTHDELI----RKSEIYQ 1260
Cdd:PRK10790 520 AAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLaaqgRYWQMYQ 573
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
361-625 |
3.09e-56 |
|
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: 205.27 E-value: 3.09e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 361 SFGTARGAASTVLRVINSHPKIDPYslegILVDNMKGDISFKDVHFRYP-SRKDIhvLKGISLELKAGDKIALVGSSGCG 439
Cdd:TIGR01842 283 QFSGARQAYKRLNELLANYPSRDPA----MPLPEPEGHLSVENVTIVPPgGKKPT--LRGISFSLQAGEALAIIGPSGSG 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 440 KSTIVNLLQRFYDPTKGRVLIDGVDLREVNVHSLREQIGIVSQEPVLFDGTIYENIKMGNEHATHDQVVEACKMANANDF 519
Cdd:TIGR01842 357 KSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKHIGYLPQDVELFPGTVAENIARFGENADPEKIIEAAKLAGVHEL 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 520 IKRLPDGYGTRVGEKGVQLSGGQKQRIAIARALVKNPKILLLDEATSALDTEAEREVQGALDQAQA-GRTTIIVAHRLST 598
Cdd:TIGR01842 437 ILRLPDGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALKArGITVVVITHRPSL 516
|
250 260
....*....|....*....|....*..
gi 124244275 599 IRNVDRIFVFKAGNIVESGSHEELMSK 625
Cdd:TIGR01842 517 LGCVDKILVLQDGRIARFGERDEVLAK 543
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
779-1260 |
3.41e-56 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 205.72 E-value: 3.41e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 779 LTMKLRFEAFKNLLRQDIAFYddLRHGTGKLCTRFATDAPnvRYVFTRLPVVLA---SIVTICGALGI-GFYYGWQLALI 854
Cdd:PRK10789 67 LAVELREDFYRQLSRQHPEFY--LRHRTGDLMARATNDVD--RVVFAAGEGVLTlvdSLVMGCAVLIVmSTQISWQLTLL 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 855 LVVMVPLLVMggyfeMQMRFGKQirdtqlLEEAGKVASQAVEhirtvhSLNRQEQfhftycEYLrepfnTNLKHAHTYGa 934
Cdd:PRK10789 143 ALLPMPVMAI-----MIKRYGDQ------LHERFKLAQAAFS------SLNDRTQ------ESL-----TSIRMIKAFG- 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 935 vFAFSQSLIFFMYAAafylgsifvnQQAMQPIDVYRV--------FFAISFC--------------GQM-IGNTTSFI-- 989
Cdd:PRK10789 194 -LEDRQSALFAADAE----------DTGKKNMRVARIdarfdptiYIAIGMAnllaigggswmvvnGSLtLGQLTSFVmy 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 990 -PDVVKARLAASLLFYLIEHPTPIDS-----LSDSGIVK---------PITGNISIRNvfFNYPTrKDTKVLQGFTLDIK 1054
Cdd:PRK10789 263 lGLMIWPMLALAWMFNIVERGSAAYSriramLAEAPVVKdgsepvpegRGELDVNIRQ--FTYPQ-TDHPALENVNFTLK 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1055 AGKTVALVGHSGCGKSTIMGLLERFYNQDKGMIMIDGDNIRNLNISSLREQVCIVSQEPTLFDCTIGENICYGtNRNVTY 1134
Cdd:PRK10789 340 PGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNIALG-RPDATQ 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1135 QEIVEAAKMANIHNFILGLPDGYDTHVGEKGTQLSGGQKQRIAIARALVRSPSVLLLDEATSALDTESEKIVQEALDAAK 1214
Cdd:PRK10789 419 QEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWG 498
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 124244275 1215 QGRTCLVIAHRLSTIQNSDVIAIVSEGKIVEKGTHDELIRKSEIYQ 1260
Cdd:PRK10789 499 EGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSGWYR 544
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
399-1257 |
2.65e-55 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 211.91 E-value: 2.65e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 399 ISFKDVHFRYPSRKDIHVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIdgvdlrevnvhsLREQIG 478
Cdd:PLN03130 615 ISIKNGYFSWDSKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDASVV------------IRGTVA 682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 479 IVSQEPVLFDGTIYENIKMGN--EHATHDQVVEACKMANANDFikrLPDGYGTRVGEKGVQLSGGQKQRIAIARALVKNP 556
Cdd:PLN03130 683 YVPQVSWIFNATVRDNILFGSpfDPERYERAIDVTALQHDLDL---LPGGDLTEIGERGVNISGGQKQRVSMARAVYSNS 759
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 557 KILLLDEATSALDTEAEREV-QGALDQAQAGRTTIIVAHRLSTIRNVDRIFVFKAGNIVESGSHEELMSKQGIFYDMtqa 635
Cdd:PLN03130 760 DVYIFDDPLSALDAHVGRQVfDKCIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSNNGPLFQKL--- 836
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 636 qvvrqqQQEAGKdIEDTISESAHSHLSRKSSTRSAISIATSIHQLAEEVEECKAPPTSMFKIFKFNGDKVGWFI------ 709
Cdd:PLN03130 837 ------MENAGK-MEEYVEENGEEEDDQTSSKPVANGNANNLKKDSSSKKKSKEGKSVLIKQEERETGVVSWKVlerykn 909
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 710 --GGIFGA---FIFGSVTPVFALVYAEIFNVYSlpaDQMQANVY---FWcgMFVLMGITFFVGFFTSANCLGRCGESL-- 779
Cdd:PLN03130 910 alGGAWVVmilFLCYVLTEVFRVSSSTWLSEWT---DQGTPKTHgplFY--NLIYALLSFGQVLVTLLNSYWLIMSSLya 984
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 780 TMKLRFEAFKNLLRQDIAFYDdlRHGTGKLCTRFATDAPNV-RYVFTRLPVVLASIVTICGALG-IGFYYGWQLALILvv 857
Cdd:PLN03130 985 AKRLHDAMLGSILRAPMSFFH--TNPLGRIINRFAKDLGDIdRNVAVFVNMFLGQIFQLLSTFVlIGIVSTISLWAIM-- 1060
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 858 mvPLLVmgGYFEMQMRFGKQIRDTQLLEEAGK--VASQ------AVEHIRTVHSLNRQEQFH---------FTYceylre 920
Cdd:PLN03130 1061 --PLLV--LFYGAYLYYQSTAREVKRLDSITRspVYAQfgealnGLSTIRAYKAYDRMAEINgrsmdnnirFTL------ 1130
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 921 pfnTNLKHAHTYGAVFAFSQSLIFFMyAAAFylgSIFVNQQAMQPIdvyrvffaiSFCGQMiG-------NTTSFIPDVV 993
Cdd:PLN03130 1131 ---VNMSSNRWLAIRLETLGGLMIWL-TASF---AVMQNGRAENQA---------AFASTM-GlllsyalNITSLLTAVL 1193
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 994 K-ARLAASLLFYLIEHPTPIDSLSDSGIVK---------PITGNISIRNVFFNYptRKD-TKVLQGFTLDIKAGKTVALV 1062
Cdd:PLN03130 1194 RlASLAENSLNAVERVGTYIDLPSEAPLVIennrpppgwPSSGSIKFEDVVLRY--RPElPPVLHGLSFEISPSEKVGIV 1271
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1063 GHSGCGKSTIMGLLERFYNQDKGMIMIDGDNIRNLNISSLREQVCIVSQEPTLFDCTIGENICYGTNRNVTyqEIVEAAK 1142
Cdd:PLN03130 1272 GRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNLDPFNEHNDA--DLWESLE 1349
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1143 MANIHNFILGLPDGYDTHVGEKGTQLSGGQKQRIAIARALVRSPSVLLLDEATSALDTESEKIVQEALDAAKQGRTCLVI 1222
Cdd:PLN03130 1350 RAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLII 1429
|
890 900 910
....*....|....*....|....*....|....*
gi 124244275 1223 AHRLSTIQNSDVIAIVSEGKIVEKGTHDELIRKSE 1257
Cdd:PLN03130 1430 AHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEG 1464
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
399-626 |
3.12e-55 |
|
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: 191.78 E-value: 3.12e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 399 ISFKDVHFRYPSRKdiHVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDLREVNVHSLREQIG 478
Cdd:COG1122 1 IELENLSFSYPGGT--PALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 479 IVSQEPV--LFDGTIYENIKMG------NEHATHDQVVEACKMANANDFIKRLPDgygtrvgekgvQLSGGQKQRIAIAR 550
Cdd:COG1122 79 LVFQNPDdqLFAPTVEEDVAFGpenlglPREEIRERVEEALELVGLEHLADRPPH-----------ELSGGQKQRVAIAG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 124244275 551 ALVKNPKILLLDEATSALDTEAEREVQGALDQ-AQAGRTTIIVAHRLSTI-RNVDRIFVFKAGNIVESGSHEELMSKQ 626
Cdd:COG1122 148 VLAMEPEVLVLDEPTAGLDPRGRRELLELLKRlNKEGKTVIIVTHDLDLVaELADRVIVLDDGRIVADGTPREVFSDY 225
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
715-1268 |
3.35e-55 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 211.43 E-value: 3.35e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 715 AFIFGSVTPVFALVYAEIFNVYSLpADQMQANVYfwcgMFVLMGITFFVGFFTSANCLGRCGESLTMKLRFEAFKNLLRQ 794
Cdd:PTZ00265 69 ATISGGTLPFFVSVFGVIMKNMNL-GENVNDIIF----SLVLIGIFQFILSFISSFCMDVVTTKILKTLKLEFLKSVFYQ 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 795 DIAFYDD-------------LRHGTGKLCTRFATdapnvryVFTRLPVVLasivticgalgiGFYYgW------QLALIL 855
Cdd:PTZ00265 144 DGQFHDNnpgskltsdldfyLEQVNAGIGTKFIT-------IFTYASAFL------------GLYI-WslfknaRLTLCI 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 856 VVMVPLLVMGGYF-EMQMRFGKQirdTQLL--EEAGKVASQAVEHIRTVHSLNRQ----EQFHFTYCEYLREPFNTNLKH 928
Cdd:PTZ00265 204 TCVFPLIYICGVIcNKKVKINKK---TSLLynNNTMSIIEEALVGIRTVVSYCGEktilKKFNLSEKLYSKYILKANFME 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 929 AHTYGAVFAFsqslIFFMYAAAFYLGSIFV-----NQQAMQPID---VYRVFFAISFCGQMIGNTTSFIPDVVKARLAAS 1000
Cdd:PTZ00265 281 SLHIGMINGF----ILASYAFGFWYGTRIIisdlsNQQPNNDFHggsVISILLGVLISMFMLTIILPNITEYMKSLEATN 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1001 LLFYLIEHPTPIDSLSDSGIVKPITgNISIRNVFFNYPTRKDTKVLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFY 1080
Cdd:PTZ00265 357 SLYEIINRKPLVENNDDGKKLKDIK-KIQFKNVRFHYDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLY 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1081 NQDKGMIMI-DGDNIRNLNISSLREQVCIVSQEPTLFDCTIGENICYG---------------TNRNVTYQ--------- 1135
Cdd:PTZ00265 436 DPTEGDIIInDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKYSlyslkdlealsnyynEDGNDSQEnknkrnscr 515
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1136 --------------------------------EIVEAAKMANIHNFILGLPDGYDTHVGEKGTQLSGGQKQRIAIARALV 1183
Cdd:PTZ00265 516 akcagdlndmsnttdsneliemrknyqtikdsEVVDVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAII 595
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1184 RSPSVLLLDEATSALDTESEKIVQEALDAAK--QGRTCLVIAHRLSTIQNSDVIAIVS---------------------- 1239
Cdd:PTZ00265 596 RNPKILILDEATSSLDNKSEYLVQKTINNLKgnENRITIIIAHRLSTIRYANTIFVLSnrergstvdvdiigedptkdnk 675
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*
gi 124244275 1240 ------------------------EGK-IVEKGTHDELIR-KSEIYQKFCETQRI 1268
Cdd:PTZ00265 676 ennnknnkddnnnnnnnnnnkinnAGSyIIEQGTHDALMKnKNGIYYTMINNQKV 730
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
933-1268 |
3.64e-55 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 202.75 E-value: 3.64e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 933 GAVFAfsqsLIFFMYAAAFylgsifvnqQAMQPIdvyrvffAISFcgQMIGNTTSfipdvvkarlAASLLFYLIEHPTPI 1012
Cdd:PRK11160 277 GALIA----LFVFAALAAF---------EALMPV-------AGAF--QHLGQVIA----------SARRINEITEQKPEV 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1013 DSLSDSGIvKPITGNISIRNVFFNYPTRKDtKVLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGMIMIDGD 1092
Cdd:PRK11160 325 TFPTTSTA-AADQVSLTLNNVSFTYPDQPQ-PVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQ 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1093 NIRNLNISSLREQVCIVSQEPTLFDCTIGENICYGtNRNVTYQEIVEAAKMANIHNFILGlPDGYDTHVGEKGTQLSGGQ 1172
Cdd:PRK11160 403 PIADYSEAALRQAISVVSQRVHLFSATLRDNLLLA-APNASDEALIEVLQQVGLEKLLED-DKGLNAWLGEGGRQLSGGE 480
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1173 KQRIAIARALVRSPSVLLLDEATSALDTESEKIVQEALDAAKQGRTCLVIAHRLSTIQNSDVIAIVSEGKIVEKGTHDEL 1252
Cdd:PRK11160 481 QRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQEL 560
|
330
....*....|....*.
gi 124244275 1253 IRKSEIYQKFCetQRI 1268
Cdd:PRK11160 561 LAQQGRYYQLK--QRL 574
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
766-1263 |
3.57e-54 |
|
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: 202.66 E-value: 3.57e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 766 FTSANCLGRCGESLTMKLRFEAFKNLLRQDIAFYDDLRhgTGKLCTRFaTDAPNVryvftrLPVVLASIVTICGALGI-- 843
Cdd:TIGR01193 214 YIQIFLLNVLGQRLSIDIILSYIKHLFELPMSFFSTRR--TGEIVSRF-TDASSI------IDALASTILSLFLDMWIlv 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 844 --GFYYGWQ---LALILVVMVPLLVMGGYFEMQMrFGKQIRDTQlleEAGKVASQA----VEHIRTVHSLNrQEQFHFTY 914
Cdd:TIGR01193 285 ivGLFLVRQnmlLFLLSLLSIPVYAVIIILFKRT-FNKLNHDAM---QANAVLNSSiiedLNGIETIKSLT-SEAERYSK 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 915 CEYLREPF-NTNLKHAHTYGAVFAFSQSLIFFMYAAAFYLGSIFVNQQAMQPIDVYRVFFAISFCGQMIGNTTSFIPDVV 993
Cdd:TIGR01193 360 IDSEFGDYlNKSFKYQKADQGQQAIKAVTKLILNVVILWTGAYLVMRGKLTLGQLITFNALLSYFLTPLENIINLQPKLQ 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 994 KARLAASLL--FYLIEhptpiDSLSDSGIVKPIT---GNISIRNVFFNYPTrkDTKVLQGFTLDIKAGKTVALVGHSGCG 1068
Cdd:TIGR01193 440 AARVANNRLneVYLVD-----SEFINKKKRTELNnlnGDIVINDVSYSYGY--GSNILSDISLTIKMNSKTTIVGMSGSG 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1069 KSTIMGLLERFYNQDKGMIMIDGDNIRNLNISSLREQVCIVSQEPTLFDCTIGENICYGTNRNVTYQEIVEAAKMANIHN 1148
Cdd:TIGR01193 513 KSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLGAKENVSQDEIWAACEIAEIKD 592
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1149 FILGLPDGYDTHVGEKGTQLSGGQKQRIAIARALVRSPSVLLLDEATSALDTESE-KIVQEALDAakQGRTCLVIAHRLS 1227
Cdd:TIGR01193 593 DIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEkKIVNNLLNL--QDKTIIFVAHRLS 670
|
490 500 510
....*....|....*....|....*....|....*.
gi 124244275 1228 TIQNSDVIAIVSEGKIVEKGTHDELIRKSEIYQKFC 1263
Cdd:TIGR01193 671 VAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYASLI 706
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
397-618 |
1.11e-53 |
|
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: 186.46 E-value: 1.11e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 397 GDISFKDVHFRYPSRKDiHVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDLREVNVHSLREQ 476
Cdd:cd03369 5 GEIEVENLSVRYAPDLP-PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 477 IGIVSQEPVLFDGTIYENIKMGNEHaTHDQVVEAckmanandfikrlpdgygTRVGEKGVQLSGGQKQRIAIARALVKNP 556
Cdd:cd03369 84 LTIIPQDPTLFSGTIRSNLDPFDEY-SDEEIYGA------------------LRVSEGGLNLSQGQRQLLCLARALLKRP 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124244275 557 KILLLDEATSALDTEAEREVQGALDQAQAGRTTIIVAHRLSTIRNVDRIFVFKAGNIVESGS 618
Cdd:cd03369 145 RVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
954-1255 |
1.64e-52 |
|
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: 194.10 E-value: 1.64e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 954 GSIFVNQqAMQPIDvyrvffaisfcgQMIGNTTSFIpdvvKARLA-ASLLFYLIEHPTPIDSLSdsgIVKPiTGNISIRN 1032
Cdd:TIGR01842 263 GSILVGR-ALAPID------------GAIGGWKQFS----GARQAyKRLNELLANYPSRDPAMP---LPEP-EGHLSVEN 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1033 VFFNYPTRKdTKVLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGMIMIDGDNIRNLNISSLREQVCIVSQE 1112
Cdd:TIGR01842 322 VTIVPPGGK-KPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKHIGYLPQD 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1113 PTLFDCTIGENICYGTnRNVTYQEIVEAAKMANIHNFILGLPDGYDTHVGEKGTQLSGGQKQRIAIARALVRSPSVLLLD 1192
Cdd:TIGR01842 401 VELFPGTVAENIARFG-ENADPEKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLD 479
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124244275 1193 EATSALDTESEKIVQEALDAAK-QGRTCLVIAHRLSTIQNSDVIAIVSEGKIVEKGTHDELIRK 1255
Cdd:TIGR01842 480 EPNSNLDEEGEQALANAIKALKaRGITVVVITHRPSLLGCVDKILVLQDGRIARFGERDEVLAK 543
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
399-613 |
2.89e-52 |
|
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: 181.26 E-value: 2.89e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 399 ISFKDVHFRYPSRKDIhVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDLREVNVHSLREQIG 478
Cdd:cd03246 1 LEVENVSFRYPGAEPP-VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 479 IVSQEPVLFDGTIYENIkmgnehathdqvveackmanandfikrlpdgygtrvgekgvqLSGGQKQRIAIARALVKNPKI 558
Cdd:cd03246 80 YLPQDDELFSGSIAENI------------------------------------------LSGGQRQRLGLARALYGNPRI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 124244275 559 LLLDEATSALDTEAEREVQGALDQAQ-AGRTTIIVAHRLSTIRNVDRIFVFKAGNI 613
Cdd:cd03246 118 LVLDEPNSHLDVEGERALNQAIAALKaAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
400-611 |
5.49e-52 |
|
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: 181.90 E-value: 5.49e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 400 SFKDVHFRYPSRkDIHVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDLREVNVHSLREQIGI 479
Cdd:cd03225 1 ELKNLSFSYPDG-ARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 480 VSQEP--VLFDGTIYENIKMGNEHATHDQ------VVEACKMANANDFIKRLPDgygtrvgekgvQLSGGQKQRIAIARA 551
Cdd:cd03225 80 VFQNPddQFFGPTVEEEVAFGLENLGLPEeeieerVEEALELVGLEGLRDRSPF-----------TLSGGQKQRVAIAGV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124244275 552 LVKNPKILLLDEATSALDTEAEREVQGALDQ-AQAGRTTIIVAHRLSTIRNV-DRIFVFKAG 611
Cdd:cd03225 149 LAMDPDILLLDEPTAGLDPAGRRELLELLKKlKAEGKTIIIVTHDLDLLLELaDRVIVLEDG 210
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
399-613 |
6.96e-52 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 181.55 E-value: 6.96e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 399 ISFKDVHFRYPSRKdihVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDLREVNVHSLREQIG 478
Cdd:COG4619 1 LELEGLSFRVGGKP---ILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 479 IVSQEPVLFDGTIYENIKMGNEHAThdqvvEACKMANANDFIKRLpdGYGTRVGEKGV-QLSGGQKQRIAIARALVKNPK 557
Cdd:COG4619 78 YVPQEPALWGGTVRDNLPFPFQLRE-----RKFDRERALELLERL--GLPPDILDKPVeRLSGGERQRLALIRALLLQPD 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 124244275 558 ILLLDEATSALDTEAEREVQGALDQ--AQAGRTTIIVAHRLSTIRNV-DRIFVFKAGNI 613
Cdd:COG4619 151 VLLLDEPTSALDPENTRRVEELLREylAEEGRAVLWVSHDPEQIERVaDRVLTLEAGRL 209
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
399-617 |
2.11e-51 |
|
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: 179.05 E-value: 2.11e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 399 ISFKDVHFRYPSrKDIHVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDLREVNvHSLREQIG 478
Cdd:cd03247 1 LSINNVSFSYPE-QEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 479 IVSQEPVLFDGTIYENIkmgnehathdqvveackmanandfikrlpdgygtrvgekGVQLSGGQKQRIAIARALVKNPKI 558
Cdd:cd03247 79 VLNQRPYLFDTTLRNNL---------------------------------------GRRFSGGERQRLALARILLQDAPI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 124244275 559 LLLDEATSALDTEAEREVQGALDQAQAGRTTIIVAHRLSTIRNVDRIFVFKAGNIVESG 617
Cdd:cd03247 120 VLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1042-1252 |
2.16e-51 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 191.98 E-value: 2.16e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1042 DTKVLQG---FTldIKAGKTVALVGHSGCGKSTIMGLLERF--YnqdKGMIMIDGDNIRNLNISSLREQVCIVSQEPTLF 1116
Cdd:PRK11174 361 DGKTLAGplnFT--LPAGQRIALVGPSGAGKTSLLNALLGFlpY---QGSLKINGIELRELDPESWRKHLSWVGQNPQLP 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1117 DCTIGENICYGtNRNVTYQEIVEAAKMANIHNFILGLPDGYDTHVGEKGTQLSGGQKQRIAIARALVRSPSVLLLDEATS 1196
Cdd:PRK11174 436 HGTLRDNVLLG-NPDASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTA 514
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 124244275 1197 ALDTESEKIVQEALDAAKQGRTCLVIAHRLSTIQNSDVIAIVSEGKIVEKGTHDEL 1252
Cdd:PRK11174 515 SLDAHSEQLVMQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAEL 570
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
399-624 |
3.21e-51 |
|
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: 189.73 E-value: 3.21e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 399 ISFKDVHFRYPSRK--DIHVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDLREVNVHSLRE- 475
Cdd:COG1123 261 LEVRNLSKRYPVRGkgGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLREl 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 476 --QIGIVSQEPV--LF-DGTIYENI-------KMGNEHATHDQVVEACKMAN-ANDFIKRLPDgygtrvgekgvQLSGGQ 542
Cdd:COG1123 341 rrRVQMVFQDPYssLNpRMTVGDIIaeplrlhGLLSRAERRERVAELLERVGlPPDLADRYPH-----------ELSGGQ 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 543 KQRIAIARALVKNPKILLLDEATSALDTEAEREVQGALD--QAQAGRTTIIVAHRLSTIRNV-DRIFVFKAGNIVESGSH 619
Cdd:COG1123 410 RQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRdlQRELGLTYLFISHDLAVVRYIaDRVAVMYDGRIVEDGPT 489
|
....*
gi 124244275 620 EELMS 624
Cdd:COG1123 490 EEVFA 494
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
399-622 |
3.32e-51 |
|
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: 180.07 E-value: 3.32e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 399 ISFKDVHFRYpsrKDIHVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYD-----PTKGRVLIDGVDLRE--VNVH 471
Cdd:cd03260 1 IELRDLNVYY---GDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDldVDVL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 472 SLREQIGIVSQEPVLFDGTIYENIKMG-------NEHATHDQVVEACKMANANDFIKRLPDGYGtrvgekgvqLSGGQKQ 544
Cdd:cd03260 78 ELRRRVGMVFQKPNPFPGSIYDNVAYGlrlhgikLKEELDERVEEALRKAALWDEVKDRLHALG---------LSGGQQQ 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124244275 545 RIAIARALVKNPKILLLDEATSALDTEAEREVQGALDQAQAGRTTIIVAHRLSTIRNV-DRIFVFKAGNIVESGSHEEL 622
Cdd:cd03260 149 RLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARVaDRTAFLLNGRLVEFGPTEQI 227
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
399-622 |
6.40e-51 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 179.80 E-value: 6.40e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 399 ISFKDVHFRYpsrKDIHVLKGISLELKAGDKIALVGSSGCGKSTI---VNLLQRfydPTKGRVLIDGVDL--REVNVHSL 473
Cdd:COG1126 2 IEIENLHKSF---GDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLlrcINLLEE---PDSGTITVDGEDLtdSKKDINKL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 474 REQIGIVSQEPVLF-DGTIYENI--------KMGNEhathdqvvEACKMANAndfikrlpdgYGTRVG--EKG----VQL 538
Cdd:COG1126 76 RRKVGMVFQQFNLFpHLTVLENVtlapikvkKMSKA--------EAEERAME----------LLERVGlaDKAdaypAQL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 539 SGGQKQRIAIARALVKNPKILLLDEATSALDTEAEREVQGALDQ-AQAGRTTIIVAHRLSTIRNV-DRIFVFKAGNIVES 616
Cdd:COG1126 138 SGGQQQRVAIARALAMEPKVMLFDEPTSALDPELVGEVLDVMRDlAKEGMTMVVVTHEMGFAREVaDRVVFMDGGRIVEE 217
|
....*.
gi 124244275 617 GSHEEL 622
Cdd:COG1126 218 GPPEEF 223
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
395-615 |
4.06e-50 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 177.16 E-value: 4.06e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 395 MKGDISFKDVHFRYPSRK-DIHVLKGISLELKAGDKIALVGSSGCGKSTIVNL---LQRfydPTKGRVLIDGVDLREVNV 470
Cdd:COG1136 1 MSPLLELRNLTKSYGTGEgEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNIlggLDR---PTSGEVLIDGQDISSLSE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 471 HSL----REQIGIVSQEPVLFDG-TIYENIKMG------NEHATHDQVVEACKMANANDFIKRLPDgygtrvgekgvQLS 539
Cdd:COG1136 78 RELarlrRRHIGFVFQFFNLLPElTALENVALPlllagvSRKERRERARELLERVGLGDRLDHRPS-----------QLS 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 124244275 540 GGQKQRIAIARALVKNPKILLLDEATSALDTEAEREVQGALDQ--AQAGRTTIIVAHRLSTIRNVDRIFVFKAGNIVE 615
Cdd:COG1136 147 GGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRElnRELGTTIVMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
782-1226 |
1.96e-49 |
|
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: 184.87 E-value: 1.96e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 782 KLRFEAFKNLLRQDIAFYDdlRHGTGKLCTRFATDAPNVRYVFTR--LPVVLASIVTICGALGIGFYYgWQLALILVVM- 858
Cdd:TIGR02868 87 ALRVRVYERLARQALAGRR--RLRRGDLLGRLGADVDALQDLYVRviVPAGVALVVGAAAVAAIAVLS-VPAALILAAGl 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 859 -VPLLVMGGYFEMQMRFGKQIRdTQLLEEAGKVASQAVEHIRTVHSLNRQEQFHFTYCEYLREpFNTNLKHAHTYGAVFA 937
Cdd:TIGR02868 164 lLAGFVAPLVSLRAARAAEQAL-ARLRGELAAQLTDALDGAAELVASGALPAALAQVEEADRE-LTRAERRAAAATALGA 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 938 FSQSLIffmyAAAFYLGSIFVNQQAMQPIDVYRVFFAI-SFCGQMIGNTTSFIPDVV----KARLAASLLFYLIEHPTPI 1012
Cdd:TIGR02868 242 ALTLLA----AGLAVLGALWAGGPAVADGRLAPVTLAVlVLLPLAAFEAFAALPAAAqqltRVRAAAERIVEVLDAAGPV 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1013 DSLSD--SGIVKPITGNISIRNVFFNYPTrkDTKVLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGMIMID 1090
Cdd:TIGR02868 318 AEGSApaAGAVGLGKPTLELRDLSAGYPG--APPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLD 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1091 GDNIRNLNISSLREQVCIVSQEPTLFDCTIGENICYGtNRNVTYQEIVEAAKMANIHNFILGLPDGYDTHVGEKGTQLSG 1170
Cdd:TIGR02868 396 GVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLA-RPDATDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSG 474
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 124244275 1171 GQKQRIAIARALVRSPSVLLLDEATSALDTESEKIVQEALDAAKQGRTCLVIAHRL 1226
Cdd:TIGR02868 475 GERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
399-617 |
3.94e-48 |
|
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: 171.53 E-value: 3.94e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 399 ISFKDVHFRYPSRKD-IHVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDLREVNVHSLRE-- 475
Cdd:cd03257 2 LEVKNLSVSFPTGGGsVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIrr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 476 -QIGIVSQE------PVLfdgTIYENIKMGNEHATHDQVVEA---------CKMANANDFIKRLPDgygtrvgekgvQLS 539
Cdd:cd03257 82 kEIQMVFQDpmsslnPRM---TIGEQIAEPLRIHGKLSKKEArkeavllllVGVGLPEEVLNRYPH-----------ELS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 540 GGQKQRIAIARALVKNPKILLLDEATSALDTEAEREVQGALDQAQA--GRTTIIVAHRLSTIRNV-DRIFVFKAGNIVES 616
Cdd:cd03257 148 GGQRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEelGLTLLFITHDLGVVAKIaDRVAVMYAGKIVEE 227
|
.
gi 124244275 617 G 617
Cdd:cd03257 228 G 228
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
395-622 |
1.38e-47 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 174.13 E-value: 1.38e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 395 MKGDISFKDVHFRYpsrKDIHVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDLREVNVHslR 474
Cdd:COG3842 2 AMPALELENVSKRY---GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPE--K 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 475 EQIGIVSQEPVLFDG-TIYENIKMG------NEHATHDQVVEACKMANANDFIKRLPDgygtrvgekgvQLSGGQKQRIA 547
Cdd:COG3842 77 RNVGMVFQDYALFPHlTVAENVAFGlrmrgvPKAEIRARVAELLELVGLEGLADRYPH-----------QLSGGQQQRVA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 548 IARALVKNPKILLLDEATSALDTEAEREVQGALD--QAQAGRTTIIVAH------RLStirnvDRIFVFKAGNIVESGSH 619
Cdd:COG3842 146 LARALAPEPRVLLLDEPLSALDAKLREEMREELRrlQRELGITFIYVTHdqeealALA-----DRIAVMNDGRIEQVGTP 220
|
...
gi 124244275 620 EEL 622
Cdd:COG3842 221 EEI 223
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
399-617 |
1.77e-47 |
|
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: 168.85 E-value: 1.77e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 399 ISFKDVHFRYpsrKDIHVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDLREVNVHslREQIG 478
Cdd:cd03259 1 LELKGLSKTY---GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE--RRNIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 479 IVSQEPVLFDG-TIYENI-------KMGNEHAThDQVVEACKMANANDFIKRLPDgygtrvgekgvQLSGGQKQRIAIAR 550
Cdd:cd03259 76 MVFQDYALFPHlTVAENIafglklrGVPKAEIR-ARVRELLELVGLEGLLNRYPH-----------ELSGGQQQRVALAR 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 124244275 551 ALVKNPKILLLDEATSALDTEAEREVQGALD--QAQAGRTTIIVAH------RLStirnvDRIFVFKAGNIVESG 617
Cdd:cd03259 144 ALAREPSLLLLDEPLSALDAKLREELREELKelQRELGITTIYVTHdqeealALA-----DRIAVMNEGRIVQVG 213
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
708-1000 |
1.93e-47 |
|
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: 172.46 E-value: 1.93e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 708 FIGGIFGAFIFGSVTPVFALVYAEIFNVYSL------------------PADQMQANVYFWCGMFVLMGITFFVGFFTSA 769
Cdd:cd18558 1 MVVGILCAIIHGGLLPAFMVIFGDMTDSFTNggmtnitgnssglnssagPFEKLEEEMTLYAYYYLIIGAIVLITAYIQG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 770 NCLGRCGESLTMKLRFEAFKNLLRQDIAFYDdlRHGTGKLCTRFATDAPNVRY-VFTRLPVVLASIVTICGALGIGFYYG 848
Cdd:cd18558 81 SFWGLAAGRQTKKIRYKFFHAIMRQEIGWFD--VNDTGELNTRLADDVSKINEgIGDKIGVIFQNIATFGTGFIIGFIRG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 849 WQLALILVVMVPLLVMGGYFEMQMRFGKQIRDTQLLEEAGKVASQAVEHIRTVHSLNRQEQFHFTYCEYLREPFNTNLKH 928
Cdd:cd18558 159 WKLTLVILAISPVLGLSAVVWAKILSGFTDKEKKAYAKAGAVAEEVLEAFRTVIAFGGQQKEETRYAQNLEIAKRNGIKK 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124244275 929 AHTYGAVFAFSQSLIFFMYAAAFYLGSIFVNQQAMQPIDVYRVFFAISFCGQMIGNTTSFIPDVVKARLAAS 1000
Cdd:cd18558 239 AITFNISMGAAFLLIYASYALAFWYGTYLVTQQEYSIGEVLTVFFSVLIGAFSAGQQVPSIEAFANARGAAY 310
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
397-627 |
3.70e-47 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 185.71 E-value: 3.70e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 397 GDISFKDVHFRYpsRKDIH-VLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDLREVNVHSLRE 475
Cdd:PLN03130 1236 GSIKFEDVVLRY--RPELPpVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRK 1313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 476 QIGIVSQEPVLFDGTIYENIKMGNEHATHDqVVEACKMANANDFIKRLPDGYGTRVGEKGVQLSGGQKQRIAIARALVKN 555
Cdd:PLN03130 1314 VLGIIPQAPVLFSGTVRFNLDPFNEHNDAD-LWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRR 1392
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124244275 556 PKILLLDEATSALDTEAEREVQGALDQAQAGRTTIIVAHRLSTIRNVDRIFVFKAGNIVESGSHEELMSKQG 627
Cdd:PLN03130 1393 SKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEG 1464
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
708-975 |
1.01e-46 |
|
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: 168.98 E-value: 1.01e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 708 FIGGIFGAFIFGSVTPVFALVYAEIFNVYSLPADQMQANVYFWCGMFVLMGITFFVGFFTSANCLGRCGESLTMKLRFEA 787
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLPDGDPETQALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 788 FKNLLRQDIAFYDdlRHGTGKLCTRFATDAPNVR-YVFTRLPVVLASIVTICGALGIGFYYGWQLALILVVMVPLLVMGG 866
Cdd:pfam00664 81 FKKILRQPMSFFD--TNSVGELLSRLTNDTSKIRdGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 867 YFEMQMRFGKQIRDTQLLEEAGKVASQAVEHIRTVHSLNRQEQFHFTYCEYLREPFNTNLKHAHTYGAVFAFSQSLIFFM 946
Cdd:pfam00664 159 AVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLS 238
|
250 260 270
....*....|....*....|....*....|.
gi 124244275 947 YAAAFYLGSIFVNQQAMQP--IDVYRVFFAI 975
Cdd:pfam00664 239 YALALWFGAYLVISGELSVgdLVAFLSLFAQ 269
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
399-613 |
1.17e-46 |
|
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: 166.90 E-value: 1.17e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 399 ISFKDVHFRYPSRKD-IHVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDLREVNVHSL---- 473
Cdd:cd03255 1 IELKNLSKTYGGGGEkVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 474 REQIGIVSQEPVLFDG-TIYENIKMGNEHAthdQVVEACKMANANDFIKRLpdGYGTRVGEKGVQLSGGQKQRIAIARAL 552
Cdd:cd03255 81 RRHIGFVFQSFNLLPDlTALENVELPLLLA---GVPKKERRERAEELLERV--GLGDRLNHYPSELSGGQQQRVAIARAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 124244275 553 VKNPKILLLDEATSALDTEAEREVQGALDQ--AQAGRTTIIVAHRLSTIRNVDRIFVFKAGNI 613
Cdd:cd03255 156 ANDPKIILADEPTGNLDSETGKEVMELLRElnKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
399-625 |
1.45e-46 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 167.16 E-value: 1.45e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 399 ISFKDVHFRYpsrKDIHVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDLREvNVHSLREQIG 478
Cdd:COG1131 1 IEVRGLTKRY---GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR-DPAEVRRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 479 IVSQEPVLFDG-TIYENIKMgneHATHDQVVEACKMANANDFIKR--LPDGYGTRVGekgvQLSGGQKQRIAIARALVKN 555
Cdd:COG1131 77 YVPQEPALYPDlTVRENLRF---FARLYGLPRKEARERIDELLELfgLTDAADRKVG----TLSGGMKQRLGLALALLHD 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124244275 556 PKILLLDEATSALDTEAEREVQGAL-DQAQAGRTTIIVAHRLSTIRNV-DRIFVFKAGNIVESGSHEELMSK 625
Cdd:COG1131 150 PELLILDEPTSGLDPEARRELWELLrELAAEGKTVLLSTHYLEEAERLcDRVAIIDKGRIVADGTPDELKAR 221
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
399-625 |
1.57e-46 |
|
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: 166.99 E-value: 1.57e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 399 ISFKDVHFRYPSR-KDIHVLKGISLELKAGDKIALVGSSGCGKST---IVNLLQRfydPTKGRVLIDGVDLREVNVHSLR 474
Cdd:cd03258 2 IELKNVSKVFGDTgGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTlirCINGLER---PTSGSVLVDGTDLTLLSGKELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 475 E---QIGIVSQEPVLFDG-TIYENIKMGNEHA------THDQVVEACKMANANDFIKRLPDgygtrvgekgvQLSGGQKQ 544
Cdd:cd03258 79 KarrRIGMIFQHFNLLSSrTVFENVALPLEIAgvpkaeIEERVLELLELVGLEDKADAYPA-----------QLSGGQKQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 545 RIAIARALVKNPKILLLDEATSALDTEAEREVQGALDQAQA--GRTTIIVAHRLSTIRNV-DRIFVFKAGNIVESGSHEE 621
Cdd:cd03258 148 RVGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRelGLTIVLITHEMEVVKRIcDRVAVMEKGEVVEEGTVEE 227
|
....
gi 124244275 622 LMSK 625
Cdd:cd03258 228 VFAN 231
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
1028-1224 |
3.67e-46 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 164.99 E-value: 3.67e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1028 ISIRNVFFnypTRKDTKVLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGMIMIDGDNIRNLNISSLREQVC 1107
Cdd:COG4619 1 LELEGLSF---RVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1108 IVSQEPTLFDCTIGENIcygtnrNVTYQEIVEAAKMANIHNFI--LGLPDGY-DTHVGEkgtqLSGGQKQRIAIARALVR 1184
Cdd:COG4619 78 YVPQEPALWGGTVRDNL------PFPFQLRERKFDRERALELLerLGLPPDIlDKPVER----LSGGERQRLALIRALLL 147
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 124244275 1185 SPSVLLLDEATSALDTESEKIVQEALD--AAKQGRTCLVIAH 1224
Cdd:COG4619 148 QPDVLLLDEPTSALDPENTRRVEELLReyLAEEGRAVLWVSH 189
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
417-566 |
1.14e-45 |
|
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: 161.28 E-value: 1.14e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 417 LKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDLREVNVHSLREQIGIVSQEPVLFDG-TIYENI 495
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 124244275 496 KMGNEHATHDQVVEACKMANANDFIkRLPDGYGTRVGEKGVQLSGGQKQRIAIARALVKNPKILLLDEATS 566
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKL-GLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
1028-1252 |
3.42e-45 |
|
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: 163.12 E-value: 3.42e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1028 ISIRNVFFNYptrKDTKVLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQ-----DKGMIMIDGDNIRNL--NIS 1100
Cdd:cd03260 1 IELRDLNVYY---GDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDIYDLdvDVL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1101 SLREQVCIVSQEPTLFDCTIGENICYG-----TNRNVTYQEIVEAA-KMAnihnfilGLPDGYDTHVgeKGTQLSGGQKQ 1174
Cdd:cd03260 78 ELRRRVGMVFQKPNPFPGSIYDNVAYGlrlhgIKLKEELDERVEEAlRKA-------ALWDEVKDRL--HALGLSGGQQQ 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124244275 1175 RIAIARALVRSPSVLLLDEATSALDTESEKIVQEALDAAKQGRTCLVIAHRLSTIQN-SDVIAIVSEGKIVEKGTHDEL 1252
Cdd:cd03260 149 RLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARvADRTAFLLNGRLVEFGPTEQI 227
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
1028-1258 |
5.71e-45 |
|
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: 162.50 E-value: 5.71e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1028 ISIRNVFFNYPtrKDTKVLQGFTLDIKAGKTVALVGHSGCGKST----IMGLLERfynqDKGMIMIDGDNIRNLNISSLR 1103
Cdd:COG1122 1 IELENLSFSYP--GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTllrlLNGLLKP----TSGEVLVDGKDITKKNLRELR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1104 EQVCIVSQEPT--LFDCTIGENICYG-TNRNVTYQEIV----EAAKManihnfiLGLpdgydTHVGEKGT-QLSGGQKQR 1175
Cdd:COG1122 75 RKVGLVFQNPDdqLFAPTVEEDVAFGpENLGLPREEIRerveEALEL-------VGL-----EHLADRPPhELSGGQKQR 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1176 IAIARALVRSPSVLLLDEATSALDTESEKIVQEALDA-AKQGRTCLVIAHRLSTI-QNSDVIAIVSEGKIVEKGTHDELI 1253
Cdd:COG1122 143 VAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRlNKEGKTVIIVTHDLDLVaELADRVIVLDDGRIVADGTPREVF 222
|
....*
gi 124244275 1254 RKSEI 1258
Cdd:COG1122 223 SDYEL 227
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
399-613 |
6.60e-45 |
|
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: 161.54 E-value: 6.60e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 399 ISFKDVHFRYpsrKDIHVLKGISLELKAGDKIALVGSSGCGKSTI---VNLLQRfydPTKGRVLIDGVDL--REVNVHSL 473
Cdd:cd03262 1 IEIKNLHKSF---GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLlrcINLLEE---PDSGTIIIDGLKLtdDKKNINEL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 474 REQIGIVSQEPVLFDG-TIYENIKMGNEHATHDQVVEAckMANANDFIKR--LPDgygtRVGEKGVQLSGGQKQRIAIAR 550
Cdd:cd03262 75 RQKVGMVFQQFNLFPHlTVLENITLAPIKVKGMSKAEA--EERALELLEKvgLAD----KADAYPAQLSGGQQQRVAIAR 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 124244275 551 ALVKNPKILLLDEATSALDTEAEREVQGALDQ-AQAGRTTIIVAHRLSTIRNV-DRIFVFKAGNI 613
Cdd:cd03262 149 ALAMNPKVMLFDEPTSALDPELVGEVLDVMKDlAEEGMTMVVVTHEMGFAREVaDRVIFMDDGRI 213
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
399-625 |
1.41e-44 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 164.87 E-value: 1.41e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 399 ISFKDVHFRYPSRK-DIHVLKGISLELKAGDKIALVGSSGCGKSTIV---NLLQRfydPTKGRVLIDGVDLREVNVHSLR 474
Cdd:COG1135 2 IELENLSKTFPTKGgPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIrciNLLER---PTSGSVLVDGVDLTALSERELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 475 E---QIGIVSQEPVLFDG-TIYENIKMGNEHAthdqvveacKMANANdfIKRlpdgygtRVGE---------KG----VQ 537
Cdd:COG1135 79 AarrKIGMIFQHFNLLSSrTVAENVALPLEIA---------GVPKAE--IRK-------RVAEllelvglsdKAdaypSQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 538 LSGGQKQRIAIARALVKNPKILLLDEATSALDTEAEREVQGALDQAQA--GRTTIIVAHRLSTIRNV-DRIFVFKAGNIV 614
Cdd:COG1135 141 LSGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRelGLTIVLITHEMDVVRRIcDRVAVLENGRIV 220
|
250
....*....|.
gi 124244275 615 ESGSHEELMSK 625
Cdd:COG1135 221 EQGPVLDVFAN 231
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
124-632 |
1.97e-44 |
|
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: 176.67 E-value: 1.97e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 124 YLVLGVL---MFFTSYVQIACFESYAERLVHklrQNYLKAILRQQIQWFDKQQTGNLTARLTDDLERVREGLgdkfALLV 200
Cdd:TIGR00957 1011 YGALGILqgfAVFGYSMAVSIGGIQASRVLH---QDLLHNKLRSPMSFFERTPSGNLVNRFSKELDTVDSMI----PPVI 1083
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 201 QMFAAflagygvGFFYSWSMTLVMMGFAPL--IVLSGAKMSKSMATR---------TRVEQETYAVAGAIAEETFSSIRT 269
Cdd:TIGR00957 1084 KMFMG-------SLFNVIGALIVILLATPIaaVIIPPLGLLYFFVQRfyvassrqlKRLESVSRSPVYSHFNETLLGVSV 1156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 270 VHSLNGHKR---ELDRFYNALEVGRQTGIVKYCYMGIGVGFSNLCMYSSYALafwygsTLIINDPTFDRGLIFTVFFAVL 346
Cdd:TIGR00957 1157 IRAFEEQERfihQSDLKVDENQKAYYPSIVANRWLAVRLECVGNCIVLFAAL------FAVISRHSLSAGLVGLSVSYSL 1230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 347 SGSTSLGGaLPHLASFGTARGAASTVLRVINSHPKIDPYSLEGILVDN---MKGDISFKDVHFRYPSRKDIhVLKGISLE 423
Cdd:TIGR00957 1231 QVTFYLNW-LVRMSSEMETNIVAVERLKEYSETEKEAPWQIQETAPPSgwpPRGRVEFRNYCLRYREDLDL-VLRHINVT 1308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 424 LKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDLREVNVHSLREQIGIVSQEPVLFDGTIYENIKMGNEHAT 503
Cdd:TIGR00957 1309 IHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLDPFSQYSD 1388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 504 HDqVVEACKMANANDFIKRLPDGYGTRVGEKGVQLSGGQKQRIAIARALVKNPKILLLDEATSALDTEAEREVQGALDQA 583
Cdd:TIGR00957 1389 EE-VWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQ 1467
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 124244275 584 QAGRTTIIVAHRLSTIRNVDRIFVFKAGNIVESGSHEELMSKQGIFYDM 632
Cdd:TIGR00957 1468 FEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRGIFYSM 1516
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
399-615 |
2.27e-44 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 161.80 E-value: 2.27e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 399 ISFKDVHFRYPSRK-DIHVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDlrevnVHSLREQI 477
Cdd:COG1116 8 LELRGVSKRFPTGGgGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKP-----VTGPGPDR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 478 GIVSQEPVLFD-GTIYENIKMGNEHAT------HDQVVEACKMANANDFIKRLPDgygtrvgekgvQLSGGQKQRIAIAR 550
Cdd:COG1116 83 GVVFQEPALLPwLTVLDNVALGLELRGvpkaerRERARELLELVGLAGFEDAYPH-----------QLSGGMRQRVAIAR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 124244275 551 ALVKNPKILLLDEATSALDTEAEREVQGALDQ--AQAGRTTIIVAH------RLStirnvDRIFVFKA--GNIVE 615
Cdd:COG1116 152 ALANDPEVLLMDEPFGALDALTRERLQDELLRlwQETGKTVLFVTHdvdeavFLA-----DRVVVLSArpGRIVE 221
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
399-621 |
2.66e-44 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 160.22 E-value: 2.66e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 399 ISFKDVHFRYPsrKDIHVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDLREVN---VHSLRE 475
Cdd:COG2884 2 IRFENVSKRYP--GGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKrreIPYLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 476 QIGIVSQE-PVLFDGTIYENIK-----MG-NEHATHDQVVEACKMANANDFIKRLPDgygtrvgekgvQLSGGQKQRIAI 548
Cdd:COG2884 80 RIGVVFQDfRLLPDRTVYENVAlplrvTGkSRKEIRRRVREVLDLVGLSDKAKALPH-----------ELSGGEQQRVAI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 124244275 549 ARALVKNPKILLLDEATSALDTEAEREVQGALDQAQAGRTTIIVA-HRLSTIRNVD-RIFVFKAGNIVESGSHEE 621
Cdd:COG2884 149 ARALVNRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIAtHDLELVDRMPkRVLELEDGRLVRDEARGV 223
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
399-611 |
3.03e-44 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 159.17 E-value: 3.03e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 399 ISFKDVHFRYPSRKDIH--VLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGvdlrevnvhslreQ 476
Cdd:cd03250 1 ISVEDASFTWDSGEQETsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-------------S 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 477 IGIVSQEPVLFDGTIYENIKMGNE--HATHDQVVEACkmANANDfIKRLPDGYGTRVGEKGVQLSGGQKQRIAIARALVK 554
Cdd:cd03250 68 IAYVSQEPWIQNGTIRENILFGKPfdEERYEKVIKAC--ALEPD-LEILPDGDLTEIGEKGINLSGGQKQRISLARAVYS 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124244275 555 NPKILLLDEATSALDTEAERE-----VQGALdqaQAGRTTIIVAHRLSTIRNVDRIFVFKAG 611
Cdd:cd03250 145 DADIYLLDDPLSAVDAHVGRHifencILGLL---LNNKTRILVTHQLQLLPHADQIVVLDNG 203
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
416-1264 |
3.39e-44 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 176.12 E-value: 3.39e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 416 VLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDgvdlrevnvhslrEQIGIVSQEPVLFDGTIYENI 495
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAE-------------RSIAYVPQQAWIMNATVRGNI 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 496 KMGNEHATHD--QVVEACKMaNANdfIKRLPDGYGTRVGEKGVQLSGGQKQRIAIARALVKNPKILLLDEATSALDTE-A 572
Cdd:PTZ00243 742 LFFDEEDAARlaDAVRVSQL-EAD--LAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHvG 818
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 573 EREVQGALDQAQAGRTTIIVAHRLSTIRNVDRIFVFKAGNIVESGSHEELMsKQGIFYDMTQAQVVRQQQQEAGKDIEDT 652
Cdd:PTZ00243 819 ERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFM-RTSLYATLAAELKENKDSKEGDADAEVA 897
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 653 ISESAH---SHLSRKSSTR-------SAISIATSIHQLAeeVEECKAP---PTSMFK-IFKFNGDKVGWfiGGIFGAFIF 718
Cdd:PTZ00243 898 EVDAAPggaVDHEPPVAKQegnaeggDGAALDAAAGRLM--TREEKASgsvPWSTYVaYLRFCGGLHAA--GFVLATFAV 973
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 719 GSVTPVFALVYAEIFNVYSLPADQmQANVYFWCGMFVLMGITFFVGFFTSANCLGRCGESLTMKLrfeaFKNLLRQDIAF 798
Cdd:PTZ00243 974 TELVTVSSGVWLSMWSTRSFKLSA-ATYLYVYLGIVLLGTFSVPLRFFLSYEAMRRGSRNMHRDL----LRSVSRGTMSF 1048
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 799 YDdlRHGTGKLCTRFATD------APNVRYVFtrlpvVLASIVTICGALGIGFYygwQLALILVVMVPLLVMggYFEMqM 872
Cdd:PTZ00243 1049 FD--TTPLGRILNRFSRDidildnTLPMSYLY-----LLQCLFSICSSILVTSA---SQPFVLVALVPCGYL--YYRL-M 1115
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 873 RF----GKQIRDTQ---------LLEEA----------GK---VASQAVEHIRTVHSlnrqeqfhftyCEYLREPFNTNL 926
Cdd:PTZ00243 1116 QFynsaNREIRRIKsvakspvftLLEEAlqgsatitayGKahlVMQEALRRLDVVYS-----------CSYLENVANRWL 1184
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 927 khahtyGAVFAFSQSLIFFMYAAAFYLGSIFVNQQamQPIDVyrvffaISFCGQMIGNTTSFIPDVVkaRLAAS------ 1000
Cdd:PTZ00243 1185 ------GVRVEFLSNIVVTVIALIGVIGTMLRATS--QEIGL------VSLSLTMAMQTTATLNWLV--RQVATveadmn 1248
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1001 ----LLFYLIEHPT----PIDSLSD-----SGIVKPITGNISI--------------------RNVFFNYptRKDTK-VL 1046
Cdd:PTZ00243 1249 sverLLYYTDEVPHedmpELDEEVDalerrTGMAADVTGTVVIepasptsaaphpvqagslvfEGVQMRY--REGLPlVL 1326
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1047 QGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGMIMIDGDNIRNLNISSLREQVCIVSQEPTLFDCTIGENIcy 1126
Cdd:PTZ00243 1327 RGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQNV-- 1404
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1127 GTNRNVTYQEIVEAAKMANIHNFILGLPDGYDTHVGEKGTQLSGGQKQRIAIARALVRSPS-VLLLDEATSALDTESEKI 1205
Cdd:PTZ00243 1405 DPFLEASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKKGSgFILMDEATANIDPALDRQ 1484
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1206 VQEALDAAKQGRTCLVIAHRLSTIQNSDVIAIVSEGKIVEKGTHDELI-RKSEIYQKFCE 1264
Cdd:PTZ00243 1485 IQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELVmNRQSIFHSMVE 1544
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
400-611 |
3.55e-44 |
|
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: 157.41 E-value: 3.55e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 400 SFKDVHFRYPSRkdiHVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDLREVNVHSLREQIGI 479
Cdd:cd00267 1 EIENLSFRYGGR---TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 480 VSQepvlfdgtiyenikmgnehathdqvveackmanandfikrlpdgygtrvgekgvqLSGGQKQRIAIARALVKNPKIL 559
Cdd:cd00267 78 VPQ-------------------------------------------------------LSGGQRQRVALARALLLNPDLL 102
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 124244275 560 LLDEATSALDTEAEREVQGAL-DQAQAGRTTIIVAHRLSTIRNV-DRIFVFKAG 611
Cdd:cd00267 103 LLDEPTSGLDPASRERLLELLrELAEEGRTVIIVTHDPELAELAaDRVIVLKDG 156
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
399-627 |
3.60e-44 |
|
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: 160.41 E-value: 3.60e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 399 ISFKDVHFRYpsrKDIHVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDLREVNVHsLREQIG 478
Cdd:COG4555 2 IEVENLSKKY---GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPRE-ARRQIG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 479 IVSQEPVLFDG-TIYENIKMgneHAT-HDQVVEACKmANANDFIKR--LPDGYGTRVGEkgvqLSGGQKQRIAIARALVK 554
Cdd:COG4555 78 VLPDERGLYDRlTVRENIRY---FAElYGLFDEELK-KRIEELIELlgLEEFLDRRVGE----LSTGMKKKVALARALVH 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 124244275 555 NPKILLLDEATSALDTEAEREVQGALDQ-AQAGRTTIIVAHRLSTIRNV-DRIFVFKAGNIVESGSHEELMSKQG 627
Cdd:COG4555 150 DPKVLLLDEPTNGLDVMARRLLREILRAlKKEGKTVLFSSHIMQEVEALcDRVVILHKGKVVAQGSLDELREEIG 224
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
1028-1247 |
6.24e-44 |
|
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: 157.47 E-value: 6.24e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1028 ISIRNVFFNYPtRKDTKVLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGMIMIDGDNIRNLNiSSLREQVC 1107
Cdd:cd03247 1 LSINNVSFSYP-EQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1108 IVSQEPTLFDCTIGENIcygtnrnvtyqeiveaakmanihnfilglpdgydthvgekGTQLSGGQKQRIAIARALVRSPS 1187
Cdd:cd03247 79 VLNQRPYLFDTTLRNNL----------------------------------------GRRFSGGERQRLALARILLQDAP 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1188 VLLLDEATSALDTESEKIVQEALDAAKQGRTCLVIAHRLSTIQNSDVIAIVSEGKIVEKG 1247
Cdd:cd03247 119 IVLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
399-624 |
6.66e-44 |
|
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: 159.97 E-value: 6.66e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 399 ISFKDVHFRYPSR-KDIHVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDLREVNVHSLREQI 477
Cdd:COG1124 2 LEVRNLSVSYGQGgRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 478 GIVSQEP---------VlfDGTIYENIKMGNEHATHDQVVEACKMAN-ANDFIKRLPDgygtrvgekgvQLSGGQKQRIA 547
Cdd:COG1124 82 QMVFQDPyaslhprhtV--DRILAEPLRIHGLPDREERIAELLEQVGlPPSFLDRYPH-----------QLSGGQRQRVA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 548 IARALVKNPKILLLDEATSALDTEAEREVQGALD--QAQAGRTTIIVAHRLSTIRNV-DRIFVFKAGNIVESGSHEELMS 624
Cdd:COG1124 149 IARALILEPELLLLDEPTSALDVSVQAEILNLLKdlREERGLTYLFVSHDLAVVAHLcDRVAVMQNGRIVEELTVADLLA 228
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
120-632 |
7.05e-44 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 174.78 E-value: 7.05e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 120 YCIYYLVLG---VLMFFTSYVQIACFESYAERLVHklrQNYLKAILRQQIQWFDKQQTGNLTARLTDD---LERVREGLG 193
Cdd:PLN03232 952 YIVVYALLGfgqVAVTFTNSFWLISSSLHAAKRLH---DAMLNSILRAPMLFFHTNPTGRVINRFSKDigdIDRNVANLM 1028
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 194 DKFA-LLVQMFAAFLAGYGVGFFYSWS-MTLVMMGFAPLIVL-SGAKMSKSMATRTRveQETYAVAGAiAEETFSSIRTv 270
Cdd:PLN03232 1029 NMFMnQLWQLLSTFALIGTVSTISLWAiMPLLILFYAAYLYYqSTSREVRRLDSVTR--SPIYAQFGE-ALNGLSSIRA- 1104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 271 hslnghkreldrfYNALEvgrQTGIVKYCYMGIGVGFSNLCMYSSYALAF----------WYGSTLII--NDPTFDRGLI 338
Cdd:PLN03232 1105 -------------YKAYD---RMAKINGKSMDNNIRFTLANTSSNRWLTIrletlggvmiWLTATFAVlrNGNAENQAGF 1168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 339 FTVFFAVLSGSTSLGGALPH-LASFGTARGAASTVLRVINShpkID-PYSLEGILVDN-------MKGDISFKDVHFRYp 409
Cdd:PLN03232 1169 ASTMGLLLSYTLNITTLLSGvLRQASKAENSLNSVERVGNY---IDlPSEATAIIENNrpvsgwpSRGSIKFEDVHLRY- 1244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 410 sRKDIH-VLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDLREVNVHSLREQIGIVSQEPVLFD 488
Cdd:PLN03232 1245 -RPGLPpVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFS 1323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 489 GTIYENIKMGNEHATHDqVVEACKMANANDFIKRLPDGYGTRVGEKGVQLSGGQKQRIAIARALVKNPKILLLDEATSAL 568
Cdd:PLN03232 1324 GTVRFNIDPFSEHNDAD-LWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASV 1402
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 124244275 569 DTEAEREVQGALDQAQAGRTTIIVAHRLSTIRNVDRIFVFKAGNIVESGSHEELMSKQG-IFYDM 632
Cdd:PLN03232 1403 DVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTsAFFRM 1467
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
395-624 |
1.31e-43 |
|
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: 167.00 E-value: 1.31e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 395 MKGDISFKDVHFRYPSRkDIHVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPT---KGRVLIDGVDLREVNVH 471
Cdd:COG1123 1 MTPLLEVRDLSVRYPGG-DVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 472 SLREQIGIVSQEP--VLFDGTIYENI-------KMGNEHAtHDQVVEACKMANANDFIKRLPDgygtrvgekgvQLSGGQ 542
Cdd:COG1123 80 LRGRRIGMVFQDPmtQLNPVTVGDQIaealenlGLSRAEA-RARVLELLEAVGLERRLDRYPH-----------QLSGGQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 543 KQRIAIARALVKNPKILLLDEATSALDTEAEREVQGALD--QAQAGRTTIIVAHRLSTI-RNVDRIFVFKAGNIVESGSH 619
Cdd:COG1123 148 RQRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRelQRERGTTVLLITHDLGVVaEIADRVVVMDDGRIVEDGPP 227
|
....*
gi 124244275 620 EELMS 624
Cdd:COG1123 228 EEILA 232
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
399-626 |
1.99e-43 |
|
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: 159.13 E-value: 1.99e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 399 ISFKDVHFRYPSRKDiHVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVD-LREVNVHSLREQI 477
Cdd:TIGR04520 1 IEVENVSFSYPESEK-PALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDtLDEENLWEIRKKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 478 GIVSQEPvlfD----GTIY--------ENI-----KMgnehatHDQVVEACKMANANDFIKRLPdgygtrvgekgVQLSG 540
Cdd:TIGR04520 80 GMVFQNP---DnqfvGATVeddvafglENLgvpreEM------RKRVDEALKLVGMEDFRDREP-----------HLLSG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 541 GQKQRIAIARALVKNPKILLLDEATSALDTEAEREVQGALDQ--AQAGRTTIIVAHRLSTIRNVDRIFVFKAGNIVESGS 618
Cdd:TIGR04520 140 GQKQRVAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKlnKEEGITVISITHDMEEAVLADRVIVMNKGKIVAEGT 219
|
....*...
gi 124244275 619 HEELMSKQ 626
Cdd:TIGR04520 220 PREIFSQV 227
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
399-615 |
2.36e-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: 157.25 E-value: 2.36e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 399 ISFKDVHFRYPSRK-DIHVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDLREVNVHslreqI 477
Cdd:cd03293 1 LEVRNVSKTYGGGGgAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD-----R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 478 GIVSQEPVLFD-GTIYENIKMGNEHA------THDQVVEACKMANANDFIKRLPDgygtrvgekgvQLSGGQKQRIAIAR 550
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNVALGLELQgvpkaeARERAEELLELVGLSGFENAYPH-----------QLSGGMRQRVALAR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 124244275 551 ALVKNPKILLLDEATSALDTEAEREVQGALDQ--AQAGRTTIIVAH------RLStirnvDRIFVFKA--GNIVE 615
Cdd:cd03293 145 ALAVDPDVLLLDEPFSALDALTREQLQEELLDiwRETGKTVLLVTHdideavFLA-----DRVVVLSArpGRIVA 214
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
399-623 |
5.23e-43 |
|
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: 157.06 E-value: 5.23e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 399 ISFKDVHFRYPSRkdiHVLKGISLELKAGDKIALVGSSGCGKST----IVNLLQrfydPTKGRVLIDGVDLREVNVH--- 471
Cdd:COG1127 6 IEVRNLTKSFGDR---VVLDGVSLDVPRGEILAIIGGSGSGKSVllklIIGLLR----PDSGEILVDGQDITGLSEKely 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 472 SLREQIGIVSQEPVLFDG-TIYENIKMG-NEHAT------HDQVVEACKMANANDFIKRLPDgygtrvgekgvQLSGGQK 543
Cdd:COG1127 79 ELRRRIGMLFQGGALFDSlTVFENVAFPlREHTDlseaeiRELVLEKLELVGLPGAADKMPS-----------ELSGGMR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 544 QRIAIARALVKNPKILLLDEATSALD--TEAE-----REVQGALdqaqaGRTTIIVAHRLSTIRNV-DRIFVFKAGNIVE 615
Cdd:COG1127 148 KRVALARALALDPEILLYDEPTAGLDpiTSAVideliRELRDEL-----GLTSVVVTHDLDSAFAIaDRVAVLADGKIIA 222
|
....*...
gi 124244275 616 SGSHEELM 623
Cdd:COG1127 223 EGTPEELL 230
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1028-1254 |
6.68e-43 |
|
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: 165.08 E-value: 6.68e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1028 ISIRNVFFNYPTRK--DTKVLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGMIMIDGDNIRNLNISSLRE- 1104
Cdd:COG1123 261 LEVRNLSKRYPVRGkgGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLREl 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1105 --QVCIVSQEP-TLFDC--TIGENICYG------TNRNVTYQEIVEAAKManihnfiLGLPDGY-DTHVGEkgtqLSGGQ 1172
Cdd:COG1123 341 rrRVQMVFQDPySSLNPrmTVGDIIAEPlrlhglLSRAERRERVAELLER-------VGLPPDLaDRYPHE----LSGGQ 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1173 KQRIAIARALVRSPSVLLLDEATSALDTESEKIVQEALD--AAKQGRTCLVIAHRLSTIQN-SDVIAIVSEGKIVEKGTH 1249
Cdd:COG1123 410 RQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRdlQRELGLTYLFISHDLAVVRYiADRVAVMYDGRIVEDGPT 489
|
....*
gi 124244275 1250 DELIR 1254
Cdd:COG1123 490 EEVFA 494
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
399-626 |
9.73e-43 |
|
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: 156.12 E-value: 9.73e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 399 ISFKDVHFRYPSRkdiHVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDLREVNVHSLRE--- 475
Cdd:cd03261 1 IELRGLTKSFGGR---TVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRlrr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 476 QIGIVSQEPVLFDG-TIYENIKMG-NEHAT------HDQVVEACKMANANDFIKRLPDgygtrvgekgvQLSGGQKQRIA 547
Cdd:cd03261 78 RMGMLFQSGALFDSlTVFENVAFPlREHTRlseeeiREIVLEKLEAVGLRGAEDLYPA-----------ELSGGMKKRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 548 IARALVKNPKILLLDEATSALD-------TEAEREVQGALdqaqaGRTTIIVAHRLSTIRNV-DRIFVFKAGNIVESGSH 619
Cdd:cd03261 147 LARALALDPELLLYDEPTAGLDpiasgviDDLIRSLKKEL-----GLTSIMVTHDLDTAFAIaDRIAVLYDGKIVAEGTP 221
|
....*..
gi 124244275 620 EELMSKQ 626
Cdd:cd03261 222 EELRASD 228
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
399-626 |
1.10e-42 |
|
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: 156.74 E-value: 1.10e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 399 ISFKDVHFRYPSRkdiHVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDLREVNVHSLREQIG 478
Cdd:COG1120 2 LEAENLSVGYGGR---PVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 479 IVSQEPVL-FDGTIYENIKMG----------NEHATHDQVVEACKMANANDFIKRlpdgygtRVGEkgvqLSGGQKQRIA 547
Cdd:COG1120 79 YVPQEPPApFGLTVRELVALGryphlglfgrPSAEDREAVEEALERTGLEHLADR-------PVDE----LSGGERQRVL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 548 IARALVKNPKILLLDEATSALDTEAEREVQGALDQ--AQAGRTTIIVAHRLS-TIRNVDRIFVFKAGNIVESGSHEELMS 624
Cdd:COG1120 148 IARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRlaRERGRTVVMVLHDLNlAARYADRLVLLKDGRIVAQGPPEEVLT 227
|
..
gi 124244275 625 KQ 626
Cdd:COG1120 228 PE 229
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
399-622 |
1.19e-42 |
|
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: 155.86 E-value: 1.19e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 399 ISFKDVHFRYpsrKDIHVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDLREVNVHslREQIG 478
Cdd:cd03300 1 IELENVSKFY---GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPH--KRPVN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 479 IVSQEPVLFDG-TIYENIKMG------NEHATHDQVVEACKMANANDFIKRLPDgygtrvgekgvQLSGGQKQRIAIARA 551
Cdd:cd03300 76 TVFQNYALFPHlTVFENIAFGlrlkklPKAEIKERVAEALDLVQLEGYANRKPS-----------QLSGGQQQRVAIARA 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124244275 552 LVKNPKILLLDEATSALDTEAEREVQGALDQAQ--AGRTTIIVAHRLSTIRNV-DRIFVFKAGNIVESGSHEEL 622
Cdd:cd03300 145 LVNEPKVLLLDEPLGALDLKLRKDMQLELKRLQkeLGITFVFVTHDQEEALTMsDRIAVMNKGKIQQIGTPEEI 218
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
399-611 |
1.28e-42 |
|
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: 153.88 E-value: 1.28e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 399 ISFKDVHFRYpsrKDIHVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDLREVNVHS--LREQ 476
Cdd:cd03229 1 LELKNVSKRY---GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELppLRRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 477 IGIVSQEPVLFDG-TIYENIKMGnehathdqvveackmanandfikrlpdgygtrvgekgvqLSGGQKQRIAIARALVKN 555
Cdd:cd03229 78 IGMVFQDFALFPHlTVLENIALG---------------------------------------LSGGQQQRVALARALAMD 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 124244275 556 PKILLLDEATSALDTEAEREVQGALDQ--AQAGRTTIIVAHRLSTIRNV-DRIFVFKAG 611
Cdd:cd03229 119 PDVLLLDEPTSALDPITRREVRALLKSlqAQLGITVVLVTHDLDEAARLaDRVVVLRDG 177
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
399-622 |
4.63e-42 |
|
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: 157.14 E-value: 4.63e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 399 ISFKDVHFRYPSRK-DIHVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDP---TKGRVLIDGVDLREVNVHSLR 474
Cdd:COG0444 2 LEVRNLKVYFPTRRgVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 475 E----QIGIVSQE------PVLfdgTIYENI-------KMGNEHATHDQVVEA---CKMANANDFIKRLPdgygtrvgek 534
Cdd:COG0444 82 KirgrEIQMIFQDpmtslnPVM---TVGDQIaeplrihGGLSKAEARERAIELlerVGLPDPERRLDRYP---------- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 535 gVQLSGGQKQRIAIARALVKNPKILLLDEATSALDTEAEREVqgaLD-----QAQAGRTTIIVAHRLSTIRNV-DRIFVF 608
Cdd:COG0444 149 -HELSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQI---LNllkdlQRELGLAILFITHDLGVVAEIaDRVAVM 224
|
250
....*....|....
gi 124244275 609 KAGNIVESGSHEEL 622
Cdd:COG0444 225 YAGRIVEEGPVEEL 238
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1028-1245 |
7.92e-42 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 153.28 E-value: 7.92e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1028 ISIRNVFFNYPTRK-DTKVLQGFTLDIKAGKTVALVGHSGCGKST---IMGLLERFynqDKGMIMIDGDNIRNLNISSL- 1102
Cdd:COG1136 5 LELRNLTKSYGTGEgEVTALRGVSLSIEAGEFVAIVGPSGSGKSTllnILGGLDRP---TSGEVLIDGQDISSLSERELa 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1103 ---REQVCIVSQEPTLFDC-TIGENICY-----GTNRNVTYQEIVEAAKManihnfiLGLPDgydtHVGEKGTQLSGGQK 1173
Cdd:COG1136 82 rlrRRHIGFVFQFFNLLPElTALENVALplllaGVSRKERRERARELLER-------VGLGD----RLDHRPSQLSGGQQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124244275 1174 QRIAIARALVRSPSVLLLDEATSALDTESEKIVQEALD--AAKQGRTCLVIAHRLSTIQNSDVIAIVSEGKIVE 1245
Cdd:COG1136 151 QRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRelNRELGTTIVMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
397-629 |
7.96e-42 |
|
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: 154.30 E-value: 7.96e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 397 GDISFKDVHFRYPSRKDiHVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDLREVNVHSLREQ 476
Cdd:cd03288 18 GEIKIHDLCVRYENNLK-PVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 477 IGIVSQEPVLFDGTIYENIKmGNEHATHDQVVEACKMANANDFIKRLPDGYGTRVGEKGVQLSGGQKQRIAIARALVKNP 556
Cdd:cd03288 97 LSIILQDPILFSGSIRFNLD-PECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKS 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124244275 557 KILLLDEATSALDTEAEREVQGALDQAQAGRTTIIVAHRLSTIRNVDRIFVFKAGNIVESGSHEELMSKQ-GIF 629
Cdd:cd03288 176 SILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEdGVF 249
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1028-1262 |
1.32e-41 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 152.84 E-value: 1.32e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1028 ISIRNVffnyptRK---DTKVLQGFTLDIKAGKTVALVGHSGCGKSTI---MGLLERFynqDKGMIMIDGDNI--RNLNI 1099
Cdd:COG1126 2 IEIENL------HKsfgDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLlrcINLLEEP---DSGTITVDGEDLtdSKKDI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1100 SSLREQVCIVSQEPTLF-DCTIGENICYG--TNRNVTYQEIVEAAkMAnihnfIL---GLPDGYDTHVGekgtQLSGGQK 1173
Cdd:COG1126 73 NKLRRKVGMVFQQFNLFpHLTVLENVTLApiKVKKMSKAEAEERA-ME-----LLervGLADKADAYPA----QLSGGQQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1174 QRIAIARALVRSPSVLLLDEATSALDTEsekIVQEALDA----AKQGRTCLVIAHRLSTIQN-SDVIAIVSEGKIVEKGT 1248
Cdd:COG1126 143 QRVAIARALAMEPKVMLFDEPTSALDPE---LVGEVLDVmrdlAKEGMTMVVVTHEMGFAREvADRVVFMDGGRIVEEGP 219
|
250
....*....|....*.
gi 124244275 1249 HDELIR--KSEIYQKF 1262
Cdd:COG1126 220 PEEFFEnpQHERTRAF 235
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
399-623 |
3.02e-41 |
|
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: 152.07 E-value: 3.02e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 399 ISFKDVHFRYPSRKDihVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDLREVNVHSLREQIG 478
Cdd:cd03295 1 IEFENVTKRYGGGKK--AVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 479 IVSQEPVLFDG-TIYENIKM------GNEHATHDQVVEACKMANAND--FIKRLPDgygtrvgekgvQLSGGQKQRIAIA 549
Cdd:cd03295 79 YVIQQIGLFPHmTVEENIALvpkllkWPKEKIRERADELLALVGLDPaeFADRYPH-----------ELSGGQQQRVGVA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 124244275 550 RALVKNPKILLLDEATSALDTEAEREVQGALD--QAQAGRTTIIVAHRL-STIRNVDRIFVFKAGNIVESGSHEELM 623
Cdd:cd03295 148 RALAADPPLLLMDEPFGALDPITRDQLQEEFKrlQQELGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEIL 224
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
1023-1248 |
3.52e-41 |
|
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: 150.64 E-value: 3.52e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1023 PITGNISIRNVFFNYptRKD-TKVLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGMIMIDGDNIRNLNISS 1101
Cdd:cd03369 2 PEHGEIEVENLSVRY--APDlPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLED 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1102 LREQVCIVSQEPTLFDCTIGENI-CYGTNRNVtyqEIVEAAKmanihnfilglpdgydthVGEKGTQLSGGQKQRIAIAR 1180
Cdd:cd03369 80 LRSSLTIIPQDPTLFSGTIRSNLdPFDEYSDE---EIYGALR------------------VSEGGLNLSQGQRQLLCLAR 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 124244275 1181 ALVRSPSVLLLDEATSALDTESEKIVQEALDAAKQGRTCLVIAHRLSTIQNSDVIAIVSEGKIVEKGT 1248
Cdd:cd03369 139 ALLKRPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
1028-1255 |
3.91e-41 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 151.75 E-value: 3.91e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1028 ISIRNVFFNYptrKDTKVLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGMIMIDGDNIRNlNISSLREQVC 1107
Cdd:COG1131 1 IEVRGLTKRY---GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR-DPAEVRRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1108 IVSQEPTLF-DCTIGENI-----CYGTNRNVTYQEIVEAAKManihnfiLGLPDGYDTHVGekgtQLSGGQKQRIAIARA 1181
Cdd:COG1131 77 YVPQEPALYpDLTVRENLrffarLYGLPRKEARERIDELLEL-------FGLTDAADRKVG----TLSGGMKQRLGLALA 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 124244275 1182 LVRSPSVLLLDEATSALDTESEKIVQEAL-DAAKQGRTCLVIAHRLSTIQN-SDVIAIVSEGKIVEKGTHDELIRK 1255
Cdd:COG1131 146 LLHDPELLILDEPTSGLDPEARRELWELLrELAAEGKTVLLSTHYLEEAERlCDRVAIIDKGRIVADGTPDELKAR 221
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
1028-1243 |
8.74e-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: 148.13 E-value: 8.74e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1028 ISIRNVFFNYPTRKDTkVLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGMIMIDGDNIRNLNISSLREQVC 1107
Cdd:cd03246 1 LEVENVSFRYPGAEPP-VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1108 IVSQEPTLFDCTIGENIcygtnrnvtyqeiveaakmanihnfilglpdgydthvgekgtqLSGGQKQRIAIARALVRSPS 1187
Cdd:cd03246 80 YLPQDDELFSGSIAENI-------------------------------------------LSGGQRQRLGLARALYGNPR 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 124244275 1188 VLLLDEATSALDTESEKIVQEALDAAK-QGRTCLVIAHRLSTIQNSDVIAIVSEGKI 1243
Cdd:cd03246 117 ILVLDEPNSHLDVEGERALNQAIAALKaAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
399-613 |
1.11e-40 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 147.93 E-value: 1.11e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 399 ISFKDVHFRYpsrKDIHVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDLREvNVHSLREQIG 478
Cdd:cd03230 1 IEVRNLSKRY---GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 479 IVSQEPVLFDG-TIYENIKmgnehathdqvveackmanandfikrlpdgygtrvgekgvqLSGGQKQRIAIARALVKNPK 557
Cdd:cd03230 77 YLPEEPSLYENlTVRENLK-----------------------------------------LSGGMKQRLALAQALLHDPE 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 124244275 558 ILLLDEATSALDTEAEREVQGALDQ-AQAGRTTIIVAHRLSTIRNV-DRIFVFKAGNI 613
Cdd:cd03230 116 LLILDEPTSGLDPESRREFWELLRElKKEGKTILLSSHILEEAERLcDRVAILNNGRI 173
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
397-622 |
1.70e-40 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 153.69 E-value: 1.70e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 397 GDISFKDVHFRYpsrKDIHVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDlreVN-VHSLRE 475
Cdd:COG3839 2 ASLELENVSKSY---GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRD---VTdLPPKDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 476 QIGIVSQEPVLFDG-TIYENI----KMGNEHAT--HDQVVEACKMANANDFIKRLPDgygtrvgekgvQLSGGQKQRIAI 548
Cdd:COG3839 76 NIAMVFQSYALYPHmTVYENIafplKLRKVPKAeiDRRVREAAELLGLEDLLDRKPK-----------QLSGGQRQRVAL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 549 ARALVKNPKILLLDEATSALD----TEAEREVQgALdQAQAGRTTIIVAH------RLStirnvDRIFVFKAGNIVESGS 618
Cdd:COG3839 145 GRALVREPKVFLLDEPLSNLDaklrVEMRAEIK-RL-HRRLGTTTIYVTHdqveamTLA-----DRIAVMNDGRIQQVGT 217
|
....
gi 124244275 619 HEEL 622
Cdd:COG3839 218 PEEL 221
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
399-622 |
2.32e-40 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 152.99 E-value: 2.32e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 399 ISFKDVHFRYPSRkdiHVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDLrEVNVHSLREQIG 478
Cdd:COG1118 3 IEVRNISKRFGSF---TLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDL-FTNLPPRERRVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 479 IVSQEPVLF-DGTIYENIKMG------NEHATHDQVVEACKMANANDFIKRLPDgygtrvgekgvQLSGGQKQRIAIARA 551
Cdd:COG1118 79 FVFQHYALFpHMTVAENIAFGlrvrppSKAEIRARVEELLELVQLEGLADRYPS-----------QLSGGQRQRVALARA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 552 LVKNPKILLLDEATSALDT----EAEREVQGALDqaQAGRTTIIVAH------RLStirnvDRIFVFKAGNIVESGSHEE 621
Cdd:COG1118 148 LAVEPEVLLLDEPFGALDAkvrkELRRWLRRLHD--ELGGTTVFVTHdqeealELA-----DRVVVMNQGRIEQVGTPDE 220
|
.
gi 124244275 622 L 622
Cdd:COG1118 221 V 221
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
399-625 |
2.56e-40 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 149.80 E-value: 2.56e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 399 ISFKDVHFRYpsrKDIHVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYD--P---TKGRVLIDGVDL--REVNVH 471
Cdd:COG1117 12 IEVRNLNVYY---GDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDliPgarVEGEILLDGEDIydPDVDVV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 472 SLREQIGIVSQEPVLFDGTIYENIKMG------NEHATHDQVVEAC-KMANANDFIK-RLpdgygtrvGEKGVQLSGGQK 543
Cdd:COG1117 89 ELRRRVGMVFQKPNPFPKSIYDNVAYGlrlhgiKSKSELDEIVEESlRKAALWDEVKdRL--------KKSALGLSGGQQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 544 QRIAIARALVKNPKILLLDEATSALDTEAEREVQGALDQAQAGRTTIIVAH------RLStirnvDRIFVFKAGNIVESG 617
Cdd:COG1117 161 QRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYTIVIVTHnmqqaaRVS-----DYTAFFYLGELVEFG 235
|
....*...
gi 124244275 618 SHEELMSK 625
Cdd:COG1117 236 PTEQIFTN 243
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
399-626 |
5.24e-40 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 148.70 E-value: 5.24e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 399 ISFKDVHFRYPSRKdihVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDLREVnvhslREQIG 478
Cdd:COG1121 7 IELENLTVSYGGRP---VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA-----RRRIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 479 IVSQEpVLFDG----TIYENIKMGNEH----------ATHDQVVEACKMANANDFIKRlpdgygtRVGEkgvqLSGGQKQ 544
Cdd:COG1121 79 YVPQR-AEVDWdfpiTVRDVVLMGRYGrrglfrrpsrADREAVDEALERVGLEDLADR-------PIGE----LSGGQQQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 545 RIAIARALVKNPKILLLDEATSALDTEAEREVQGALDQ-AQAGRTTIIVAHRLSTIR-NVDRIFVFkAGNIVESGSHEEL 622
Cdd:COG1121 147 RVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRElRREGKTILVVTHDLGAVReYFDRVLLL-NRGLVAHGPPEEV 225
|
....
gi 124244275 623 MSKQ 626
Cdd:COG1121 226 LTPE 229
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
1046-1196 |
1.53e-39 |
|
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: 143.94 E-value: 1.53e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1046 LQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGMIMIDGDNIRNLNISSLREQVCIVSQEPTLF-DCTIGENI 1124
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFpRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124244275 1125 CYGTnRNVTYQEIVEAAKMANIHNFiLGLPDGYDTHVGEKGTQLSGGQKQRIAIARALVRSPSVLLLDEATS 1196
Cdd:pfam00005 81 RLGL-LLKGLSKREKDARAEEALEK-LGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
1029-1242 |
1.74e-39 |
|
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: 146.07 E-value: 1.74e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1029 SIRNVFFNYPtRKDTKVLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGMIMIDGDNIRNLNISSLREQVCI 1108
Cdd:cd03225 1 ELKNLSFSYP-DGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1109 VSQEPT--LFDCTIGENICYG-TNRNVTYQEIVEAAKMANIHNFILGLPDgYDTHvgekgtQLSGGQKQRIAIARALVRS 1185
Cdd:cd03225 80 VFQNPDdqFFGPTVEEEVAFGlENLGLPEEEIEERVEEALELVGLEGLRD-RSPF------TLSGGQKQRVAIAGVLAMD 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 124244275 1186 PSVLLLDEATSALDTESEKIVQEALDA-AKQGRTCLVIAHRLSTIQN-SDVIAIVSEGK 1242
Cdd:cd03225 153 PDILLLDEPTAGLDPAGRRELLELLKKlKAEGKTIIIVTHDLDLLLElADRVIVLEDGK 211
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1028-1247 |
2.02e-39 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 146.50 E-value: 2.02e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1028 ISIRNVFFNYPTRKDT-KVLQGFTLDIKAGKTVALVGHSGCGKST----IMGLLErfynQDKGMIMIDGDNIRNLN---I 1099
Cdd:cd03257 2 LEVKNLSVSFPTGGGSvKALDDVSFSIKKGETLGLVGESGSGKSTlaraILGLLK----PTSGSIIFDGKDLLKLSrrlR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1100 SSLREQVCIVSQE------PTLfdcTIGENIC-----YGTNRNVTYQEIVEAAKMANIhnfilGLPDgydTHVGEKGTQL 1168
Cdd:cd03257 78 KIRRKEIQMVFQDpmsslnPRM---TIGEQIAeplriHGKLSKKEARKEAVLLLLVGV-----GLPE---EVLNRYPHEL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1169 SGGQKQRIAIARALVRSPSVLLLDEATSALDTESEKIVQEALDAAKQ--GRTCLVIAHRLSTIQN-SDVIAIVSEGKIVE 1245
Cdd:cd03257 147 SGGQRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEelGLTLLFITHDLGVVAKiADRVAVMYAGKIVE 226
|
..
gi 124244275 1246 KG 1247
Cdd:cd03257 227 EG 228
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
115-372 |
2.89e-39 |
|
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: 148.09 E-value: 2.89e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 115 SEVVKYCIYYLVLGVLMFFTSYVQIACFESYAERLVHKLRQNYLKAILRQQIQWFDKQQTGNLTARLTDDLERVREGLGD 194
Cdd:cd18557 33 DVLNELALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFSSLLRQEIAFFDKHKTGELTSRLSSDTSVLQSAVTD 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 195 KFALLVQMFAAFLAGYGVGFFYSWSMTLVMMGFAPLIVLSGAKMSKSMATRTRVEQETYAVAGAIAEETFSSIRTVHSLN 274
Cdd:cd18557 113 NLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASKIYGRYIRKLSKEVQDALAKAGQVAEESLSNIRTVRSFS 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 275 GHKRELDRFYNALE----VGRQTGIVKYCYMGIgvgfSNLCMYSSYALAFWYGSTLIINDpTFDRGLIFTVFFAVLSGST 350
Cdd:cd18557 193 AEEKEIRRYSEALDrsyrLARKKALANALFQGI----TSLLIYLSLLLVLWYGGYLVLSG-QLTVGELTSFILYTIMVAS 267
|
250 260
....*....|....*....|..
gi 124244275 351 SLGGALPHLASFGTARGAASTV 372
Cdd:cd18557 268 SVGGLSSLLADIMKALGASERV 289
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
399-623 |
1.09e-38 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 145.90 E-value: 1.09e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 399 ISFKDVHFRYPSRKDiHVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDLREVNVHSLREQIG 478
Cdd:PRK13632 8 IKVENVSFSYPNSEN-NALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 479 IVSQEP-VLFDG-TIYENIKMGNEHathdqvveacKMANANDfIKRLPDGYGTRVGEKGV------QLSGGQKQRIAIAR 550
Cdd:PRK13632 87 IIFQNPdNQFIGaTVEDDIAFGLEN----------KKVPPKK-MKDIIDDLAKKVGMEDYldkepqNLSGGQKQRVAIAS 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 124244275 551 ALVKNPKILLLDEATSALDTEAEREVQGALD--QAQAGRTTIIVAHRLSTIRNVDRIFVFKAGNIVESGSHEELM 623
Cdd:PRK13632 156 VLALNPEIIIFDESTSMLDPKGKREIKKIMVdlRKTRKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEIL 230
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
1039-1247 |
1.38e-38 |
|
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: 143.43 E-value: 1.38e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1039 TRKDTKVLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGMIMIDGDNIRNLNISslREQVCIVSQEPTLFD- 1117
Cdd:cd03259 9 TYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE--RRNIGMVFQDYALFPh 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1118 CTIGENICYG-TNRNVTYQEIV----EAAKMANIHNFILGLPDgydthvgekgtQLSGGQKQRIAIARALVRSPSVLLLD 1192
Cdd:cd03259 87 LTVAENIAFGlKLRGVPKAEIRarvrELLELVGLEGLLNRYPH-----------ELSGGQQQRVALARALAREPSLLLLD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 124244275 1193 EATSALDTESEKIVQEALDA--AKQGRTCLVIAHRLS-TIQNSDVIAIVSEGKIVEKG 1247
Cdd:cd03259 156 EPLSALDAKLREELREELKElqRELGITTIYVTHDQEeALALADRIAVMNEGRIVQVG 213
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
399-622 |
1.56e-38 |
|
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: 144.25 E-value: 1.56e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 399 ISFKDVHFRYPSRKdiHVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVD---LREVNVHSLRE 475
Cdd:cd03256 1 IEVENLSKTYPNGK--KALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDinkLKGKALRQLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 476 QIGIVSQEPVLFDG-TIYENIKMG--NEHAT--------HDQVVEACKMAnandfIKR--LPDGYGTRVGekgvQLSGGQ 542
Cdd:cd03256 79 QIGMIFQQFNLIERlSVLENVLSGrlGRRSTwrslfglfPKEEKQRALAA-----LERvgLLDKAYQRAD----QLSGGQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 543 KQRIAIARALVKNPKILLLDEATSALDTEAEREVQGALDQA--QAGRTTIIVAHRLSTIR-NVDRIFVFKAGNIVESGSH 619
Cdd:cd03256 150 QQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRInrEEGITVIVSLHQVDLAReYADRIVGLKDGRIVFDGPP 229
|
...
gi 124244275 620 EEL 622
Cdd:cd03256 230 AEL 232
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
420-623 |
1.65e-38 |
|
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: 145.09 E-value: 1.65e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 420 ISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDLREVNVHSLRE----QIGIVSQEPVLF-DGTIYEN 494
Cdd:cd03294 43 VSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRElrrkKISMVFQSFALLpHRTVLEN 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 495 IKMG------NEHATHDQVVEACKMANANDFIKRLPDgygtrvgekgvQLSGGQKQRIAIARALVKNPKILLLDEATSAL 568
Cdd:cd03294 123 VAFGlevqgvPRAEREERAAEALELVGLEGWEHKYPD-----------ELSGGMQQRVGLARALAVDPDILLMDEAFSAL 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 124244275 569 DTEAEREVQGALDQAQA--GRTTIIVAHRLS-TIRNVDRIFVFKAGNIVESGSHEELM 623
Cdd:cd03294 192 DPLIRREMQDELLRLQAelQKTIVFITHDLDeALRLGDRIAIMKDGRLVQVGTPEEIL 249
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
399-622 |
2.43e-38 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 144.04 E-value: 2.43e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 399 ISFKDVHFRYPSRKdiHVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVD---LREVNVHSLRE 475
Cdd:COG3638 3 LELRNLSKRYPGGT--PALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDvtaLRGRALRRLRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 476 QIGIVSQEPVLFDG-TIYENIKMGNEHATH-----------DQVVEACkmananDFIKR--LPDGYGTRVGekgvQLSGG 541
Cdd:COG3638 81 RIGMIFQQFNLVPRlSVLTNVLAGRLGRTStwrsllglfppEDRERAL------EALERvgLADKAYQRAD----QLSGG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 542 QKQRIAIARALVKNPKILLLDEATSALDTEAEREVQGAL-DQAQA-GRTTIIVAHRLSTIRN-VDRIFVFKAGNIVESGS 618
Cdd:COG3638 151 QQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLrRIAREdGITVVVNLHQVDLARRyADRIIGLRDGRVVFDGP 230
|
....
gi 124244275 619 HEEL 622
Cdd:COG3638 231 PAEL 234
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1028-1261 |
7.63e-38 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 146.01 E-value: 7.63e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1028 ISIRNVFFNYptrKDTKVLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGMIMIDGDNIRNLNISslREQVC 1107
Cdd:COG3842 6 LELENVSKRY---GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPE--KRNVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1108 IVSQEPTLF-DCTIGENICYG-TNRNVTYQEIVE-AAKMANIhnfiLGLPDGYDTHVGekgtQLSGGQKQRIAIARALVR 1184
Cdd:COG3842 81 MVFQDYALFpHLTVAENVAFGlRMRGVPKAEIRArVAELLEL----VGLEGLADRYPH----QLSGGQQQRVALARALAP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1185 SPSVLLLDEATSALDTESEKIVQEALDA--AKQGRTCLVIAHRLS---TIqnSDVIAIVSEGKIVEKGThdelirKSEIY 1259
Cdd:COG3842 153 EPRVLLLDEPLSALDAKLREEMREELRRlqRELGITFIYVTHDQEealAL--ADRIAVMNDGRIEQVGT------PEEIY 224
|
..
gi 124244275 1260 QK 1261
Cdd:COG3842 225 ER 226
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
399-618 |
9.71e-38 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 145.33 E-value: 9.71e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 399 ISFKDVHFRYP-SRKDIHVLKGISLELKAGDKIALVGSSGCGKST---IVNLLQRfydPTKGRVLIDGVDLREVNVHSLR 474
Cdd:PRK11153 2 IELKNISKVFPqGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTlirCINLLER---PTSGRVLVDGQDLTALSEKELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 475 E---QIGIVSQEPVLFDG-TIYENIKMgnehathdqvveACKMANAN-DFIKRLPDGYGTRVG--EKG----VQLSGGQK 543
Cdd:PRK11153 79 KarrQIGMIFQHFNLLSSrTVFDNVAL------------PLELAGTPkAEIKARVTELLELVGlsDKAdrypAQLSGGQK 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 124244275 544 QRIAIARALVKNPKILLLDEATSALDTEAEREVQGALDQAQA--GRTTIIVAHRLSTIRNV-DRIFVFKAGNIVESGS 618
Cdd:PRK11153 147 QRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRelGLTIVLITHEMDVVKRIcDRVAVIDAGRLVEQGT 224
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1028-1266 |
1.31e-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: 141.53 E-value: 1.31e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1028 ISIRNVFFNYptrKDTKVLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGMIMIDGDNIRNLNISsLREQVC 1107
Cdd:COG4555 2 IEVENLSKKY---GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPRE-ARRQIG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1108 IVSQEPTLFD-CTIGENICY-GTNRNVTYQEIVEAAKMAnIHNFilGLPDGYDTHVGEkgtqLSGGQKQRIAIARALVRS 1185
Cdd:COG4555 78 VLPDERGLYDrLTVRENIRYfAELYGLFDEELKKRIEEL-IELL--GLEEFLDRRVGE----LSTGMKKKVALARALVHD 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1186 PSVLLLDEATSALDTESEKIVQEAL-DAAKQGRTCLVIAHRLSTIQN-SDVIAIVSEGKIVEKGThdelirKSEIYQKFC 1263
Cdd:COG4555 151 PKVLLLDEPTNGLDVMARRLLREILrALKKEGKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGS------LDELREEIG 224
|
...
gi 124244275 1264 ETQ 1266
Cdd:COG4555 225 EEN 227
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1028-1254 |
1.53e-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: 1.53e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1028 ISIRNVFFNYPTRkDTKVLQGFTLDIKAGKTVALVGHSGCGKST----IMGLLeRFYNQDKGMIMIDGDNIRNLNISSLR 1103
Cdd:COG1123 5 LEVRDLSVRYPGG-DVPAVDGVSLTIAPGETVALVGESGSGKSTlalaLMGLL-PHGGRISGEVLLDGRDLLELSEALRG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1104 EQVCIVSQEPT--LFDCTIGENICYG-TNRNVTYQEI----VEAAKMANIHNFILGLPDgydthvgekgtQLSGGQKQRI 1176
Cdd:COG1123 83 RRIGMVFQDPMtqLNPVTVGDQIAEAlENLGLSRAEArarvLELLEAVGLERRLDRYPH-----------QLSGGQRQRV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1177 AIARALVRSPSVLLLDEATSALDTESEKIVQEALDAAKQ--GRTCLVIAHRLSTI-QNSDVIAIVSEGKIVEKGTHDELI 1253
Cdd:COG1123 152 AIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRerGTTVLLITHDLGVVaEIADRVVVMDDGRIVEDGPPEEIL 231
|
.
gi 124244275 1254 R 1254
Cdd:COG1123 232 A 232
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
400-613 |
1.89e-37 |
|
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: 139.98 E-value: 1.89e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 400 SFKDVHFRYPSRkdiHVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDLREVnvhslREQIGI 479
Cdd:cd03235 1 EVEDLTVSYGGH---PVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE-----RKRIGY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 480 VSQEPVL---FDGTIYENIKMGNEH----------ATHDQVVEACKMANANDFIKRlpdgygtRVGEkgvqLSGGQKQRI 546
Cdd:cd03235 73 VPQRRSIdrdFPISVRDVVLMGLYGhkglfrrlskADKAKVDEALERVGLSELADR-------QIGE----LSGGQQQRV 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124244275 547 AIARALVKNPKILLLDEATSALDTEAEREVQGALDQ-AQAGRTTIIVAHRLSTI-RNVDRIFVFKAGNI 613
Cdd:cd03235 142 LLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRElRREGMTILVVTHDLGLVlEYFDRVLLLNRTVV 210
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
394-622 |
1.92e-37 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 142.46 E-value: 1.92e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 394 NMKGDISFKDVHFRYPSRKDiHVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDLREVNVHSL 473
Cdd:PRK13635 1 MKEEIIRVEHISFRYPDAAT-YALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 474 REQIGIVSQEP-VLFDG-TIYENIKMG--NEHATHDQVVE----ACKMANANDFIKRLPDgygtrvgekgvQLSGGQKQR 545
Cdd:PRK13635 80 RRQVGMVFQNPdNQFVGaTVQDDVAFGleNIGVPREEMVErvdqALRQVGMEDFLNREPH-----------RLSGGQKQR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124244275 546 IAIARALVKNPKILLLDEATSALDTEAEREVQGALDQ--AQAGRTTIIVAHRLSTIRNVDRIFVFKAGNIVESGSHEEL 622
Cdd:PRK13635 149 VAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQlkEQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEI 227
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1028-1254 |
2.15e-37 |
|
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: 141.09 E-value: 2.15e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1028 ISIRNVFFNYPTR-KDTKVLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGMIMIDGDNIRNLNISSLREQV 1106
Cdd:COG1124 2 LEVRNLSVSYGQGgRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1107 CIVSQEP--------TLFDcTIGE--NICYGTNRNvtyQEIVEAAKmanihnfILGLPDGYDT---HvgekgtQLSGGQK 1173
Cdd:COG1124 82 QMVFQDPyaslhprhTVDR-ILAEplRIHGLPDRE---ERIAELLE-------QVGLPPSFLDrypH------QLSGGQR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1174 QRIAIARALVRSPSVLLLDEATSALDTesekIVQ-EALDA-----AKQGRTCLVIAHRLSTIQN-SDVIAIVSEGKIVEK 1246
Cdd:COG1124 145 QRVAIARALILEPELLLLDEPTSALDV----SVQaEILNLlkdlrEERGLTYLFVSHDLAVVAHlCDRVAVMQNGRIVEE 220
|
....*...
gi 124244275 1247 GTHDELIR 1254
Cdd:COG1124 221 LTVADLLA 228
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
1010-1267 |
4.81e-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: 4.81e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1010 TPIDSLSDSGIVKpITGNISIRNVFFNYPTRKdTKVLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGMIMI 1089
Cdd:cd03288 3 ASISGSSNSGLVG-LGGEIKIHDLCVRYENNL-KPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1090 DGDNIRNLNISSLREQVCIVSQEPTLFDCTIGENIcyGTNRNVTYQEIVEAAKMANIHNFILGLPDGYDTHVGEKGTQLS 1169
Cdd:cd03288 81 DGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNL--DPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1170 GGQKQRIAIARALVRSPSVLLLDEATSALDTESEKIVQEALDAAKQGRTCLVIAHRLSTIQNSDVIAIVSEGKIVEKGTH 1249
Cdd:cd03288 159 VGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTP 238
|
250
....*....|....*....
gi 124244275 1250 DELI-RKSEIYQKFCETQR 1267
Cdd:cd03288 239 ENLLaQEDGVFASLVRTDK 257
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
402-617 |
1.23e-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: 136.41 E-value: 1.23e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 402 KDVHFRYPSRKdihVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDLREVNVHSLREQIGIVS 481
Cdd:cd03214 3 ENLSVGYGGRT---VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 482 QepvlfdgtiyenikmgnehathdqvveACKMANANDFIKRLPDgygtrvgekgvQLSGGQKQRIAIARALVKNPKILLL 561
Cdd:cd03214 80 Q---------------------------ALELLGLAHLADRPFN-----------ELSGGERQRVLLARALAQEPPILLL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 124244275 562 DEATSALDTEAEREVQGALDQ--AQAGRTTIIVAHRLS-TIRNVDRIFVFKAGNIVESG 617
Cdd:cd03214 122 DEPTSHLDIAHQIELLELLRRlaRERGKTVVMVLHDLNlAARYADRVILLKDGRIVAQG 180
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
1028-1245 |
1.66e-36 |
|
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: 137.60 E-value: 1.66e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1028 ISIRNVFFNYPTRK-DTKVLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGMIMIDGDNIRNLNisslrEQV 1106
Cdd:cd03293 1 LEVRNVSKTYGGGGgAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPG-----PDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1107 CIVSQEPTLFD-CTIGENICYG-TNRNVTYQEIVEAAKMAnihnfiLGLpdgydthVGEKGT------QLSGGQKQRIAI 1178
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNVALGlELQGVPKAEARERAEEL------LEL-------VGLSGFenayphQLSGGMRQRVAL 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124244275 1179 ARALVRSPSVLLLDEATSALDTESEKIVQEALDA--AKQGRTCLVIAHRLS-TIQNSDVIAIVSE--GKIVE 1245
Cdd:cd03293 143 ARALAVDPDVLLLDEPFSALDALTREQLQEELLDiwRETGKTVLLVTHDIDeAVFLADRVVVLSArpGRIVA 214
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1029-1242 |
2.59e-36 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 134.68 E-value: 2.59e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1029 SIRNVFFNYPTRKdtkVLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGMIMIDGDNIRNLNISSLREQVCI 1108
Cdd:cd00267 1 EIENLSFRYGGRT---ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1109 VSQeptlfdctigenicygtnrnvtyqeiveaakmanihnfilglpdgydthvgekgtqLSGGQKQRIAIARALVRSPSV 1188
Cdd:cd00267 78 VPQ--------------------------------------------------------LSGGQRQRVALARALLLNPDL 101
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 124244275 1189 LLLDEATSALDTESEKIVQEAL-DAAKQGRTCLVIAHRLSTIQN-SDVIAIVSEGK 1242
Cdd:cd00267 102 LLLDEPTSGLDPASRERLLELLrELAEEGRTVIIVTHDPELAELaADRVIVLKDGK 157
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
1028-1254 |
2.80e-36 |
|
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: 137.63 E-value: 2.80e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1028 ISIRNVFFNYPTRKdtkVLQGFTLDIKAGKTVALVGHSGCGKSTIM----GLLErfynQDKGMIMIDGDNIRNLNISSLR 1103
Cdd:cd03261 1 IELRGLTKSFGGRT---VLKGVDLDVRRGEILAIIGPSGSGKSTLLrlivGLLR----PDSGEVLIDGEDISGLSEAELY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1104 E---QVCIVSQEPTLFDC-TIGENICYG--TNRNVTYQEIVEAAKMAnIHnfILGLPDGYDTHVGEkgtqLSGGQKQRIA 1177
Cdd:cd03261 74 RlrrRMGMLFQSGALFDSlTVFENVAFPlrEHTRLSEEEIREIVLEK-LE--AVGLRGAEDLYPAE----LSGGMKKRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1178 IARALVRSPSVLLLDEATSALD-TESEKIVQEALDAAKQ-GRTCLVIAHRLSTI-QNSDVIAIVSEGKIVEKGTHDELIR 1254
Cdd:cd03261 147 LARALALDPELLLYDEPTAGLDpIASGVIDDLIRSLKKElGLTSIMVTHDLDTAfAIADRIAVLYDGKIVAEGTPEELRA 226
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1028-1260 |
3.02e-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: 3.02e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1028 ISIRNVFFNYPTRKdtkVLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGMIMIDGDNIRNLNISSLREQVC 1107
Cdd:COG1120 2 LEAENLSVGYGGRP---VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1108 IVSQEPTL-FDCTIGENICYG------TNRNVTYQ--EIVEAA-KMANIHNFIlglpdgyDTHVgekgTQLSGGQKQRIA 1177
Cdd:COG1120 79 YVPQEPPApFGLTVRELVALGryphlgLFGRPSAEdrEAVEEAlERTGLEHLA-------DRPV----DELSGGERQRVL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1178 IARALVRSPSVLLLDEATSALD----TESEKIVQEAldAAKQGRTCLVIAHRLS-TIQNSDVIAIVSEGKIVEKGTHDEL 1252
Cdd:COG1120 148 IARALAQEPPLLLLDEPTSHLDlahqLEVLELLRRL--ARERGRTVVMVLHDLNlAARYADRLVLLKDGRIVAQGPPEEV 225
|
250
....*....|.
gi 124244275 1253 IRK---SEIYQ 1260
Cdd:COG1120 226 LTPellEEVYG 236
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1028-1261 |
3.39e-36 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 138.59 E-value: 3.39e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1028 ISIRNVFFNYPTRKdTKVLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGMIMIDGDNIRNLNISSLREQVC 1107
Cdd:PRK13632 8 IKVENVSFSYPNSE-NNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1108 IVSQEP--TLFDCTIGENICYG-TNRNVTYQE----IVEAAKMANIHNFIlglpdgydthvgEKGTQ-LSGGQKQRIAIA 1179
Cdd:PRK13632 87 IIFQNPdnQFIGATVEDDIAFGlENKKVPPKKmkdiIDDLAKKVGMEDYL------------DKEPQnLSGGQKQRVAIA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1180 RALVRSPSVLLLDEATSALDTESEK-IVQEALDAAKQGRTCLV-IAHRLSTIQNSDVIAIVSEGKIVEKGTHDELIRKSE 1257
Cdd:PRK13632 155 SVLALNPEIIIFDESTSMLDPKGKReIKKIMVDLRKTRKKTLIsITHDMDEAILADKVIVFSEGKLIAQGKPKEILNNKE 234
|
....
gi 124244275 1258 IYQK 1261
Cdd:PRK13632 235 ILEK 238
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1028-1245 |
3.79e-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: 3.79e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1028 ISIRNVFFNYPTRK-DTKVLQGFTLDIKAGKTVALVGHSGCGKST----IMGLLErfynQDKGMIMIDGDNIRnlnisSL 1102
Cdd:COG1116 8 LELRGVSKRFPTGGgGVTALDDVSLTVAAGEFVALVGPSGCGKSTllrlIAGLEK----PTSGEVLVDGKPVT-----GP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1103 REQVCIVSQEPTLFD-CTIGENICYG-TNRNVTYQEIVEAAkMANIHnfILGLpDGYDTHvgeKGTQLSGGQKQRIAIAR 1180
Cdd:COG1116 79 GPDRGVVFQEPALLPwLTVLDNVALGlELRGVPKAERRERA-RELLE--LVGL-AGFEDA---YPHQLSGGMRQRVAIAR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1181 ALVRSPSVLLLDEATSALD--------TESEKIVQEaldaakQGRTCLVIAH------RLstiqnSDVIAIVSE--GKIV 1244
Cdd:COG1116 152 ALANDPEVLLMDEPFGALDaltrerlqDELLRLWQE------TGKTVLFVTHdvdeavFL-----ADRVVVLSArpGRIV 220
|
.
gi 124244275 1245 E 1245
Cdd:COG1116 221 E 221
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1028-1257 |
4.30e-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: 136.94 E-value: 4.30e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1028 ISIRNVFFNYP-TRKDTKVLQGFTLDIKAGKTVALVGHSGCGKST---IMGLLERfynQDKGMIMIDGDNIRNLNISSLR 1103
Cdd:cd03258 2 IELKNVSKVFGdTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTlirCINGLER---PTSGSVLVDGTDLTLLSGKELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1104 E---QVCIVSQEPTLFDC-TIGENICY-----GTNRNVTYQEIVEAAKmanihnfILGLPDGYDTHVGekgtQLSGGQKQ 1174
Cdd:cd03258 79 KarrRIGMIFQHFNLLSSrTVFENVALpleiaGVPKAEIEERVLELLE-------LVGLEDKADAYPA----QLSGGQKQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1175 RIAIARALVRSPSVLLLDEATSALDTES-EKIVQEALDAAKQ-GRTCLVIAHRLSTIQN-SDVIAIVSEGKIVEKGTHDE 1251
Cdd:cd03258 148 RVGIARALANNPKVLLCDEATSALDPETtQSILALLRDINRElGLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEE 227
|
....*.
gi 124244275 1252 LIRKSE 1257
Cdd:cd03258 228 VFANPQ 233
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
399-624 |
5.10e-36 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 136.81 E-value: 5.10e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 399 ISFKDVHFRYPsrkdiHVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDLREVNVHslREQIG 478
Cdd:COG3840 2 LRLDDLTYRYG-----DFPLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPA--ERPVS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 479 IVSQEPVLFDG-TIYENIKMG-------NEhATHDQVVEACKMANANDFIKRLPDgygtrvgekgvQLSGGQKQRIAIAR 550
Cdd:COG3840 75 MLFQENNLFPHlTVAQNIGLGlrpglklTA-EQRAQVEQALERVGLAGLLDRLPG-----------QLSGGQRQRVALAR 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 124244275 551 ALVKNPKILLLDEATSALDTEAEREVQGALDQ--AQAGRTTIIVAHRLSTIRNV-DRIFVFKAGNIVESGSHEELMS 624
Cdd:COG3840 143 CLVRKRPILLLDEPFSALDPALRQEMLDLVDElcRERGLTVLMVTHDPEDAARIaDRVLLVADGRIAADGPTAALLD 219
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
399-624 |
5.33e-36 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 137.15 E-value: 5.33e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 399 ISFKDVHFRYpsrKDIHVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDLR--EVNVHSLREQ 476
Cdd:PRK09493 2 IEFKNVSKHF---GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpKVDERLIRQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 477 IGIVSQEPVLFDG-TIYENIKMGNEHathdqvVEACKMANANDFIKRLPD--GYGTRVGEKGVQLSGGQKQRIAIARALV 553
Cdd:PRK09493 79 AGMVFQQFYLFPHlTALENVMFGPLR------VRGASKEEAEKQARELLAkvGLAERAHHYPSELSGGQQQRVAIARALA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 124244275 554 KNPKILLLDEATSALDTEAEREVQGAL-DQAQAGRTTIIVAHRLSTIRNV-DRIFVFKAGNIVESGSHEELMS 624
Cdd:PRK09493 153 VKPKLMLFDEPTSALDPELRHEVLKVMqDLAEEGMTMVIVTHEIGFAEKVaSRLIFIDKGRIAEDGDPQVLIK 225
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
395-625 |
1.00e-35 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 137.56 E-value: 1.00e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 395 MKGDISFKDVHFRYPSRKDIHVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDLREVNVHSLR 474
Cdd:PRK13650 1 MSNIIEVKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 475 EQIGIVSQEP-VLFDG-TIYENIKMG--NEHATHDQ----VVEACKMANANDFIKRLPdgygtrvgekgVQLSGGQKQRI 546
Cdd:PRK13650 81 HKIGMVFQNPdNQFVGaTVEDDVAFGleNKGIPHEEmkerVNEALELVGMQDFKEREP-----------ARLSGGQKQRV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 547 AIARALVKNPKILLLDEATSALDTEAERE----VQGALDQAQAgrTTIIVAHRLSTIRNVDRIFVFKAGNIVESGSHEEL 622
Cdd:PRK13650 150 AIAGAVAMRPKIIILDEATSMLDPEGRLEliktIKGIRDDYQM--TVISITHDLDEVALSDRVLVMKNGQVESTSTPREL 227
|
...
gi 124244275 623 MSK 625
Cdd:PRK13650 228 FSR 230
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
1028-1243 |
1.12e-35 |
|
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: 135.31 E-value: 1.12e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1028 ISIRNVFFNYPTRKD-TKVLQGFTLDIKAGKTVALVGHSGCGKST---IMGLLERfynQDKGMIMIDGDNIRNLNISSL- 1102
Cdd:cd03255 1 IELKNLSKTYGGGGEkVQALKGVSLSIEKGEFVAIVGPSGSGKSTllnILGGLDR---PTSGEVRVDGTDISKLSEKELa 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1103 ---REQVCIVSQE----PTLfdcTIGENICYGtnrnVTYQEIVEAAKMANIHNFI--LGLPDGYDTHVGekgtQLSGGQK 1173
Cdd:cd03255 78 afrRRHIGFVFQSfnllPDL---TALENVELP----LLLAGVPKKERRERAEELLerVGLGDRLNHYPS----ELSGGQQ 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124244275 1174 QRIAIARALVRSPSVLLLDEATSALDTESEKIVQEALD--AAKQGRTCLVIAHRLSTIQNSDVIAIVSEGKI 1243
Cdd:cd03255 147 QRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRelNKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
399-623 |
1.15e-35 |
|
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: 136.37 E-value: 1.15e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 399 ISFKDVHFRYPSRKdihVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKG---RVLidGVDLREVNVHSLRE 475
Cdd:COG1119 4 LELRNVTVRRGGKT---ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGndvRLF--GERRGGEDVWELRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 476 QIGIVS---------QEPVL------FDGTI--YENIkmgnEHATHDQVVEACKMANANDFIKRLpdgYGTrvgekgvqL 538
Cdd:COG1119 79 RIGLVSpalqlrfprDETVLdvvlsgFFDSIglYREP----TDEQRERARELLELLGLAHLADRP---FGT--------L 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 539 SGGQKQRIAIARALVKNPKILLLDEATSALDTEAEREVQGALDQ-AQAGRTTII-VAHRLSTI-RNVDRIFVFKAGNIVE 615
Cdd:COG1119 144 SQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKlAAEGAPTLVlVTHHVEEIpPGITHVLLLKDGRVVA 223
|
....*...
gi 124244275 616 SGSHEELM 623
Cdd:COG1119 224 AGPKEEVL 231
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1028-1257 |
1.43e-35 |
|
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: 135.88 E-value: 1.43e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1028 ISIRNVFFNYptrKDTKVLQGFTLDIKAGKTVALVGHSGCGKST----IMGLLErfynQDKGMIMIDGDNIRNLNIS--- 1100
Cdd:COG1127 6 IEVRNLTKSF---GDRVVLDGVSLDVPRGEILAIIGGSGSGKSVllklIIGLLR----PDSGEILVDGQDITGLSEKely 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1101 SLREQVCIVSQEPTLFDC-TIGENICYG--TNRNVTYQEIVEAAKMAnihnfiLGLpdgydthVGEKGT------QLSGG 1171
Cdd:COG1127 79 ELRRRIGMLFQGGALFDSlTVFENVAFPlrEHTDLSEAEIRELVLEK------LEL-------VGLPGAadkmpsELSGG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1172 QKQRIAIARALVRSPSVLLLDEATSALD--TeSEKIV------QEALDAakqgrTCLVIAHRLSTIQN-SDVIAIVSEGK 1242
Cdd:COG1127 146 MRKRVALARALALDPEILLYDEPTAGLDpiT-SAVIDelirelRDELGL-----TSVVVTHDLDSAFAiADRVAVLADGK 219
|
250
....*....|....*
gi 124244275 1243 IVEKGTHDElIRKSE 1257
Cdd:COG1127 220 IIAEGTPEE-LLASD 233
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
1028-1252 |
2.09e-35 |
|
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: 135.06 E-value: 2.09e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1028 ISIRNVFFNYptrKDTKVLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGMIMIDGDNIRNLNISslREQVC 1107
Cdd:cd03300 1 IELENVSKFY---GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPH--KRPVN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1108 IVSQEPTLF-DCTIGENICYG-----TNRNVTYQEIVEAAKMANIHNFILGLPDgydthvgekgtQLSGGQKQRIAIARA 1181
Cdd:cd03300 76 TVFQNYALFpHLTVFENIAFGlrlkkLPKAEIKERVAEALDLVQLEGYANRKPS-----------QLSGGQQQRVAIARA 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124244275 1182 LVRSPSVLLLDEATSALDTESEKIVQEALDAAKQ--GRTCLVIAHRLS-TIQNSDVIAIVSEGKIVEKGTHDEL 1252
Cdd:cd03300 145 LVNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKelGITFVFVTHDQEeALTMSDRIAVMNKGKIQQIGTPEEI 218
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
1028-1258 |
3.05e-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: 135.64 E-value: 3.05e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1028 ISIRNVFFNYPtRKDTKVLQGFTLDIKAGKTVALVGHSGCGKST----IMGLLErfynQDKGMIMIDGDNIRNL-NISSL 1102
Cdd:TIGR04520 1 IEVENVSFSYP-ESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTlaklLNGLLL----PTSGKVTVDGLDTLDEeNLWEI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1103 REQVCIVSQEPtlfD-----CTIGENICYG-TNRNVTYQEIV----EAAKMANIHNFILglpdgYDTHvgekgtQLSGGQ 1172
Cdd:TIGR04520 76 RKKVGMVFQNP---DnqfvgATVEDDVAFGlENLGVPREEMRkrvdEALKLVGMEDFRD-----REPH------LLSGGQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1173 KQRIAIARALVRSPSVLLLDEATSALDTESEKIVQEALDA--AKQGRTCLVIAHRLSTIQNSDVIAIVSEGKIVEKGTHD 1250
Cdd:TIGR04520 142 KQRVAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKlnKEEGITVISITHDMEEAVLADRVIVMNKGKIVAEGTPR 221
|
....*...
gi 124244275 1251 ELIRKSEI 1258
Cdd:TIGR04520 222 EIFSQVEL 229
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
416-625 |
3.77e-35 |
|
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: 134.39 E-value: 3.77e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 416 VLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDLreVNVHSLREQIGIVSQEPVLFDG-TIYEN 494
Cdd:cd03299 14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDI--TNLPPEKRDISYVPQNYALFPHmTVYKN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 495 IKMGNEHATHD------QVVEACKMANANDFIKRLPDgygtrvgekgvQLSGGQKQRIAIARALVKNPKILLLDEATSAL 568
Cdd:cd03299 92 IAYGLKKRKVDkkeierKVLEIAEMLGIDHLLNRKPE-----------TLSGGEQQRVAIARALVVNPKILLLDEPFSAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 569 DTEAEREVQGALDQAQ--AGRTTIIVAHRLSTIRNV-DRIFVFKAGNIVESGSHEELMSK 625
Cdd:cd03299 161 DVRTKEKLREELKKIRkeFGVTVLHVTHDFEEAWALaDKVAIMLNGKLIQVGKPEEVFKK 220
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
1028-1243 |
4.12e-35 |
|
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: 132.14 E-value: 4.12e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1028 ISIRNVFFNYptrKDTKVLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGMIMIDGDNIRNlNISSLREQVC 1107
Cdd:cd03230 1 IEVRNLSKRY---GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1108 IVSQEPTLFDctigenicygtnrNVTYQEIVEaakmanihnfilglpdgydthvgekgtqLSGGQKQRIAIARALVRSPS 1187
Cdd:cd03230 77 YLPEEPSLYE-------------NLTVRENLK----------------------------LSGGMKQRLALAQALLHDPE 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 124244275 1188 VLLLDEATSALDTESEKIVQEALDA-AKQGRTCLVIAHRLSTIQN-SDVIAIVSEGKI 1243
Cdd:cd03230 116 LLILDEPTSGLDPESRREFWELLRElKKEGKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
402-624 |
5.99e-35 |
|
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: 133.33 E-value: 5.99e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 402 KDVHFRYpsrKDIHVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDLREVNVHS-LREQIGIV 480
Cdd:cd03224 4 ENLNAGY---GKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHErARAGIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 481 SQEPVLFDG-TIYENIKMGnEHATHDQVVEAcKMANANDFIKRLPDgygtRVGEKGVQLSGGQKQRIAIARALVKNPKIL 559
Cdd:cd03224 81 PEGRRIFPElTVEENLLLG-AYARRRAKRKA-RLERVYELFPRLKE----RRKQLAGTLSGGEQQMLAIARALMSRPKLL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 124244275 560 LLDEATSALDTEAEREVQGALDQ-AQAGRTTIIVAHRLSTIRNV-DRIFVFKAGNIVESGSHEELMS 624
Cdd:cd03224 155 LLDEPSEGLAPKIVEEIFEAIRElRDEGVTILLVEQNARFALEIaDRAYVLERGRVVLEGTAAELLA 221
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
399-622 |
6.57e-35 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 140.54 E-value: 6.57e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 399 ISFKDVHFRYPSrkdIHVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDLREVNVH-SLREQI 477
Cdd:COG1129 5 LEMRGISKSFGG---VKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRdAQAAGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 478 GIVSQEPVLFDG-TIYENIKMGNEHATHDQVVEAcKM-ANANDFIKRL-----PDgygTRVGEkgvqLSGGQKQRIAIAR 550
Cdd:COG1129 82 AIIHQELNLVPNlSVAENIFLGREPRRGGLIDWR-AMrRRARELLARLgldidPD---TPVGD----LSVAQQQLVEIAR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 124244275 551 ALVKNPKILLLDEATSALDteaEREVQGALDQ----AQAGRTTIIVAHRLSTIRNV-DRIFVFKAGNIVESGSHEEL 622
Cdd:COG1129 154 ALSRDARVLILDEPTASLT---EREVERLFRIirrlKAQGVAIIYISHRLDEVFEIaDRVTVLRDGRLVGTGPVAEL 227
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
399-621 |
7.86e-35 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 137.77 E-value: 7.86e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 399 ISFKDVHFRYPSRKdihVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDLreVNVHSLREQIG 478
Cdd:PRK09452 15 VELRGISKSFDGKE---VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDI--THVPAENRHVN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 479 IVSQEPVLFDG-TIYENIKMG------NEHATHDQVVEACKMANANDFIKRLPDgygtrvgekgvQLSGGQKQRIAIARA 551
Cdd:PRK09452 90 TVFQSYALFPHmTVFENVAFGlrmqktPAAEITPRVMEALRMVQLEEFAQRKPH-----------QLSGGQQQRVAIARA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 124244275 552 LVKNPKILLLDEATSALDTEAEREVQGALD--QAQAGRTTIIVAH------RLStirnvDRIFVFKAGNIVESGSHEE 621
Cdd:PRK09452 159 VVNKPKVLLLDESLSALDYKLRKQMQNELKalQRKLGITFVFVTHdqeealTMS-----DRIVVMRDGRIEQDGTPRE 231
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
399-601 |
9.04e-35 |
|
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: 132.53 E-value: 9.04e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 399 ISFKDVHFRYPSrkDIHVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVD---LREVNVHSLRE 475
Cdd:cd03292 1 IEFINVTKTYPN--GTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDvsdLRGRAIPYLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 476 QIGIVSQE-PVLFDGTIYENIKMGNEhathdqvveaCKMANANDFIKRLPD-----GYGTRVGEKGVQLSGGQKQRIAIA 549
Cdd:cd03292 79 KIGVVFQDfRLLPDRNVYENVAFALE----------VTGVPPREIRKRVPAalelvGLSHKHRALPAELSGGEQQRVAIA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 124244275 550 RALVKNPKILLLDEATSALDTEAEREVQGALDQAQAGRTTIIVA-----------HRLSTIRN 601
Cdd:cd03292 149 RAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVAthakelvdttrHRVIALER 211
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1028-1254 |
9.98e-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: 135.95 E-value: 9.98e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1028 ISIRNVFFNYPTRKDT-KVLQGFTLDIKAGKTVALVGHSGCGKST----IMGLLERfYNQDKGMIMIDGDNIRNLNISSL 1102
Cdd:COG0444 2 LEVRNLKVYFPTRRGVvKAVDGVSFDVRRGETLGLVGESGSGKSTlaraILGLLPP-PGITSGEILFDGEDLLKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1103 RE----QVCIVSQEPT-----LFdcTIGENIC------YGTNRNVTYQEIVEAAKManihnfiLGLPDGYDT-----Hvg 1162
Cdd:COG0444 81 RKirgrEIQMIFQDPMtslnpVM--TVGDQIAeplrihGGLSKAEARERAIELLER-------VGLPDPERRldrypH-- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1163 ekgtQLSGGQKQRIAIARALVRSPSVLLLDEATSALDTesekIVQ-EALD-----AAKQGRTCLVIAHRLSTI-QNSDVI 1235
Cdd:COG0444 150 ----ELSGGMRQRVMIARALALEPKLLIADEPTTALDV----TIQaQILNllkdlQRELGLAILFITHDLGVVaEIADRV 221
|
250
....*....|....*....
gi 124244275 1236 AIVSEGKIVEKGTHDELIR 1254
Cdd:COG0444 222 AVMYAGRIVEEGPVEELFE 240
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
399-622 |
1.69e-34 |
|
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: 132.46 E-value: 1.69e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 399 ISFKDVHFRYPsrkDIHVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDLREVNVHslREQIG 478
Cdd:cd03296 3 IEVRNVSKRFG---DFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQ--ERNVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 479 IVSQEPVLFDG-TIYENIKMG----------NEHATHDQVVEACKMANANDFIKRLPDgygtrvgekgvQLSGGQKQRIA 547
Cdd:cd03296 78 FVFQHYALFRHmTVFDNVAFGlrvkprserpPEAEIRAKVHELLKLVQLDWLADRYPA-----------QLSGGQRQRVA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 124244275 548 IARALVKNPKILLLDEATSALDTEAEREVQGALDQA--QAGRTTIIVAHRLSTIRNV-DRIFVFKAGNIVESGSHEEL 622
Cdd:cd03296 147 LARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLhdELHVTTVFVTHDQEEALEVaDRVVVMNKGRIEQVGTPDEV 224
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1028-1252 |
2.81e-34 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 132.47 E-value: 2.81e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1028 ISIRNVFFNYptrKDTKVLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYnqD-------KGMIMIDGDNI--RNLN 1098
Cdd:COG1117 12 IEVRNLNVYY---GDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMN--DlipgarvEGEILLDGEDIydPDVD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1099 ISSLREQVCIVSQEPTLFDCTIGENICYG------TNRNVTyQEIVEAA-KMAnihnfilGLPDgydtHV----GEKGTQ 1167
Cdd:COG1117 87 VVELRRRVGMVFQKPNPFPKSIYDNVAYGlrlhgiKSKSEL-DEIVEESlRKA-------ALWD----EVkdrlKKSALG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1168 LSGGQKQRIAIARALVRSPSVLLLDEATSALDTESEKIVQEALDAAKQGRTCLVIAH------RLstiqnSDVIAIVSEG 1241
Cdd:COG1117 155 LSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYTIVIVTHnmqqaaRV-----SDYTAFFYLG 229
|
250
....*....|.
gi 124244275 1242 KIVEKGTHDEL 1252
Cdd:COG1117 230 ELVEFGPTEQI 240
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1028-1262 |
5.09e-34 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 134.43 E-value: 5.09e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1028 ISIRNVFFNYPTRK-DTKVLQGFTLDIKAGKTVALVGHSGCGKST---IMGLLERFynqDKGMIMIDGDNIRNLNISSLR 1103
Cdd:COG1135 2 IELENLSKTFPTKGgPVTALDDVSLTIEKGEIFGIIGYSGAGKSTlirCINLLERP---TSGSVLVDGVDLTALSERELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1104 E---QVCIVSQEPTLFD-CTIGENICY-----GTNRnvtyQEIveAAKMANIHNFIlGLPDgydthvgeKG----TQLSG 1170
Cdd:COG1135 79 AarrKIGMIFQHFNLLSsRTVAENVALpleiaGVPK----AEI--RKRVAELLELV-GLSD--------KAdaypSQLSG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1171 GQKQRIAIARALVRSPSVLLLDEATSALD---TES-----EKIVQEaldaakQGRTCLVIAHRLSTIQN-SDVIAIVSEG 1241
Cdd:COG1135 144 GQKQRVGIARALANNPKVLLCDEATSALDpetTRSildllKDINRE------LGLTIVLITHEMDVVRRiCDRVAVLENG 217
|
250 260
....*....|....*....|...
gi 124244275 1242 KIVEKGTHDELIR--KSEIYQKF 1262
Cdd:COG1135 218 RIVEQGPVLDVFAnpQSELTRRF 240
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
1028-1242 |
7.33e-34 |
|
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: 128.46 E-value: 7.33e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1028 ISIRNVFFNYptrKDTKVLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGMIMIDGDNIRNLNISS--LREQ 1105
Cdd:cd03229 1 LELKNVSKRY---GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELppLRRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1106 VCIVSQEPTLF-DCTIGENICYGtnrnvtyqeiveaakmanihnfilglpdgydthvgekgtqLSGGQKQRIAIARALVR 1184
Cdd:cd03229 78 IGMVFQDFALFpHLTVLENIALG----------------------------------------LSGGQQQRVALARALAM 117
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 124244275 1185 SPSVLLLDEATSALDTESEKIVQEALDA--AKQGRTCLVIAHRLSTIQN-SDVIAIVSEGK 1242
Cdd:cd03229 118 DPDVLLLDEPTSALDPITRREVRALLKSlqAQLGITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
1028-1254 |
8.42e-34 |
|
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: 130.50 E-value: 8.42e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1028 ISIRNVFFNYPTRKdtKVLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGMIMIDGDNIRNLNISSLREQVC 1107
Cdd:cd03295 1 IEFENVTKRYGGGK--KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1108 IVSQEPTLF-DCTIGENICY-----GTNRNVTYQEIVEAAKManihnfiLGLPDGydTHVGEKGTQLSGGQKQRIAIARA 1181
Cdd:cd03295 79 YVIQQIGLFpHMTVEENIALvpkllKWPKEKIRERADELLAL-------VGLDPA--EFADRYPHELSGGQQQRVGVARA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 124244275 1182 LVRSPSVLLLDEATSALDTESEKIVQEALDAAKQ--GRTCLVIAHRL-STIQNSDVIAIVSEGKIVEKGTHDELIR 1254
Cdd:cd03295 150 LAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQelGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEILR 225
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
1028-1242 |
8.78e-34 |
|
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: 129.13 E-value: 8.78e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1028 ISIRNVFFNYPTRKDT--KVLQGFTLDIKAGKTVALVGHSGCGKST-IMGLL-ErfYNQDKGMIMIDGdnirnlnisslr 1103
Cdd:cd03250 1 ISVEDASFTWDSGEQEtsFTLKDINLEVPKGELVAIVGPVGSGKSSlLSALLgE--LEKLSGSVSVPG------------ 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1104 eQVCIVSQEPTLFDCTIGENICYGTNRNVT-YQEIVEAA------KManihnfilgLPDGYDTHVGEKGTQLSGGQKQRI 1176
Cdd:cd03250 67 -SIAYVSQEPWIQNGTIRENILFGKPFDEErYEKVIKACalepdlEI---------LPDGDLTEIGEKGINLSGGQKQRI 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 124244275 1177 AIARALVRSPSVLLLDEATSALDTE-SEKIVQEAL-DAAKQGRTCLVIAHRLSTIQNSDVIAIVSEGK 1242
Cdd:cd03250 137 SLARAVYSDADIYLLDDPLSAVDAHvGRHIFENCIlGLLLNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
417-621 |
2.77e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 130.55 E-value: 2.77e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 417 LKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDL--REVNVHSLREQIGIVSQEP--VLFDGTIY 492
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdKKVKLSDIRKKVGLVFQYPeyQLFEETIE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 493 ENIKMG------NEHATHDQVVEACKMA--NANDFIKRLPdgygtrvgekgVQLSGGQKQRIAIARALVKNPKILLLDEA 564
Cdd:PRK13637 103 KDIAFGpinlglSEEEIENRVKRAMNIVglDYEDYKDKSP-----------FELSGGQKRRVAIAGVVAMEPKILILDEP 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 565 TSALDTEAEREVQGALD--QAQAGRTTIIVAHRLSTI-RNVDRIFVFKAGNIVESGSHEE 621
Cdd:PRK13637 172 TAGLDPKGRDEILNKIKelHKEYNMTIILVSHSMEDVaKLADRIIVMNKGKCELQGTPRE 231
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
419-625 |
3.51e-33 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 131.39 E-value: 3.51e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 419 GISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDLREVNVHSLRE---QIGIVSQEPvlFDG-----T 490
Cdd:COG4608 36 GVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELRPlrrRMQMVFQDP--YASlnprmT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 491 IYENI-------KMGNEHATHDQVVEACKMANAN-DFIKRLPDgygtrvgekgvQLSGGQKQRIAIARALVKNPKILLLD 562
Cdd:COG4608 114 VGDIIaeplrihGLASKAERRERVAELLELVGLRpEHADRYPH-----------EFSGGQRQRIGIARALALNPKLIVCD 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 124244275 563 EATSALDTEAEREVQGALD--QAQAGRTTIIVAHRLSTIRNV-DRIFVFKAGNIVESGSHEELMSK 625
Cdd:COG4608 183 EPVSALDVSIQAQVLNLLEdlQDELGLTYLFISHDLSVVRHIsDRVAVMYLGKIVEIAPRDELYAR 248
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
363-632 |
4.24e-33 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 139.91 E-value: 4.24e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 363 GTARGAASTVLRVINSHPKIDPYSLEGilvdnmkGDISFKDVHFRYpsRKDIH-VLKGISLELKAGDKIALVGSSGCGKS 441
Cdd:PTZ00243 1280 GMAADVTGTVVIEPASPTSAAPHPVQA-------GSLVFEGVQMRY--REGLPlVLRGVSFRIAPREKVGIVGRTGSGKS 1350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 442 TIVNLLQRFYDPTKGRVLIDGVDLREVNVHSLREQIGIVSQEPVLFDGTIYENIKMGNEhATHDQVVEACKMANANDFIK 521
Cdd:PTZ00243 1351 TLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQNVDPFLE-ASSAEVWAALELVGLRERVA 1429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 522 RLPDGYGTRVGEKGVQLSGGQKQRIAIARALVK-NPKILLLDEATSALDTEAEREVQGALDQAQAGRTTIIVAHRLSTIR 600
Cdd:PTZ00243 1430 SESEGIDSRVLEGGSNYSVGQRQLMCMARALLKkGSGFILMDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVA 1509
|
250 260 270
....*....|....*....|....*....|...
gi 124244275 601 NVDRIFVFKAGNIVESGSHEEL-MSKQGIFYDM 632
Cdd:PTZ00243 1510 QYDKIIVMDHGAVAEMGSPRELvMNRQSIFHSM 1542
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
73-329 |
7.15e-33 |
|
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: 129.59 E-value: 7.15e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 73 LLAIVLGGMTTVFLRAQNSDFVVGVDNVNPEGLVPIsldefnseVVKYCIYYLVLGVLMFFTSYVQIACFESYAERLVHK 152
Cdd:cd07346 2 LLALLLLLLATALGLALPLLTKLLIDDVIPAGDLSL--------LLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 153 LRQNYLKAILRQQIQWFDKQQTGNLTARLTDDLERVREGLGDKFALLVQMFAAFLAGYGVGFFYSWSMTLVMMGFAPLIV 232
Cdd:cd07346 74 LRRDLFRHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 233 LSGAKMSKSMATRTRVEQETYAVAGAIAEETFSSIRTVHSLNGHKRELDRFYNALEVGRQTGIVKYCYMGIGVGFSNLCM 312
Cdd:cd07346 154 LILRYFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLT 233
|
250
....*....|....*..
gi 124244275 313 YSSYALAFWYGSTLIIN 329
Cdd:cd07346 234 ALGTALVLLYGGYLVLQ 250
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
399-614 |
1.01e-32 |
|
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: 124.85 E-value: 1.01e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 399 ISFKDVHFRYPSrkdIHVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGvdlREVNVHSLRE--Q 476
Cdd:cd03216 1 LELRGITKRFGG---VKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDG---KEVSFASPRDarR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 477 IGIvsqepvlfdGTIYenikmgnehathdqvveackmanandfikrlpdgygtrvgekgvQLSGGQKQRIAIARALVKNP 556
Cdd:cd03216 75 AGI---------AMVY--------------------------------------------QLSVGERQMVEIARALARNA 101
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124244275 557 KILLLDEATSAL-DTEAER--EVQGALdqAQAGRTTIIVAHRLSTIRNV-DRIFVFKAGNIV 614
Cdd:cd03216 102 RLLILDEPTAALtPAEVERlfKVIRRL--RAQGVAVIFISHRLDEVFEIaDRVTVLRDGRVV 161
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
1028-1224 |
1.58e-32 |
|
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: 126.11 E-value: 1.58e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1028 ISIRNVFFNYptrKDTKVLQGFTLDIKAGKTVALVGHSGCGKSTI---MGLLERFynqDKGMIMIDGDNIRN--LNISSL 1102
Cdd:cd03262 1 IEIKNLHKSF---GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLlrcINLLEEP---DSGTIIIDGLKLTDdkKNINEL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1103 REQVCIVSQEPTLF-DCTIGENICYG--TNRNVTYQEIVEAAKManihnfIL---GLPDGYDTHVGekgtQLSGGQKQRI 1176
Cdd:cd03262 75 RQKVGMVFQQFNLFpHLTVLENITLApiKVKGMSKAEAEERALE------LLekvGLADKADAYPA----QLSGGQQQRV 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 124244275 1177 AIARALVRSPSVLLLDEATSALDTEsekIVQEALD----AAKQGRTCLVIAH 1224
Cdd:cd03262 145 AIARALAMNPKVMLFDEPTSALDPE---LVGEVLDvmkdLAEEGMTMVVVTH 193
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1028-1254 |
5.07e-32 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 128.73 E-value: 5.07e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1028 ISIRNVFFNYPtrkDTKVLQGFTLDIKAGKTVALVGHSGCGKSTIMGL---LERfynQDKGMIMIDGDNIrNLNISSLRE 1104
Cdd:COG1118 3 IEVRNISKRFG---SFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIiagLET---PDSGRIVLNGRDL-FTNLPPRER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1105 QVCIVSQEPTLF-DCTIGENICYG-TNRNVTYQEI----------VEAAKMANihnfilglpdgydthvgEKGTQLSGGQ 1172
Cdd:COG1118 76 RVGFVFQHYALFpHMTVAENIAFGlRVRPPSKAEIrarveellelVQLEGLAD-----------------RYPSQLSGGQ 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1173 KQRIAIARALVRSPSVLLLDEATSALDT----ESEKIVQEALDaaKQGRTCLVIAH------RLstiqnSDVIAIVSEGK 1242
Cdd:COG1118 139 RQRVALARALAVEPEVLLLDEPFGALDAkvrkELRRWLRRLHD--ELGGTTVFVTHdqeealEL-----ADRVVVMNQGR 211
|
250
....*....|..
gi 124244275 1243 IVEKGTHDELIR 1254
Cdd:COG1118 212 IEQVGTPDEVYD 223
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
1028-1252 |
6.56e-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: 124.99 E-value: 6.56e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1028 ISIRNVFFNYPTrkDTKVLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGMIMIDGDNIRNLNISSLRE--- 1104
Cdd:cd03256 1 IEVENLSKTYPN--GKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQlrr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1105 QVCIVSQEPTLFD-CTIGENICYG----------TNRNVTYQEIVEAAKMANIhnfiLGLPDGYDTHVGekgtQLSGGQK 1173
Cdd:cd03256 79 QIGMIFQQFNLIErLSVLENVLSGrlgrrstwrsLFGLFPKEEKQRALAALER----VGLLDKAYQRAD----QLSGGQQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1174 QRIAIARALVRSPSVLLLDEATSALDTESEKIVQEAL--DAAKQGRTCLVIAHRLSTI-QNSDVIAIVSEGKIVEKGTHD 1250
Cdd:cd03256 151 QRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLkrINREEGITVIVSLHQVDLArEYADRIVGLKDGRIVFDGPPA 230
|
..
gi 124244275 1251 EL 1252
Cdd:cd03256 231 EL 232
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
402-614 |
6.75e-32 |
|
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: 123.91 E-value: 6.75e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 402 KDVHFRYpsRKDIHVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDLREvnvHSLREQIGIVS 481
Cdd:cd03226 3 ENISFSY--KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKA---KERRKSIGYVM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 482 QEP--VLFDGTIYENIKMGNE--HATHDQVVEACKMANANDFIKRLPdgygtrvgekgVQLSGGQKQRIAIARALVKNPK 557
Cdd:cd03226 78 QDVdyQLFTDSVREELLLGLKelDAGNEQAETVLKDLDLYALKERHP-----------LSLSGGQKQRLAIAAALLSGKD 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 124244275 558 ILLLDEATSALDTEAEREVQGALDQAQA-GRTTIIVAHRLSTIRNV-DRIFVFKAGNIV 614
Cdd:cd03226 147 LLIFDEPTSGLDYKNMERVGELIRELAAqGKAVIVITHDYEFLAKVcDRVLLLANGAIV 205
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
399-622 |
7.59e-32 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 125.27 E-value: 7.59e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 399 ISFKDVHFRYPSRKdihVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDLREVNVHS------ 472
Cdd:PRK14239 6 LQVSDLSVYYNKKK---ALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNPEVTITGSIVYNGHNIYSprtdtv 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 473 -LREQIGIVSQEPVLFDGTIYENIKMG------NEHATHDQVVE-ACKMANANDFIKrlpdgygTRVGEKGVQLSGGQKQ 544
Cdd:PRK14239 83 dLRKEIGMVFQQPNPFPMSIYENVVYGlrlkgiKDKQVLDEAVEkSLKGASIWDEVK-------DRLHDSALGLSGGQQQ 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124244275 545 RIAIARALVKNPKILLLDEATSALDTEAEREVQGALDQAQAGRTTIIVAHRLSTI-RNVDRIFVFKAGNIVESGSHEEL 622
Cdd:PRK14239 156 RVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQAsRISDRTGFFLDGDLIEYNDTKQM 234
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
1050-1255 |
1.24e-31 |
|
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: 125.45 E-value: 1.24e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1050 TLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGMIMIDGDNIRNLNISSLRE----QVCIVSQEPTLF-DCTIGENI 1124
Cdd:cd03294 44 SLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRElrrkKISMVFQSFALLpHRTVLENV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1125 CY-----GTNRNVTYQEIVEAAKMANIHNFILGLPDgydthvgekgtQLSGGQKQRIAIARALVRSPSVLLLDEATSALD 1199
Cdd:cd03294 124 AFglevqGVPRAEREERAAEALELVGLEGWEHKYPD-----------ELSGGMQQRVGLARALAVDPDILLMDEAFSALD 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 124244275 1200 TESEKIVQEALDA--AKQGRTCLVIAHRLS-TIQNSDVIAIVSEGKIVEKGTHDELIRK 1255
Cdd:cd03294 193 PLIRREMQDELLRlqAELQKTIVFITHDLDeALRLGDRIAIMKDGRLVQVGTPEEILTN 251
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
1029-1247 |
1.34e-31 |
|
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: 122.16 E-value: 1.34e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1029 SIRNVFFNYPTRKdtkVLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGMIMIDGDNIRNLNISSLREQVCI 1108
Cdd:cd03214 1 EVENLSVGYGGRT---VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1109 VSQeptlfdctigenicygtnrnvtyqeiveAAKMANIHNFIlglpdgydthvgEKG-TQLSGGQKQRIAIARALVRSPS 1187
Cdd:cd03214 78 VPQ----------------------------ALELLGLAHLA------------DRPfNELSGGERQRVLLARALAQEPP 117
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 124244275 1188 VLLLDEATSALDTESEKIVQEALD--AAKQGRTCLVIAHRLS-TIQNSDVIAIVSEGKIVEKG 1247
Cdd:cd03214 118 ILLLDEPTSHLDIAHQIELLELLRrlARERGKTVVMVLHDLNlAARYADRVILLKDGRIVAQG 180
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
399-617 |
1.64e-31 |
|
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: 123.07 E-value: 1.64e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 399 ISFKDVHFRYPSRkdiHVLKGISLELKAGdKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDLREvNVHSLREQIG 478
Cdd:cd03264 1 LQLENLTKRYGKK---RALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLRRRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 479 IVSQEPVLFDG-TIYE---------NIKMGNEHATHDQVVEAckmANANDFIKRlpdgygtRVGekgvQLSGGQKQRIAI 548
Cdd:cd03264 76 YLPQEFGVYPNfTVREfldyiawlkGIPSKEVKARVDEVLEL---VNLGDRAKK-------KIG----SLSGGMRRRVGI 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 124244275 549 ARALVKNPKILLLDEATSALDTEaERE-VQGALDQAQAGRTTIIVAHRLSTIRNV-DRIFVFKAGNIVESG 617
Cdd:cd03264 142 AQALVGDPSILIVDEPTAGLDPE-ERIrFRNLLSELGEDRIVILSTHIVEDVESLcNQVAVLNKGKLVFEG 211
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
1044-1247 |
1.70e-31 |
|
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: 123.17 E-value: 1.70e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1044 KVLQGFTLDIK---AGKTVALVGHSGCGKSTIMGLLERFYNQDKGMIMIDG----DNIRNLNISSLREQVCIVSQEPTLF 1116
Cdd:cd03297 8 KRLPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvlfDSRKKINLPPQQRKIGLVFQQYALF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1117 -DCTIGENICYGTNRNVTYQEIVEAAKMANIhnfiLGLpdgydTHVGEKGT-QLSGGQKQRIAIARALVRSPSVLLLDEA 1194
Cdd:cd03297 88 pHLNVRENLAFGLKRKRNREDRISVDELLDL----LGL-----DHLLNRYPaQLSGGEKQRVALARALAAQPELLLLDEP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 124244275 1195 TSALDTESEKIVQEALDAAKQ--GRTCLVIAHRLSTIQN-SDVIAIVSEGKIVEKG 1247
Cdd:cd03297 159 FSALDRALRLQLLPELKQIKKnlNIPVIFVTHDLSEAEYlADRIVVMEDGRLQYIG 214
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
399-615 |
1.77e-31 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 123.70 E-value: 1.77e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 399 ISFKDVHFRYPSR-KDIHVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDLrevnvHSL---- 473
Cdd:COG4181 9 IELRGLTKTVGTGaGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDL-----FALdeda 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 474 -----REQIGIVSQE----PVLfdgTIYENIKMGNEHATHDQVveackMANANDFIKRLpdGYGTRVGEKGVQLSGGQKQ 544
Cdd:COG4181 84 rarlrARHVGFVFQSfqllPTL---TALENVMLPLELAGRRDA-----RARARALLERV--GLGHRLDHYPAQLSGGEQQ 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 124244275 545 RIAIARALVKNPKILLLDEATSALDTEAEREVQGALD--QAQAGRTTIIVAHRLSTIRNVDRIFVFKAGNIVE 615
Cdd:COG4181 154 RVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFelNRERGTTLVLVTHDPALAARCDRVLRLRAGRLVE 226
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
416-624 |
1.97e-31 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 124.09 E-value: 1.97e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 416 VLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDL---REVN-----VHSLREQIGIVSQEPVLF 487
Cdd:PRK11264 18 VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIdtaRSLSqqkglIRQLRQHVGFVFQNFNLF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 488 -DGTIYENIKMGnehathDQVVEACKMANANDFIKRLPdgygTRVGEKGVQ------LSGGQKQRIAIARALVKNPKILL 560
Cdd:PRK11264 98 pHRTVLENIIEG------PVIVKGEPKEEATARARELL----AKVGLAGKEtsyprrLSGGQQQRVAIARALAMRPEVIL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 124244275 561 LDEATSALDTEAEREVQGALDQ-AQAGRTTIIVAHRLSTIRNV-DRIFVFKAGNIVESGSHEELMS 624
Cdd:PRK11264 168 FDEPTSALDPELVGEVLNTIRQlAQEKRTMVIVTHEMSFARDVaDRAIFMDQGRIVEQGPAKALFA 233
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
395-626 |
2.47e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 124.46 E-value: 2.47e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 395 MKGDISFKDVHFRYpsRKDIHVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDLREVNVHSLR 474
Cdd:PRK13647 1 MDNIIEVEDLHFRY--KDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 475 EQIGIVSQEP--VLFDGTIYENIKMG--NEHATHDQVV----EACKMANANDFIKRLPdgygtrvgekgVQLSGGQKQRI 546
Cdd:PRK13647 79 SKVGLVFQDPddQVFSSTVWDDVAFGpvNMGLDKDEVErrveEALKAVRMWDFRDKPP-----------YHLSYGQKKRV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 547 AIARALVKNPKILLLDEATSALDTEAEREVQGALDQ-AQAGRTTIIVAHRLS-TIRNVDRIFVFKAGNIVESGSHEELMS 624
Cdd:PRK13647 148 AIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRlHNQGKTVIVATHDVDlAAEWADQVIVLKEGRVLAEGDKSLLTD 227
|
..
gi 124244275 625 KQ 626
Cdd:PRK13647 228 ED 229
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
414-624 |
4.29e-31 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 122.55 E-value: 4.29e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 414 IHVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDLREVNVHsLREQIGIVS--QEPVLFDG-T 490
Cdd:cd03219 13 LVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPH-EIARLGIGRtfQIPRLFPElT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 491 IYENIKMGNEHATHDQVVEACKMAN-------ANDFIKRLpdGYGTRVGEKGVQLSGGQKQRIAIARALVKNPKILLLDE 563
Cdd:cd03219 92 VLENVMVAAQARTGSGLLLARARREerearerAEELLERV--GLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDE 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124244275 564 ATSALdTEAEREVQGAL--DQAQAGRTTIIVAHRLSTIRNV-DRIFVFKAGNIVESGSHEELMS 624
Cdd:cd03219 170 PAAGL-NPEETEELAELirELRERGITVLLVEHDMDVVMSLaDRVTVLDQGRVIAEGTPDEVRN 232
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1028-1245 |
6.34e-31 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 121.70 E-value: 6.34e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1028 ISIRNVFFNYPtrKDTKVLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGMIMIDGDNIRNLN---ISSLRE 1104
Cdd:COG2884 2 IRFENVSKRYP--GGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKrreIPYLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1105 QVCIVSQE-PTLFDCTIGENICY-----GTNRNVTYQEIVEAAKManihnfiLGLPDGYDTHVGEkgtqLSGGQKQRIAI 1178
Cdd:COG2884 80 RIGVVFQDfRLLPDRTVYENVALplrvtGKSRKEIRRRVREVLDL-------VGLSDKAKALPHE----LSGGEQQRVAI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1179 ARALVRSPSVLLLDEATSALDTE-SEKIVQEALDAAKQGRTCLVIAHRLSTIQNSD--VIAIvSEGKIVE 1245
Cdd:COG2884 149 ARALVNRPELLLADEPTGNLDPEtSWEIMELLEEINRRGTTVLIATHDLELVDRMPkrVLEL-EDGRLVR 217
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
399-605 |
8.39e-31 |
|
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: 120.66 E-value: 8.39e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 399 ISFKDVHFRYPSRKdihVLKGISLELKAGDKIALVGSSGCGKST----IVNLLQrfydPTKGRVLIDGVDLREVNVHsLR 474
Cdd:COG4133 3 LEAENLSCRRGERL---LFSGLSFTLAAGEALALTGPNGSGKTTllriLAGLLP----PSAGEVLWNGEPIRDARED-YR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 475 EQIGIVSQEPVLFDG-TIYENI----KMGNEHATHDQVVEACKMANandfikrLPDGYGTRVGekgvQLSGGQKQRIAIA 549
Cdd:COG4133 75 RRLAYLGHADGLKPElTVRENLrfwaALYGLRADREAIDEALEAVG-------LAGLADLPVR----QLSAGQKRRVALA 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 124244275 550 RALVKNPKILLLDEATSALDTEAEREVQGALDQ-AQAGRTTIIVAHRLSTIRNVDRI 605
Cdd:COG4133 144 RLLLSPAPLWLLDEPFTALDAAGVALLAELIAAhLARGGAVLLTTHQPLELAAARVL 200
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1022-1260 |
8.56e-31 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 125.83 E-value: 8.56e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1022 KPItgnISIRNVFFNYptrKDTKVLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGMIMIDGDNIRNLniSS 1101
Cdd:PRK09452 12 SPL---VELRGISKSF---DGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHV--PA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1102 LREQVCIVSQEPTLF-DCTIGENICYGTN-RNVTYQEI----VEAAKMANIHNFIlglpdgydthvGEKGTQLSGGQKQR 1175
Cdd:PRK09452 84 ENRHVNTVFQSYALFpHMTVFENVAFGLRmQKTPAAEItprvMEALRMVQLEEFA-----------QRKPHQLSGGQQQR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1176 IAIARALVRSPSVLLLDEATSALDTESEKIVQEALDA--AKQGRTCLVIAH-RLSTIQNSDVIAIVSEGKIVEKGThdel 1252
Cdd:PRK09452 153 VAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKAlqRKLGITFVFVTHdQEEALTMSDRIVVMRDGRIEQDGT---- 228
|
....*...
gi 124244275 1253 irKSEIYQ 1260
Cdd:PRK09452 229 --PREIYE 234
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
416-1226 |
9.46e-31 |
|
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: 132.34 E-value: 9.46e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 416 VLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLidgvdlrevnvHSLReqIGIVSQEPVLFDGTIYENI 495
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIK-----------HSGR--ISFSPQTSWIMPGTIKDNI 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 496 KMGnehATHDQ-----VVEACKManaNDFIKRLPDGYGTRVGEKGVQLSGGQKQRIAIARALVKNPKILLLDEATSALDT 570
Cdd:TIGR01271 508 IFG---LSYDEyrytsVIKACQL---EEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDV 581
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 571 EAEREV-QGALDQAQAGRTTIIVAHRLSTIRNVDRIFVFKAGNIVESGSHEELMSKQGIF---------YD--------- 631
Cdd:TIGR01271 582 VTEKEIfESCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAKRPDFsslllgleaFDnfsaerrns 661
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 632 -MTQAQVVRQQQQEA--------------------------------------------------GKDIEDTISESAHSH 660
Cdd:TIGR01271 662 iLTETLRRVSIDGDStvfsgpetikqsfkqpppefaekrkqsiilnpiasarkfsfvqmgpqkaqATTIEDAVREPSERK 741
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 661 LS------------------------------------------------RKSSTRSAISIAT----------------- 675
Cdd:TIGR01271 742 FSlvpedeqgeeslprgnqyhhglqhqaqrrqsvlqlmthsnrgenrreqLQTSFRKKSSITQqnelaseldiysrrlsk 821
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 676 -SIHQLAEEV-----EECKA------PPTSMFKIF------KFNGDKVGWFIGGIFGAFIFGSVTPVFALVYAEIFNVY- 736
Cdd:TIGR01271 822 dSVYEISEEIneedlKECFAderenvFETTTWNTYlryittNRNLVFVLIFCLVIFLAEVAASLLGLWLITDNPSAPNYv 901
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 737 ------------SLPADQMQANVYFWCGMFVLMGITFF-VGFFTSANcLGRCGESLTMKLRFEAFKNLLRQDIAFYDDLR 803
Cdd:TIGR01271 902 dqqhanasspdvQKPVIITPTSAYYIFYIYVGTADSVLaLGFFRGLP-LVHTLLTVSKRLHEQMLHSVLQAPMAVLNTMK 980
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 804 hgTGKLCTRFATDAPNVR-----YVFTRLPVVLASIVTICGALGIGFYygwqlalILVVMVPLLV----MGGYFemqMRF 874
Cdd:TIGR01271 981 --AGRILNRFTKDMAIIDdmlplTLFDFIQLTLIVLGAIFVVSVLQPY-------IFIAAIPVAVifimLRAYF---LRT 1048
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 875 GKQIRdtQLLEEA-GKVASQAVEHIR---TVHSLNRQEQFHFTYCEYLrepfNTNLKHAHTYGAV---FAFSQSLIFFMY 947
Cdd:TIGR01271 1049 SQQLK--QLESEArSPIFSHLITSLKglwTIRAFGRQSYFETLFHKAL----NLHTANWFLYLSTlrwFQMRIDIIFVFF 1122
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 948 AAAFYLGSIFVNQQAMQPIDVYrVFFAISFCGQMIGNTTSFIpDVVKARLAASLLFYLIEHPTPI---------DSLSDS 1018
Cdd:TIGR01271 1123 FIAVTFIAIGTNQDGEGEVGII-LTLAMNILSTLQWAVNSSI-DVDGLMRSVSRVFKFIDLPQEEprpsggggkYQLSTV 1200
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1019 GIVK--------PITGNISIRNVFFNYpTRKDTKVLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDkGMIMID 1090
Cdd:TIGR01271 1201 LVIEnphaqkcwPSGGQMDVQGLTAKY-TEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQID 1278
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1091 GDNIRNLNISSLREQVCIVSQEPTLFDCTIGENIcyGTNRNVTYQEIVEAAKMANIHNFILGLPDGYDTHVGEKGTQLSG 1170
Cdd:TIGR01271 1279 GVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNL--DPYEQWSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSN 1356
|
970 980 990 1000 1010
....*....|....*....|....*....|....*....|....*....|....*.
gi 124244275 1171 GQKQRIAIARALVRSPSVLLLDEATSALDTESEKIVQEALDAAKQGRTCLVIAHRL 1226
Cdd:TIGR01271 1357 GHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRV 1412
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
399-617 |
9.64e-31 |
|
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: 120.82 E-value: 9.64e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 399 ISFKDVHFRYPSRKdihVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDLRevNVHSLREQIG 478
Cdd:cd03301 1 VELENVTKRFGNVT---ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVT--DLPPKDRDIA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 479 IVSQEPVLF-DGTIYENIKMG------NEHATHDQVVEACKMANANDFIKRLPDgygtrvgekgvQLSGGQKQRIAIARA 551
Cdd:cd03301 76 MVFQNYALYpHMTVYDNIAFGlklrkvPKDEIDERVREVAELLQIEHLLDRKPK-----------QLSGGQRQRVALGRA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124244275 552 LVKNPKILLLDEATSALDTEAEREVQGALD--QAQAGRTTIIVAH-RLSTIRNVDRIFVFKAGNIVESG 617
Cdd:cd03301 145 IVREPKVFLMDEPLSNLDAKLRVQMRAELKrlQQRLGTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
1045-1262 |
1.20e-30 |
|
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: 121.29 E-value: 1.20e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1045 VLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGMIMIDGDNIRNLNisSLREQVCIVSQEPTLF-DCTIGEN 1123
Cdd:cd03299 14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLP--PEKRDISYVPQNYALFpHMTVYKN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1124 ICYGTnRNVTY------QEIVEAAKMANIhnfilglpdgydTHV-GEKGTQLSGGQKQRIAIARALVRSPSVLLLDEATS 1196
Cdd:cd03299 92 IAYGL-KKRKVdkkeieRKVLEIAEMLGI------------DHLlNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFS 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 124244275 1197 ALDTES-EKIVQEALDAAKQ-GRTCLVIAHRLSTIQN-SDVIAIVSEGKIVEKGTHDELIRK--SEIYQKF 1262
Cdd:cd03299 159 ALDVRTkEKLREELKKIRKEfGVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEVFKKpkNEFVAEF 229
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1028-1252 |
1.76e-30 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 124.42 E-value: 1.76e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1028 ISIRNVFFNYptrKDTKVLQGFTLDIKAGKTVALVGHSGCGKST----IMGLLErfynQDKGMIMIDGDNIRNL-----N 1098
Cdd:COG3839 4 LELENVSKSY---GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTllrmIAGLED----PTSGEILIGGRDVTDLppkdrN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1099 ISslreqvcIVSQEPTLFD-CTIGENICYG-TNRNVTYQEI----VEAAKManihnfiLGLpdgydTHVGE-KGTQLSGG 1171
Cdd:COG3839 77 IA-------MVFQSYALYPhMTVYENIAFPlKLRKVPKAEIdrrvREAAEL-------LGL-----EDLLDrKPKQLSGG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1172 QKQRIAIARALVRSPSVLLLDEATSALDtesekivqealdaAK---QGRTCLVIAHR---LSTI-----QN-----SDVI 1235
Cdd:COG3839 138 QRQRVALGRALVREPKVFLLDEPLSNLD-------------AKlrvEMRAEIKRLHRrlgTTTIyvthdQVeamtlADRI 204
|
250
....*....|....*..
gi 124244275 1236 AIVSEGKIVEKGTHDEL 1252
Cdd:COG3839 205 AVMNDGRIQQVGTPEEL 221
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
399-622 |
1.81e-30 |
|
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: 120.30 E-value: 1.81e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 399 ISFKDVHFRYPSRKDiHVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDLREvNVHSLREQIG 478
Cdd:cd03263 1 LQIRNLTKTYKKGTK-PAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 479 IVSQEPVLFDG-TIYENIKM-----GNEHATHDQVVEA-CKMANANDFIKRlpdgygtRVGekgvQLSGGQKQRIAIARA 551
Cdd:cd03263 79 YCPQFDALFDElTVREHLRFyarlkGLPKSEIKEEVELlLRVLGLTDKANK-------RAR----TLSGGMKRKLSLAIA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124244275 552 LVKNPKILLLDEATSALDTEAEREVQGALDQAQAGRTTIIVAHRLSTIRNV-DRIFVFKAGNIVESGSHEEL 622
Cdd:cd03263 148 LIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEALcDRIAIMSDGKLRCIGSPQEL 219
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1028-1257 |
1.89e-30 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 122.05 E-value: 1.89e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1028 ISIRNVFFNYPTRKDtKVLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGMIMIDGDNIRNLNISSLREQVC 1107
Cdd:PRK13635 6 IRVEHISFRYPDAAT-YALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1108 IVSQEP--TLFDCTIGENICYG-TNRNVTYQEIVE----AAKMANIHNFILGLPdgydthvgekgTQLSGGQKQRIAIAR 1180
Cdd:PRK13635 85 MVFQNPdnQFVGATVQDDVAFGlENIGVPREEMVErvdqALRQVGMEDFLNREP-----------HRLSGGQKQRVAIAG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1181 ALVRSPSVLLLDEATSALDTESEkivQEALDA-----AKQGRTCLVIAHRLSTIQNSDVIAIVSEGKIVEKGTHDELIRK 1255
Cdd:PRK13635 154 VLALQPDIIILDEATSMLDPRGR---REVLETvrqlkEQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFKS 230
|
..
gi 124244275 1256 SE 1257
Cdd:PRK13635 231 GH 232
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
1028-1252 |
3.98e-30 |
|
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: 119.15 E-value: 3.98e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1028 ISIRNVFFNYPTrKDTKVLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGMIMIDGDNIRNlNISSLREQVC 1107
Cdd:cd03263 1 LQIRNLTKTYKK-GTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1108 IVSQEPTLFD-CTIGENICY-----GTNRNvtyQEIVEAAKMANIhnfiLGLPDGYDTHVGekgtQLSGGQKQRIAIARA 1181
Cdd:cd03263 79 YCPQFDALFDeLTVREHLRFyarlkGLPKS---EIKEEVELLLRV----LGLTDKANKRAR----TLSGGMKRKLSLAIA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124244275 1182 LVRSPSVLLLDEATSALDTESEKIVQEALDAAKQGRTCLVIAHRLSTIQN-SDVIAIVSEGKIVEKGTHDEL 1252
Cdd:cd03263 148 LIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEAlCDRIAIMSDGKLRCIGSPQEL 219
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
402-624 |
4.06e-30 |
|
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: 126.72 E-value: 4.06e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 402 KDVHFRYPSRK--------DIHVLKGISLELKAGDKIALVGSSGCGKST----IVNLLqrfydPTKGRVLIDGVDLREVN 469
Cdd:COG4172 279 RDLKVWFPIKRglfrrtvgHVKAVDGVSLTLRRGETLGLVGESGSGKSTlglaLLRLI-----PSEGEIRFDGQDLDGLS 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 470 VH---SLREQIGIVSQEP-------------------VLFDGtiyenikmGNEHATHDQVVEAckMANAN---DFIKRLP 524
Cdd:COG4172 354 RRalrPLRRRMQVVFQDPfgslsprmtvgqiiaeglrVHGPG--------LSAAERRARVAEA--LEEVGldpAARHRYP 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 525 DgygtrvgekgvQLSGGQKQRIAIARALVKNPKILLLDEATSALDteaeREVQGA-LD-----QAQAGRTTIIVAHRLST 598
Cdd:COG4172 424 H-----------EFSGGQRQRIAIARALILEPKLLVLDEPTSALD----VSVQAQiLDllrdlQREHGLAYLFISHDLAV 488
|
250 260
....*....|....*....|....*..
gi 124244275 599 IRNV-DRIFVFKAGNIVESGSHEELMS 624
Cdd:COG4172 489 VRALaHRVMVMKDGKVVEQGPTEQVFD 515
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1049-1254 |
4.75e-30 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 119.47 E-value: 4.75e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1049 FTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGMIMIDGDNIRNLNISslREQVCIVSQEPTLFD-CTIGENICYG 1127
Cdd:COG3840 18 FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPA--ERPVSMLFQENNLFPhLTVAQNIGLG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1128 TNRNVTY-----QEIVEAAKMANIHNFILGLPDgydthvgekgtQLSGGQKQRIAIARALVRSPSVLLLDEATSALD--- 1199
Cdd:COG3840 96 LRPGLKLtaeqrAQVEQALERVGLAGLLDRLPG-----------QLSGGQRQRVALARCLVRKRPILLLDEPFSALDpal 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 124244275 1200 -TESEKIVQEAldAAKQGRTCLVIAHRLSTIQN-SDVIAIVSEGKIVEKGTHDELIR 1254
Cdd:COG3840 165 rQEMLDLVDEL--CRERGLTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAALLD 219
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1009-1252 |
4.97e-30 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 122.15 E-value: 4.97e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1009 PTPIdsLSDSGIVK--PITGNISIRnvffnypTRKDTKVLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGM 1086
Cdd:COG4608 4 AEPL--LEVRDLKKhfPVRGGLFGR-------TVGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1087 IMIDGDNIRNLNISSLRE---QVCIVSQEP--------TLFDcTIGENIcyGTNRNVTYQEIVEAAK--MANIhnfilGL 1153
Cdd:COG4608 75 ILFDGQDITGLSGRELRPlrrRMQMVFQDPyaslnprmTVGD-IIAEPL--RIHGLASKAERRERVAelLELV-----GL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1154 -PDGYD--THvgekgtQLSGGQKQRIAIARALVRSPSVLLLDEATSALDTESEKIV-------QEALdaakqGRTCLVIA 1223
Cdd:COG4608 147 rPEHADryPH------EFSGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVlnlledlQDEL-----GLTYLFIS 215
|
250 260 270
....*....|....*....|....*....|
gi 124244275 1224 HRLSTIQN-SDVIAIVSEGKIVEKGTHDEL 1252
Cdd:COG4608 216 HDLSVVRHiSDRVAVMYLGKIVEIAPRDEL 245
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
115-330 |
1.24e-29 |
|
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: 119.96 E-value: 1.24e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 115 SEVVKYCIYYLVLGVL-MFFTSyVQIACFeSYAE-RLVHKLRQNYLKAILRQQIQWFDKQQTGNLTARLTDDLERVREGL 192
Cdd:cd18572 33 EAFYRAVLLLLLLSVLsGLFSG-LRGGCF-SYAGtRLVRRLRRDLFRSLLRQDIAFFDATKTGELTSRLTSDCQKVSDPL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 193 GDKFALLVQMFAAFLAGYGVGFFYSWSMTLV-MMGFAPLIVLSG--AKMSKSMATRTrveQETYAVAGAIAEETFSSIRT 269
Cdd:cd18572 111 STNLNVFLRNLVQLVGGLAFMFSLSWRLTLLaFITVPVIALITKvyGRYYRKLSKEI---QDALAEANQVAEEALSNIRT 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 124244275 270 VHSLNGHKRELDRFYNALEVGRQTGIVKYCYMGIGVGFSNLCMYSSYALAFWYGSTLIIND 330
Cdd:cd18572 188 VRSFATEEREARRYERALDKALKLSVRQALAYAGYVAVNTLLQNGTQVLVLFYGGHLVLSG 248
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
402-624 |
1.31e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 119.80 E-value: 1.31e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 402 KDVHFRYPsrKDIHVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDLREVNvHSL---REQIG 478
Cdd:PRK13639 5 RDLKYSYP--DGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDK-KSLlevRKTVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 479 IVSQEP--VLFDGTIYENIKMG------NEHATHDQVVEACKMANANDFIKRLPDgygtrvgekgvQLSGGQKQRIAIAR 550
Cdd:PRK13639 82 IVFQNPddQLFAPTVEEDVAFGplnlglSKEEVEKRVKEALKAVGMEGFENKPPH-----------HLSGGQKKRVAIAG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 124244275 551 ALVKNPKILLLDEATSALDTEAEREVQGAL-DQAQAGRTTIIVAHRLSTI-RNVDRIFVFKAGNIVESGSHEELMS 624
Cdd:PRK13639 151 ILAMKPEIIVLDEPTSGLDPMGASQIMKLLyDLNKEGITIIISTHDVDLVpVYADKVYVMSDGKIIKEGTPKEVFS 226
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
1021-1272 |
1.92e-29 |
|
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: 127.75 E-value: 1.92e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1021 VKPITGN-ISIRNVFFNYpTRKDTKVLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGMIMIDGdnirnlni 1099
Cdd:TIGR00957 629 IKPGEGNsITVHNATFTW-ARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG-------- 699
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1100 sslreQVCIVSQEPTLFDCTIGENICYGTNRNVT-YQEIVEA-AKMANIHNfilgLPDGYDTHVGEKGTQLSGGQKQRIA 1177
Cdd:TIGR00957 700 -----SVAYVPQQAWIQNDSLRENILFGKALNEKyYQQVLEAcALLPDLEI----LPSGDRTEIGEKGVNLSGGQKQRVS 770
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1178 IARALVRSPSVLLLDEATSALDTESEKIVQEALDAAK---QGRTCLVIAHRLSTIQNSDVIAIVSEGKIVEKGTHDELIR 1254
Cdd:TIGR00957 771 LARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVIGPEgvlKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQ 850
|
250
....*....|....*...
gi 124244275 1255 KSEIYQKFCETQRIVESQ 1272
Cdd:TIGR00957 851 RDGAFAEFLRTYAPDEQQ 868
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1045-1255 |
2.56e-29 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 120.98 E-value: 2.56e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1045 VLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGMIMIDGDNIRNLNISslREQVCIVSQEPTLF-DCTIGEN 1123
Cdd:PRK11432 21 VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQ--QRDICMVFQSYALFpHMSLGEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1124 ICYGTN-RNVTYQEIVEAAKMAnihnfiLGLPD--GY-DTHVgekgTQLSGGQKQRIAIARALVRSPSVLLLDEATSALD 1199
Cdd:PRK11432 99 VGYGLKmLGVPKEERKQRVKEA------LELVDlaGFeDRYV----DQISGGQQQRVALARALILKPKVLLFDEPLSNLD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 124244275 1200 TESEKIVQEALDAAKQ--GRTCLVIAHRLS-TIQNSDVIAIVSEGKIVEKGTHDELIRK 1255
Cdd:PRK11432 169 ANLRRSMREKIRELQQqfNITSLYVTHDQSeAFAVSDTVIVMNKGKIMQIGSPQELYRQ 227
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
122-372 |
3.25e-29 |
|
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: 119.16 E-value: 3.25e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 122 IYYLVLGVLMF--FTSYVQIACFESYAERLVHKLRQNYLKAILRQQIQWFDKQQTGNLTARLTDDLERVREGLGDKFALL 199
Cdd:cd18573 43 FALALLGVFVVgaAANFGRVYLLRIAGERIVARLRKRLFKSILRQDAAFFDKNKTGELVSRLSSDTSVVGKSLTQNLSDG 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 200 VQMFAAFLAGYGVGFFYSWSMTLVMMGFAPLIVLSGAKMSKSMATRTRVEQETYAVAGAIAEETFSSIRTVHSLNGHKRE 279
Cdd:cd18573 123 LRSLVSGVGGIGMMLYISPKLTLVMLLVVPPIAVGAVFYGRYVRKLSKQVQDALADATKVAEERLSNIRTVRAFAAERKE 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 280 LDRFY----NALEVGRQTGIVKYCYMGiGVGFS-NLCMYSsyalAFWYGSTLIINdptfdrGLIfTV-----F--FAVLS 347
Cdd:cd18573 203 VERYAkkvdEVFDLAKKEALASGLFFG-STGFSgNLSLLS----VLYYGGSLVAS------GEL-TVgdltsFlmYAVYV 270
|
250 260
....*....|....*....|....*....
gi 124244275 348 GStSLGGalphLASFGT----ARGAASTV 372
Cdd:cd18573 271 GS-SVSG----LSSFYSelmkGLGASSRL 294
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
399-626 |
3.70e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 118.41 E-value: 3.70e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 399 ISFKDVHFRYPSrkDIHVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDG--VDLREVNVHSLREQ 476
Cdd:PRK13636 6 LKVEELNYNYSD--GTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkpIDYSRKGLMKLRES 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 477 IGIVSQEP--VLFDGTIYENIKMG--NEHATHDQVVEACKMANANDFIKRLPDgygtrvgEKGVQLSGGQKQRIAIARAL 552
Cdd:PRK13636 84 VGMVFQDPdnQLFSASVYQDVSFGavNLKLPEDEVRKRVDNALKRTGIEHLKD-------KPTHCLSFGQKKRVAIAGVL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 124244275 553 VKNPKILLLDEATSALDTEAEREVQGALDQAQA--GRTTIIVAHRLSTIR-NVDRIFVFKAGNIVESGSHEELMSKQ 626
Cdd:PRK13636 157 VMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKelGLTIIIATHDIDIVPlYCDNVFVMKEGRVILQGNPKEVFAEK 233
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
399-629 |
4.51e-29 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 117.83 E-value: 4.51e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 399 ISFKDVHFRYPSRKdihVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYD-----PTKGRVLIDGVDL--REVNVH 471
Cdd:PRK14258 8 IKVNNLSFYYDTQK---ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNElesevRVEGRVEFFNQNIyeRRVNLN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 472 SLREQIGIVSQEPVLFDGTIYENIKMG------NEHATHDQVVE-ACKMANANDFIKRlpdgygtRVGEKGVQLSGGQKQ 544
Cdd:PRK14258 85 RLRRQVSMVHPKPNLFPMSVYDNVAYGvkivgwRPKLEIDDIVEsALKDADLWDEIKH-------KIHKSALDLSGGQQQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 545 RIAIARALVKNPKILLLDEATSALDTEAEREVQGALDQA--QAGRTTIIVAHRLSTIRNVDRIFVFKAGNIVESGSHEEL 622
Cdd:PRK14258 158 RLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLrlRSELTMVIVSHNLHQVSRLSDFTAFFKGNENRIGQLVEF 237
|
....*..
gi 124244275 623 MSKQGIF 629
Cdd:PRK14258 238 GLTKKIF 244
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1028-1260 |
4.55e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 118.30 E-value: 4.55e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1028 ISIRNVFFNYPTRKDTKVLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGMIMIDGDNIRNLNISSLREQVC 1107
Cdd:PRK13650 5 IEVKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1108 IVSQEP--TLFDCTIGENICYG-TNRNVTYQEIVEAAKMAnihnfiLGLPDGYDTHVGEKgTQLSGGQKQRIAIARALVR 1184
Cdd:PRK13650 85 MVFQNPdnQFVGATVEDDVAFGlENKGIPHEEMKERVNEA------LELVGMQDFKEREP-ARLSGGQKQRVAIAGAVAM 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1185 SPSVLLLDEATSALDTESE----KIVQEALDaaKQGRTCLVIAHRLSTIQNSDVIAIVSEGKIVEKGTHDELI-RKSEIY 1259
Cdd:PRK13650 158 RPKIIILDEATSMLDPEGRleliKTIKGIRD--DYQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFsRGNDLL 235
|
.
gi 124244275 1260 Q 1260
Cdd:PRK13650 236 Q 236
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
395-621 |
5.46e-29 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 124.45 E-value: 5.46e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 395 MKGDISFKDVHFRYPS-RKDIHVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDLREVNVHSL 473
Cdd:PRK10535 1 MTALLELKDIRRSYPSgEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 474 ----REQIGIVSQEPVLFdgtiyenikmgnEHATHDQVVE----------ACKMANANDFIKRLpdGYGTRVGEKGVQLS 539
Cdd:PRK10535 81 aqlrREHFGFIFQRYHLL------------SHLTAAQNVEvpavyaglerKQRLLRAQELLQRL--GLEDRVEYQPSQLS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 540 GGQKQRIAIARALVKNPKILLLDEATSALDTEAEREVQGALDQAQA-GRTTIIVAHRLSTIRNVDRIFVFKAGNIV-ESG 617
Cdd:PRK10535 147 GGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDrGHTVIIVTHDPQVAAQAERVIEIRDGEIVrNPP 226
|
....
gi 124244275 618 SHEE 621
Cdd:PRK10535 227 AQEK 230
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
421-617 |
5.60e-29 |
|
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: 115.67 E-value: 5.60e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 421 SLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDLREVNVHslREQIGIVSQEPVLFDG-TIYENIKMGN 499
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA--DRPVSMLFQENNLFAHlTVEQNVGLGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 500 EHATHDQVVEACKMANA------NDFIKRLPDgygtrvgekgvQLSGGQKQRIAIARALVKNPKILLLDEATSALDTEAE 573
Cdd:cd03298 96 SPGLKLTAEDRQAIEVAlarvglAGLEKRLPG-----------ELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALR 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 124244275 574 REVQGALDQ--AQAGRTTIIVAHRLSTIRNVDRIFVFKA-GNIVESG 617
Cdd:cd03298 165 AEMLDLVLDlhAETKMTVLMVTHQPEDAKRLAQRVVFLDnGRIAAQG 211
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
395-624 |
6.17e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 117.89 E-value: 6.17e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 395 MKGDISFKDVHFRYPSRKDIHVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDLREVNVHSLR 474
Cdd:PRK13642 1 MNKILEVENLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 475 EQIGIVSQEP--VLFDGTIYENIKMGNEHA------THDQVVEACKMANANDFIKRLPdgygtrvgekgVQLSGGQKQRI 546
Cdd:PRK13642 81 RKIGMVFQNPdnQFVGATVEDDVAFGMENQgipreeMIKRVDEALLAVNMLDFKTREP-----------ARLSGGQKQRV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 547 AIARALVKNPKILLLDEATSALDTEAEREVQGALDQAQAGR--TTIIVAHRLSTIRNVDRIFVFKAGNIVESGSHEELMS 624
Cdd:PRK13642 150 AVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYqlTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFA 229
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
417-649 |
6.75e-29 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 120.91 E-value: 6.75e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 417 LKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDLREVNVHSLRE----QIGIVSQEPVLFDG-TI 491
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREvrrkKIAMVFQSFALMPHmTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 492 YENIKMGNEHA------THDQVVEACKMANANDFIKRLPDgygtrvgekgvQLSGGQKQRIAIARALVKNPKILLLDEAT 565
Cdd:PRK10070 124 LDNTAFGMELAginaeeRREKALDALRQVGLENYAHSYPD-----------ELSGGMRQRVGLARALAINPDILLMDEAF 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 566 SALDTEAEREVQGALDQAQAG--RTTIIVAHRL-STIRNVDRIFVFKAGNIVESGSHEELMSKQGIFYDMTQAQVVRQQQ 642
Cdd:PRK10070 193 SALDPLIRTEMQDELVKLQAKhqRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFRGVDISQ 272
|
....*..
gi 124244275 643 QEAGKDI 649
Cdd:PRK10070 273 VFSAKDI 279
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
403-617 |
7.90e-29 |
|
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: 115.47 E-value: 7.90e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 403 DVHFRYPSrkdiHVLKgISLELKaGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDLRE----VNVHSLREQIG 478
Cdd:cd03297 5 DIEKRLPD----FTLK-IDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDsrkkINLPPQQRKIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 479 IVSQEPVLFDG-TIYENIKMGNEHATH----DQVVEACKMANANDFIKRLPDgygtrvgekgvQLSGGQKQRIAIARALV 553
Cdd:cd03297 79 LVFQQYALFPHlNVRENLAFGLKRKRNredrISVDELLDLLGLDHLLNRYPA-----------QLSGGEKQRVALARALA 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 124244275 554 KNPKILLLDEATSALDTEAEREVQGALDQAQA--GRTTIIVAHRLSTI-RNVDRIFVFKAGNIVESG 617
Cdd:cd03297 148 AQPELLLLDEPFSALDRALRLQLLPELKQIKKnlNIPVIFVTHDLSEAeYLADRIVVMEDGRLQYIG 214
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
1028-1260 |
9.11e-29 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 116.31 E-value: 9.11e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1028 ISIRNVFFNYPTrkDTKVLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGMIMIDGDNIRNLNISSLRE--- 1104
Cdd:COG3638 3 LELRNLSKRYPG--GTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRlrr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1105 QVCIVSQEPTLFD-CTIGENICYG------TNRNVT---YQEIVEAAkMANIHnfILGLPDgydtHVGEKGTQLSGGQKQ 1174
Cdd:COG3638 81 RIGMIFQQFNLVPrLSVLTNVLAGrlgrtsTWRSLLglfPPEDRERA-LEALE--RVGLAD----KAYQRADQLSGGQQQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1175 RIAIARALVRSPSVLLLDEATSALDTESEKIVQEAL--DAAKQGRTCLVIAHRLSTIQN-SDVIAIVSEGKIVEKGTHDE 1251
Cdd:COG3638 154 RVAIARALVQEPKLILADEPVASLDPKTARQVMDLLrrIAREDGITVVVNLHQVDLARRyADRIIGLRDGRVVFDGPPAE 233
|
250
....*....|.
gi 124244275 1252 LIRK--SEIYQ 1260
Cdd:COG3638 234 LTDAvlREIYG 244
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
402-624 |
9.22e-29 |
|
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: 115.85 E-value: 9.22e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 402 KDVHFRYPsrkDIHVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDLREVNVHSL-REQIGIV 480
Cdd:COG0410 7 ENLHAGYG---GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIaRLGIGYV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 481 SQEPVLFDG-TIYENIKMGnEHATHDQVVEACKMANANDFIKRLpdgyGTRVGEKGVQLSGGQKQRIAIARALVKNPKIL 559
Cdd:COG0410 84 PEGRRIFPSlTVEENLLLG-AYARRDRAEVRADLERVYELFPRL----KERRRQRAGTLSGGEQQMLAIGRALMSRPKLL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 560 LLDEATSALdteAE---REVQGALDQ-AQAGRTTIIVAHRLSTIRNV-DRIFVFKAGNIVESGSHEELMS 624
Cdd:COG0410 159 LLDEPSLGL---APlivEEIFEIIRRlNREGVTILLVEQNARFALEIaDRAYVLERGRIVLEGTAAELLA 225
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
399-625 |
1.09e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 117.21 E-value: 1.09e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 399 ISFKDVHFRYPSRKDiHVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDP---TKGRVLIDGVDLREVNVHSLRE 475
Cdd:PRK13640 6 VEFKHVSFTYPDSKK-PALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDGITLTAKTVWDIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 476 QIGIVSQEP--VLFDGTIYENIKMGNEH---------ATHDQVVEACKMAnanDFIKRLPDgygtrvgekgvQLSGGQKQ 544
Cdd:PRK13640 85 KVGIVFQNPdnQFVGATVGDDVAFGLENravprpemiKIVRDVLADVGML---DYIDSEPA-----------NLSGGQKQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 545 RIAIARALVKNPKILLLDEATSALDTEAEREVQGALDQAQA--GRTTIIVAHRLSTIRNVDRIFVFKAGNIVESGSHEEL 622
Cdd:PRK13640 151 RVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKknNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEI 230
|
...
gi 124244275 623 MSK 625
Cdd:PRK13640 231 FSK 233
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
399-624 |
1.16e-28 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 115.45 E-value: 1.16e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 399 ISFKDVHFRY---PSRKDIHVlkgislelKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDlrevnvHSL-- 473
Cdd:PRK10771 2 LKLTDITWLYhhlPMRFDLTV--------ERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQD------HTTtp 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 474 --REQIGIVSQEPVLFDG-TIYENIKMGNE------HATHDQVVEACKMANANDFIKRLPDgygtrvgekgvQLSGGQKQ 544
Cdd:PRK10771 68 psRRPVSMLFQENNLFSHlTVAQNIGLGLNpglklnAAQREKLHAIARQMGIEDLLARLPG-----------QLSGGQRQ 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 545 RIAIARALVKNPKILLLDEATSALDTEAEREVQGALDQAQAGR--TTIIVAHRLS-TIRNVDRIFVFKAGNIVESGSHEE 621
Cdd:PRK10771 137 RVALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQVCQERqlTLLMVSHSLEdAARIAPRSLVVADGRIAWDGPTDE 216
|
...
gi 124244275 622 LMS 624
Cdd:PRK10771 217 LLS 219
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1028-1261 |
1.59e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 116.69 E-value: 1.59e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1028 ISIRNVFFNY--PTRKDTKVLQGFTLDIKAGKTVALVGHSGCGKSTIM----GLLErfynQDKGMIMIDGDNI--RNLNI 1099
Cdd:PRK13637 3 IKIENLTHIYmeGTPFEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIqhlnGLLK----PTSGKIIIDGVDItdKKVKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1100 SSLREQVCIVSQEP--TLFDCTIGENICYG-TNRNVTYQEIVEAAKMANIhnfILGLPdgYDTHVGEKGTQLSGGQKQRI 1176
Cdd:PRK13637 79 SDIRKKVGLVFQYPeyQLFEETIEKDIAFGpINLGLSEEEIENRVKRAMN---IVGLD--YEDYKDKSPFELSGGQKRRV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1177 AIARALVRSPSVLLLDEATSALDTES-EKIVQEALDAAKQ-GRTCLVIAHRLSTIQN-SDVIAIVSEGKIVEKGTHDELI 1253
Cdd:PRK13637 154 AIAGVVAMEPKILILDEPTAGLDPKGrDEILNKIKELHKEyNMTIILVSHSMEDVAKlADRIIVMNKGKCELQGTPREVF 233
|
....*...
gi 124244275 1254 RKSEIYQK 1261
Cdd:PRK13637 234 KEVETLES 241
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
109-330 |
1.72e-28 |
|
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: 116.97 E-value: 1.72e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 109 SLDEFNSEVVKYCIYYLVLGVLMFFTSYvqiaCFESYAERLVHKLRQNYLKAILRQQIQWFDKQQTGNLTARLTDDLERV 188
Cdd:cd18780 37 ALRALNQAVLILLGVVLIGSIATFLRSW----LFTLAGERVVARLRKRLFSAIIAQEIAFFDVTRTGELLNRLSSDTQVL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 189 REGLGDKFALLVQMFAAFLAGYGVGFFYSWSMTLVMMGFAPLIVLSGAKMSKSMATRTRVEQETYAVAGAIAEETFSSIR 268
Cdd:cd18780 113 QNAVTVNLSMLLRYLVQIIGGLVFMFTTSWKLTLVMLSVVPPLSIGAVIYGKYVRKLSKKFQDALAAASTVAEESISNIR 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 124244275 269 TVHSLNGHKRELDRF----YNALEVGRQTGIVkycyMGIGVGFSNLCMYSSYALAFWYGSTLIIND 330
Cdd:cd18780 193 TVRSFAKETKEVSRYsekiNESYLLGKKLARA----SGGFNGFMGAAAQLAIVLVLWYGGRLVIDG 254
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1043-1255 |
1.84e-28 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 121.28 E-value: 1.84e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1043 TKVLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGMIMIDGDNIRNLNIS-SLREQVCIVSQEPTLF-DCTI 1120
Cdd:COG1129 17 VKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRdAQAAGIAIIHQELNLVpNLSV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1121 GENICYGT--------NRNVTYQEIVEAAKManihnfiLGLPDGYDTHVGEkgtqLSGGQKQRIAIARALVRSPSVLLLD 1192
Cdd:COG1129 97 AENIFLGReprrggliDWRAMRRRARELLAR-------LGLDIDPDTPVGD----LSVAQQQLVEIARALSRDARVLILD 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 124244275 1193 EATSAL-DTESE---KIVQEaLdaAKQGRTCLVIAHRLSTIQN-SDVIAIVSEGKIVEKG-----THDELIRK 1255
Cdd:COG1129 166 EPTASLtEREVErlfRIIRR-L--KAQGVAIIYISHRLDEVFEiADRVTVLRDGRLVGTGpvaelTEDELVRL 235
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
399-624 |
2.46e-28 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 115.45 E-value: 2.46e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 399 ISFKDVHFRYPSRKdihVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDLREV---------- 468
Cdd:PRK10619 6 LNVIDLHKRYGEHE---VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVrdkdgqlkva 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 469 ---NVHSLREQIGIVSQEPVLFDG-TIYENIKmgnehATHDQVVEACKMANANDFIKRLPD-GYGTRV-GEKGVQLSGGQ 542
Cdd:PRK10619 83 dknQLRLLRTRLTMVFQHFNLWSHmTVLENVM-----EAPIQVLGLSKQEARERAVKYLAKvGIDERAqGKYPVHLSGGQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 543 KQRIAIARALVKNPKILLLDEATSALDTEAEREVQGALDQ-AQAGRTTIIVAHRLSTIRNVDRIFVF-KAGNIVESGSHE 620
Cdd:PRK10619 158 QQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQlAEEGKTMVVVTHEMGFARHVSSHVIFlHQGKIEEEGAPE 237
|
....
gi 124244275 621 ELMS 624
Cdd:PRK10619 238 QLFG 241
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
414-622 |
2.70e-28 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 118.40 E-value: 2.70e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 414 IHVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDLREVNVHslREQIGIVSQEPVLFDG-TIY 492
Cdd:PRK11607 32 QHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPY--QRPINMMFQSYALFPHmTVE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 493 ENIKMGNEH------ATHDQVVEACKMANANDFIKRLPDgygtrvgekgvQLSGGQKQRIAIARALVKNPKILLLDEATS 566
Cdd:PRK11607 110 QNIAFGLKQdklpkaEIASRVNEMLGLVHMQEFAKRKPH-----------QLSGGQRQRVALARSLAKRPKLLLLDEPMG 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 124244275 567 ALDTE----AEREVQGALDqaQAGRTTIIVAH-RLSTIRNVDRIFVFKAGNIVESGSHEEL 622
Cdd:PRK11607 179 ALDKKlrdrMQLEVVDILE--RVGVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
398-617 |
4.02e-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: 112.64 E-value: 4.02e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 398 DISFKDVHFRYPSRKDIhvLKGISLELKAGDKIALVGSSGCGKSTIVNLL--QRFYDPTKGRVLIDGVDLREvnvHSLRE 475
Cdd:cd03213 8 NLTVTVKSSPSKSGKQL--LKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGRPLDK---RSFRK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 476 QIGIVSQEPVLFDG-TIYENIkmgnehathdqvveackmananDFIKRLpdgygtrvgeKGvqLSGGQKQRIAIARALVK 554
Cdd:cd03213 83 IIGYVPQDDILHPTlTVRETL----------------------MFAAKL----------RG--LSGGERKRVSIALELVS 128
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 124244275 555 NPKILLLDEATSALDTEAEREVQGALDQ-AQAGRTTIIVAHRLST--IRNVDRIFVFKAGNIVESG 617
Cdd:cd03213 129 NPSLLFLDEPTSGLDSSSALQVMSLLRRlADTGRTIICSIHQPSSeiFELFDKLLLLSQGRVIYFG 194
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1023-1261 |
4.04e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 116.49 E-value: 4.04e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1023 PITGNISIR----NVFFNYPTRKDTKVLQGFTLDIKAGKTVALVGHSGCGKSTIM----GLL---------ERFYNQDK- 1084
Cdd:PRK13631 15 PLSDDIILRvknlYCVFDEKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVthfnGLIkskygtiqvGDIYIGDKk 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1085 -GMIMIDGDNIRNL-NISSLREQVCIVSQEP--TLFDCTIGENICYGTnrnVTY-QEIVEAAKMANIHNFILGLPDGYdt 1159
Cdd:PRK13631 95 nNHELITNPYSKKIkNFKELRRRVSMVFQFPeyQLFKDTIEKDIMFGP---VALgVKKSEAKKLAKFYLNKMGLDDSY-- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1160 hVGEKGTQLSGGQKQRIAIARALVRSPSVLLLDEATSALDTESEK-IVQEALDAAKQGRTCLVIAHRLSTI-QNSDVIAI 1237
Cdd:PRK13631 170 -LERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHeMMQLILDAKANNKTVFVITHTMEHVlEVADEVIV 248
|
250 260
....*....|....*....|....
gi 124244275 1238 VSEGKIVEKGTHDELIRKSEIYQK 1261
Cdd:PRK13631 249 MDKGKILKTGTPYEIFTDQHIINS 272
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1028-1257 |
5.31e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 115.19 E-value: 5.31e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1028 ISIRNVFFNYPTRKDTKVLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGMIMIDGDNIRNLNISSLREQVC 1107
Cdd:PRK13642 5 LEVENLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1108 IVSQEP--TLFDCTIGENICYGT-NRNVTYQEIV----EAAKMANIHNFILGLPdgydthvgekgTQLSGGQKQRIAIAR 1180
Cdd:PRK13642 85 MVFQNPdnQFVGATVEDDVAFGMeNQGIPREEMIkrvdEALLAVNMLDFKTREP-----------ARLSGGQKQRVAVAG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1181 ALVRSPSVLLLDEATSALD----TESEKIVQEALDaaKQGRTCLVIAHRLSTIQNSDVIAIVSEGKIVEKGTHDELIRKS 1256
Cdd:PRK13642 154 IIALRPEIIILDESTSMLDptgrQEIMRVIHEIKE--KYQLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFATS 231
|
.
gi 124244275 1257 E 1257
Cdd:PRK13642 232 E 232
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
399-622 |
6.88e-28 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 119.36 E-value: 6.88e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 399 ISFKDVHFRYPSrkdIHVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGvdlREVNVHS----LR 474
Cdd:COG3845 6 LELRGITKRFGG---VVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDG---KPVRIRSprdaIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 475 EQIGIVSQEPVLFDG-TIYENIKMGNEHATHDQVveacKMANANDFIKRLPDGYG------TRVGekgvQLSGGQKQRIA 547
Cdd:COG3845 80 LGIGMVHQHFMLVPNlTVAENIVLGLEPTKGGRL----DRKAARARIRELSERYGldvdpdAKVE----DLSVGEQQRVE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 548 IARALVKNPKILLLDEATSALdTEAE-REVQGALDQ-AQAGRTTIIVAHRLSTIRNV-DRIFVFKAGNIVESG-----SH 619
Cdd:COG3845 152 ILKALYRGARILILDEPTAVL-TPQEaDELFEILRRlAAEGKSIIFITHKLREVMAIaDRVTVLRRGKVVGTVdtaetSE 230
|
...
gi 124244275 620 EEL 622
Cdd:COG3845 231 EEL 233
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1028-1252 |
7.84e-28 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 113.98 E-value: 7.84e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1028 ISIRNVFFNYPTRKdtkVLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFyNQDKGMIMIDG------DNI--RNLNI 1099
Cdd:PRK14258 8 IKVNNLSFYYDTQK---ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRM-NELESEVRVEGrveffnQNIyeRRVNL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1100 SSLREQVCIVSQEPTLFDCTIGENICYGT-----NRNVTYQEIVEAA-KMANihnfilgLPDGYDTHVGEKGTQLSGGQK 1173
Cdd:PRK14258 84 NRLRRQVSMVHPKPNLFPMSVYDNVAYGVkivgwRPKLEIDDIVESAlKDAD-------LWDEIKHKIHKSALDLSGGQQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1174 QRIAIARALVRSPSVLLLDEATSALDTESEKIVQEALDAA--KQGRTCLVIAHRLSTIQN-SDVIAIVSE-----GKIVE 1245
Cdd:PRK14258 157 QRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLrlRSELTMVIVSHNLHQVSRlSDFTAFFKGnenriGQLVE 236
|
....*..
gi 124244275 1246 KGTHDEL 1252
Cdd:PRK14258 237 FGLTKKI 243
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
402-576 |
8.97e-28 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 112.89 E-value: 8.97e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 402 KDVHFRYPSRKdihVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDLREVNVHSLREQIGIVS 481
Cdd:PRK10247 11 QNVGYLAGDAK---ILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 482 QEPVLFDGTIYENIKMgnEHATHDQVVEACKMAnanDFIKR--LPDgygtRVGEKGV-QLSGGQKQRIAIARALVKNPKI 558
Cdd:PRK10247 88 QTPTLFGDTVYDNLIF--PWQIRNQQPDPAIFL---DDLERfaLPD----TILTKNIaELSGGEKQRISLIRNLQFMPKV 158
|
170
....*....|....*...
gi 124244275 559 LLLDEATSALDTEAEREV 576
Cdd:PRK10247 159 LLLDEITSALDESNKHNV 176
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
420-624 |
2.87e-27 |
|
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: 114.81 E-value: 2.87e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 420 ISLELKAGDKIALVGSSGCGKSTIVNL---LQRfydPTKGRVLIDGVDL----REVNV--HslREQIGIVSQEPVLFD-- 488
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTTLLRAiagLER---PDSGRIRLGGEVLqdsaRGIFLppH--RRRIGYVFQEARLFPhl 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 489 ---GTI---YENIKMGNEHATHDQVVEACKMAnanDFIKRLPDgygtrvgekgvQLSGGQKQRIAIARALVKNPKILLLD 562
Cdd:COG4148 93 svrGNLlygRKRAPRAERRISFDEVVELLGIG---HLLDRRPA-----------TLSGGERQRVAIGRALLSSPRLLLMD 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 563 EATSALDTEAEREVQGALDQ-AQAGRTTII-VAH------RLStirnvDRIFVFKAGNIVESGSHEELMS 624
Cdd:COG4148 159 EPLAALDLARKAEILPYLERlRDELDIPILyVSHsldevaRLA-----DHVVLLEQGRVVASGPLAEVLS 223
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
416-622 |
3.08e-27 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 114.82 E-value: 3.08e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 416 VLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDLREVNVHslREQIGIVSQEPVLFDG-TIYEN 494
Cdd:PRK11432 21 VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQ--QRDICMVFQSYALFPHmSLGEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 495 I----KMGNEHATH--DQVVEACKMANANDFIKRLPDgygtrvgekgvQLSGGQKQRIAIARALVKNPKILLLDEATSAL 568
Cdd:PRK11432 99 VgyglKMLGVPKEErkQRVKEALELVDLAGFEDRYVD-----------QISGGQQQRVALARALILKPKVLLFDEPLSNL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 124244275 569 DTEAEREVQGALD--QAQAGRTTIIVAHRLSTIRNV-DRIFVFKAGNIVESGSHEEL 622
Cdd:PRK11432 168 DANLRRSMREKIRelQQQFNITSLYVTHDQSEAFAVsDTVIVMNKGKIMQIGSPQEL 224
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1028-1261 |
3.43e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 112.97 E-value: 3.43e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1028 ISIRNVFFNYPtrkDTK--VLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFY---NQDKGMIMIDGDNIRNLNISSL 1102
Cdd:PRK13640 6 VEFKHVSFTYP---DSKkpALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLlpdDNPNSKITVDGITLTAKTVWDI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1103 REQVCIVSQEP--TLFDCTIGENICYG-TNRNVTYQEiveaakMANIHNFIL---GLPDGYDThvgeKGTQLSGGQKQRI 1176
Cdd:PRK13640 83 REKVGIVFQNPdnQFVGATVGDDVAFGlENRAVPRPE------MIKIVRDVLadvGMLDYIDS----EPANLSGGQKQRV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1177 AIARALVRSPSVLLLDEATSALDTESE----KIVQEALDaaKQGRTCLVIAHRLSTIQNSDVIAIVSEGKIVEKGTHDEL 1252
Cdd:PRK13640 153 AIAGILAVEPKIIILDESTSMLDPAGKeqilKLIRKLKK--KNNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEI 230
|
....*....
gi 124244275 1253 IRKSEIYQK 1261
Cdd:PRK13640 231 FSKVEMLKE 239
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
1028-1224 |
3.94e-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: 110.58 E-value: 3.94e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1028 ISIRNVFFNYPTrkDTKVLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGMIMIDGDNIRNLN---ISSLRE 1104
Cdd:cd03292 1 IEFINVTKTYPN--GTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRgraIPYLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1105 QVCIVSQEPTLF-DCTIGENICYGTNrnVTYQEIVEAAKMANIHNFILGLPDGYDTHvgekGTQLSGGQKQRIAIARALV 1183
Cdd:cd03292 79 KIGVVFQDFRLLpDRNVYENVAFALE--VTGVPPREIRKRVPAALELVGLSHKHRAL----PAELSGGEQQRVAIARAIV 152
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 124244275 1184 RSPSVLLLDEATSALDTE-SEKIVQEALDAAKQGRTCLVIAH 1224
Cdd:cd03292 153 NSPTILIADEPTGNLDPDtTWEIMNLLKKINKAGTTVVVATH 194
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
1029-1244 |
4.84e-27 |
|
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: 110.04 E-value: 4.84e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1029 SIRNVFFNYptRKDTKVLQGFTLDIKAGKTVALVGHSGCGKST----IMGLLERfynqDKGMIMIDGDNIRNlniSSLRE 1104
Cdd:cd03226 1 RIENISFSY--KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTlakiLAGLIKE----SSGSILLNGKPIKA---KERRK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1105 QVCIVSQEPT--LFDCTIGENICYGTNRNVTYQEIVEAA-KMANIHNFILGLPdgydthvgekgTQLSGGQKQRIAIARA 1181
Cdd:cd03226 72 SIGYVMQDVDyqLFTDSVREELLLGLKELDAGNEQAETVlKDLDLYALKERHP-----------LSLSGGQKQRLAIAAA 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 124244275 1182 LVRSPSVLLLDEATSALDTESEKIVQEA-LDAAKQGRTCLVIAHRLSTIQN-SDVIAIVSEGKIV 1244
Cdd:cd03226 141 LLSGKDLLIFDEPTSGLDYKNMERVGELiRELAAQGKAVIVITHDYEFLAKvCDRVLLLANGAIV 205
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
412-611 |
5.32e-27 |
|
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: 110.60 E-value: 5.32e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 412 KDIHVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLID----GVDL-----REVnvHSLREQ-IGIVS 481
Cdd:COG4778 22 KRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRhdggWVDLaqaspREI--LALRRRtIGYVS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 482 Q---------------EPVLfdgtiyeniKMGNEHAthdqvvEACkmANANDFIKRLpdgygtRVGEKGVQL-----SGG 541
Cdd:COG4778 100 QflrviprvsaldvvaEPLL---------ERGVDRE------EAR--ARARELLARL------NLPERLWDLppatfSGG 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124244275 542 QKQRIAIARALVKNPKILLLDEATSALDTEAEREVQGALDQAQAGRTTII-VAHRLSTIRNV-DRIFVFKAG 611
Cdd:COG4778 157 EQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIgIFHDEEVREAVaDRVVDVTPF 228
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1049-1253 |
5.40e-27 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 110.83 E-value: 5.40e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1049 FTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGMIMIDGDNIRNLNISslREQVCIVSQEPTLFD-CTIGENICYG 1127
Cdd:PRK10771 18 FDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS--RRPVSMLFQENNLFShLTVAQNIGLG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1128 TNRNV--------TYQEIveAAKMAnIHNFILGLPdgydthvgekgTQLSGGQKQRIAIARALVRSPSVLLLDEATSALD 1199
Cdd:PRK10771 96 LNPGLklnaaqreKLHAI--ARQMG-IEDLLARLP-----------GQLSGGQRQRVALARCLVREQPILLLDEPFSALD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124244275 1200 ----TESEKIVQEALDaaKQGRTCLVIAHRLstiQNSDVIA----IVSEGKIVEKGTHDELI 1253
Cdd:PRK10771 162 palrQEMLTLVSQVCQ--ERQLTLLMVSHSL---EDAARIAprslVVADGRIAWDGPTDELL 218
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1028-1270 |
6.58e-27 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 110.95 E-value: 6.58e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1028 ISIRNVFFNYPTRKdtkVLQGFTLDIKAGKTVALVGHSGCGKST----IMGLLERfynqDKGMIMIDGDNIRnlnisSLR 1103
Cdd:COG1121 7 IELENLTVSYGGRP---VLEDVSLTIPPGEFVAIVGPNGAGKSTllkaILGLLPP----TSGTVRLFGKPPR-----RAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1104 EQVCIVSQEPTL---FDCTIGENICYGTNRNV---------TYQEIVEAAKMANIHNFIlglpdgyDTHVGEkgtqLSGG 1171
Cdd:COG1121 75 RRIGYVPQRAEVdwdFPITVRDVVLMGRYGRRglfrrpsraDREAVDEALERVGLEDLA-------DRPIGE----LSGG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1172 QKQRIAIARALVRSPSVLLLDEATSALDTESEKIVQEALDA-AKQGRTCLVIAHRLSTI-QNSDVIAIVSEGKIVEkGTH 1249
Cdd:COG1121 144 QQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRElRREGKTILVVTHDLGAVrEYFDRVLLLNRGLVAH-GPP 222
|
250 260
....*....|....*....|.
gi 124244275 1250 DELIRKSEIYQKFCETQRIVE 1270
Cdd:COG1121 223 EEVLTPENLSRAYGGPVALLA 243
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
402-625 |
6.90e-27 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 113.14 E-value: 6.90e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 402 KDVHFRYPSRKDI-------HVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDLREVN---VH 471
Cdd:PRK11308 9 IDLKKHYPVKRGLfkperlvKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADpeaQK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 472 SLREQIGIVSQEP---------VlfdGTIYE-----NIKMGNEHAThDQVVEAckMANAN---DFIKRLPDGYgtrvgek 534
Cdd:PRK11308 89 LLRQKIQIVFQNPygslnprkkV---GQILEeplliNTSLSAAERR-EKALAM--MAKVGlrpEHYDRYPHMF------- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 535 gvqlSGGQKQRIAIARALVKNPKILLLDEATSALDTEAEREVQGAL-D-QAQAGRTTIIVAHRLSTIRNV-DRIFVFKAG 611
Cdd:PRK11308 156 ----SGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMmDlQQELGLSYVFISHDLSVVEHIaDEVMVMYLG 231
|
250
....*....|....
gi 124244275 612 NIVESGSHEELMSK 625
Cdd:PRK11308 232 RCVEKGTKEQIFNN 245
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
416-615 |
8.63e-27 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 111.32 E-value: 8.63e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 416 VLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDLREVN---VHSLREQIGIVSQEP---VLFDG 489
Cdd:PRK10419 27 VLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNraqRKAFRRDIQMVFQDSisaVNPRK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 490 TIYENIKMGNEHATH----DQVVEACKMANANDfikrLPDGYGTRVGEkgvQLSGGQKQRIAIARALVKNPKILLLDEAT 565
Cdd:PRK10419 107 TVREIIREPLRHLLSldkaERLARASEMLRAVD----LDDSVLDKRPP---QLSGGQLQRVCLARALAVEPKLLILDEAV 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 124244275 566 SALDTEAEREVQGALD--QAQAGRTTIIVAHRLSTI-RNVDRIFVFKAGNIVE 615
Cdd:PRK10419 180 SNLDLVLQAGVIRLLKklQQQFGTACLFITHDLRLVeRFCQRVMVMDNGQIVE 232
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1039-1237 |
9.17e-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: 109.11 E-value: 9.17e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1039 TRKDTKVLQGFTLDIKAGKTVALVGHSGCGKST----IMGLLERfynqDKGMIMIDGDNIRNlNISSLREQVCIVSQEPT 1114
Cdd:COG4133 11 RRGERLLFSGLSFTLAAGEALALTGPNGSGKTTllriLAGLLPP----SAGEVLWNGEPIRD-AREDYRRRLAYLGHADG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1115 LF-DCTIGENI---CYGTNRNVTYQEIVEAAKmanihnfILGLPDGYDTHVGekgtQLSGGQKQRIAIARALVRSPSVLL 1190
Cdd:COG4133 86 LKpELTVRENLrfwAALYGLRADREAIDEALE-------AVGLAGLADLPVR----QLSAGQKRRVALARLLLSPAPLWL 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 124244275 1191 LDEATSALDTESEKIVQEALDA-AKQGRTCLVIAHRLSTIQNSDVIAI 1237
Cdd:COG4133 155 LDEPFTALDAAGVALLAELIAAhLARGGAVLLTTHQPLELAAARVLDL 202
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1042-1253 |
9.38e-27 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 110.18 E-value: 9.38e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1042 DTKVLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGMIMIDGDNIR--NLNISSLREQVCIVSQEPTLF-DC 1118
Cdd:PRK09493 13 PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpKVDERLIRQEAGMVFQQFYLFpHL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1119 TIGENICYGTNRnvtyqeiVEAAKMANIHNFILGLPD--GYDTHVGEKGTQLSGGQKQRIAIARALVRSPSVLLLDEATS 1196
Cdd:PRK09493 93 TALENVMFGPLR-------VRGASKEEAEKQARELLAkvGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTS 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 124244275 1197 ALDTEsekIVQEAL----DAAKQGRTCLVIAHRLSTIQN--SDVIAIvSEGKIVEKGTHDELI 1253
Cdd:PRK09493 166 ALDPE---LRHEVLkvmqDLAEEGMTMVIVTHEIGFAEKvaSRLIFI-DKGRIAEDGDPQVLI 224
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
401-572 |
9.93e-27 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 116.32 E-value: 9.93e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 401 FKDVHFRYPSRKdihVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGvDLRevnvhslreqIGIV 480
Cdd:COG0488 1 LENLSKSFGGRP---LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK-GLR----------IGYL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 481 SQEPVLFDG-TIYENIKMGNEH--ATHDQVVEAC-KMANANDFIKRLP---------DGY-------------------- 527
Cdd:COG0488 67 PQEPPLDDDlTVLDTVLDGDAElrALEAELEELEaKLAEPDEDLERLAelqeefealGGWeaearaeeilsglgfpeedl 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 124244275 528 GTRVGEkgvqLSGGQKQRIAIARALVKNPKILLLDEATSALDTEA 572
Cdd:COG0488 147 DRPVSE----LSGGWRRRVALARALLSEPDLLLLDEPTNHLDLES 187
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1028-1244 |
1.45e-26 |
|
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: 107.13 E-value: 1.45e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1028 ISIRNVFFNYPtrkDTKVLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGMIMIDGdniRNLNISSLREqvc 1107
Cdd:cd03216 1 LELRGITKRFG---GVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDG---KEVSFASPRD--- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1108 ivsqeptlfdctigenicygtnrnvtyqeiVEAAKMANIHnfilglpdgydthvgekgtQLSGGQKQRIAIARALVRSPS 1187
Cdd:cd03216 72 ------------------------------ARRAGIAMVY-------------------QLSVGERQMVEIARALARNAR 102
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 124244275 1188 VLLLDEATSAL-DTESEKIVQEALDAAKQGRTCLVIAHRLSTIQN-SDVIAIVSEGKIV 1244
Cdd:cd03216 103 LLILDEPTAALtPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEiADRVTVLRDGRVV 161
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
753-1000 |
1.78e-26 |
|
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: 111.07 E-value: 1.78e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 753 MFVLMGITFFVG---FFTSANCLGRCGESLTMKLRFEAFKNLLRQDIAFYDdlRHGTGKLCTRFATDAPNVRYVFT-RLP 828
Cdd:cd18573 43 FALALLGVFVVGaaaNFGRVYLLRIAGERIVARLRKRLFKSILRQDAAFFD--KNKTGELVSRLSSDTSVVGKSLTqNLS 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 829 VVLASIVTICGALGIGFYYGWQLALILVVMVPLLVMGGYFemqmrFGKQIRD--TQLLE---EAGKVASQAVEHIRTVHS 903
Cdd:cd18573 121 DGLRSLVSGVGGIGMMLYISPKLTLVMLLVVPPIAVGAVF-----YGRYVRKlsKQVQDalaDATKVAEERLSNIRTVRA 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 904 LNRQEQFHFTYCEYLREPFNTNLKHAHTYGAVFAFSQSLIFFMYAAAFYLGSIFVNQQAMQPIDV-----YRVFFAISFc 978
Cdd:cd18573 196 FAAERKEVERYAKKVDEVFDLAKKEALASGLFFGSTGFSGNLSLLSVLYYGGSLVASGELTVGDLtsflmYAVYVGSSV- 274
|
250 260
....*....|....*....|..
gi 124244275 979 gqmiGNTTSFIPDVVKARLAAS 1000
Cdd:cd18573 275 ----SGLSSFYSELMKGLGASS 292
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
407-623 |
1.89e-26 |
|
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: 109.17 E-value: 1.89e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 407 RYPSRKdihVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDLREVNVHSlREQIGI--VSQEP 484
Cdd:cd03218 9 RYGKRK---VVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHK-RARLGIgyLPQEA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 485 VLFDG-TIYENIKMGNEhATHDQVVEACKMANA--NDF-IKRLPDgygtrvgEKGVQLSGGQKQRIAIARALVKNPKILL 560
Cdd:cd03218 85 SIFRKlTVEENILAVLE-IRGLSKKEREEKLEEllEEFhITHLRK-------SKASSLSGGERRRVEIARALATNPKFLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 124244275 561 LDEATSALDTEAEREVQGALDQ-AQAGRTTIIVAHRLS-TIRNVDRIFVFKAGNIVESGSHEELM 623
Cdd:cd03218 157 LDEPFAGVDPIAVQDIQKIIKIlKDRGIGVLITDHNVReTLSITDRAYIIYEGKVLAEGTPEEIA 221
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
1021-1272 |
2.06e-26 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 118.15 E-value: 2.06e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1021 VKPITGNISIRNVFFNYPTRKDTKVLQGFTLDIKAGKTVALVGHSGCGK-STIMGLLERFYNQDKGMIMIDGdnirnlni 1099
Cdd:PLN03232 608 LQPGAPAISIKNGYFSWDSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKtSLISAMLGELSHAETSSVVIRG-------- 679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1100 sslreQVCIVSQEPTLFDCTIGENICYGTN-RNVTYQEIVEAAKMAniHNfiLGLPDGYD-THVGEKGTQLSGGQKQRIA 1177
Cdd:PLN03232 680 -----SVAYVPQVSWIFNATVRENILFGSDfESERYWRAIDVTALQ--HD--LDLLPGRDlTEIGERGVNISGGQKQRVS 750
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1178 IARALVRSPSVLLLDEATSALDTE-SEKIVQEALDAAKQGRTCLVIAHRLSTIQNSDVIAIVSEGKIVEKGTHDELIRKS 1256
Cdd:PLN03232 751 MARAVYSNSDIYIFDDPLSALDAHvAHQVFDSCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELSKSG 830
|
250
....*....|....*.
gi 124244275 1257 EIYQKFCETQRIVESQ 1272
Cdd:PLN03232 831 SLFKKLMENAGKMDAT 846
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
392-622 |
2.24e-26 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 111.72 E-value: 2.24e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 392 VDNMKG--DISFKDVHFRYPSrKDIHVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDLR--- 466
Cdd:PRK15079 11 VADLKVhfDIKDGKQWFWQPP-KTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLgmk 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 467 EVNVHSLREQIGIVSQEPV-------LFDGTIYENIKMGNEHATHDQVVEACK--MANAN---DFIKRLPDgygtrvgek 534
Cdd:PRK15079 90 DDEWRAVRSDIQMIFQDPLaslnprmTIGEIIAEPLRTYHPKLSRQEVKDRVKamMLKVGllpNLINRYPH--------- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 535 gvQLSGGQKQRIAIARALVKNPKILLLDEATSALDTEAEREVQGALDQAQA--GRTTIIVAHRLSTIRNV-DRIFVFKAG 611
Cdd:PRK15079 161 --EFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQRemGLSLIFIAHDLAVVKHIsDRVLVMYLG 238
|
250
....*....|.
gi 124244275 612 NIVESGSHEEL 622
Cdd:PRK15079 239 HAVELGTYDEV 249
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
408-625 |
2.46e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 110.28 E-value: 2.46e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 408 YPSRKDIHVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDLREVNVHSLREQIGIVSQEP--V 485
Cdd:PRK13652 11 YSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQNPddQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 486 LFDGTIYENIKMG------NEHATHDQVVEACKMANANDFIKRLPDgygtrvgekgvQLSGGQKQRIAIARALVKNPKIL 559
Cdd:PRK13652 91 IFSPTVEQDIAFGpinlglDEETVAHRVSSALHMLGLEELRDRVPH-----------HLSGGEKKRVAIAGVIAMEPQVL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124244275 560 LLDEATSALDTEAEREVQGALDQ--AQAGRTTIIVAHRLSTIRNV-DRIFVFKAGNIVESGSHEELMSK 625
Cdd:PRK13652 160 VLDEPTAGLDPQGVKELIDFLNDlpETYGMTVIFSTHQLDLVPEMaDYIYVMDKGRIVAYGTVEEIFLQ 228
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
399-626 |
2.58e-26 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 108.95 E-value: 2.58e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 399 ISFKDVHFRYPSRKdihVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDG------VDLREVNVHS 472
Cdd:COG4161 3 IQLKNINCFYGSHQ---ALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGhqfdfsQKPSEKAIRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 473 LREQIGIVSQE----PVLfdgTIYENI--------KMGNEHAthdqvveackMANANDFIKRLpdgygtRVGEKG----V 536
Cdd:COG4161 80 LRQKVGMVFQQynlwPHL---TVMENLieapckvlGLSKEQA----------REKAMKLLARL------RLTDKAdrfpL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 537 QLSGGQKQRIAIARALVKNPKILLLDEATSALDTEAEREVQGALDQ-AQAGRTTIIVAHRLSTIRNV-DRIFVFKAGNIV 614
Cdd:COG4161 141 HLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQVVEIIRElSQTGITQVIVTHEVEFARKVaSQVVYMEKGRII 220
|
250
....*....|..
gi 124244275 615 ESGSHEELMSKQ 626
Cdd:COG4161 221 EQGDASHFTQPQ 232
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
399-618 |
3.09e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 109.83 E-value: 3.09e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 399 ISFKDVHFRYPSRKDIH--VLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDLREV----NVHS 472
Cdd:PRK13649 3 INLQNVSYTYQAGTPFEgrALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTsknkDIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 473 LREQIGIVSQ--EPVLFDGTIYENIKMGNEHATHDQvVEACKMAN--------ANDFIKRLPdgygtrvgekgVQLSGGQ 542
Cdd:PRK13649 83 IRKKVGLVFQfpESQLFEETVLKDVAFGPQNFGVSQ-EEAEALAReklalvgiSESLFEKNP-----------FELSGGQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 124244275 543 KQRIAIARALVKNPKILLLDEATSALDTEAEREVQGALDQA-QAGRTTIIVAHRLSTIRN-VDRIFVFKAGNIVESGS 618
Cdd:PRK13649 151 MRRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLhQSGMTIVLVTHLMDDVANyADFVYVLEKGKLVLSGK 228
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1028-1248 |
3.15e-26 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 111.43 E-value: 3.15e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1028 ISIRNVFFNYPTRKDTKV-LQGFTLDIKAGKTVALVGHSGCGKST---IMGLLERfynQDKGMIMIDGDNIRNLNISSLR 1103
Cdd:PRK11153 2 IELKNISKVFPQGGRTIHaLNNVSLHIPAGEIFGVIGASGAGKSTlirCINLLER---PTSGRVLVDGQDLTALSEKELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1104 E---QVCIVSQEPTLFDC-TIGENICY-----GTNRNVTYQEIVEAAKManihnfiLGLPDGYDTHvgekGTQLSGGQKQ 1174
Cdd:PRK11153 79 KarrQIGMIFQHFNLLSSrTVFDNVALplelaGTPKAEIKARVTELLEL-------VGLSDKADRY----PAQLSGGQKQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1175 RIAIARALVRSPSVLLLDEATSALDTESEKIVqeaLDAAKQ-----GRTCLVIAHRLSTI-QNSDVIAIVSEGKIVEKGT 1248
Cdd:PRK11153 148 RVAIARALASNPKVLLCDEATSALDPATTRSI---LELLKDinrelGLTIVLITHEMDVVkRICDRVAVIDAGRLVEQGT 224
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
416-624 |
3.82e-26 |
|
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: 109.12 E-value: 3.82e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 416 VLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDLREVNVHS---LREQIGIVSQE-PVLFDG-- 489
Cdd:TIGR02769 26 VLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQrraFRRDVQLVFQDsPSAVNPrm 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 490 TIYENIKMGNEHAThdQVVEACKMANANDFIKR--LPDGYGTRVGEkgvQLSGGQKQRIAIARALVKNPKILLLDEATSA 567
Cdd:TIGR02769 106 TVRQIIGEPLRHLT--SLDESEQKARIAELLDMvgLRSEDADKLPR---QLSGGQLQRINIARALAVKPKLIVLDEAVSN 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 568 LDTEAEREVQGALD--QAQAGRTTIIVAHRLSTIRNV-DRIFVFKAGNIVESGSHEELMS 624
Cdd:TIGR02769 181 LDMVLQAVILELLRklQQAFGTAYLFITHDLRLVQSFcQRVAVMDKGQIVEECDVAQLLS 240
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
393-625 |
4.00e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 109.79 E-value: 4.00e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 393 DNMkgdISFKDVHFRY---PSRKDIHVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVD-LREV 468
Cdd:PRK13633 2 NEM---IKCKNVSYKYesnEESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDtSDEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 469 NVHSLREQIGIVSQEPvlfDGTIY-----ENIKMGNEH------ATHDQVVEACKMANANDFIKRLPDgygtrvgekgvQ 537
Cdd:PRK13633 79 NLWDIRNKAGMVFQNP---DNQIVativeEDVAFGPENlgippeEIRERVDESLKKVGMYEYRRHAPH-----------L 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 538 LSGGQKQRIAIARALVKNPKILLLDEATSALDTEAEREVQGALDQ--AQAGRTTIIVAHRLSTIRNVDRIFVFKAGNIVE 615
Cdd:PRK13633 145 LSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKElnKKYGITIILITHYMEEAVEADRIIVMDSGKVVM 224
|
250
....*....|
gi 124244275 616 SGSHEELMSK 625
Cdd:PRK13633 225 EGTPKEIFKE 234
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
414-624 |
5.32e-26 |
|
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: 108.59 E-value: 5.32e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 414 IHVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDLREVNVHslreQI---GIVS--QEPVLFD 488
Cdd:COG0411 17 LVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPH----RIarlGIARtfQNPRLFP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 489 G-TIYENIKMGNEHATHDQVVEACK------------MANANDFIKRLpdGYGTRVGEKGVQLSGGQKQRIAIARALVKN 555
Cdd:COG0411 93 ElTVLENVLVAAHARLGRGLLAALLrlprarreereaRERAEELLERV--GLADRADEPAGNLSYGQQRRLEIARALATE 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 124244275 556 PKILLLDEATSALDTEaerEVQGALD-----QAQAGRTTIIVAHRLSTIRNV-DRIFVFKAGNIVESGSHEELMS 624
Cdd:COG0411 171 PKLLLLDEPAAGLNPE---ETEELAElirrlRDERGITILLIEHDMDLVMGLaDRIVVLDFGRVIAEGTPAEVRA 242
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1028-1252 |
5.72e-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: 114.01 E-value: 5.72e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1028 ISIRNVFFNYPTRK--------DTKVLQGFTLDIKAGKTVALVGHSGCGKST----IMGLLERfynqdKGMIMIDGDNIR 1095
Cdd:COG4172 276 LEARDLKVWFPIKRglfrrtvgHVKAVDGVSLTLRRGETLGLVGESGSGKSTlglaLLRLIPS-----EGEIRFDGQDLD 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1096 NLNIS---SLREQVCIVSQEPtlFDC-----TIGENI-------CYGTNRNVTYQEIVEA-------AKMAN--IHNFil 1151
Cdd:COG4172 351 GLSRRalrPLRRRMQVVFQDP--FGSlsprmTVGQIIaeglrvhGPGLSAAERRARVAEAleevgldPAARHryPHEF-- 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1152 glpdgydthvgekgtqlSGGQKQRIAIARALVRSPSVLLLDEATSALDteseKIVQ-EALD-----AAKQGRTCLVIAHR 1225
Cdd:COG4172 427 -----------------SGGQRQRIAIARALILEPKLLVLDEPTSALD----VSVQaQILDllrdlQREHGLAYLFISHD 485
|
250 260
....*....|....*....|....*...
gi 124244275 1226 LSTIQN-SDVIAIVSEGKIVEKGTHDEL 1252
Cdd:COG4172 486 LAVVRAlAHRVMVMKDGKVVEQGPTEQV 513
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
708-963 |
5.85e-26 |
|
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: 109.56 E-value: 5.85e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 708 FIGGIFGAFIFGSVTPVFALVYAEIFNVYsLPADQMQANVYFWCGMFVLMGITFFVGFFTSAnCLGRCGESLTMKLRFEA 787
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLLIDDV-IPAGDLSLLLWIALLLLLLALLRALLSYLRRY-LAARLGQRVVFDLRRDL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 788 FKNLLRQDIAFYDdlRHGTGKLCTRFATDAPNVRYVFTR-LPVVLASIVTICGALGIGFYYGWQLALILVVMVPLLVMGG 866
Cdd:cd07346 79 FRHLQRLSLSFFD--RNRTGDLMSRLTSDVDAVQNLVSSgLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLIL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 867 YFemqmrFGKQIRDT--QLLEEAGKVASQAVEH---IRTVHSLNRQEQFHFTYCEYLREPFNTNLKHAHTYGAVFAFSQS 941
Cdd:cd07346 157 RY-----FRRRIRKAsrEVRESLAELSAFLQESlsgIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGL 231
|
250 260
....*....|....*....|..
gi 124244275 942 LIFFMYAAAFYLGSIFVNQQAM 963
Cdd:cd07346 232 LTALGTALVLLYGGYLVLQGSL 253
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1028-1252 |
6.05e-26 |
|
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: 107.81 E-value: 6.05e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1028 ISIRNVFFNYPtrkDTKVLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGMIMIDGDNIRNLNISslREQVC 1107
Cdd:cd03296 3 IEVRNVSKRFG---DFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQ--ERNVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1108 IVSQEPTLF-DCTIGENICYGTNRNVTYQEIVEAAKMANIHNFIL-----GLPDGYDThvgekgtQLSGGQKQRIAIARA 1181
Cdd:cd03296 78 FVFQHYALFrHMTVFDNVAFGLRVKPRSERPPEAEIRAKVHELLKlvqldWLADRYPA-------QLSGGQRQRVALARA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124244275 1182 LVRSPSVLLLDEATSALDTESEKIVQEALDAA--KQGRTCLVIAHRLS-TIQNSDVIAIVSEGKIVEKGTHDEL 1252
Cdd:cd03296 151 LAVEPKVLLLDEPFGALDAKVRKELRRWLRRLhdELHVTTVFVTHDQEeALEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
1028-1245 |
6.33e-26 |
|
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: 108.74 E-value: 6.33e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1028 ISIRNVFFNYPT------RKDTKVLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGMIMIDGDNIRNLNISS 1101
Cdd:TIGR02769 3 LEVRDVTHTYRTgglfgaKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1102 ---LREQVCIVSQEptlfdctigeniCYGT-NRNVTYQEIV-----------EAAKMANIHNFI--LGLPDgydTHVGEK 1164
Cdd:TIGR02769 83 rraFRRDVQLVFQD------------SPSAvNPRMTVRQIIgeplrhltsldESEQKARIAELLdmVGLRS---EDADKL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1165 GTQLSGGQKQRIAIARALVRSPSVLLLDEATSALDTESEKIVQEALDAAKQ--GRTCLVIAHRLSTIQN-SDVIAIVSEG 1241
Cdd:TIGR02769 148 PRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQafGTAYLFITHDLRLVQSfCQRVAVMDKG 227
|
....
gi 124244275 1242 KIVE 1245
Cdd:TIGR02769 228 QIVE 231
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
398-625 |
7.75e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 108.95 E-value: 7.75e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 398 DISFKDVHFRY----PSRKDihVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDL----REVN 469
Cdd:PRK13634 2 DITFQKVEHRYqyktPFERR--ALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVItagkKNKK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 470 VHSLREQIGIVSQ--EPVLFDGTIYENIKMGnehATHDQVVEACKMANANDFIKR--LPDGYGTRvgeKGVQLSGGQKQR 545
Cdd:PRK13634 80 LKPLRKKVGIVFQfpEHQLFEETVEKDICFG---PMNFGVSEEDAKQKAREMIELvgLPEELLAR---SPFELSGGQMRR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 546 IAIARALVKNPKILLLDEATSALDTEAEREVQGALDQ--AQAGRTTIIVAHRLSTIRN-VDRIFVFKAGNIVESGSHEEL 622
Cdd:PRK13634 154 VAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKlhKEKGLTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTPREI 233
|
...
gi 124244275 623 MSK 625
Cdd:PRK13634 234 FAD 236
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
416-622 |
8.12e-26 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 110.56 E-value: 8.12e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 416 VLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDLREVnvHSLREQIGIVSQEPVLFDG-TIYEN 494
Cdd:PRK10851 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRL--HARDRKVGFVFQHYALFRHmTVFDN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 495 IKMG----------NEHATHDQVVEACKMANANDFIKRLPdgygtrvgekgVQLSGGQKQRIAIARALVKNPKILLLDEA 564
Cdd:PRK10851 95 IAFGltvlprrerpNAAAIKAKVTQLLEMVQLAHLADRYP-----------AQLSGGQKQRVALARALAVEPQILLLDEP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 124244275 565 TSALDTEAEREVQGALDQ--AQAGRTTIIVAHRLSTIRNV-DRIFVFKAGNIVESGSHEEL 622
Cdd:PRK10851 164 FGALDAQVRKELRRWLRQlhEELKFTSVFVTHDQEEAMEVaDRVVVMSQGNIEQAGTPDQV 224
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
417-608 |
8.24e-26 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 106.41 E-value: 8.24e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 417 LKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDP---TKGRVLIDGVDLREVNVHslREQIGIVSQEPVLFDG-TIY 492
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALPAE--QRRIGILFQDDLLFPHlSVG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 493 ENIKMG-----NEHATHDQVVEACKMANANDFIKRLPDgygtrvgekgvQLSGGQKQRIAIARALVKNPKILLLDEATSA 567
Cdd:COG4136 95 ENLAFAlpptiGRAQRRARVEQALEEAGLAGFADRDPA-----------TLSGGQRARVALLRALLAEPRALLLDEPFSK 163
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 124244275 568 LDTEAEREV-QGALDQA-QAGRTTIIVAHRLSTIRNVDRIFVF 608
Cdd:COG4136 164 LDAALRAQFrEFVFEQIrQRGIPALLVTHDEEDAPAAGRVLDL 206
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
399-569 |
8.98e-26 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 108.03 E-value: 8.98e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 399 ISFKDVHFRYP-SRKDIHVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDL------Revnvh 471
Cdd:COG4525 4 LTVRHVSVRYPgGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVtgpgadR----- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 472 slreqiGIVSQEPVLFDG-TIYENIKMG------NEHATHDQVVEACKMANANDFIKRLPDgygtrvgekgvQLSGGQKQ 544
Cdd:COG4525 79 ------GVVFQKDALLPWlNVLDNVAFGlrlrgvPKAERRARAEELLALVGLADFARRRIW-----------QLSGGMRQ 141
|
170 180
....*....|....*....|....*
gi 124244275 545 RIAIARALVKNPKILLLDEATSALD 569
Cdd:COG4525 142 RVGIARALAADPRFLLMDEPFGALD 166
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1033-1247 |
9.06e-26 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 107.94 E-value: 9.06e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1033 VFFNyptrkDTKVLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQD-----KGMIMIDGDNI--RNLNISSLREQ 1105
Cdd:PRK14239 13 VYYN-----KKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNpevtiTGSIVYNGHNIysPRTDTVDLRKE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1106 VCIVSQEPTLFDCTIGENICYGTNRN-VTYQEIVEAA-----KMANIHnfilglpDGYDTHVGEKGTQLSGGQKQRIAIA 1179
Cdd:PRK14239 88 IGMVFQQPNPFPMSIYENVVYGLRLKgIKDKQVLDEAvekslKGASIW-------DEVKDRLHDSALGLSGGQQQRVCIA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 124244275 1180 RALVRSPSVLLLDEATSALDTESEKIVQEALDAAKQGRTCLVIAHRL---STIqnSDVIAIVSEGKIVEKG 1247
Cdd:PRK14239 161 RVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMqqaSRI--SDRTGFFLDGDLIEYN 229
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
412-617 |
1.05e-25 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 106.15 E-value: 1.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 412 KDIHVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDLreVNVHSLREQIGIVSQEPVLFDG-T 490
Cdd:cd03268 11 GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSY--QKNIEALRRIGALIEAPGFYPNlT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 491 IYENIK-----MGNEHATHDQVVEACKMANANDfikrlpdgygTRVGekgvQLSGGQKQRIAIARALVKNPKILLLDEAT 565
Cdd:cd03268 89 ARENLRllarlLGIRKKRIDEVLDVVGLKDSAK----------KKVK----GFSLGMKQRLGIALALLGNPDLLILDEPT 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 124244275 566 SALDTEAEREVQGAL-DQAQAGRTTIIVAHRLSTIRNV-DRIFVFKAGNIVESG 617
Cdd:cd03268 155 NGLDPDGIKELRELIlSLRDQGITVLISSHLLSEIQKVaDRIGIINKGKLIEEG 208
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1028-1261 |
1.30e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 107.86 E-value: 1.30e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1028 ISIRNVFFNYPtrKDTKVLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGMIMIDGDNIRNLNISSL--REQ 1105
Cdd:PRK13639 2 LETRDLKYSYP--DGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLevRKT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1106 VCIVSQEP--TLFDCTIGENICYG-TNRNVTYQEIVEAAKMANIHNFILGLPDGYDTHvgekgtqLSGGQKQRIAIARAL 1182
Cdd:PRK13639 80 VGIVFQNPddQLFAPTVEEDVAFGpLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHH-------LSGGQKKRVAIAGIL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1183 VRSPSVLLLDEATSALDTE-SEKIVQEALDAAKQGRTCLVIAHRLSTIQ-NSDVIAIVSEGKIVEKGTHDELIRKSEIYQ 1260
Cdd:PRK13639 153 AMKPEIIVLDEPTSGLDPMgASQIMKLLYDLNKEGITIIISTHDVDLVPvYADKVYVMSDGKIIKEGTPKEVFSDIETIR 232
|
.
gi 124244275 1261 K 1261
Cdd:PRK13639 233 K 233
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
399-626 |
1.44e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 107.53 E-value: 1.44e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 399 ISFKDVHFRYPSRKDIhVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDLREVNVHSLREQIG 478
Cdd:PRK13648 8 IVFKNVSFQYQSDASF-TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 479 IVSQEPV-LFDGTIYE-NIKMGNE-HAT-----HDQVVEACKMANANDFIKRLPDGygtrvgekgvqLSGGQKQRIAIAR 550
Cdd:PRK13648 87 IVFQNPDnQFVGSIVKyDVAFGLEnHAVpydemHRRVSEALKQVDMLERADYEPNA-----------LSGGQKQRVAIAG 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 124244275 551 ALVKNPKILLLDEATSALDTEAEREVQGALDQAQAGR--TTIIVAHRLSTIRNVDRIFVFKAGNIVESGSHEELMSKQ 626
Cdd:PRK13648 156 VLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFDHA 233
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1042-1250 |
1.56e-25 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 106.34 E-value: 1.56e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1042 DTKVLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGMIMIDGDNIRNLNISSLREQVCIVSQEPTLFDCTIG 1121
Cdd:PRK10247 19 DAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTLFGDTVY 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1122 ENICYGTN-RNVTYQEIVEAAKMANihnfiLGLPDgydtHVGEKG-TQLSGGQKQRIAIARALVRSPSVLLLDEATSALD 1199
Cdd:PRK10247 99 DNLIFPWQiRNQQPDPAIFLDDLER-----FALPD----TILTKNiAELSGGEKQRISLIRNLQFMPKVLLLDEITSALD 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 124244275 1200 TESEKIVQEALD--AAKQGRTCLVIAHRLSTIQNSD-VIAIVSEGKIVEKGTHD 1250
Cdd:PRK10247 170 ESNKHNVNEIIHryVREQNIAVLWVTHDKDEINHADkVITLQPHAGEMQEARYE 223
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
125-369 |
1.60e-25 |
|
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: 107.95 E-value: 1.60e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 125 LVLGVLMF--FTSYVQIACFESYAERLVHKLRQNYLKAILRQQIQWFDKQQTGNLTARLTDDLERVREGLGDKFALLVQM 202
Cdd:cd18576 41 LLLGLFLLqaVFSFFRIYLFARVGERVVADLRKDLYRHLQRLPLSFFHERRVGELTSRLSNDVTQIQDTLTTTLAEFLRQ 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 203 FAAFLAGYGVGFFYSWSMTLVMMGFAPLIVLSGA-------KMSKSMatrtrveQETYAVAGAIAEETFSSIRTVHSLNG 275
Cdd:cd18576 121 ILTLIGGVVLLFFISWKLTLLMLATVPVVVLVAVlfgrrirKLSKKV-------QDELAEANTIVEETLQGIRVVKAFTR 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 276 HKRELDRFYNALEVGRQTGIVKYCYMGIGVGFSNLCMYSSYALAFWYGSTLIINDpTFDRG-----LIFTVFFAvlsgsT 350
Cdd:cd18576 194 EDYEIERYRKALERVVKLALKRARIRALFSSFIIFLLFGAIVAVLWYGGRLVLAG-ELTAGdlvafLLYTLFIA-----G 267
|
250
....*....|....*....
gi 124244275 351 SLGGALPHLASFGTARGAA 369
Cdd:cd18576 268 SIGSLADLYGQLQKALGAS 286
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
399-620 |
2.14e-25 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 106.25 E-value: 2.14e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 399 ISFKDVHFRYPSRKdihVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDG--VDLR----EVNVHS 472
Cdd:PRK11124 3 IQLNGINCFYGAHQ---ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhFDFSktpsDKAIRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 473 LREQIGIVSQE----PVLfdgTIYENIkmgnehathdqvVEA-CK---------MANANDFIKRLpdgygtRVGEKG--- 535
Cdd:PRK11124 80 LRRNVGMVFQQynlwPHL---TVQQNL------------IEApCRvlglskdqaLARAEKLLERL------RLKPYAdrf 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 536 -VQLSGGQKQRIAIARALVKNPKILLLDEATSALDTEAEREVQGALDQ-AQAGRTTIIVAHRLSTIRNV-DRIFVFKAGN 612
Cdd:PRK11124 139 pLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRElAETGITQVIVTHEVEVARKTaSRVVYMENGH 218
|
....*...
gi 124244275 613 IVESGSHE 620
Cdd:PRK11124 219 IVEQGDAS 226
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
395-622 |
2.53e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 106.46 E-value: 2.53e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 395 MKGDISFKDVHFRYPSRkdiHVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYD-----PTKGRVLIDGVDL--RE 467
Cdd:PRK14267 1 MKFAIETVNLRVYYGSN---HVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGRNIysPD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 468 VNVHSLREQIGIVSQEPVLFDG-TIYENIKMG-------NEHATHDQVVE-ACKMANANDFIKrlpdgygTRVGEKGVQL 538
Cdd:PRK14267 78 VDPIEVRREVGMVFQYPNPFPHlTIYDNVAIGvklnglvKSKKELDERVEwALKKAALWDEVK-------DRLNDYPSNL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 539 SGGQKQRIAIARALVKNPKILLLDEATSALDTEAEREVQGALDQAQAGRTTIIVAHRLSTIRNV-DRIFVFKAGNIVESG 617
Cdd:PRK14267 151 SGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSPAQAARVsDYVAFLYLGKLIEVG 230
|
....*
gi 124244275 618 SHEEL 622
Cdd:PRK14267 231 PTRKV 235
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
404-624 |
3.59e-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: 3.59e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 404 VHFRYPSRkDIHVLKGISLELKAGDKIALVGSSGCGKS----TIVNLLQRFYDPTKGRVLIDGVDLREVNVHSLRE---- 475
Cdd:COG4172 14 VAFGQGGG-TVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERELRRirgn 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 476 QIGIVSQEPV-----LFdgTIYENI--------KMGNEHAtHDQVVEACKMAnandfikRLPDGyGTRVGEKGVQLSGGQ 542
Cdd:COG4172 93 RIAMIFQEPMtslnpLH--TIGKQIaevlrlhrGLSGAAA-RARALELLERV-------GIPDP-ERRLDAYPHQLSGGQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 543 KQRIAIARALVKNPKILLLDEATSALDTEAEREVqgaLD-----QAQAGRTTIIVAHRLSTIRNV-DRIFVFKAGNIVES 616
Cdd:COG4172 162 RQRVMIAMALANEPDLLIADEPTTALDVTVQAQI---LDllkdlQRELGMALLLITHDLGVVRRFaDRVAVMRQGEIVEQ 238
|
....*...
gi 124244275 617 GSHEELMS 624
Cdd:COG4172 239 GPTAELFA 246
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1028-1262 |
3.80e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 105.77 E-value: 3.80e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1028 ISIRNVFFNYptrKDTKVLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERF---YNQDK--GMIMIDGDNIRNLNISSL 1102
Cdd:PRK14247 4 IEIRDLKVSF---GQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielYPEARvsGEVYLDGQDIFKMDVIEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1103 REQVCIVSQEPT-LFDCTIGENICYG-------TNRNVTYQEIVEAAKMANIHNFI---LGLPDGydthvgekgtQLSGG 1171
Cdd:PRK14247 81 RRRVQMVFQIPNpIPNLSIFENVALGlklnrlvKSKKELQERVRWALEKAQLWDEVkdrLDAPAG----------KLSGG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1172 QKQRIAIARALVRSPSVLLLDEATSALDTESEKIVQEALDAAKQGRTCLVIAH-RLSTIQNSDVIAIVSEGKIVEKGTHD 1250
Cdd:PRK14247 151 QQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHfPQQAARISDYVAFLYKGQIVEWGPTR 230
|
250
....*....|....
gi 124244275 1251 ELIR--KSEIYQKF 1262
Cdd:PRK14247 231 EVFTnpRHELTEKY 244
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
417-618 |
3.91e-25 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 106.40 E-value: 3.91e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 417 LKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYD--PT---KGRVLIDGVDL--REVNVHSLREQIGIVSQEPVLFDG 489
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDliPGfrvEGKVTFHGKNLyaPDVDPVEVRRRIGMVFQKPNPFPK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 490 TIYENIKMGNE----HATHDQVVE-ACKMANANDFIKrlpdgygTRVGEKGVQLSGGQKQRIAIARALVKNPKILLLDEA 564
Cdd:PRK14243 106 SIYDNIAYGARingyKGDMDELVErSLRQAALWDEVK-------DKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEP 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 124244275 565 TSALDTEAEREVQGALDQAQAGRTTIIVAHRLSTIRNVDRIFVFKAGNIVESGS 618
Cdd:PRK14243 179 CSALDPISTLRIEELMHELKEQYTIIIVTHNMQQAARVSDMTAFFNVELTEGGG 232
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1028-1255 |
4.37e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 106.36 E-value: 4.37e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1028 ISIRNVFFNYptRKDTKVLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGMIMIDGDNIRNLNISSLREQVC 1107
Cdd:PRK13647 5 IEVEDLHFRY--KDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1108 IVSQEP--TLFDCTIGENICYG-TNRNVTYQEIVEAAKMAnihnfiLGLPDGYDthVGEKGT-QLSGGQKQRIAIARALV 1183
Cdd:PRK13647 83 LVFQDPddQVFSSTVWDDVAFGpVNMGLDKDEVERRVEEA------LKAVRMWD--FRDKPPyHLSYGQKKRVAIAGVLA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124244275 1184 RSPSVLLLDEATSALDTESEKIVQEALDA-AKQGRTCLVIAHRLS-TIQNSDVIAIVSEGKIVEKGTHDELIRK 1255
Cdd:PRK13647 155 MDPDVIVLDEPMAYLDPRGQETLMEILDRlHNQGKTVIVATHDVDlAAEWADQVIVLKEGRVLAEGDKSLLTDE 228
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
399-626 |
5.81e-25 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 105.62 E-value: 5.81e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 399 ISFKDVHFRYPSRkdiHVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDLREVNVHSLREQIG 478
Cdd:PRK13548 3 LEARNLSVRLGGR---TLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 479 IVSQEPVL-FDGTIYENIKMG-----NEHATHDQVVEACkMANAN--DFIKRLpdgYgtrvgekgVQLSGGQKQRIAIAR 550
Cdd:PRK13548 80 VLPQHSSLsFPFTVEEVVAMGraphgLSRAEDDALVAAA-LAQVDlaHLAGRD---Y--------PQLSGGEQQRVQLAR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 551 ALV------KNPKILLLDEATSALDTEAEREVQGALDQ--AQAGRTTIIVAHRLS-TIRNVDRIFVFKAGNIVESGSHEE 621
Cdd:PRK13548 148 VLAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQlaHERGLAVIVVLHDLNlAARYADRIVLLHQGRLVADGTPAE 227
|
....*
gi 124244275 622 LMSKQ 626
Cdd:PRK13548 228 VLTPE 232
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
1028-1247 |
5.90e-25 |
|
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: 104.26 E-value: 5.90e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1028 ISIRNVFFNYPtrkDTKVLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGMIMIDGDNIRNL-----NISsl 1102
Cdd:cd03301 1 VELENVTKRFG---NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLppkdrDIA-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1103 reqvcIVSQEPTLF-DCTIGENICYG-TNRNVTYQEIVE----AAKMANIhnfilglpdgyDTHVGEKGTQLSGGQKQRI 1176
Cdd:cd03301 76 -----MVFQNYALYpHMTVYDNIAFGlKLRKVPKDEIDErvreVAELLQI-----------EHLLDRKPKQLSGGQRQRV 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1177 AIARALVRSPSVLLLDEATSALD--------TESEKIVQEaldaakQGRTCLVIAH-RLSTIQNSDVIAIVSEGKIVEKG 1247
Cdd:cd03301 140 ALGRAIVREPKVFLMDEPLSNLDaklrvqmrAELKRLQQR------LGTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
415-614 |
6.06e-25 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 105.55 E-value: 6.06e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 415 HVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDLREVNVHSLREQIGIVSQEPVL---FDGTI 491
Cdd:COG1101 20 RALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAKYIGRVFQDPMMgtaPSMTI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 492 YEN------------IKMGNEHATHDQVVEACKMANaNDFIKRLpdgyGTRVGekgvQLSGGQKQRIAIARALVKNPKIL 559
Cdd:COG1101 100 EENlalayrrgkrrgLRRGLTKKRRELFRELLATLG-LGLENRL----DTKVG----LLSGGQRQALSLLMATLTKPKLL 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 124244275 560 LLDEATSALDTEAEREVQGALDQ--AQAGRTTIIVAHRLS-TIRNVDRIFVFKAGNIV 614
Cdd:COG1101 171 LLDEHTAALDPKTAALVLELTEKivEENNLTTLMVTHNMEqALDYGNRLIMMHEGRII 228
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1028-1257 |
6.11e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 105.99 E-value: 6.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1028 ISIRNVFFNYptRKDTkvlqGFTLD-----IKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGMIMIDGDNIRNLNISSL 1102
Cdd:PRK13648 8 IVFKNVSFQY--QSDA----SFTLKdvsfnIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1103 REQVCIVSQEP--TLFDCTIGENICYG-TNRNVTYQEIVEAAKMAnihnfiLGLPDGYDTHVGEKGTqLSGGQKQRIAIA 1179
Cdd:PRK13648 82 RKHIGIVFQNPdnQFVGSIVKYDVAFGlENHAVPYDEMHRRVSEA------LKQVDMLERADYEPNA-LSGGQKQRVAIA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1180 RALVRSPSVLLLDEATSALDTESEKIVQEALDAAKQGR--TCLVIAHRLSTIQNSDVIAIVSEGKIVEKGTHDELIRKSE 1257
Cdd:PRK13648 155 GVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFDHAE 234
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
1028-1264 |
6.39e-25 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 113.29 E-value: 6.39e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1028 ISIRNVFFNYPTRKDTKVLQGFTLDIKAGKTVALVGHSGCGK-STIMGLLERFYNQDKGMIMIDGdnirnlnisslreQV 1106
Cdd:PLN03130 615 ISIKNGYFSWDSKAERPTLSNINLDVPVGSLVAIVGSTGEGKtSLISAMLGELPPRSDASVVIRG-------------TV 681
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1107 CIVSQEPTLFDCTIGENICYGTNRN-VTYQEIVEAAKMAniHNFILgLPDGYDTHVGEKGTQLSGGQKQRIAIARALVRS 1185
Cdd:PLN03130 682 AYVPQVSWIFNATVRDNILFGSPFDpERYERAIDVTALQ--HDLDL-LPGGDLTEIGERGVNISGGQKQRVSMARAVYSN 758
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1186 PSVLLLDEATSALDTE-SEKIVQEALDAAKQGRTCLVIAHRLSTIQNSDVIAIVSEGKIVEKGTHDELIRKSEIYQKFCE 1264
Cdd:PLN03130 759 SDVYIFDDPLSALDAHvGRQVFDKCIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSNNGPLFQKLME 838
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
402-613 |
6.73e-25 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 105.53 E-value: 6.73e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 402 KDVHFRYPSRKdihVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDLREVnvhslREQIGIVS 481
Cdd:PRK11247 16 NAVSKRYGERT---VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEA-----REDTRLMF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 482 QEPVLFD-GTIYENIKMG---NEHATHDQVVEACKMANandfikrlpdgygtRVGEKGVQLSGGQKQRIAIARALVKNPK 557
Cdd:PRK11247 88 QDARLLPwKKVIDNVGLGlkgQWRDAALQALAAVGLAD--------------RANEWPAALSGGQKQRVALARALIHRPG 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 124244275 558 ILLLDEATSALDTEAEREVQGALDQ--AQAGRTTIIVAHRLS-TIRNVDRIFVFKAGNI 613
Cdd:PRK11247 154 LLLLDEPLGALDALTRIEMQDLIESlwQQHGFTVLLVTHDVSeAVAMADRVLLIEEGKI 212
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
413-625 |
7.06e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 104.99 E-value: 7.06e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 413 DIHVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYD-----PTKGRVLIDGVDLREVNVHSLREQIGIVSQEP-VL 486
Cdd:PRK14247 15 QVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDIFKMDVIELRRRVQMVFQIPnPI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 487 FDGTIYENIKMG--------NEHATHDQVVEACKMANANDFIKrlpdgygTRVGEKGVQLSGGQKQRIAIARALVKNPKI 558
Cdd:PRK14247 95 PNLSIFENVALGlklnrlvkSKKELQERVRWALEKAQLWDEVK-------DRLDAPAGKLSGGQQQRLCIARALAFQPEV 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 124244275 559 LLLDEATSALDTEAEREVQGALDQAQAGRTTIIVAH-RLSTIRNVDRIFVFKAGNIVESGSHEELMSK 625
Cdd:PRK14247 168 LLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHfPQQAARISDYVAFLYKGQIVEWGPTREVFTN 235
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
120-563 |
8.80e-25 |
|
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: 110.27 E-value: 8.80e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 120 YCIYYLVLGVLMFFTS-YVQIAcFESYAERLVHKLRQNYLKAILRQQIQWFDKQQTGNLTARLTDDLERVREGLGDkFAL 198
Cdd:COG4615 50 LLLLFAGLLVLLLLSRlASQLL-LTRLGQHAVARLRLRLSRRILAAPLERLERIGAARLLAALTEDVRTISQAFVR-LPE 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 199 LVQMFAAFLAGYGVGFFYSWSMTLVMMGFAPLIVLSG-AKMSKSMA--TRTRVEQETYavagaiaeetFSSIRTVhsLNG 275
Cdd:COG4615 128 LLQSVALVLGCLAYLAWLSPPLFLLTLVLLGLGVAGYrLLVRRARRhlRRAREAEDRL----------FKHFRAL--LEG 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 276 HKrEL-------DRFYN-----ALEVGRQTGIVKYCYMGIGVGFSNLCMYSSYALAFWYGSTLIINDPTFDRGLIFTVFF 343
Cdd:COG4615 196 FK-ELklnrrrrRAFFDedlqpTAERYRDLRIRADTIFALANNWGNLLFFALIGLILFLLPALGWADPAVLSGFVLVLLF 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 344 avLSGS-TSLGGALPHLASFGTARGAASTVLRVINSHPKIDPYSLEGILVDNMKGdISFKDVHFRYPSRKDIH--VLKGI 420
Cdd:COG4615 275 --LRGPlSQLVGALPTLSRANVALRKIEELELALAAAEPAAADAAAPPAPADFQT-LELRGVTYRYPGEDGDEgfTLGPI 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 421 SLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDLREVNVHSLREQIGIVSQEPVLFDGTiyenikMGNE 500
Cdd:COG4615 352 DLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQLFSAVFSDFHLFDRL------LGLD 425
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 124244275 501 HATHDqvveackmANANDFIKRLpdGYGTRVGEKG-----VQLSGGQKQRIAIARALVKNPKILLLDE 563
Cdd:COG4615 426 GEADP--------ARARELLERL--ELDHKVSVEDgrfstTDLSQGQRKRLALLVALLEDRPILVFDE 483
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
754-1000 |
9.81e-25 |
|
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: 105.72 E-value: 9.81e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 754 FVLMGITFFVGFFTSAN--CLGRCGESLTMKLRFEAFKNLLRQDIAFYDdlRHGTGKLCTRFATDAPNVRYVFT-RLPVV 830
Cdd:cd18557 40 LILLAIYLLQSVFTFVRyyLFNIAGERIVARLRRDLFSSLLRQEIAFFD--KHKTGELTSRLSSDTSVLQSAVTdNLSQL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 831 LASIVTICGALGIGFYYGWQLALILVVMVPLLVMGGYFemqmrFGKQIR----DTQ-LLEEAGKVASQAVEHIRTVHSLN 905
Cdd:cd18557 118 LRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASKI-----YGRYIRklskEVQdALAKAGQVAEESLSNIRTVRSFS 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 906 RQEQFHFTYCEYLREPFNTNLKHAHTYGAVFAFSQSLIFFMYAAAFYLGSIFVNQQAMQPIDVYRVFFAISFCGQMIGNT 985
Cdd:cd18557 193 AEEKEIRRYSEALDRSYRLARKKALANALFQGITSLLIYLSLLLVLWYGGYLVLSGQLTVGELTSFILYTIMVASSVGGL 272
|
250
....*....|....*
gi 124244275 986 TSFIPDVVKArLAAS 1000
Cdd:cd18557 273 SSLLADIMKA-LGAS 286
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1041-1252 |
1.17e-24 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 104.45 E-value: 1.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1041 KDTKVLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGMI-----MIDGDniRNLN-----ISSLREQVCIVS 1110
Cdd:PRK11264 14 HGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIrvgdiTIDTA--RSLSqqkglIRQLRQHVGFVF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1111 QEPTLFDC-TIGENICYGTnrnVTYQEIVEAAKMANIHNFI--LGLPDGYDTHvgekGTQLSGGQKQRIAIARALVRSPS 1187
Cdd:PRK11264 92 QNFNLFPHrTVLENIIEGP---VIVKGEPKEEATARARELLakVGLAGKETSY----PRRLSGGQQQRVAIARALAMRPE 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1188 VLLLDEATSALDTEsekIVQEALDA----AKQGRTCLVIAHRLSTIQN-SDVIAIVSEGKIVEKGTHDEL 1252
Cdd:PRK11264 165 VILFDEPTSALDPE---LVGEVLNTirqlAQEKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKAL 231
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
1028-1247 |
1.18e-24 |
|
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: 103.07 E-value: 1.18e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1028 ISIRNVFFNYPTRKdtkVLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGMIMIDGDNIRNlNISSLREQVC 1107
Cdd:cd03268 1 LKTNDLTKTYGKKR---VLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQK-NIEALRRIGA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1108 IVSqEPTLFD-CTIGENICY-GTNRNVTYQEIVEAAKMANIHNfilglpdgydtHVGEKGTQLSGGQKQRIAIARALVRS 1185
Cdd:cd03268 77 LIE-APGFYPnLTARENLRLlARLLGIRKKRIDEVLDVVGLKD-----------SAKKKVKGFSLGMKQRLGIALALLGN 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124244275 1186 PSVLLLDEATSALDTESEKIVQEAL-DAAKQGRTCLVIAHRLSTIQN-SDVIAIVSEGKIVEKG 1247
Cdd:cd03268 145 PDLLILDEPTNGLDPDGIKELRELIlSLRDQGITVLISSHLLSEIQKvADRIGIINKGKLIEEG 208
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
121-330 |
1.24e-24 |
|
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: 105.58 E-value: 1.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 121 CIYYLVLGVLMFFTSYVQIACFESYAERLVHKLRQNYLKAILRQQIQWFDKQQTGNLTARLTDDLERVREGLGDKFALLV 200
Cdd:cd18552 42 PLAIIGLFLLRGLASYLQTYLMAYVGQRVVRDLRNDLFDKLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLV 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 201 QMFAAFLAGYGVGFFYSWSMTLVMMGFAPLIVLSGAKMSKSMATRTRVEQETYAVAGAIAEETFSSIRTVHSLNGHKREL 280
Cdd:cd18552 122 RDPLTVIGLLGVLFYLDWKLTLIALVVLPLAALPIRRIGKRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYEI 201
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 124244275 281 DRFYNALE--VGRQTGIVKycYMGIGVGFSNLCMYSSYALAFWYGSTLIIND 330
Cdd:cd18552 202 KRFRKANErlRRLSMKIAR--ARALSSPLMELLGAIAIALVLWYGGYQVISG 251
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
117-329 |
1.52e-24 |
|
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: 105.21 E-value: 1.52e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 117 VVKYCIYYLVLGVLMFFTSYVQIACFESYAERLVHKLRQNYLKAILRQQIQWFDKQQTGNLTARLTDDLERVREGLGDKF 196
Cdd:cd18542 38 LWLLALLILGVALLRGVFRYLQGYLAEKASQKVAYDLRNDLYDHLQRLSFSFHDKARTGDLMSRCTSDVDTIRRFLAFGL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 197 ALLVQMFAAFLAGYGVGFFYSWSMTLVMMGFAPLIVLSGAKMSKSMATRTRVEQETYAVAGAIAEETFSSIRTVHSLNGH 276
Cdd:cd18542 118 VELVRAVLLFIGALIIMFSINWKLTLISLAIIPFIALFSYVFFKKVRPAFEEIREQEGELNTVLQENLTGVRVVKAFARE 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 124244275 277 KRELDRF--YNA--LEVGRQTGIVKYCYMGIGVGFSNLCMyssyALAFWYGSTLIIN 329
Cdd:cd18542 198 DYEIEKFdkENEeyRDLNIKLAKLLAKYWPLMDFLSGLQI----VLVLWVGGYLVIN 250
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
1049-1247 |
1.62e-24 |
|
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: 102.96 E-value: 1.62e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1049 FTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGMIMIDGDNIRNLNISslREQVCIVSQEPTLF-DCTIGENICYG 1127
Cdd:cd03298 17 FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA--DRPVSMLFQENNLFaHLTVEQNVGLG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1128 TN-----RNVTYQEIVEAAKMANIHNFILGLPDgydthvgekgtQLSGGQKQRIAIARALVRSPSVLLLDEATSALDTes 1202
Cdd:cd03298 95 LSpglklTAEDRQAIEVALARVGLAGLEKRLPG-----------ELSGGERQRVALARVLVRDKPVLLLDEPFAALDP-- 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 124244275 1203 eKIVQEALD-----AAKQGRTCLVIAHRLSTIQN-SDVIAIVSEGKIVEKG 1247
Cdd:cd03298 162 -ALRAEMLDlvldlHAETKMTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
413-611 |
1.63e-24 |
|
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: 103.18 E-value: 1.63e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 413 DIHVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDLREVNVHSL----REQIGIVSQEPVLFD 488
Cdd:cd03290 13 GLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATrsrnRYSVAYAAQKPWLLN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 489 GTIYENIKMGN--EHATHDQVVEACKMANANDFikrLPDGYGTRVGEKGVQLSGGQKQRIAIARALVKNPKILLLDEATS 566
Cdd:cd03290 93 ATVEENITFGSpfNKQRYKAVTDACSLQPDIDL---LPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFS 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 124244275 567 ALDTEAEREV--QGALDQAQAG-RTTIIVAHRLSTIRNVDRIFVFKAG 611
Cdd:cd03290 170 ALDIHLSDHLmqEGILKFLQDDkRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
399-625 |
2.05e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 104.86 E-value: 2.05e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 399 ISFKDVHFRY----PSRKDihVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDL----REVNV 470
Cdd:PRK13646 3 IRFDNVSYTYqkgtPYEHQ--AIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIthktKDKYI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 471 HSLREQIGIVSQ--EPVLFDGTIYENIKMGNEHATHDqvVEACKmANANDFIKRLpdGYGTRVGEKG-VQLSGGQKQRIA 547
Cdd:PRK13646 81 RPVRKRIGMVFQfpESQLFEDTVEREIIFGPKNFKMN--LDEVK-NYAHRLLMDL--GFSRDVMSQSpFQMSGGQMRKIA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 548 IARALVKNPKILLLDEATSALDTEAEREVQGALDQAQA--GRTTIIVAHRLSTI-RNVDRIFVFKAGNIVESGSHEELMS 624
Cdd:PRK13646 156 IVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTdeNKTIILVSHDMNEVaRYADEVIVMKEGSIVSQTSPKELFK 235
|
.
gi 124244275 625 K 625
Cdd:PRK13646 236 D 236
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
397-686 |
2.17e-24 |
|
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: 104.55 E-value: 2.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 397 GDISFKDVHFRYPSRKDIhVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDpTKGRVLIDGVDLREVNVHSLREQ 476
Cdd:cd03289 1 GQMTVKDLTAKYTEGGNA-VLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 477 IGIVSQEPVLFDGTIYENIKMGNEHaTHDQVVEACKMANANDFIKRLPDGYGTRVGEKGVQLSGGQKQRIAIARALVKNP 556
Cdd:cd03289 79 FGVIPQKVFIFSGTFRKNLDPYGKW-SDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 557 KILLLDEATSALDTEAEREVQGALDQAQAGRTTIIVAHRLSTIRNVDRIFVFKAGNIVESGSHEELMSKQGIFydmtqaq 636
Cdd:cd03289 158 KILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHF------- 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 124244275 637 vvrqqqqeagkdiEDTISESAHSHL-SRKSSTRSAISIATSIHQLAEEVEE 686
Cdd:cd03289 231 -------------KQAISPSDRLKLfPRRNSSKSKRKPRPQIQALQEETEE 268
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
416-629 |
3.06e-24 |
|
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: 104.17 E-value: 3.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 416 VLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVlidgvdlrevnVHSLReqIGIVSQEPVLFDGTIYENI 495
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKI-----------KHSGR--ISFSSQFSWIMPGTIKENI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 496 KMGnehATHDQ-----VVEACKManaNDFIKRLPDGYGTRVGEKGVQLSGGQKQRIAIARALVKNPKILLLDEATSALDT 570
Cdd:cd03291 119 IFG---VSYDEyryksVVKACQL---EEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDV 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 571 EAEREV-QGALDQAQAGRTTIIVAHRLSTIRNVDRIFVFKAGNIVESGSHEELMSKQGIF 629
Cdd:cd03291 193 FTEKEIfESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSLRPDF 252
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
399-617 |
3.16e-24 |
|
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: 102.45 E-value: 3.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 399 ISFKDVHFRY-PSRKDIHVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDL----REVnvhsl 473
Cdd:cd03266 2 ITADALTKRFrDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVvkepAEA----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 474 REQIGIVSQEPVLFDG-TIYENIKM-----G-NEHATHDQVVEACKMANANDFIKRlpdgygtRVGEkgvqLSGGQKQRI 546
Cdd:cd03266 77 RRRLGFVSDSTGLYDRlTARENLEYfaglyGlKGDELTARLEELADRLGMEELLDR-------RVGG----FSTGMRQKV 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 124244275 547 AIARALVKNPKILLLDEATSALDTEAEREVQGALDQAQAGRTTIIVA-HRLSTIRNV-DRIFVFKAGNIVESG 617
Cdd:cd03266 146 AIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFStHIMQEVERLcDRVVVLHRGRVVYEG 218
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
399-626 |
3.40e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 104.14 E-value: 3.40e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 399 ISFKDVHFRYPSRKDIHV--LKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDLR----EVNVHS 472
Cdd:PRK13641 3 IKFENVDYIYSPGTPMEKkgLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgNKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 473 LREQIGIVSQ--EPVLFDGTIYENIKMG--NEHATHDQVVEAckmanANDFIKRLpdGYGTRVGEKG-VQLSGGQKQRIA 547
Cdd:PRK13641 83 LRKKVSLVFQfpEAQLFENTVLKDVEFGpkNFGFSEDEAKEK-----ALKWLKKV--GLSEDLISKSpFELSGGQMRRVA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 548 IARALVKNPKILLLDEATSALDTEAEREV-QGALDQAQAGRTTIIVAHRLSTIRN-VDRIFVFKAGNIVESGSHEELMSK 625
Cdd:PRK13641 156 IAGVMAYEPEILCLDEPAAGLDPEGRKEMmQLFKDYQKAGHTVILVTHNMDDVAEyADDVLVLEHGKLIKHASPKEIFSD 235
|
.
gi 124244275 626 Q 626
Cdd:PRK13641 236 K 236
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
415-622 |
3.52e-24 |
|
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: 102.60 E-value: 3.52e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 415 HVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDLREVNVHSL-REQIGIVSQEPVLF-DGTIY 492
Cdd:TIGR03410 14 HILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERaRAGIAYVPQGREIFpRLTVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 493 ENIKMG------NEHATHDQVVE---ACKmananDFIKRlpdgygtrvgeKGVQLSGGQKQRIAIARALVKNPKILLLDE 563
Cdd:TIGR03410 94 ENLLTGlaalprRSRKIPDEIYElfpVLK-----EMLGR-----------RGGDLSGGQQQQLAIARALVTRPKLLLLDE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124244275 564 ATSALDTEAEREVQGALDQ--AQAGRTTIIVAHRLSTIRNV-DRIFVFKAGNIVESGSHEEL 622
Cdd:TIGR03410 158 PTEGIQPSIIKDIGRVIRRlrAEGGMAILLVEQYLDFARELaDRYYVMERGRVVASGAGDEL 219
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
416-624 |
4.43e-24 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 102.78 E-value: 4.43e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 416 VLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDLREVNVHSLREQIGIVSQEPVLFDG-TIYEN 494
Cdd:PRK11231 17 ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHHLTPEGiTVREL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 495 IKMG-------------NEHATHDQVVEACKMANANDfiKRLPDgygtrvgekgvqLSGGQKQRIAIARALVKNPKILLL 561
Cdd:PRK11231 97 VAYGrspwlslwgrlsaEDNARVNQAMEQTRINHLAD--RRLTD------------LSGGQRQRAFLAMVLAQDTPVVLL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 124244275 562 DEATSALDTEAEREVQGALDQ-AQAGRTTIIVAHRLS-TIRNVDRIFVFKAGNIVESGSHEELMS 624
Cdd:PRK11231 163 DEPTTYLDINHQVELMRLMRElNTQGKTVVTVLHDLNqASRYCDHLVVLANGHVMAQGTPEEVMT 227
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
417-594 |
5.59e-24 |
|
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: 101.77 E-value: 5.59e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 417 LKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDLREVNVHSLreqigIVSQEPVLFDG-TIYENI 495
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM-----VVFQNYSLLPWlTVRENI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 496 KMGNEHATHDqVVEACKMANANDFIKRLpdGYGTRVGEKGVQLSGGQKQRIAIARALVKNPKILLLDEATSALDTEAERE 575
Cdd:TIGR01184 76 ALAVDRVLPD-LSKSERRAIVEEHIALV--GLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGN 152
|
170 180
....*....|....*....|.
gi 124244275 576 VQGALDQ--AQAGRTTIIVAH 594
Cdd:TIGR01184 153 LQEELMQiwEEHRVTVLMVTH 173
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
1042-1252 |
5.64e-24 |
|
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: 101.74 E-value: 5.64e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1042 DTKVLQGFTLDIKAGKTVALVGHSGCGKST----IMGLLERFynqdKGMIMIDGDNIRNLniSS---LREQVCIVSQEPT 1114
Cdd:cd03224 12 KSQILFGVSLTVPEGEIVALLGRNGAGKTTllktIMGLLPPR----SGSIRFDGRDITGL--PPherARAGIGYVPEGRR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1115 LF-DCTIGENICYG--TNRNVTYQEIVEAakmanihnfILGL-PDGYDTHvGEKGTQLSGGQKQRIAIARALVRSPSVLL 1190
Cdd:cd03224 86 IFpELTVEENLLLGayARRRAKRKARLER---------VYELfPRLKERR-KQLAGTLSGGEQQMLAIARALMSRPKLLL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 124244275 1191 LDEATSALdteSEKIVQEALDA----AKQGRTCLVIAHRLSTIQN-SDVIAIVSEGKIVEKGTHDEL 1252
Cdd:cd03224 156 LDEPSEGL---APKIVEEIFEAirelRDEGVTILLVEQNARFALEiADRAYVLERGRVVLEGTAAEL 219
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
1028-1248 |
5.82e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 103.29 E-value: 5.82e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1028 ISIRNVFFNYP--TRKDTKVLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGMIMIDGDNI----RNLNISS 1101
Cdd:PRK13649 3 INLQNVSYTYQagTPFEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLItstsKNKDIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1102 LREQVCIVSQ--EPTLFDCTIGENICYGTNRNVTYQEivEAAKMANIHNFILGLPDGYdthVGEKGTQLSGGQKQRIAIA 1179
Cdd:PRK13649 83 IRKKVGLVFQfpESQLFEETVLKDVAFGPQNFGVSQE--EAEALAREKLALVGISESL---FEKNPFELSGGQMRRVAIA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124244275 1180 RALVRSPSVLLLDEATSALDTESEKivqEALDAAKQ----GRTCLVIAHRLSTIQN-SDVIAIVSEGKIVEKGT 1248
Cdd:PRK13649 158 GILAMEPKILVLDEPTAGLDPKGRK---ELMTLFKKlhqsGMTIVLVTHLMDDVANyADFVYVLEKGKLVLSGK 228
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
1029-1231 |
6.06e-24 |
|
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: 101.07 E-value: 6.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1029 SIRNVFFNYPTRKdtkVLQGFTLDIKAGKTVALVGHSGCGKST----IMGLLERfynqDKGMIMIDGdnirnLNISSLRE 1104
Cdd:cd03235 1 EVEDLTVSYGGHP---VLEDVSFEVKPGEFLAIVGPNGAGKSTllkaILGLLKP----TSGSIRVFG-----KPLEKERK 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1105 QVCIVSQEpTLFDCT-------------IGENICYGTNRNVTYQEIVEAAKMANIHNFIlglpdgyDTHVGEkgtqLSGG 1171
Cdd:cd03235 69 RIGYVPQR-RSIDRDfpisvrdvvlmglYGHKGLFRRLSKADKAKVDEALERVGLSELA-------DRQIGE----LSGG 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 124244275 1172 QKQRIAIARALVRSPSVLLLDEATSALDTESEKIVQEALDAAKQ-GRTCLVIAHRLSTIQN 1231
Cdd:cd03235 137 QQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRReGMTILVVTHDLGLVLE 197
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
400-623 |
6.34e-24 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 102.94 E-value: 6.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 400 SFKDVHFRYPSRKDIHVLkgiSLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDLREVNVHSLREQIGI 479
Cdd:PRK10575 13 ALRNVSFRVPGRTLLHPL---SLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 480 VSQEPVLFDG-TIYENIKMGNE--H--------ATHDQVVEACKMANANDFIKRLPDgygtrvgekgvQLSGGQKQRIAI 548
Cdd:PRK10575 90 LPQQLPAAEGmTVRELVAIGRYpwHgalgrfgaADREKVEEAISLVGLKPLAHRLVD-----------SLSGGERQRAWI 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 124244275 549 ARALVKNPKILLLDEATSALDTEAEREVQGALDQ--AQAGRTTIIVAHRLS-TIRNVDRIFVFKAGNIVESGSHEELM 623
Cdd:PRK10575 159 AMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRlsQERGLTVIAVLHDINmAARYCDYLVALRGGEMIAQGTPAELM 236
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1038-1247 |
6.54e-24 |
|
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: 100.70 E-value: 6.54e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1038 PTRKDTKVLQGFTLDIKAGKTVALVGHSGCGKSTIMGLL--ERFYNQDKGMIMIDGdniRNLNISSLREQVCIVSQEPTL 1115
Cdd:cd03213 17 PSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLING---RPLDKRSFRKIIGYVPQDDIL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1116 FDC-TIGENICYgtnrnvtyqeiveAAKManihnfilglpdgydthvgeKGtqLSGGQKQRIAIARALVRSPSVLLLDEA 1194
Cdd:cd03213 94 HPTlTVRETLMF-------------AAKL--------------------RG--LSGGERKRVSIALELVSNPSLLFLDEP 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 124244275 1195 TSALDTESEKIVQEALDA-AKQGRTCLVIAHRLST--IQNSDVIAIVSEGKIVEKG 1247
Cdd:cd03213 139 TSGLDSSSALQVMSLLRRlADTGRTIICSIHQPSSeiFELFDKLLLLSQGRVIYFG 194
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
1028-1241 |
1.14e-23 |
|
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: 100.87 E-value: 1.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1028 ISIRNVFFNYPTrkDTKVLQGFTLDIKAGKTVALVGHSGCGKST----IMGLLER------FYNQDKGMIMIDGDNIRNl 1097
Cdd:cd03290 1 VQVTNGYFSWGS--GLATLSNINIRIPTGQLTMIVGQVGCGKSSlllaILGEMQTlegkvhWSNKNESEPSFEATRSRN- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1098 nisslREQVCIVSQEPTLFDCTIGENICYGTNRNVT-YQEIVEAAkmaNIHNFILGLPDGYDTHVGEKGTQLSGGQKQRI 1176
Cdd:cd03290 78 -----RYSVAYAAQKPWLLNATVEENITFGSPFNKQrYKAVTDAC---SLQPDIDLLPFGDQTEIGERGINLSGGQRQRI 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 124244275 1177 AIARALVRSPSVLLLDEATSALDTE-SEKIVQEALDAAKQG--RTCLVIAHRLSTIQNSDVIAIVSEG 1241
Cdd:cd03290 150 CVARALYQNTNIVFLDDPFSALDIHlSDHLMQEGILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
420-624 |
1.18e-23 |
|
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: 104.04 E-value: 1.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 420 ISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDLRE----VNVHSLREQIGIVSQEPVLFDG-TIYEN 494
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDsrkgIFLPPEKRRIGYVFQEARLFPHlSVRGN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 495 IKMGNEHATHDQVV----EACKMANANDFIKRLPDgygtrvgekgvQLSGGQKQRIAIARALVKNPKILLLDEATSALDT 570
Cdd:TIGR02142 96 LRYGMKRARPSERRisfeRVIELLGIGHLLGRLPG-----------RLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDD 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 124244275 571 EAEREVQGALDQ--AQAGRTTIIVAHRLSTI-RNVDRIFVFKAGNIVESGSHEELMS 624
Cdd:TIGR02142 165 PRKYEILPYLERlhAEFGIPILYVSHSLQEVlRLADRVVVLEDGRVAAAGPIAEVWA 221
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
337-595 |
1.32e-23 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 106.82 E-value: 1.32e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 337 LIFTVFFA---VLSGSTSLGGALPHLASFGTARGA--------------ASTVLRVI-----NSHPKIDPYSLEGILVDN 394
Cdd:COG4178 280 VIFPILVAaprYFAGEITLGGLMQAASAFGQVQGAlswfvdnyqslaewRATVDRLAgfeeaLEAADALPEAASRIETSE 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 395 mKGDISFKDVHFRYPSRKDIhvLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLI-DGvdlrevnvhsl 473
Cdd:COG4178 360 -DGALALEDLTLRTPDGRPL--LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpAG----------- 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 474 rEQIGIVSQEPVLFDGT-----IYENikmGNEHATHDQVVEACKMANANDFIKRLpdgygTRVGEKGVQLSGGQKQRIAI 548
Cdd:COG4178 426 -ARVLFLPQRPYLPLGTlrealLYPA---TAEAFSDAELREALEAVGLGHLAERL-----DEEADWDQVLSLGEQQRLAF 496
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 124244275 549 ARALVKNPKILLLDEATSALDTEAEREVQGALDQAQAGRTTIIVAHR 595
Cdd:COG4178 497 ARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHR 543
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
402-620 |
1.43e-23 |
|
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: 99.91 E-value: 1.43e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 402 KDVHFrypSRKDIHVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRF--YDPTKGRVLIDGVDLREVNVHS-LREQIG 478
Cdd:cd03217 4 KDLHV---SVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPEErARLGIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 479 IVSQEPVLFDGtiyenIKMgnehathdqvveackmanaNDFIKRLPDGygtrvgekgvqLSGGQKQRIAIARALVKNPKI 558
Cdd:cd03217 81 LAFQYPPEIPG-----VKN-------------------ADFLRYVNEG-----------FSGGEKKRNEILQLLLLEPDL 125
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 124244275 559 LLLDEATSALDTEAEREVQGALDQ-AQAGRTTIIVAH--RLSTIRNVDRIFVFKAGNIVESGSHE 620
Cdd:cd03217 126 AILDEPDSGLDIDALRLVAEVINKlREEGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVKSGDKE 190
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1028-1261 |
1.90e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 101.83 E-value: 1.90e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1028 ISIRNVFFNYP--TRKDTKVLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGMIMIDGDNIR----NLNISS 1101
Cdd:PRK13641 3 IKFENVDYIYSpgTPMEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgNKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1102 LREQVCIVSQ--EPTLFDCTIGENICYG-TNRNVTYQEIVEAAK--MANIhnfilglpdGYDTHVGEKGT-QLSGGQKQR 1175
Cdd:PRK13641 83 LRKKVSLVFQfpEAQLFENTVLKDVEFGpKNFGFSEDEAKEKALkwLKKV---------GLSEDLISKSPfELSGGQMRR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1176 IAIARALVRSPSVLLLDEATSALDTESEK-IVQEALDAAKQGRTCLVIAHRLSTI-QNSDVIAIVSEGKIVEKGTHDELI 1253
Cdd:PRK13641 154 VAIAGVMAYEPEILCLDEPAAGLDPEGRKeMMQLFKDYQKAGHTVILVTHNMDDVaEYADDVLVLEHGKLIKHASPKEIF 233
|
....*...
gi 124244275 1254 RKSEIYQK 1261
Cdd:PRK13641 234 SDKEWLKK 241
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
413-624 |
2.35e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 100.89 E-value: 2.35e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 413 DIHVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRF---YDP---TKGRVLIDGVDLREVNVHSLREQIGIVSQEPVL 486
Cdd:PRK14246 22 DKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLieiYDSkikVDGKVLYFGKDIFQIDAIKLRKEVGMVFQQPNP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 487 FDG-TIYENIKMG-NEHATHDQ-----VVEACkmANANDFIKRLPDgygtRVGEKGVQLSGGQKQRIAIARALVKNPKIL 559
Cdd:PRK14246 102 FPHlSIYDNIAYPlKSHGIKEKreikkIVEEC--LRKVGLWKEVYD----RLNSPASQLSGGQQQRLTIARALALKPKVL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 124244275 560 LLDEATSALDTEAEREVQGALDQAQAGRTTIIVAHRLSTI-RNVDRIFVFKAGNIVESGSHEELMS 624
Cdd:PRK14246 176 LMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVaRVADYVAFLYNGELVEWGSSNEIFT 241
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
403-628 |
2.45e-23 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 101.24 E-value: 2.45e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 403 DVHFRYpsrKDIHVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDG--VDLREVNVHSLREQIGIV 480
Cdd:PRK13638 6 DLWFRY---QDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGkpLDYSKRGLLALRQQVATV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 481 SQEPvlfDGTI-YENIKMGNEHATHDQVVEACKMANANDFIKRLPDGYGTRvgEKGVQ-LSGGQKQRIAIARALVKNPKI 558
Cdd:PRK13638 83 FQDP---EQQIfYTDIDSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFR--HQPIQcLSHGQKKRVAIAGALVLQARY 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 124244275 559 LLLDEATSALDTEAEREVQGALDQ-AQAGRTTIIVAHRLSTIRNV-DRIFVFKAGNIVESG------SHEELMSKQGI 628
Cdd:PRK13638 158 LLLDEPTAGLDPAGRTQMIAIIRRiVAQGNHVIISSHDIDLIYEIsDAVYVLRQGQILTHGapgevfACTEAMEQAGL 235
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
1028-1257 |
2.98e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 101.64 E-value: 2.98e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1028 ISIRNVFFNYPTRK--DTKVLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGMIMIDGDNI----RNLNISS 1101
Cdd:PRK13634 3 ITFQKVEHRYQYKTpfERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVItagkKNKKLKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1102 LREQVCIVSQ--EPTLFDCTIGENICYG-TNRNVTYQEIVE-AAKMANIhnfiLGLPDGYDTHvgeKGTQLSGGQKQRIA 1177
Cdd:PRK13634 83 LRKKVGIVFQfpEHQLFEETVEKDICFGpMNFGVSEEDAKQkAREMIEL----VGLPEELLAR---SPFELSGGQMRRVA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1178 IARALVRSPSVLLLDEATSALDTESEKIVQEALDA--AKQGRTCLVIAHRLSTIQN-SDVIAIVSEGKIVEKGTHDELIR 1254
Cdd:PRK13634 156 IAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKlhKEKGLTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTPREIFA 235
|
...
gi 124244275 1255 KSE 1257
Cdd:PRK13634 236 DPD 238
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
115-329 |
3.32e-23 |
|
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: 101.33 E-value: 3.32e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 115 SEVVKYCIYYLVLGVLMFFTSYVQIACFESYAERLVHKLRQNYLKAILRQQIQWFDKQQTGNLTARLTDDLERVREGLGd 194
Cdd:cd18541 37 SQLLRYALLILLLALLIGIFRFLWRYLIFGASRRIEYDLRNDLFAHLLTLSPSFYQKNRTGDLMARATNDLNAVRMALG- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 195 kFALLVQMFAAFLAGYGVG--FFYSWSMTLVMMGFAPLIVLSGAKMSKSMATRTRVEQETYAVAGAIAEETFSSIRTVHS 272
Cdd:cd18541 116 -PGILYLVDALFLGVLVLVmmFTISPKLTLIALLPLPLLALLVYRLGKKIHKRFRKVQEAFSDLSDRVQESFSGIRVIKA 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 124244275 273 LNGHKRELDRFYNALE--VGRQTGIVKycYMGIGVGFSNLCMYSSYALAFWYGSTLIIN 329
Cdd:cd18541 195 FVQEEAEIERFDKLNEeyVEKNLRLAR--VDALFFPLIGLLIGLSFLIVLWYGGRLVIR 251
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
752-1193 |
3.79e-23 |
|
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: 105.27 E-value: 3.79e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 752 GMFVLMGITFFVGFFTSANCLGRCGESLTMKLRFEAFKNLLRQDIAFYDdlRHGTGKLCTRFATDAPNVRYVFTRLPVVL 831
Cdd:COG4615 52 LLFAGLLVLLLLSRLASQLLLTRLGQHAVARLRLRLSRRILAAPLERLE--RIGAARLLAALTEDVRTISQAFVRLPELL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 832 ASIVTICGALGIGFYYGWQLALILVVMVPLLVMGGYFEMQ--MRFGKQIRDTQlleeagkvaSQAVEHIRTVHS------ 903
Cdd:COG4615 130 QSVALVLGCLAYLAWLSPPLFLLTLVLLGLGVAGYRLLVRraRRHLRRAREAE---------DRLFKHFRALLEgfkelk 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 904 LNRQEQFHFtYCEYLREPFNT----NLKHAHTYGAVFAFSQSLIFFMYAAAFYLgsiFVNQQAMQPIDVYRVFFAISFcg 979
Cdd:COG4615 201 LNRRRRRAF-FDEDLQPTAERyrdlRIRADTIFALANNWGNLLFFALIGLILFL---LPALGWADPAVLSGFVLVLLF-- 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 980 qMIG---NTTSFIPDVVKARLA----ASLLFYLIEHPTPIDSLSDSGIVKPITGnISIRNVFFNYPTRKDTKvlqGFT-- 1050
Cdd:COG4615 275 -LRGplsQLVGALPTLSRANVAlrkiEELELALAAAEPAAADAAAPPAPADFQT-LELRGVTYRYPGEDGDE---GFTlg 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1051 ---LDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGMIMIDGDNIRNLNISSLREQVCIVSQEPTLFDctigenicyg 1127
Cdd:COG4615 350 pidLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQLFSAVFSDFHLFD---------- 419
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 124244275 1128 tnRNVTYQEIVEAAKmanIHNFI--LGLpdgyDTHVGEKG-----TQLSGGQKQRIAIARALVRSPSVLLLDE 1193
Cdd:COG4615 420 --RLLGLDGEADPAR---ARELLerLEL----DHKVSVEDgrfstTDLSQGQRKRLALLVALLEDRPILVFDE 483
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
412-620 |
3.94e-23 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 99.76 E-value: 3.94e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 412 KDIHV-------LKGISLELKAGDKIALVGSSGCGKSTIVNLL--QRFYDPTKGRVLIDGVDLREVNVHSlREQIGI-VS 481
Cdd:COG0396 4 KNLHVsvegkeiLKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLmgHPKYEVTSGSILLDGEDILELSPDE-RARAGIfLA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 482 -QEPVLFDG--------TIYENIKMGNEHAT--HDQVVEACKMAN-ANDFIKR-LPDGygtrvgekgvqLSGGQKQRIAI 548
Cdd:COG0396 83 fQYPVEIPGvsvsnflrTALNARRGEELSARefLKLLKEKMKELGlDEDFLDRyVNEG-----------FSGGEKKRNEI 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 124244275 549 ARALVKNPKILLLDEATSALDTEAEREV-QGALDQAQAGRTTIIVAH--RLSTIRNVDRIFVFKAGNIVESGSHE 620
Cdd:COG0396 152 LQMLLLEPKLAILDETDSGLDIDALRIVaEGVNKLRSPDRGILIITHyqRILDYIKPDFVHVLVDGRIVKSGGKE 226
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
1043-1202 |
4.09e-23 |
|
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: 102.49 E-value: 4.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1043 TKVLQGFTLDIK-----AGKTvALVGHSGCGKSTIMGL---LERFynqDKGMIMIDG----DNIRNLNISSLREQVCIVS 1110
Cdd:COG4148 8 RLRRGGFTLDVDftlpgRGVT-ALFGPSGSGKTTLLRAiagLERP---DSGRIRLGGevlqDSARGIFLPPHRRRIGYVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1111 QEPTLFD-CTIGENICYG------TNRNVTYQEIVEaakmanihnfILGLpdgydTHVGEKG-TQLSGGQKQRIAIARAL 1182
Cdd:COG4148 84 QEARLFPhLSVRGNLLYGrkraprAERRISFDEVVE----------LLGI-----GHLLDRRpATLSGGERQRVAIGRAL 148
|
170 180
....*....|....*....|
gi 124244275 1183 VRSPSVLLLDEATSALDTES 1202
Cdd:COG4148 149 LSSPRLLLMDEPLAALDLAR 168
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
1044-1256 |
5.49e-23 |
|
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: 102.11 E-value: 5.49e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1044 KVLQGFTLDIK----AGKTVALVGHSGCGKSTIMGLLERFYNQDKGMIMIDG----DNIRNLNISSLREQVCIVSQEPTL 1115
Cdd:TIGR02142 7 KRLGDFSLDADftlpGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGrtlfDSRKGIFLPPEKRRIGYVFQEARL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1116 F-DCTIGENICYG------TNRNVTYQEIVEaakmanihnfILGLpdgydTHVGEKGT-QLSGGQKQRIAIARALVRSPS 1187
Cdd:TIGR02142 87 FpHLSVRGNLRYGmkrarpSERRISFERVIE----------LLGI-----GHLLGRLPgRLSGGEKQRVAIGRALLSSPR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124244275 1188 VLLLDEATSALDTESEKIVQEALD--AAKQGRTCLVIAHRLSTIQN-SDVIAIVSEGKIVEKGTHDELIRKS 1256
Cdd:TIGR02142 152 LLLMDEPLAALDDPRKYEILPYLErlHAEFGIPILYVSHSLQEVLRlADRVVVLEDGRVAAAGPIAEVWASP 223
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
400-624 |
6.53e-23 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 99.91 E-value: 6.53e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 400 SFKDvHFRYPSRKDIHVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDLREVN---------- 469
Cdd:COG4167 13 TFKY-RTGLFRRQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDykyrckhirm 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 470 -----VHSL--REQIGIVSQEPVLFdgtiyeNIKMgNEHATHDQVVEACKMA-----NANDFIKrlpdgygtrvgekgvQ 537
Cdd:COG4167 92 ifqdpNTSLnpRLNIGQILEEPLRL------NTDL-TAEEREERIFATLRLVgllpeHANFYPH---------------M 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 538 LSGGQKQRIAIARALVKNPKILLLDEATSALDTEAERE-VQGALD-QAQAGRTTIIVAHRLSTIRNV-DRIFVFKAGNIV 614
Cdd:COG4167 150 LSSGQKQRVALARALILQPKIIIADEALAALDMSVRSQiINLMLElQEKLGISYIYVSQHLGIVKHIsDKVLVMHQGEVV 229
|
250
....*....|
gi 124244275 615 ESGSHEELMS 624
Cdd:COG4167 230 EYGKTAEVFA 239
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
1044-1257 |
6.83e-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: 99.05 E-value: 6.83e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1044 KVLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGMIMIDGDNIRNLNISslreQVC---IVS--QEPTLF-D 1117
Cdd:cd03219 14 VALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPH----EIArlgIGRtfQIPRLFpE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1118 CTIGENI----------CYGTNRNV-TYQEIVEAAkMANIHnfILGLPDGYDTHVGEkgtqLSGGQKQRIAIARALVRSP 1186
Cdd:cd03219 90 LTVLENVmvaaqartgsGLLLARARrEEREARERA-EELLE--RVGLADLADRPAGE----LSYGQQRRLEIARALATDP 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 124244275 1187 SVLLLDEATSAL-DTESEKIVQEALDAAKQGRTCLVIAHRLSTIQN-SDVIAIVSEGKIVEKGTHDElIRKSE 1257
Cdd:cd03219 163 KLLLLDEPAAGLnPEETEELAELIRELRERGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGTPDE-VRNNP 234
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
394-629 |
7.81e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 101.08 E-value: 7.81e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 394 NMKGDISFKDVH----FRYPSRKDIHVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLI-------DG 462
Cdd:PRK13631 15 PLSDDIILRVKNlycvFDEKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyigdKK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 463 VDLREVNVHS---------LREQIGIVSQEP--VLFDGTIYENIKMG-------NEHATHDQVVEACKMANANDFIKRLP 524
Cdd:PRK13631 95 NNHELITNPYskkiknfkeLRRRVSMVFQFPeyQLFKDTIEKDIMFGpvalgvkKSEAKKLAKFYLNKMGLDDSYLERSP 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 525 DGygtrvgekgvqLSGGQKQRIAIARALVKNPKILLLDEATSALDTEAERE-VQGALDQAQAGRTTIIVAHRLSTIRNV- 602
Cdd:PRK13631 175 FG-----------LSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEmMQLILDAKANNKTVFVITHTMEHVLEVa 243
|
250 260
....*....|....*....|....*..
gi 124244275 603 DRIFVFKAGNIVESGSHEELMSKQGIF 629
Cdd:PRK13631 244 DEVIVMDKGKILKTGTPYEIFTDQHII 270
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
411-617 |
9.06e-23 |
|
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: 98.11 E-value: 9.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 411 RKDIHVLKGISLELKAGDKIALVGSSGCGKSTIVNLL---QRFYDPTKGRVLIDGvdlREVNVHSLREQIGIVSQEPVLF 487
Cdd:cd03234 17 NKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAIsgrVEGGGTTSGQILFNG---QPRKPDQFQKCVAYVRQDDILL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 488 DG-TIYENIKMGNEHATHDQVVEACKMANANDF-IKRLPDgygTRVGEKGVQ-LSGGQKQRIAIARALVKNPKILLLDEA 564
Cdd:cd03234 94 PGlTVRETLTYTAILRLPRKSSDAIRKKRVEDVlLRDLAL---TRIGGNLVKgISGGERRRVSIAVQLLWDPKVLILDEP 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 124244275 565 TSALDTEAEREVQGALDQ-AQAGRTTIIVAH--RLSTIRNVDRIFVFKAGNIVESG 617
Cdd:cd03234 171 TSGLDSFTALNLVSTLSQlARRNRIVILTIHqpRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1045-1254 |
1.13e-22 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 99.38 E-value: 1.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1045 VLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGMIMIDGDNIRNLN---ISSLREQVCIVSQE-PTLFDC-- 1118
Cdd:PRK10419 27 VLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNraqRKAFRRDIQMVFQDsISAVNPrk 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1119 TIGEnICYGTNRNVTyqEIVEAAKMANIHNFI--LGLPDgydTHVGEKGTQLSGGQKQRIAIARALVRSPSVLLLDEATS 1196
Cdd:PRK10419 107 TVRE-IIREPLRHLL--SLDKAERLARASEMLraVDLDD---SVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVS 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 124244275 1197 ALDTESEKIVQEALDAAKQ--GRTCLVIAHRLSTIQN-SDVIAIVSEGKIVEKGTHDELIR 1254
Cdd:PRK10419 181 NLDLVLQAGVIRLLKKLQQqfGTACLFITHDLRLVERfCQRVMVMDNGQIVETQPVGDKLT 241
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1022-1252 |
1.14e-22 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 101.84 E-value: 1.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1022 KPITGNISIRNVffnyptrkdTKVLQG------FTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGMIMIDGDNIR 1095
Cdd:PRK11607 14 KALTPLLEIRNL---------TKSFDGqhavddVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1096 NlnISSLREQVCIVSQEPTLF-DCTIGENICYGTNrnvtyQEIVEAAKMANIHNFILGLpdgydTHVGE----KGTQLSG 1170
Cdd:PRK11607 85 H--VPPYQRPINMMFQSYALFpHMTVEQNIAFGLK-----QDKLPKAEIASRVNEMLGL-----VHMQEfakrKPHQLSG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1171 GQKQRIAIARALVRSPSVLLLDEATSALDTE-SEKIVQEALDAAKQ-GRTCLVIAH-RLSTIQNSDVIAIVSEGKIVEKG 1247
Cdd:PRK11607 153 GQRQRVALARSLAKRPKLLLLDEPMGALDKKlRDRMQLEVVDILERvGVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIG 232
|
....*
gi 124244275 1248 THDEL 1252
Cdd:PRK11607 233 EPEEI 237
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
417-622 |
1.45e-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: 97.44 E-value: 1.45e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 417 LKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDL----REVnvhslREQIGIVSQEPVLFDG-TI 491
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVvrepREV-----RRRIGIVFQDLSVDDElTG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 492 YENIKMgneHAThdqvVEACKMANANDFIKRLPDGYGtrVGEKGVQL----SGGQKQRIAIARALVKNPKILLLDEATSA 567
Cdd:cd03265 91 WENLYI---HAR----LYGVPGAERRERIDELLDFVG--LLEAADRLvktySGGMRRRLEIARSLVHRPEVLFLDEPTIG 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 124244275 568 LDTEAEREVQGALDQAQA--GRTTIIVAHRLSTIRNV-DRIFVFKAGNIVESGSHEEL 622
Cdd:cd03265 162 LDPQTRAHVWEYIEKLKEefGMTILLTTHYMEEAEQLcDRVAIIDHGRIIAEGTPEEL 219
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
399-624 |
1.53e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 98.91 E-value: 1.53e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 399 ISFKDVHFRYPSrkDIHVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDLREVN-VHSLREQI 477
Cdd:PRK13644 2 IRLENVSYSYPD--GTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSkLQGIRKLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 478 GIVSQEP-VLFDG-TIYENIKMGNEH------ATHDQVVEACKMANANDFIKRLPDgygtrvgekgvQLSGGQKQRIAIA 549
Cdd:PRK13644 80 GIVFQNPeTQFVGrTVEEDLAFGPENlclppiEIRKRVDRALAEIGLEKYRHRSPK-----------TLSGGQGQCVALA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 124244275 550 RALVKNPKILLLDEATSALDTEAEREVQGALDQA-QAGRTTIIVAHRLSTIRNVDRIFVFKAGNIVESGSHEELMS 624
Cdd:PRK13644 149 GILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLhEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLS 224
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
1050-1253 |
1.71e-22 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 101.65 E-value: 1.71e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1050 TLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGMIMIDGDNIRNLNISSLRE----QVCIVSQEPTLF-DCTIGENI 1124
Cdd:PRK10070 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREvrrkKIAMVFQSFALMpHMTVLDNT 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1125 CYGTN-----RNVTYQEIVEAAKMANIHNFILGLPDgydthvgekgtQLSGGQKQRIAIARALVRSPSVLLLDEATSALD 1199
Cdd:PRK10070 128 AFGMElaginAEERREKALDALRQVGLENYAHSYPD-----------ELSGGMRQRVGLARALAINPDILLMDEAFSALD 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 124244275 1200 TESEKIVQEALDA--AKQGRTCLVIAHRL-STIQNSDVIAIVSEGKIVEKGTHDELI 1253
Cdd:PRK10070 197 PLIRTEMQDELVKlqAKHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
1046-1226 |
1.83e-22 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 98.32 E-value: 1.83e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1046 LQGFTLDIKAGKTVALVGHSGCGKSTIMglleRFYNQ---------DKGMIMIDGDNIRNLNI--SSLREQVCIVSQEPT 1114
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTIL----RCFNRlndlipgfrVEGKVTFHGKNLYAPDVdpVEVRRRIGMVFQKPN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1115 LFDCTIGENICYGTNRNvTYQ----EIVEAA-KMAnihnfilGLPDGYDTHVGEKGTQLSGGQKQRIAIARALVRSPSVL 1189
Cdd:PRK14243 102 PFPKSIYDNIAYGARIN-GYKgdmdELVERSlRQA-------ALWDEVKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVI 173
|
170 180 190
....*....|....*....|....*....|....*..
gi 124244275 1190 LLDEATSALDTESEKIVQEALDAAKQGRTCLVIAHRL 1226
Cdd:PRK14243 174 LMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNM 210
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
405-617 |
1.93e-22 |
|
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: 97.22 E-value: 1.93e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 405 HFRYPSRKDIHVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGvdlrevNVHSLRE-QIGIvsqE 483
Cdd:cd03220 26 LGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG------RVSSLLGlGGGF---N 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 484 PVLfdgTIYENIK-----MGNEHATHDQVVEACKM-ANANDFIKRlpdgygtRVGEkgvqLSGGQKQRIAIARALVKNPK 557
Cdd:cd03220 97 PEL---TGRENIYlngrlLGLSRKEIDEKIDEIIEfSELGDFIDL-------PVKT----YSSGMKARLAFAIATALEPD 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124244275 558 ILLLDEATSALDTEAEREVQGALDQAQA-GRTTIIVAHRLSTIRNV-DRIFVFKAGNIVESG 617
Cdd:cd03220 163 ILLIDEVLAVGDAAFQEKCQRRLRELLKqGKTVILVSHDPSSIKRLcDRALVLEKGKIRFDG 224
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
416-604 |
2.25e-22 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 97.19 E-value: 2.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 416 VLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDLREVNVHS---LR-EQIGIVSQ-EPVLFDGT 490
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAkaeLRnQKLGFIYQfHHLLPDFT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 491 IYENIKM----GNEHATHDQVvEACKMANANdfikrlpdGYGTRVGEKGVQLSGGQKQRIAIARALVKNPKILLLDEATS 566
Cdd:PRK11629 104 ALENVAMplliGKKKPAEINS-RALEMLAAV--------GLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTG 174
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 124244275 567 ALD---TEAEREVQGALDQAQaGRTTIIVAHRLSTIRNVDR 604
Cdd:PRK11629 175 NLDarnADSIFQLLGELNRLQ-GTAFLVVTHDLQLAKRMSR 214
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
399-615 |
3.27e-22 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 102.07 E-value: 3.27e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 399 ISFKDVHFRYPSRKdihVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIdGVDLRevnvhslreqIG 478
Cdd:COG0488 316 LELEGLSKSYGDKT---LLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVK----------IG 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 479 IVSQEPVLFDG--TIYENIKMGNEHATHdqvveackmANANDFIKRL---PDGYGTRVGEkgvqLSGGQKQRIAIARALV 553
Cdd:COG0488 382 YFDQHQEELDPdkTVLDELRDGAPGGTE---------QEVRGYLGRFlfsGDDAFKPVGV----LSGGEKARLALAKLLL 448
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 124244275 554 KNPKILLLDEATSALDTEAEREVQGALDQAQaGrTTIIVAH-R--LSTIrnVDRIFVFKAGNIVE 615
Cdd:COG0488 449 SPPNVLLLDEPTNHLDIETLEALEEALDDFP-G-TVLLVSHdRyfLDRV--ATRILEFEDGGVRE 509
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
1046-1224 |
4.50e-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: 96.38 E-value: 4.50e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1046 LQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGMIMIDGDNIRNLNISSLreqvcIVSQEPTLFD-CTIGENI 1124
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM-----VVFQNYSLLPwLTVRENI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1125 CYGTNRNVTYQEIVEAAKMANIHNFILGLpdgydTHVGEKG-TQLSGGQKQRIAIARALVRSPSVLLLDEATSALDTESE 1203
Cdd:TIGR01184 76 ALAVDRVLPDLSKSERRAIVEEHIALVGL-----TEAADKRpGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTR 150
|
170 180
....*....|....*....|...
gi 124244275 1204 KIVQEAL--DAAKQGRTCLVIAH 1224
Cdd:TIGR01184 151 GNLQEELmqIWEEHRVTVLMVTH 173
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
399-625 |
4.98e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 97.88 E-value: 4.98e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 399 ISFKDVHFRYPSRKDI--HVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDL----REVNVHS 472
Cdd:PRK13643 2 IKFEKVNYTYQPNSPFasRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVsstsKQKEIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 473 LREQIGIVSQEP--VLFDGTIYENIKMG------NEHATHDQVVEACKMAN-ANDFIKRLPdgygtrvgekgVQLSGGQK 543
Cdd:PRK13643 82 VRKKVGVVFQFPesQLFEETVLKDVAFGpqnfgiPKEKAEKIAAEKLEMVGlADEFWEKSP-----------FELSGGQM 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 544 QRIAIARALVKNPKILLLDEATSALDTEAEREVQGALDQA-QAGRTTIIVAHRLSTIRN-VDRIFVFKAGNIVESGSHEE 621
Cdd:PRK13643 151 RRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIhQSGQTVVLVTHLMDDVADyADYVYLLEKGHIISCGTPSD 230
|
....
gi 124244275 622 LMSK 625
Cdd:PRK13643 231 VFQE 234
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1018-1230 |
6.86e-22 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 101.42 E-value: 6.86e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1018 SGIVKPITGNISIRNVFFNypTRKDTKVLQGFTLDIKAGKTVALVGHSGCGKSTIM----GLlerfYNQDKGMIMIDGDn 1093
Cdd:COG4178 353 SRIETSEDGALALEDLTLR--TPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLraiaGL----WPYGSGRIARPAG- 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1094 irnlnisslrEQVCIVSQEPTLFDCTIGENICY-GTNRNVTYQEIVEAAKMANIHNFILGLPDGYD-THVgekgtqLSGG 1171
Cdd:COG4178 426 ----------ARVLFLPQRPYLPLGTLREALLYpATAEAFSDAELREALEAVGLGHLAERLDEEADwDQV------LSLG 489
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 124244275 1172 QKQRIAIARALVRSPSVLLLDEATSALDTESEKIVQEALDAAKQGRTCLVIAHRLSTIQ 1230
Cdd:COG4178 490 EQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHRSTLAA 548
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1042-1262 |
6.92e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 96.65 E-value: 6.92e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1042 DTKVLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGMIMIDGD------NIRNLNISSLREQVCIVSQEPTL 1115
Cdd:PRK14246 22 DKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkDIFQIDAIKLRKEVGMVFQQPNP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1116 F-DCTIGENICY-----GTNRNVTYQEIVEAAKMAnihnfiLGLPDGYDTHVGEKGTQLSGGQKQRIAIARALVRSPSVL 1189
Cdd:PRK14246 102 FpHLSIYDNIAYplkshGIKEKREIKKIVEECLRK------VGLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVL 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 124244275 1190 LLDEATSALDTESEKIVQEALDAAKQGRTCLVIAHRLSTIQN-SDVIAIVSEGKIVEKGTHDELIR--KSEIYQKF 1262
Cdd:PRK14246 176 LMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARvADYVAFLYNGELVEWGSSNEIFTspKNELTEKY 251
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
398-622 |
8.42e-22 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 98.95 E-value: 8.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 398 DISFKDVhfrYPSRKDIHVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDLREVNvHSLREqI 477
Cdd:PRK11000 3 SVTLRNV---TKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVP-PAERG-V 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 478 GIVSQEPVLFDG-TIYENIKMGNEHATHD---------QVVEACKMANandFIKRLPDGygtrvgekgvqLSGGQKQRIA 547
Cdd:PRK11000 78 GMVFQSYALYPHlSVAENMSFGLKLAGAKkeeinqrvnQVAEVLQLAH---LLDRKPKA-----------LSGGQRQRVA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 548 IARALVKNPKILLLDEATSALDteAEREVQGALD----QAQAGRTTIIVAH-RLSTIRNVDRIFVFKAGNIVESGSHEEL 622
Cdd:PRK11000 144 IGRTLVAEPSVFLLDEPLSNLD--AALRVQMRIEisrlHKRLGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
399-624 |
8.57e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 97.46 E-value: 8.57e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 399 ISFKDVHFRYPSRKDIH--VLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVD------------ 464
Cdd:PRK13651 3 IKVKNIVKIFNKKLPTElkALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDeknkkktkekek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 465 -----------LREV-NVHSLREQIGIVSQ--EPVLFDGTIYENI-----KMGNEHAthdqvvEACKMANanDFIKR--L 523
Cdd:PRK13651 83 vleklviqktrFKKIkKIKEIRRRVGVVFQfaEYQLFEQTIEKDIifgpvSMGVSKE------EAKKRAA--KYIELvgL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 524 PDGYGTRvgeKGVQLSGGQKQRIAIARALVKNPKILLLDEATSALDTEAEREVQGALDQA-QAGRTTIIVAHRL-STIRN 601
Cdd:PRK13651 155 DESYLQR---SPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLnKQGKTIILVTHDLdNVLEW 231
|
250 260
....*....|....*....|...
gi 124244275 602 VDRIFVFKAGNIVESGSHEELMS 624
Cdd:PRK13651 232 TKRTIFFKDGKIIKDGDTYDILS 254
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
407-605 |
9.28e-22 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 94.22 E-value: 9.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 407 RYPSRKdihVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVlidgvdlrevnVHSLREQIGIVSQ---E 483
Cdd:NF040873 1 GYGGRP---VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV-----------RRAGGARVAYVPQrseV 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 484 PVLFDGTIYENIKMG--------NEHATHD-QVVEACKMA-NANDFIKRlpdgygtRVGEkgvqLSGGQKQRIAIARALV 553
Cdd:NF040873 67 PDSLPLTVRDLVAMGrwarrglwRRLTRDDrAAVDDALERvGLADLAGR-------QLGE----LSGGQRQRALLAQGLA 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 124244275 554 KNPKILLLDEATSALDTEAEREVQGALDQAQA-GRTTIIVAHRLSTIRNVDRI 605
Cdd:NF040873 136 QEADLLLLDEPTTGLDAESRERIIALLAEEHArGATVVVVTHDLELVRRADPC 188
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1028-1252 |
9.53e-22 |
|
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: 100.91 E-value: 9.53e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1028 ISIRN--VFFNYPTRkDTKVLQGFTLDIKAGKTVALVGHSGCGKS----TIMGLLERFYNQDKGMIMIDGDNIRNLNISS 1101
Cdd:COG4172 7 LSVEDlsVAFGQGGG-TVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1102 LRE----QVCIVSQEP-T----LFdcTIGENIC------YGTNRNVTYQEIVEAAKMANIHN--FILG-LPdgydtHvge 1163
Cdd:COG4172 86 LRRirgnRIAMIFQEPmTslnpLH--TIGKQIAevlrlhRGLSGAAARARALELLERVGIPDpeRRLDaYP-----H--- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1164 kgtQLSGGQKQRIAIARALVRSPSVLLLDEATSALDTesekIVQ-EALD-----AAKQGRTCLVIAHRLSTIQN-SDVIA 1236
Cdd:COG4172 156 ---QLSGGQRQRVMIAMALANEPDLLIADEPTTALDV----TVQaQILDllkdlQRELGMALLLITHDLGVVRRfADRVA 228
|
250
....*....|....*.
gi 124244275 1237 IVSEGKIVEKGTHDEL 1252
Cdd:COG4172 229 VMRQGEIVEQGPTAEL 244
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
1028-1247 |
1.08e-21 |
|
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: 94.57 E-value: 1.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1028 ISIRNVFFNYPtrkDTKVLQGFTLDIKAGKTvALVGHSGCGKSTIMGLLERFYNQDKGMIMIDGDNIRNlNISSLREQVC 1107
Cdd:cd03264 1 LQLENLTKRYG---KKRALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLRRRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1108 IVSQEPTLFDctigenicygtnrNVTYQEIVE-AAKMANIHN--------FILGLPDGYDtHVGEKGTQLSGGQKQRIAI 1178
Cdd:cd03264 76 YLPQEFGVYP-------------NFTVREFLDyIAWLKGIPSkevkarvdEVLELVNLGD-RAKKKIGSLSGGMRRRVGI 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1179 ARALVRSPSVLLLDEATSALDTESEKIVQEALDAAKQGRTCLVIAHRLSTIQNS-DVIAIVSEGKIVEKG 1247
Cdd:cd03264 142 AQALVGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESLcNQVAVLNKGKLVFEG 211
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1029-1258 |
1.11e-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: 95.43 E-value: 1.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1029 SIRNVFFNYPtrkDTKVLQGFTLDIKAGKTVALVGHSGCGKST----IMGLLERFynqdKGMIMIDGDNIRNLNISSL-R 1103
Cdd:COG0410 5 EVENLHAGYG---GIHVLHGVSLEVEEGEIVALLGRNGAGKTTllkaISGLLPPR----SGSIRFDGEDITGLPPHRIaR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1104 EQVCIVSQE----PTLfdcTIGENI---CYGTNRNVTYQEIVEaakmanihnFILGL-PDgydthVGE----KGTQLSGG 1171
Cdd:COG0410 78 LGIGYVPEGrrifPSL---TVEENLllgAYARRDRAEVRADLE---------RVYELfPR-----LKErrrqRAGTLSGG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1172 QKQRIAIARALVRSPSVLLLDEATSALdteSEKIVQEALDA----AKQGRTCLVI---AHRLSTIqnSDVIAIVSEGKIV 1244
Cdd:COG0410 141 EQQMLAIGRALMSRPKLLLLDEPSLGL---APLIVEEIFEIirrlNREGVTILLVeqnARFALEI--ADRAYVLERGRIV 215
|
250
....*....|....
gi 124244275 1245 EKGTHDELIRKSEI 1258
Cdd:COG0410 216 LEGTAAELLADPEV 229
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1042-1257 |
1.17e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 95.68 E-value: 1.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1042 DTKVLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERF--YNQD---KGMIMIDGDNIRNLNISSL--REQVCIVSQEPT 1114
Cdd:PRK14267 16 SNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLleLNEEarvEGEVRLFGRNIYSPDVDPIevRREVGMVFQYPN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1115 LF-DCTIGENICYGTNRNVTYQ------EIVE-AAKMAnihnfilGLPDGYDTHVGEKGTQLSGGQKQRIAIARALVRSP 1186
Cdd:PRK14267 96 PFpHLTIYDNVAIGVKLNGLVKskkeldERVEwALKKA-------ALWDEVKDRLNDYPSNLSGGQRQRLVIARALAMKP 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124244275 1187 SVLLLDEATSALDTESEKIVQEALDAAKQGRTCLVIAHrlSTIQN---SDVIAIVSEGKIVEKGTHDELIRKSE 1257
Cdd:PRK14267 169 KILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTH--SPAQAarvSDYVAFLYLGKLIEVGPTRKVFENPE 240
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1028-1261 |
1.23e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 96.46 E-value: 1.23e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1028 ISIRNVFFNYPtrKDTKVLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGMIMIDGDNI--RNLNISSLREQ 1105
Cdd:PRK13636 6 LKVEELNYNYS--DGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIdySRKGLMKLRES 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1106 VCIVSQEP--TLFDCTIGENICYGT-NRNVTYQEIVEAAKMANIHNFIlglpdgydTHVGEKGTQ-LSGGQKQRIAIARA 1181
Cdd:PRK13636 84 VGMVFQDPdnQLFSASVYQDVSFGAvNLKLPEDEVRKRVDNALKRTGI--------EHLKDKPTHcLSFGQKKRVAIAGV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1182 LVRSPSVLLLDEATSALD----TESEKIVQEALDaaKQGRTCLVIAHRLSTIQ-NSDVIAIVSEGKIVEKGTHDELIRKS 1256
Cdd:PRK13636 156 LVMEPKVLVLDEPTAGLDpmgvSEIMKLLVEMQK--ELGLTIIIATHDIDIVPlYCDNVFVMKEGRVILQGNPKEVFAEK 233
|
....*
gi 124244275 1257 EIYQK 1261
Cdd:PRK13636 234 EMLRK 238
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
399-624 |
1.56e-21 |
|
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: 100.26 E-value: 1.56e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 399 ISFKDVHFRYPS--RKDIHVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRV-------LIDGVDLREVN 469
Cdd:TIGR03269 280 IKVRNVSKRYISvdRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnvrvgdeWVDMTKPGPDG 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 470 VHSLREQIGIVSQEPVLF-DGTIYENI----------KMGNEHATHDQVVEACKMANANDFIKRLPDgygtrvgekgvQL 538
Cdd:TIGR03269 360 RGRAKRYIGILHQEYDLYpHRTVLDNLteaiglelpdELARMKAVITLKMVGFDEEKAEEILDKYPD-----------EL 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 539 SGGQKQRIAIARALVKNPKILLLDEATSALDTEAEREVQGALDQA--QAGRTTIIVAHRLSTIRNV-DRIFVFKAGNIVE 615
Cdd:TIGR03269 429 SEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAreEMEQTFIIVSHDMDFVLDVcDRAALMRDGKIVK 508
|
....*....
gi 124244275 616 SGSHEELMS 624
Cdd:TIGR03269 509 IGDPEEIVE 517
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1027-1254 |
1.81e-21 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 97.46 E-value: 1.81e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1027 NISIRNV--FFNYptrkdTKVLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGMIMIDGDNIRNLnisSLRE 1104
Cdd:PRK10851 2 SIEIANIkkSFGR-----TQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRL---HARD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1105 -QVCIVSQEPTLF-DCTIGENICYG---------TNRNVTYQEIVEAAKMANIhnfilglpdgydTHVGEK-GTQLSGGQ 1172
Cdd:PRK10851 74 rKVGFVFQHYALFrHMTVFDNIAFGltvlprrerPNAAAIKAKVTQLLEMVQL------------AHLADRyPAQLSGGQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1173 KQRIAIARALVRSPSVLLLDEATSALDTESEKIVQEALDAAKQ--GRTCLVIAH-RLSTIQNSDVIAIVSEGKIVEKGTH 1249
Cdd:PRK10851 142 KQRVALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEelKFTSVFVTHdQEEAMEVADRVVVMSQGNIEQAGTP 221
|
....*
gi 124244275 1250 DELIR 1254
Cdd:PRK10851 222 DQVWR 226
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1039-1201 |
2.20e-21 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 93.70 E-value: 2.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1039 TRKDTKVLQGFTLDIKAGKTVALVGHSGCGKST----IMGLLER-FYNQdkGMIMIDGDNIRNLNIssLREQVCIVSQEP 1113
Cdd:COG4136 10 TLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTllaaIAGTLSPaFSAS--GEVLLNGRRLTALPA--EQRRIGILFQDD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1114 TLFD-CTIGENICYGTNRNVTYQE---IVEAAkMANIhnfilGLPDGYDTHVGekgtQLSGGQKQRIAIARALVRSPSVL 1189
Cdd:COG4136 86 LLFPhLSVGENLAFALPPTIGRAQrraRVEQA-LEEA-----GLAGFADRDPA----TLSGGQRARVALLRALLAEPRAL 155
|
170
....*....|..
gi 124244275 1190 LLDEATSALDTE 1201
Cdd:COG4136 156 LLDEPFSKLDAA 167
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
1040-1247 |
2.52e-21 |
|
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: 94.26 E-value: 2.52e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1040 RKDTKVLQGFTLDIKAGKTVALVGHSGCGKST----IMGLLERFYNQdKGMIMIDGdniRNLNISSLREQVCIVSQEPTL 1115
Cdd:cd03234 17 NKYARILNDVSLHVESGQVMAILGSSGSGKTTlldaISGRVEGGGTT-SGQILFNG---QPRKPDQFQKCVAYVRQDDIL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1116 FDC-TIGENICY-----GTNRNVTYQEIVEAAkmanihnfILGLPDGYDTHVG-EKGTQLSGGQKQRIAIARALVRSPSV 1188
Cdd:cd03234 93 LPGlTVRETLTYtailrLPRKSSDAIRKKRVE--------DVLLRDLALTRIGgNLVKGISGGERRRVSIAVQLLWDPKV 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124244275 1189 LLLDEATSALDTESE-KIVQEALDAAKQGRTCLVIAH--RLSTIQNSDVIAIVSEGKIVEKG 1247
Cdd:cd03234 165 LILDEPTSGLDSFTAlNLVSTLSQLARRNRIVILTIHqpRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
708-965 |
3.22e-21 |
|
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: 95.57 E-value: 3.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 708 FIGGIFGAFIFGSVTPVFALVYAEIFNVysLPADQMQANVYFWCGMFVLMGITFFVGFFTSANCLGRCGESLTMKLRFEA 787
Cdd:cd18552 1 LALAILGMILVAATTAALAWLLKPLLDD--IFVEKDLEALLLVPLAIIGLFLLRGLASYLQTYLMAYVGQRVVRDLRNDL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 788 FKNLLRQDIAFYDdlRHGTGKLCTRFATDAPNVRYVFTR-LPVVLASIVTICGALGIGFYYGWQLALILVVMVPL--LVM 864
Cdd:cd18552 79 FDKLLRLPLSFFD--RNSSGDLISRITNDVNQVQNALTSaLTVLVRDPLTVIGLLGVLFYLDWKLTLIALVVLPLaaLPI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 865 GgyfemqmRFGKQIRD--TQLLEEAGKVAS---QAVEHIRTVHSLNRQEQFHFTYCEYLREPFNTNLKHAHTYGAVFAFS 939
Cdd:cd18552 157 R-------RIGKRLRKisRRSQESMGDLTSvlqETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIARARALSSPLM 229
|
250 260
....*....|....*....|....*.
gi 124244275 940 QSLIFFMYAAAFYLGSIFVNQQAMQP 965
Cdd:cd18552 230 ELLGAIAIALVLWYGGYQVISGELTP 255
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1028-1250 |
3.63e-21 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 93.93 E-value: 3.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1028 ISIRNVFFNYPTrkdTKVLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGMIMIDGD------NIRNLNISS 1101
Cdd:PRK11124 3 IQLNGINCFYGA---HQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNhfdfskTPSDKAIRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1102 LREQVCIVSQEPTLF-DCTIGENI------CYGTNRNvtyqeivEAAKMANIHNFILGLPDgydtHVGEKGTQLSGGQKQ 1174
Cdd:PRK11124 80 LRRNVGMVFQQYNLWpHLTVQQNLieapcrVLGLSKD-------QALARAEKLLERLRLKP----YADRFPLHLSGGQQQ 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124244275 1175 RIAIARALVRSPSVLLLDEATSALDTE-SEKIVQEALDAAKQGRTCLVIAHRLSTIQN--SDVIAIvSEGKIVEKGTHD 1250
Cdd:PRK11124 149 RVAIARALMMEPQVLLFDEPTAALDPEiTAQIVSIIRELAETGITQVIVTHEVEVARKtaSRVVYM-ENGHIVEQGDAS 226
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1042-1253 |
3.68e-21 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 94.31 E-value: 3.68e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1042 DTKVLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGMIMIDGDNIRNLNISSLREQVCIVSQE-PTLFDCTI 1120
Cdd:PRK11231 14 TKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHhLTPEGITV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1121 GENICYGTNRNVTY--------QEIVEAAkMANIHnfILGLPDgydthvgEKGTQLSGGQKQRIAIARALVRSPSVLLLD 1192
Cdd:PRK11231 94 RELVAYGRSPWLSLwgrlsaedNARVNQA-MEQTR--INHLAD-------RRLTDLSGGQRQRAFLAMVLAQDTPVVLLD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 124244275 1193 EATSALD----TESEKIVQEaldAAKQGRTCLVIAHRLStiQNS---DVIAIVSEGKIVEKGTHDELI 1253
Cdd:PRK11231 164 EPTTYLDinhqVELMRLMRE---LNTQGKTVVTVLHDLN--QASrycDHLVVLANGHVMAQGTPEEVM 226
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
410-624 |
4.24e-21 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 97.22 E-value: 4.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 410 SRKDIHVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDLREVNVHSLREQIGIVSQEPVL-FD 488
Cdd:PRK09536 12 EFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLsFE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 489 GTIYENIKMG-NEH----ATHDQ-----VVEACKMANANDFIKRLPDgygtrvgekgvQLSGGQKQRIAIARALVKNPKI 558
Cdd:PRK09536 92 FDVRQVVEMGrTPHrsrfDTWTEtdraaVERAMERTGVAQFADRPVT-----------SLSGGERQRVLLARALAQATPV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 124244275 559 LLLDEATSALD-TEAEREVQGALDQAQAGRTTIIVAHRLS-TIRNVDRIFVFKAGNIVESGSHEELMS 624
Cdd:PRK09536 161 LLLDEPTASLDiNHQVRTLELVRRLVDDGKTAVAAIHDLDlAARYCDELVLLADGRVRAAGPPADVLT 228
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1044-1262 |
5.84e-21 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 93.88 E-value: 5.84e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1044 KVLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGMIMIDGDNIRNL-------------NISSLREQVCIVS 1110
Cdd:PRK10619 19 EVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVrdkdgqlkvadknQLRLLRTRLTMVF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1111 QEPTLFD-CTIGENICYGTNRNVTYQEiVEAAKMANIHNFILGLPDGYDthvGEKGTQLSGGQKQRIAIARALVRSPSVL 1189
Cdd:PRK10619 99 QHFNLWShMTVLENVMEAPIQVLGLSK-QEARERAVKYLAKVGIDERAQ---GKYPVHLSGGQQQRVSIARALAMEPEVL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1190 LLDEATSALDTEsekIVQEAL----DAAKQGRTCLVIAHRLSTIQN-SDVIAIVSEGKIVEKGTHDELIR--KSEIYQKF 1262
Cdd:PRK10619 175 LFDEPTSALDPE---LVGEVLrimqQLAEEGKTMVVVTHEMGFARHvSSHVIFLHQGKIEEEGAPEQLFGnpQSPRLQQF 251
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
749-965 |
5.89e-21 |
|
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: 94.53 E-value: 5.89e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 749 FWCGMFVLMGITFFVGFFTSAN--CLGRCGESLTMKLRFEAFKNLLRQDIAFYDdlRHGTGKLCTRFATDAPNV-RYVFT 825
Cdd:cd18572 35 FYRAVLLLLLLSVLSGLFSGLRggCFSYAGTRLVRRLRRDLFRSLLRQDIAFFD--ATKTGELTSRLTSDCQKVsDPLST 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 826 RLPVVLASIVTICGALGIGFYYGWQLALILVVMVPLLVM-----GGYFEmqmRFGKQIRDTqlLEEAGKVASQAVEHIRT 900
Cdd:cd18572 113 NLNVFLRNLVQLVGGLAFMFSLSWRLTLLAFITVPVIALitkvyGRYYR---KLSKEIQDA--LAEANQVAEEALSNIRT 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 124244275 901 VHSLNRQEQFHFTYCEYLREPFNTNLKHAHTYGAVFAFSQSLIFFMYAAAFYLGSIFVNQQAMQP 965
Cdd:cd18572 188 VRSFATEEREARRYERALDKALKLSVRQALAYAGYVAVNTLLQNGTQVLVLFYGGHLVLSGRMSA 252
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1044-1259 |
6.14e-21 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 95.42 E-value: 6.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1044 KVLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGMIMIDGDNIRNLN---ISSLREQVCIVSQEPtlfdcti 1120
Cdd:PRK11308 29 KALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADpeaQKLLRQKIQIVFQNP------- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1121 genicYGT-----------------NRNVTYQEIVE--AAKMANIhnfilGL-PDGYD--THVgekgtqLSGGQKQRIAI 1178
Cdd:PRK11308 102 -----YGSlnprkkvgqileeplliNTSLSAAERREkaLAMMAKV-----GLrPEHYDryPHM------FSGGQRQRIAI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1179 ARALVRSPSVLLLDEATSALDTESEKIV-------QEALdaakqGRTCLVIAHRLSTIQN-SDVIAIVSEGKIVEKGThd 1250
Cdd:PRK11308 166 ARALMLDPDVVVADEPVSALDVSVQAQVlnlmmdlQQEL-----GLSYVFISHDLSVVEHiADEVMVMYLGRCVEKGT-- 238
|
....*....
gi 124244275 1251 elirKSEIY 1259
Cdd:PRK11308 239 ----KEQIF 243
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
415-622 |
6.25e-21 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 98.97 E-value: 6.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 415 HVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQrFYDPT----KGRVLIDGvdlREVNVHSLREQIGIVSQEPVLFDG- 489
Cdd:TIGR00955 39 HLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALA-FRSPKgvkgSGSVLLNG---MPIDAKEMRAISAYVQQDDLFIPTl 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 490 TIYENIKMGNEHATHDQVVEACKMANANDFIKR--LPDGYGTRVGEKGVQ--LSGGQKQRIAIARALVKNPKILLLDEAT 565
Cdd:TIGR00955 115 TVREHLMFQAHLRMPRRVTKKEKRERVDEVLQAlgLRKCANTRIGVPGRVkgLSGGERKRLAFASELLTDPPLLFCDEPT 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 566 SALD-TEAEREVQGALDQAQAGRTTIIVAHRLST--IRNVDRIFVFKAGNIVESGSHEEL 622
Cdd:TIGR00955 195 SGLDsFMAYSVVQVLKGLAQKGKTIICTIHQPSSelFELFDKIILMAEGRVAYLGSPDQA 254
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1027-1199 |
6.49e-21 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 96.07 E-value: 6.49e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1027 NISIRNVFFNYPTrkDTKVLQGFTLDIKAGKTVALVGHSGCGKSTIMGL---LERFynqDKGMIMIDGDNIRNLnisslr 1103
Cdd:PRK11650 3 GLKLQAVRKSYDG--KTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMvagLERI---TSGEIWIGGRVVNEL------ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1104 eqvcivsqEPTLFDC-------------TIGENICYG-TNRNVTYQEI----VEAAKmanihnfILGLPDGYDthvgEKG 1165
Cdd:PRK11650 72 --------EPADRDIamvfqnyalyphmSVRENMAYGlKIRGMPKAEIeervAEAAR-------ILELEPLLD----RKP 132
|
170 180 190
....*....|....*....|....*....|....
gi 124244275 1166 TQLSGGQKQRIAIARALVRSPSVLLLDEATSALD 1199
Cdd:PRK11650 133 RELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLD 166
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1028-1266 |
6.62e-21 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 94.30 E-value: 6.62e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1028 ISIRNVFFNYptrKDTKVLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGMIMIDGD--NIRNLNISSLREQ 1105
Cdd:PRK13638 2 LATSDLWFRY---QDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKplDYSKRGLLALRQQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1106 VCIVSQEP--TLFDCTIGENICYG-TNRNVTYQEIVEAAKMAnihnfiLGLPDGydTHVGEKGTQ-LSGGQKQRIAIARA 1181
Cdd:PRK13638 79 VATVFQDPeqQIFYTDIDSDIAFSlRNLGVPEAEITRRVDEA------LTLVDA--QHFRHQPIQcLSHGQKKRVAIAGA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1182 LVRSPSVLLLDEATSALD----TESEKIVQEaldAAKQGRTCLVIAHRLSTI-QNSDVIAIVSEGKIVEKGTHDELIRKS 1256
Cdd:PRK13638 151 LVLQARYLLLDEPTAGLDpagrTQMIAIIRR---IVAQGNHVIISSHDIDLIyEISDAVYVLRQGQILTHGAPGEVFACT 227
|
250
....*....|
gi 124244275 1257 EIYQKFCETQ 1266
Cdd:PRK13638 228 EAMEQAGLTQ 237
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
1027-1250 |
9.32e-21 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 92.77 E-value: 9.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1027 NISIRNVFFNYPTrkdTKVLQGFTLDIKAGKTVALVGHSGCGKST---IMGLLErfyNQDKGMIMIDG---DNIRNLN-- 1098
Cdd:COG4161 2 SIQLKNINCFYGS---HQALFDINLECPSGETLVLLGPSGAGKSSllrVLNLLE---TPDSGQLNIAGhqfDFSQKPSek 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1099 -ISSLREQVCIVSQEPTLF-DCTIGENICYGTNRnVTYQEIVEAAKMANIHNFILGLPDGYDTHvgekGTQLSGGQKQRI 1176
Cdd:COG4161 76 aIRLLRQKVGMVFQQYNLWpHLTVMENLIEAPCK-VLGLSKEQAREKAMKLLARLRLTDKADRF----PLHLSGGQQQRV 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 124244275 1177 AIARALVRSPSVLLLDEATSALDTE-SEKIVQEALDAAKQGRTCLVIAHRLSTIQN--SDVIAIvSEGKIVEKGTHD 1250
Cdd:COG4161 151 AIARALMMEPQVLLFDEPTAALDPEiTAQVVEIIRELSQTGITQVIVTHEVEFARKvaSQVVYM-EKGRIIEQGDAS 226
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
399-617 |
1.06e-20 |
|
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: 91.96 E-value: 1.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 399 ISFKDVHFRYpsrKDIHVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDLREvnvhSLREQIG 478
Cdd:cd03269 1 LEVENVTKRF---GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDI----AARNRIG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 479 IVSQEPVLF-DGTIYENIK-------MGNEHATHDqvveackmanANDFIKRLpdGYGTRVGEKGVQLSGGQKQRIAIAR 550
Cdd:cd03269 74 YLPEERGLYpKMKVIDQLVylaqlkgLKKEEARRR----------IDEWLERL--ELSEYANKRVEELSKGNQQKVQFIA 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124244275 551 ALVKNPKILLLDEATSALDTEAEREVQGAL-DQAQAGRTTIIVAHRLSTIRNV-DRIFVFKAGNIVESG 617
Cdd:cd03269 142 AVIHDPELLILDEPFSGLDPVNVELLKDVIrELARAGKTVILSTHQMELVEELcDRVLLLNKGRAVLYG 210
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
395-621 |
1.23e-20 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 92.45 E-value: 1.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 395 MKGDISFKDVHFRYP-------------------SRKDIHVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTK 455
Cdd:COG1134 1 MSSMIEVENVSKSYRlyhepsrslkelllrrrrtRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 456 GRVLIDGvdlrevNVHSLRE-QIGivsqepvlFDG--TIYENIK-----MGNEHATHDQVVEACK-MANANDFIKrLPdg 526
Cdd:COG1134 81 GRVEVNG------RVSALLElGAG--------FHPelTGRENIYlngrlLGLSRKEIDEKFDEIVeFAELGDFID-QP-- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 527 ygtrVGekgvQLSGGQKQRIAIARALVKNPKILLLDEATSALDTEAEREVQGALDQ-AQAGRTTIIVAHRLSTIRNV-DR 604
Cdd:COG1134 144 ----VK----TYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRElRESGRTVIFVSHSMGAVRRLcDR 215
|
250
....*....|....*..
gi 124244275 605 IFVFKAGNIVESGSHEE 621
Cdd:COG1134 216 AIWLEKGRLVMDGDPEE 232
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
399-622 |
1.61e-20 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 93.63 E-value: 1.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 399 ISFKDVHFRYpsrKDIHVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDLRevnvHSLREQIG 478
Cdd:COG4152 2 LELKGLTKRF---GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLD----PEDRRRIG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 479 IVSQEPVLfdgtiYENIKMGnehathDQVV-----------EAckMANANDFIKR--LPDGYGTRVGEkgvqLSGGQKQR 545
Cdd:COG4152 75 YLPEERGL-----YPKMKVG------EQLVylarlkglskaEA--KRRADEWLERlgLGDRANKKVEE----LSKGNQQK 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124244275 546 IAIARALVKNPKILLLDEATSALDTEAEREVQGAL-DQAQAGRTTIIVAHRLSTI-RNVDRIFVFKAGNIVESGSHEEL 622
Cdd:COG4152 138 VQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIrELAAKGTTVIFSSHQMELVeELCDRIVIINKGRKVLSGSVDEI 216
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
416-613 |
1.74e-20 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 90.18 E-value: 1.74e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 416 VLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDLREVNVHSLREQ-IGIVSQEP----VLFDGT 490
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAgIAYVPEDRkregLVLDLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 491 IYENIKMGnehathdqvveackmanandfikrlpdgygtrvgekgVQLSGGQKQRIAIARALVKNPKILLLDEATSALDT 570
Cdd:cd03215 95 VAENIALS-------------------------------------SLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDV 137
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 124244275 571 EAEREVQGAL-DQAQAGRTTIIVAHRLSTIRNV-DRIFVFKAGNI 613
Cdd:cd03215 138 GAKAEIYRLIrELADAGKAVLLISSELDELLGLcDRILVMYEGRI 182
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1028-1253 |
1.81e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 92.74 E-value: 1.81e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1028 ISIRNVFFNYPtrKDTKVLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGMIMIDG-DNIRNLNISSLREQV 1106
Cdd:PRK13644 2 IRLENVSYSYP--DGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGiDTGDFSKLQGIRKLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1107 CIVSQEP-TLF-DCTIGENICYG-TNRNVTYQEIVEAAKMAnihnfilgLPD-GYDTHVGEKGTQLSGGQKQRIAIARAL 1182
Cdd:PRK13644 80 GIVFQNPeTQFvGRTVEEDLAFGpENLCLPPIEIRKRVDRA--------LAEiGLEKYRHRSPKTLSGGQGQCVALAGIL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124244275 1183 VRSPSVLLLDEATSALDTESEKIVQEALDAA-KQGRTCLVIAHRLSTIQNSDVIAIVSEGKIVEKGTHDELI 1253
Cdd:PRK13644 152 TMEPECLIFDEVTSMLDPDSGIAVLERIKKLhEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVL 223
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
394-626 |
2.10e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 93.15 E-value: 2.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 394 NMKGDISFKDVHFRYPSRK--DIHVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDG----VDLRE 467
Cdd:PRK13645 2 DFSKDIILDNVSYTYAKKTpfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDyaipANLKK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 468 VN-VHSLREQIGIVSQEP--VLFDGTIYENIKMGNEHATHDQVVEACKMANANDFIKrLPDGYGTRvgeKGVQLSGGQKQ 544
Cdd:PRK13645 82 IKeVKRLRKEIGLVFQFPeyQLFQETIEKDIAFGPVNLGENKQEAYKKVPELLKLVQ-LPEDYVKR---SPFELSGGQKR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 545 RIAIARALVKNPKILLLDEATSALDTEAEREVQGALDQ--AQAGRTTIIVAHRLSTI-RNVDRIFVFKAGNIVESGSHEE 621
Cdd:PRK13645 158 RVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERlnKEYKKRIIMVTHNMDQVlRIADEVIVMHEGKVISIGSPFE 237
|
....*
gi 124244275 622 LMSKQ 626
Cdd:PRK13645 238 IFSNQ 242
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1027-1255 |
2.20e-20 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 92.14 E-value: 2.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1027 NISIRnvffnyptRKDTKVLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGMIMIDGDNIRNLNISSLREQV 1106
Cdd:PRK13548 7 NLSVR--------LGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1107 CIVSQEPTL-FDCTIGENICYG----TNRNVTYQEIVEAAkMAnihnfILGLpdgydTHVGEKG-TQLSGGQKQRIAIAR 1180
Cdd:PRK13548 79 AVLPQHSSLsFPFTVEEVVAMGraphGLSRAEDDALVAAA-LA-----QVDL-----AHLAGRDyPQLSGGEQQRVQLAR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1181 ALVR------SPSVLLLDEATSALDTESEKIVQEALD--AAKQGRTCLVIAHRLS-TIQNSDVIAIVSEGKIVEKGT--- 1248
Cdd:PRK13548 148 VLAQlwepdgPPRWLLLDEPTSALDLAHQHHVLRLARqlAHERGLAVIVVLHDLNlAARYADRIVLLHQGRLVADGTpae 227
|
....*....
gi 124244275 1249 --HDELIRK 1255
Cdd:PRK13548 228 vlTPETLRR 236
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
399-632 |
2.59e-20 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 91.68 E-value: 2.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 399 ISFKDVHFRYPSRKdihVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDLREVNVHSLREQIG 478
Cdd:COG4604 2 IEIKNVSKRYGGKV---VLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 479 IVSQEPV----LfdgTIYENIKMG-----------NEHATHDQVVEACKMAN-ANDFIKrlpdgygtrvgekgvQLSGGQ 542
Cdd:COG4604 79 ILRQENHinsrL---TVRELVAFGrfpyskgrltaEDREIIDEAIAYLDLEDlADRYLD---------------ELSGGQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 543 KQRIAIARALVKNPKILLLDEATSALDTEAEREVQGALDQA--QAGRTTIIVAHRLstirNV-----DRIFVFKAGNIVE 615
Cdd:COG4604 141 RQRAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLadELGKTVVIVLHDI----NFascyaDHIVAMKDGRVVA 216
|
250 260
....*....|....*....|
gi 124244275 616 SGSHEELMSK---QGIfYDM 632
Cdd:COG4604 217 QGTPEEIITPevlSDI-YDT 235
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
374-622 |
3.21e-20 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 95.93 E-value: 3.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 374 RVINSHPKIDPYSLEG-----ILVDNMKgdISFkdvhfryPSRKDI--------HVLKGISLELKAGDKIALVGSSGCGK 440
Cdd:PRK15134 255 KLLNSEPSGDPVPLPEpasplLDVEQLQ--VAF-------PIRKGIlkrtvdhnVVVKNISFTLRPGETLGLVGESGSGK 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 441 STIVNLLQRFYdPTKGRVLIDGVDLREVNVHSL---REQIGIVSQEP---------VLfdGTIYENIKMG----NEHATH 504
Cdd:PRK15134 326 STTGLALLRLI-NSQGEIWFDGQPLHNLNRRQLlpvRHRIQVVFQDPnsslnprlnVL--QIIEEGLRVHqptlSAAQRE 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 505 DQVVEACKMANAN-DFIKRLPdgygtrvgekgVQLSGGQKQRIAIARALVKNPKILLLDEATSALDTEAEREVQGALDQA 583
Cdd:PRK15134 403 QQVIAVMEEVGLDpETRHRYP-----------AEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSL 471
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 124244275 584 QAGR--TTIIVAHRLSTIRNV-DRIFVFKAGNIVESGSHEEL 622
Cdd:PRK15134 472 QQKHqlAYLFISHDLHVVRALcHQVIVLRQGEVVEQGDCERV 513
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
414-660 |
3.90e-20 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 95.62 E-value: 3.90e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 414 IHVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDLREVNvHSLREQ--IGIVSQEPVLFDG-T 490
Cdd:PRK09700 18 VHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLD-HKLAAQlgIGIIYQELSVIDElT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 491 IYENIKMGnEHATHD----QVVEACKM-ANANDFIKRLpdGYGTRVGEKGVQLSGGQKQRIAIARALVKNPKILLLDEAT 565
Cdd:PRK09700 97 VLENLYIG-RHLTKKvcgvNIIDWREMrVRAAMMLLRV--GLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPT 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 566 SALdTEAEREVQGA-LDQAQA-GRTTIIVAHRLSTIRNV-DRIFVFKAGNIVESGSHEELmSKQGIFYDMTqaqvvrqqq 642
Cdd:PRK09700 174 SSL-TNKEVDYLFLiMNQLRKeGTAIVYISHKLAEIRRIcDRYTVMKDGSSVCSGMVSDV-SNDDIVRLMV--------- 242
|
250
....*....|....*...
gi 124244275 643 qeaGKDIEDTISESAHSH 660
Cdd:PRK09700 243 ---GRELQNRFNAMKENV 257
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1039-1247 |
4.07e-20 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 94.52 E-value: 4.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1039 TRKDTKVLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGMIMIDGDNIRNLNISSLREQVCIVSQEPTL-FD 1117
Cdd:PRK09536 12 EFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLsFE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1118 CTIGENICYG----TNRNVTYQEIVEAA---KMANIhnfilglpdGYDTHVGEKGTQLSGGQKQRIAIARALVRSPSVLL 1190
Cdd:PRK09536 92 FDVRQVVEMGrtphRSRFDTWTETDRAAverAMERT---------GVAQFADRPVTSLSGGERQRVLLARALAQATPVLL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 124244275 1191 LDEATSALDTESE-KIVQEALDAAKQGRTCLVIAHRLS-TIQNSDVIAIVSEGKIVEKG 1247
Cdd:PRK09536 163 LDEPTASLDINHQvRTLELVRRLVDDGKTAVAAIHDLDlAARYCDELVLLADGRVRAAG 221
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
404-594 |
5.75e-20 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 90.91 E-value: 5.75e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 404 VHFRYPSRKdihVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVdlrevNVHSLREQIGIVSQ- 482
Cdd:PRK11248 7 LYADYGGKP---ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGK-----PVEGPGAERGVVFQn 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 483 EPVLFDGTIYENIKMGNEHAThdqVVEACKMANANDFIKRLP-DGYGTRvgeKGVQLSGGQKQRIAIARALVKNPKILLL 561
Cdd:PRK11248 79 EGLLPWRNVQDNVAFGLQLAG---VEKMQRLEIAHQMLKKVGlEGAEKR---YIWQLSGGQRQRVGIARALAANPQLLLL 152
|
170 180 190
....*....|....*....|....*....|....*
gi 124244275 562 DEATSALDTEAEREVQGALDQ--AQAGRTTIIVAH 594
Cdd:PRK11248 153 DEPFGALDAFTREQMQTLLLKlwQETGKQVLLITH 187
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
416-624 |
5.84e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 91.31 E-value: 5.84e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 416 VLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKG-----RVLIDGVDLREV-NVHSLREQIGIVSQEPVLFDG 489
Cdd:PRK14271 36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFNYrDVLEFRRRVGMLFQRPNPFPM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 490 TIYENIKMGNEHATHDQVVEACKMANANDFIKRLPDGYGTRVGEKGVQLSGGQKQRIAIARALVKNPKILLLDEATSALD 569
Cdd:PRK14271 116 SIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALD 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 124244275 570 TEAEREVQGALDQAQAGRTTIIVAHRLS-TIRNVDRIFVFKAGNIVESGSHEELMS 624
Cdd:PRK14271 196 PTTTEKIEEFIRSLADRLTVIIVTHNLAqAARISDRAALFFDGRLVEEGPTEQLFS 251
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
363-629 |
5.99e-20 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 96.90 E-value: 5.99e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 363 GTARGAASTVLRVINSH-PKIDPyslegilvdnMKGDISFKDVHFRYPSRKDiHVLKGISLELKAGDKIALVGSSGCGKS 441
Cdd:TIGR01271 1191 GGGKYQLSTVLVIENPHaQKCWP----------SGGQMDVQGLTAKYTEAGR-AVLQDLSFSVEGGQRVGLLGRTGSGKS 1259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 442 TIVNLLQRFYDpTKGRVLIDGVDLREVNVHSLREQIGIVSQEPVLFDGTIYENIKmGNEHATHDQVVEACKMANANDFIK 521
Cdd:TIGR01271 1260 TLLSALLRLLS-TEGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNLD-PYEQWSDEEIWKVAEEVGLKSVIE 1337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 522 RLPDGYGTRVGEKGVQLSGGQKQRIAIARALVKNPKILLLDEATSALDTEAEREVQGALDQAQAGRTTIIVAHRLSTIRN 601
Cdd:TIGR01271 1338 QFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLE 1417
|
250 260
....*....|....*....|....*...
gi 124244275 602 VDRIFVFKAGNIVESGSHEELMSKQGIF 629
Cdd:TIGR01271 1418 CQQFLVIEGSSVKQYDSIQKLLNETSLF 1445
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
399-611 |
6.32e-20 |
|
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: 87.50 E-value: 6.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 399 ISFKDVHFRYPSRKdihVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVlidgvdlrevnvhslreqig 478
Cdd:cd03221 1 IELENLSKTYGGKL---LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV-------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 479 ivsqepvlfdgtiyenikmgnehaTHDQVVEACKMAnandfikrlpdgygtrvgekgvQLSGGQKQRIAIARALVKNPKI 558
Cdd:cd03221 58 ------------------------TWGSTVKIGYFE----------------------QLSGGEKMRLALAKLLLENPNL 91
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 124244275 559 LLLDEATSALDTEAEREVQGALDQAQagRTTIIVAHRLSTIRNV-DRIFVFKAG 611
Cdd:cd03221 92 LLLDEPTNHLDLESIEALEEALKEYP--GTVILVSHDRYFLDQVaTKIIELEDG 143
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
417-611 |
6.36e-20 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 95.00 E-value: 6.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 417 LKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYdPT---KGRVLIDGVDLREVNVH-SLREQIGIVSQEPVLFDG-TI 491
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHgtyEGEIIFEGEELQASNIRdTERAGIAIIHQELALVKElSV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 492 YENIKMGNEhATHDQVVEACKM-ANANDFIKRL-----PDgygTRVGEkgvqLSGGQKQRIAIARALVKNPKILLLDEAT 565
Cdd:PRK13549 100 LENIFLGNE-ITPGGIMDYDAMyLRAQKLLAQLkldinPA---TPVGN----LGLGQQQLVEIAKALNKQARLLILDEPT 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 124244275 566 SALdTEAEREVQGAL--DQAQAGRTTIIVAHRLSTIRNV-DRIFVFKAG 611
Cdd:PRK13549 172 ASL-TESETAVLLDIirDLKAHGIACIYISHKLNEVKAIsDTICVIRDG 219
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
1025-1261 |
8.51e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 91.22 E-value: 8.51e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1025 TGNISIRNVFFNYPTRK--DTKVLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGMIMIdGD-----NIRNL 1097
Cdd:PRK13645 4 SKDIILDNVSYTYAKKTpfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIV-GDyaipaNLKKI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1098 N-ISSLREQVCIVSQEP--TLFDCTIGENICYG-----TNRNVTYQEIVEAAKMANihnfilgLPDGYdthVGEKGTQLS 1169
Cdd:PRK13645 83 KeVKRLRKEIGLVFQFPeyQLFQETIEKDIAFGpvnlgENKQEAYKKVPELLKLVQ-------LPEDY---VKRSPFELS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1170 GGQKQRIAIARALVRSPSVLLLDEATSALDTESEKIVQEALDA--AKQGRTCLVIAHRLSTI-QNSDVIAIVSEGKIVEK 1246
Cdd:PRK13645 153 GGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERlnKEYKKRIIMVTHNMDQVlRIADEVIVMHEGKVISI 232
|
250
....*....|....*
gi 124244275 1247 GTHDELIRKSEIYQK 1261
Cdd:PRK13645 233 GSPFEIFSNQELLTK 247
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
407-622 |
8.66e-20 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 90.09 E-value: 8.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 407 RYPSRKdihVLKGISLELKAGDKIALVGSSGCGKST----IVNLLQrfydPTKGRVLIDGVDLREVNVHsLREQIGI--V 480
Cdd:COG1137 12 SYGKRT---VVKDVSLEVNQGEIVGLLGPNGAGKTTtfymIVGLVK----PDSGRIFLDGEDITHLPMH-KRARLGIgyL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 481 SQEPVLFDG-TIYENIKMgnehathdqVVEACKMANA----------NDF-IKRLPDgygtrvgEKGVQLSGGQKQRIAI 548
Cdd:COG1137 84 PQEASIFRKlTVEDNILA---------VLELRKLSKKereerleellEEFgITHLRK-------SKAYSLSGGERRRVEI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 549 ARALVKNPKILLLDEATSALDTEAEREVQGaldqaqagrttiIVAH---R----LSTIRNV-------DRIFVFKAGNIV 614
Cdd:COG1137 148 ARALATNPKFILLDEPFAGVDPIAVADIQK------------IIRHlkeRgigvLITDHNVretlgicDRAYIISEGKVL 215
|
....*...
gi 124244275 615 ESGSHEEL 622
Cdd:COG1137 216 AEGTPEEI 223
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1028-1226 |
8.75e-20 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 90.53 E-value: 8.75e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1028 ISIRNVF--FNYPTRKDTKVLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGMIMIDGDNIRNL-------N 1098
Cdd:COG1101 2 LELKNLSktFNPGTVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLpeykrakY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1099 ISslReqvciVSQEP---TLFDCTIGEN--ICY--GTNRNVTYqeiveAAKMANIHNFI-------LGLPDGYDTHVGek 1164
Cdd:COG1101 82 IG--R-----VFQDPmmgTAPSMTIEENlaLAYrrGKRRGLRR-----GLTKKRRELFRellatlgLGLENRLDTKVG-- 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1165 gtQLSGGQKQRIAIARALVRSPSVLLLDEATSALD-------TE-SEKIVQEaldaakQGRTCLVIAHRL 1226
Cdd:COG1101 148 --LLSGGQRQALSLLMATLTKPKLLLLDEHTAALDpktaalvLElTEKIVEE------NNLTTLMVTHNM 209
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1028-1253 |
8.76e-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: 90.14 E-value: 8.76e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1028 ISIRNVFFnypTRKDTKVLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGM-IMIDGDNIRNLNISSLREQV 1106
Cdd:COG1119 4 LELRNVTV---RRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdVRLFGERRGGEDVWELRKRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1107 CIVSQEPTLF---DCTIGENIC---YGTN---RNVTYQEIVEAAKMANIhnfiLGLpdgydTHVGEKG-TQLSGGQKQRI 1176
Cdd:COG1119 81 GLVSPALQLRfprDETVLDVVLsgfFDSIglyREPTDEQRERARELLEL----LGL-----AHLADRPfGTLSQGEQRRV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1177 AIARALVRSPSVLLLDEATSALDTESEKIVQEALDA-AKQGRTCLV-IAHRLstiqnSDVIAIVS------EGKIVEKGT 1248
Cdd:COG1119 152 LIARALVKDPELLILDEPTAGLDLGARELLLALLDKlAAEGAPTLVlVTHHV-----EEIPPGIThvlllkDGRVVAAGP 226
|
....*
gi 124244275 1249 HDELI 1253
Cdd:COG1119 227 KEEVL 231
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1042-1242 |
1.10e-19 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 94.23 E-value: 1.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1042 DTKVLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQD--KGMIMIDGDNIRNLNIS-SLREQVCIVSQEPTLF-D 1117
Cdd:PRK13549 17 GVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGtyEGEIIFEGEELQASNIRdTERAGIAIIHQELALVkE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1118 CTIGENICYG--------TNRNVTYQEIVEAAKMANIhnfilglpdgyDTHVGEKGTQLSGGQKQRIAIARALVRSPSVL 1189
Cdd:PRK13549 97 LSVLENIFLGneitpggiMDYDAMYLRAQKLLAQLKL-----------DINPATPVGNLGLGQQQLVEIAKALNKQARLL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 124244275 1190 LLDEATSALdTESE-----KIVQealDAAKQGRTCLVIAHRLSTIQN-SDVIAIVSEGK 1242
Cdd:PRK13549 166 ILDEPTASL-TESEtavllDIIR---DLKAHGIACIYISHKLNEVKAiSDTICVIRDGR 220
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
399-613 |
1.41e-19 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 91.83 E-value: 1.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 399 ISFKDVHFRYPSrkDIHVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGvdlREVNVHSLREQ-I 477
Cdd:PRK11650 4 LKLQAVRKSYDG--KTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGG---RVVNELEPADRdI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 478 GIVSQEPVLFDG-TIYENI-------KMGNEHATHdQVVEACKMANANDFIKRLPdgygtRvgekgvQLSGGQKQRIAIA 549
Cdd:PRK11650 79 AMVFQNYALYPHmSVRENMayglkirGMPKAEIEE-RVAEAARILELEPLLDRKP-----R------ELSGGQRQRVAMG 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124244275 550 RALVKNPKILLLDEATSALDteAEREVQGALD----QAQAGRTTIIVAH-RLSTIRNVDRIFVFKAGNI 613
Cdd:PRK11650 147 RAIVREPAVFLFDEPLSNLD--AKLRVQMRLEiqrlHRRLKTTSLYVTHdQVEAMTLADRVVVMNGGVA 213
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
1042-1252 |
1.76e-19 |
|
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: 88.58 E-value: 1.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1042 DTKVLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGMIMIDGDNIRNlNISSLREQVCIVSQEPTLFDCTIG 1121
Cdd:cd03265 12 DFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREVRRRIGIVFQDLSVDDELTG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1122 -ENI-----CYGTNRNVTYQEIVEAAKManihnfiLGLPDGYDTHVGekgtQLSGGQKQRIAIARALVRSPSVLLLDEAT 1195
Cdd:cd03265 91 wENLyiharLYGVPGAERRERIDELLDF-------VGLLEAADRLVK----TYSGGMRRRLEIARSLVHRPEVLFLDEPT 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1196 SALDTESEKIVQEALDA--AKQGRTCLVIAHRLSTI-QNSDVIAIVSEGKIVEKGTHDEL 1252
Cdd:cd03265 160 IGLDPQTRAHVWEYIEKlkEEFGMTILLTTHYMEEAeQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
395-628 |
1.77e-19 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 89.17 E-value: 1.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 395 MKGDISFKDVHFRYpsrKDIHVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDLRE-VNVHSL 473
Cdd:PRK11614 2 EKVMLSFDKVSAHY---GKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDwQTAKIM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 474 REQIGIVSQEPVLFDG-TIYENIKMGNEHATHDQVVEacKMANANDFIKRLPDGYGTRVGekgvQLSGGQKQRIAIARAL 552
Cdd:PRK11614 79 REAVAIVPEGRRVFSRmTVEENLAMGGFFAERDQFQE--RIKWVYELFPRLHERRIQRAG----TMSGGEQQMLAIGRAL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 124244275 553 VKNPKILLLDEATSALDTEAEREVQGALDQAQAGRTTIIVAHRLS--TIRNVDRIFVFKAGNIVESGSHEELMSKQGI 628
Cdd:PRK11614 153 MSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNAnqALKLADRGYVLENGHVVLEDTGDALLANEAV 230
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
417-614 |
1.78e-19 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 88.78 E-value: 1.78e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 417 LKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVD---LREVNVHSLREQIGIVSQEP-VLFDGTIY 492
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDitrLKNREVPFLRRQIGMIFQDHhLLMDRTVY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 493 ENIKM------GNEHATHDQVVEACKMANANDFIKRLPdgygtrvgekgVQLSGGQKQRIAIARALVKNPKILLLDEATS 566
Cdd:PRK10908 98 DNVAIpliiagASGDDIRRRVSAALDKVGLLDKAKNFP-----------IQLSGGEQQRVGIARAVVNKPAVLLADEPTG 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 124244275 567 ALDTEAEREVQGALDQ-AQAGRTTIIVAHRLSTI-RNVDRIFVFKAGNIV 614
Cdd:PRK10908 167 NLDDALSEGILRLFEEfNRVGVTVLMATHDIGLIsRRSYRMLTLSDGHLH 216
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1045-1224 |
2.00e-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: 88.65 E-value: 2.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1045 VLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGMIMIDGDNiRNLNISS--------LREQVcI--VSQ--- 1111
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDG-GWVDLAQaspreilaLRRRT-IgyVSQflr 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1112 ------------EPTLFDctigenicyGTNRNVTYQEiveAAKMANIhnfiLGLPdgydthvgEKGTQL-----SGGQKQ 1174
Cdd:COG4778 104 viprvsaldvvaEPLLER---------GVDREEARAR---ARELLAR----LNLP--------ERLWDLppatfSGGEQQ 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 124244275 1175 RIAIARALVRSPSVLLLDEATSALDTESEKIVQEALDAAKQGRTCLV-IAH 1224
Cdd:COG4778 160 RVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIgIFH 210
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
1026-1261 |
3.21e-19 |
|
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: 89.14 E-value: 3.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1026 GNISIRNVFFNYpTRKDTKVLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDkGMIMIDGDNIRNLNISSLREQ 1105
Cdd:cd03289 1 GQMTVKDLTAKY-TEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSWNSVPLQKWRKA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1106 VCIVSQEPTLFDCTIGENI-CYGTNRNvtyQEIVEAAKMANIHNFILGLPDGYDTHVGEKGTQLSGGQKQRIAIARALVR 1184
Cdd:cd03289 79 FGVIPQKVFIFSGTFRKNLdPYGKWSD---EEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLS 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 124244275 1185 SPSVLLLDEATSALDTESEKIVQEALDAAKQGRTCLVIAHRLSTIQNSDVIAIVSEGKIVEKGTHDELIRKSEIYQK 1261
Cdd:cd03289 156 KAKILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHFKQ 232
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
125-625 |
3.24e-19 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 93.11 E-value: 3.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 125 LVLGVLMFFTSYVQIAcFESYAERLVHKLRQNYLKAILRQQIQWFDKQQTGNLTARLTDDLERVreglgdKFAL-----L 199
Cdd:PRK10522 56 GLLLLLMAVTLGSQLA-LTTLGHHFVYRLRSEFIKRILDTHVERIEQLGSASLLASLTSDVRNI------TIAFvrlpeL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 200 VQMFAAFLAGYGVGFFYSWSMTLVMMGFAPLIVLSG----AKMSKSMATRTRVEQETYavagaiaeETFSSIrtvhsLNG 275
Cdd:PRK10522 129 VQGIILTLGSAAYLAWLSPKMLLVTAIWMAVTIWGGfvlvARVYKHMATLRETEDKLY--------NDYQTV-----LEG 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 276 HK-----RELDRFY-------NALEVgRQTGIVKYCYMGIGVGFSNLCMYSSYALAFWYGSTLIINDPTFDRGLIFTVFF 343
Cdd:PRK10522 196 RKeltlnRERAEYVfeneyepDAQEY-RHHIIRADTFHLSAVNWSNIMMLGAIGLVFYMANSLGWADTNVAATYSLTLLF 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 344 AvlsgSTSLG---GALPHLASfgtargaASTVLRVINSHpKIDPYSlEGILVDNMKGD---ISFKDVHFRYPSRKdiHVL 417
Cdd:PRK10522 275 L----RTPLLsavGALPTLLS-------AQVAFNKLNKL-ALAPYK-AEFPRPQAFPDwqtLELRNVTFAYQDNG--FSV 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 418 KGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDLREVNVHSLREQIGIVSQEPVLFDGTiyenikM 497
Cdd:PRK10522 340 GPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSAVFTDFHLFDQL------L 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 498 GNE-HATHDQVVEAckmanandFIKRLpdGYGTRVGEKG-----VQLSGGQKQRIAIARALVKNPKILLLDEATSALDTE 571
Cdd:PRK10522 414 GPEgKPANPALVEK--------WLERL--KMAHKLELEDgrisnLKLSKGQKKRLALLLALAEERDILLLDEWAADQDPH 483
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 124244275 572 AEREV-QGALDQAQA-GRTTIIVAHRLSTIRNVDRIFVFKAGNIVE-SGSHEELMSK 625
Cdd:PRK10522 484 FRREFyQVLLPLLQEmGKTIFAISHDDHYFIHADRLLEMRNGQLSElTGEERDAASR 540
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
1045-1269 |
3.74e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 89.00 E-value: 3.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1045 VLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGM-----IMIDGDNIRNL-NISSLREQVCIVSQEPTLFDC 1118
Cdd:PRK14271 36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYrysgdVLLGGRSIFNYrDVLEFRRRVGMLFQRPNPFPM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1119 TIGENICYGT--NRNVTYQEI--VEAAKMANIhnfilGLPDGYDTHVGEKGTQLSGGQKQRIAIARALVRSPSVLLLDEA 1194
Cdd:PRK14271 116 SIMDNVLAGVraHKLVPRKEFrgVAQARLTEV-----GLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEP 190
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 124244275 1195 TSALDTESEKIVQEALDAAKQGRTCLVIAHRLSTIQN-SDVIAIVSEGKIVEKGTHDELIRKSeiyqKFCETQRIV 1269
Cdd:PRK14271 191 TSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARiSDRAALFFDGRLVEEGPTEQLFSSP----KHAETARYV 262
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1030-1244 |
5.34e-19 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 92.86 E-value: 5.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1030 IRNVFFNYPT-RKDTKVLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGMIMIDGDNIRNLNISSL----RE 1104
Cdd:PRK10535 7 LKDIRRSYPSgEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALaqlrRE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1105 QVCIVSQEPTLFDCTIGEnicygtnRNV----TYQEIVEAAKMANIHNFI--LGLPDgydtHVGEKGTQLSGGQKQRIAI 1178
Cdd:PRK10535 87 HFGFIFQRYHLLSHLTAA-------QNVevpaVYAGLERKQRLLRAQELLqrLGLED----RVEYQPSQLSGGQQQRVSI 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 124244275 1179 ARALVRSPSVLLLDEATSALDTESEKIVQEALDAAK-QGRTCLVIAHRLSTIQNSDVIAIVSEGKIV 1244
Cdd:PRK10535 156 ARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRdRGHTVIIVTHDPQVAAQAERVIEIRDGEIV 222
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
417-616 |
6.65e-19 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 91.90 E-value: 6.65e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 417 LKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDLREVNVH-SLREQIGIVSQE----PVLfdgTI 491
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTaALAAGVAIIYQElhlvPEM---TV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 492 YENIKMGNEHATHDQVVEACKMANANDFIKRL-----PDgygTRVGEkgvqLSGGQKQRIAIARALVKNPKILLLDEATS 566
Cdd:PRK11288 97 AENLYLGQLPHKGGIVNRRLLNYEAREQLEHLgvdidPD---TPLKY----LSIGQRQMVEIAKALARNARVIAFDEPTS 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 124244275 567 ALdteAEREVQ---GALDQAQA-GRTTIIVAHRLSTI-RNVDRIFVFKAGNIVES 616
Cdd:PRK11288 170 SL---SAREIEqlfRVIRELRAeGRVILYVSHRMEEIfALCDAITVFKDGRYVAT 221
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1043-1255 |
7.03e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 88.64 E-value: 7.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1043 TKVLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGMIMIdGDNI-----RNLNISSLREQVCIVSQEP--TL 1115
Cdd:PRK13643 19 SRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTV-GDIVvsstsKQKEIKPVRKKVGVVFQFPesQL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1116 FDCTIGENICYGTNRNVTYQEivEAAKMANIHNFILGLPDGYdthvGEKGT-QLSGGQKQRIAIARALVRSPSVLLLDEA 1194
Cdd:PRK13643 98 FEETVLKDVAFGPQNFGIPKE--KAEKIAAEKLEMVGLADEF----WEKSPfELSGGQMRRVAIAGILAMEPEVLVLDEP 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 124244275 1195 TSALDTESEKIVQEALDAAKQ-GRTCLVIAHRLSTIQN-SDVIAIVSEGKIVEKGTHDELIRK 1255
Cdd:PRK13643 172 TAGLDPKARIEMMQLFESIHQsGQTVVLVTHLMDDVADyADYVYLLEKGHIISCGTPSDVFQE 234
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1038-1247 |
7.83e-19 |
|
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: 86.65 E-value: 7.83e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1038 PTRKDTKVLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGMIMIDGDNIrNLNISSLREQVCIVSQEPTLFD 1117
Cdd:cd03266 13 DVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDV-VKEPAEARRRLGFVSDSTGLYD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1118 -CTIGENICY-----GTNRNVTYQEIVEAAKMANIHNFIlglpdgyDTHVGEkgtqLSGGQKQRIAIARALVRSPSVLLL 1191
Cdd:cd03266 92 rLTARENLEYfaglyGLKGDELTARLEELADRLGMEELL-------DRRVGG----FSTGMRQKVAIARALVHDPPVLLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 124244275 1192 DEATSALDTESEKIVQEALDAAKQGRTCLVIA-HRLSTIQN-SDVIAIVSEGKIVEKG 1247
Cdd:cd03266 161 DEPTTGLDVMATRALREFIRQLRALGKCILFStHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
417-616 |
8.21e-19 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 91.39 E-value: 8.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 417 LKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYdPT---KGRVLIDGvdlREVNVHSLR--EQIGIV--SQE----PV 485
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PHgsyEGEILFDG---EVCRFKDIRdsEALGIViiHQElaliPY 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 486 LfdgTIYENIKMGNEHATHDQVVEACKMANANDFIKR--LPDGYGTRVGEKGVqlsgGQKQRIAIARALVKNPKILLLDE 563
Cdd:NF040905 93 L---SIAENIFLGNERAKRGVIDWNETNRRARELLAKvgLDESPDTLVTDIGV----GKQQLVEIAKALSKDVKLLILDE 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 124244275 564 ATSALDteaEREVQGALD-----QAQaGRTTIIVAHRLSTIRNV-DRIFVFKAGNIVES 616
Cdd:NF040905 166 PTAALN---EEDSAALLDlllelKAQ-GITSIIISHKLNEIRRVaDSITVLRDGRTIET 220
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1028-1224 |
8.22e-19 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 87.61 E-value: 8.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1028 ISIRNVFFNYPTRKDTK-VLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGMIMIDGDNIRNlniSSLREQV 1106
Cdd:COG4525 4 LTVRHVSVRYPGGGQPQpALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTG---PGADRGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1107 ciVSQEPTLFD-CTIGENICYGTN-RNVTYQEIVEAAKmANIHnfILGLpDGYDTHvgeKGTQLSGGQKQRIAIARALVR 1184
Cdd:COG4525 81 --VFQKDALLPwLNVLDNVAFGLRlRGVPKAERRARAE-ELLA--LVGL-ADFARR---RIWQLSGGMRQRVGIARALAA 151
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 124244275 1185 SPSVLLLDEATSALDTESEKIVQE-ALDA-AKQGRTCLVIAH 1224
Cdd:COG4525 152 DPRFLLMDEPFGALDALTREQMQElLLDVwQRTGKGVFLITH 193
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
1041-1262 |
1.16e-18 |
|
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: 86.44 E-value: 1.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1041 KDTKVLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGMIMIDGDNIRNLNISS-LREQVCIVSQEPTLF-DC 1118
Cdd:cd03218 11 GKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKrARLGIGYLPQEASIFrKL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1119 TIGENI-CYGTNRNVTYQEIVEAAKmANIHNFILglpdgydTHV-GEKGTQLSGGQKQRIAIARALVRSPSVLLLDEATS 1196
Cdd:cd03218 91 TVEENIlAVLEIRGLSKKEREEKLE-ELLEEFHI-------THLrKSKASSLSGGERRRVEIARALATNPKFLLLDEPFA 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 124244275 1197 ALD----TESEKIVQEALDaakQGRTCLVIAHRLS-TIQNSDVIAIVSEGKIVEKGTHDELIRKSEIYQKF 1262
Cdd:cd03218 163 GVDpiavQDIQKIIKILKD---RGIGVLITDHNVReTLSITDRAYIIYEGKVLAEGTPEEIAANELVRKVY 230
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1028-1261 |
1.16e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 87.84 E-value: 1.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1028 ISIRNVFFNYPTRKDTK---VLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGMIMIDGDNIRNL-NISSLR 1103
Cdd:PRK13633 5 IKCKNVSYKYESNEESTeklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEeNLWDIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1104 EQVCIVSQEP--TLFDCTIGENICYG-TNRNVTYQEIV----EAAKMANIHNFilglpDGYDTHVgekgtqLSGGQKQRI 1176
Cdd:PRK13633 85 NKAGMVFQNPdnQIVATIVEEDVAFGpENLGIPPEEIRervdESLKKVGMYEY-----RRHAPHL------LSGGQKQRV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1177 AIARALVRSPSVLLLDEATSALDTESEKIVQEALDA--AKQGRTCLVIAHRLSTIQNSDVIAIVSEGKIVEKGTHDELIR 1254
Cdd:PRK13633 154 AIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKElnKKYGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEIFK 233
|
....*..
gi 124244275 1255 KSEIYQK 1261
Cdd:PRK13633 234 EVEMMKK 240
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
121-283 |
1.25e-18 |
|
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: 88.34 E-value: 1.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 121 CIYYLVLGVLMFFTSYVQIACFESYAERLVHKLRQNYLKAILRQQIQWFDKQQTGNLTARLTDDLERVREGLGDkfaLLV 200
Cdd:cd18564 57 AAALVGIALLRGLASYAGTYLTALVGQRVVLDLRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGAIQDLLVS---GVL 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 201 QMFAAF--LAGY-GVGFFYSWSMTLVMMGFAPLIVLSGAKMSKSMATRTRVEQETYAVAGAIAEETFSSIRTVHSLNGHK 277
Cdd:cd18564 134 PLLTNLltLVGMlGVMFWLDWQLALIALAVAPLLLLAARRFSRRIKEASREQRRREGALASVAQESLSAIRVVQAFGREE 213
|
....*.
gi 124244275 278 RELDRF 283
Cdd:cd18564 214 HEERRF 219
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1028-1245 |
1.29e-18 |
|
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: 86.33 E-value: 1.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1028 ISIRNVFFNYPTRKDT-KVLQGFTLDIKAGKTVALVGHSGCGKSTIMGL---LERfynQDKGMIMIDGDNIRNLN---IS 1100
Cdd:COG4181 9 IELRGLTKTVGTGAGElTILKGISLEVEAGESVAIVGASGSGKSTLLGLlagLDR---PTSGTVRLAGQDLFALDedaRA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1101 SLR-EQVCIVSQE----PTLfdcTIGENIcygtnrnVTYQEIV---EAAKMANIhnfIL---GLpdgydthvGEKGT--- 1166
Cdd:COG4181 86 RLRaRHVGFVFQSfqllPTL---TALENV-------MLPLELAgrrDARARARA---LLervGL--------GHRLDhyp 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1167 -QLSGGQKQRIAIARALVRSPSVLLLDEATSALDTESEKIVQEALDA--AKQGRTCLVIAHRLSTIQNSDVIAIVSEGKI 1243
Cdd:COG4181 145 aQLSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFElnRERGTTLVLVTHDPALAARCDRVLRLRAGRL 224
|
..
gi 124244275 1244 VE 1245
Cdd:COG4181 225 VE 226
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1028-1260 |
1.37e-18 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 86.68 E-value: 1.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1028 ISIRNVFFNYptrKDTKVLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGMIMIDGDNIRNLNISSLREQVC 1107
Cdd:COG4604 2 IEIKNVSKRY---GGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1108 IVSQEPTL-FDCTIGENICYG---------TNRNvtyQEIVEAAkmanIHNFILG-LPDGY-DthvgekgtQLSGGQKQR 1175
Cdd:COG4604 79 ILRQENHInSRLTVRELVAFGrfpyskgrlTAED---REIIDEA----IAYLDLEdLADRYlD--------ELSGGQRQR 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1176 IAIARALVRSPSVLLLDEATSALD----TESEKIVQEALDaaKQGRTCLVIAHRLstiqN-----SDVIAIVSEGKIVEK 1246
Cdd:COG4604 144 AFIAMVLAQDTDYVLLDEPLNNLDmkhsVQMMKLLRRLAD--ELGKTVVIVLHDI----NfascyADHIVAMKDGRVVAQ 217
|
250
....*....|....*..
gi 124244275 1247 GTHDELIRK---SEIYQ 1260
Cdd:COG4604 218 GTPEEIITPevlSDIYD 234
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1003-1247 |
1.51e-18 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 91.46 E-value: 1.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1003 FYLI--EHPTPIDSLSDSGIVKPITGNISIRNVFFNYPTR--------KDTKVLQGFTLDIKAGKTVALVGHSGCGKSTI 1072
Cdd:PRK10261 287 FPLIslEHPAKQEPPIEQDTVVDGEPILQVRNLVTRFPLRsgllnrvtREVHAVEKVSFDLWPGETLSLVGESGSGKSTT 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1073 MGLLERFYNQDKGMIMIDGDNIRNLN---ISSLREQVCIVSQEP-TLFD--CTIGENICYGTNRNVTYQEIVEAAKMANI 1146
Cdd:PRK10261 367 GRALLRLVESQGGEIIFNGQRIDTLSpgkLQALRRDIQFIFQDPyASLDprQTVGDSIMEPLRVHGLLPGKAAAARVAWL 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1147 HNFILGLPDgydtHVGEKGTQLSGGQKQRIAIARALVRSPSVLLLDEATSALDTE-SEKIVQEALDAAKQ-GRTCLVIAH 1224
Cdd:PRK10261 447 LERVGLLPE----HAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSiRGQIINLLLDLQRDfGIAYLFISH 522
|
250 260
....*....|....*....|....
gi 124244275 1225 RLSTIQN-SDVIAIVSEGKIVEKG 1247
Cdd:PRK10261 523 DMAVVERiSHRVAVMYLGQIVEIG 546
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
416-620 |
1.80e-18 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 88.35 E-value: 1.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 416 VLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDLREvNVHSLREQIGIVSQepvlFDG-----T 490
Cdd:PRK13536 56 VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA-RARLARARIGVVPQ----FDNldlefT 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 491 IYEN-IKMGNEHATHDQVVEACkMANANDFiKRLPDGYGTRVGEkgvqLSGGQKQRIAIARALVKNPKILLLDEATSALD 569
Cdd:PRK13536 131 VRENlLVFGRYFGMSTREIEAV-IPSLLEF-ARLESKADARVSD----LSGGMKRRLTLARALINDPQLLILDEPTTGLD 204
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 124244275 570 TEAEREVQGALDQAQA-GRTTIIVAHRLSTI-RNVDRIFVFKAG-NIVESGSHE 620
Cdd:PRK13536 205 PHARHLIWERLRSLLArGKTILLTTHFMEEAeRLCDRLCVLEAGrKIAEGRPHA 258
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
416-622 |
2.32e-18 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 90.11 E-value: 2.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 416 VLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDLREVNvHSLREQIGI--VSQEPVLFDG-TIY 492
Cdd:PRK15439 26 VLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLT-PAKAHQLGIylVPQEPLLFPNlSVK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 493 ENIKMGnehathdqvveackMANANDFIKRLPDgygtRVGEKGVQL----SGG-----QKQRIAIARALVKNPKILLLDE 563
Cdd:PRK15439 105 ENILFG--------------LPKRQASMQKMKQ----LLAALGCQLdldsSAGslevaDRQIVEILRGLMRDSRILILDE 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 124244275 564 ATSALdTEAE-----REVQGALDQaqaGRTTIIVAHRLSTIRNV-DRIFVFKAGNIVESGSHEEL 622
Cdd:PRK15439 167 PTASL-TPAEterlfSRIRELLAQ---GVGIVFISHKLPEIRQLaDRISVMRDGTIALSGKTADL 227
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
120-288 |
2.70e-18 |
|
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: 86.77 E-value: 2.70e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 120 YCIYYLVLGVLMFFTSYVQIACFESYAERLVHKLRQNYLKAILRQQIQWFDKQQTGNLTARLTDDLERVREGLGDKFALL 199
Cdd:cd18575 38 AFLLLLAVALVLALASALRFYLVSWLGERVVADLRKAVFAHLLRLSPSFFETTRTGEVLSRLTTDTTLIQTVVGSSLSIA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 200 VQMFAAFLAGYGVGFFYSWSMTLVMMGFAPLIVLSGAKMSKSMATRTRVEQETYAVAGAIAEETFSSIRTVHSLNGHKRE 279
Cdd:cd18575 118 LRNLLLLIGGLVMLFITSPKLTLLVLLVIPLVVLPIILFGRRVRRLSRASQDRLADLSAFAEETLSAIKTVQAFTREDAE 197
|
....*....
gi 124244275 280 LDRFYNALE 288
Cdd:cd18575 198 RQRFATAVE 206
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
371-623 |
4.82e-18 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 88.92 E-value: 4.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 371 TVLR---VINSHPkIDPYSLEGIlVDNMKGdisfKDVHFRYPSRKDI--------------HVLKGISLELKAGDKIALV 433
Cdd:COG1129 211 TVLRdgrLVGTGP-VAELTEDEL-VRLMVG----RELEDLFPKRAAApgevvleveglsvgGVVRDVSFSVRAGEILGIA 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 434 GSSGCGKSTIVNLLQRFYDPTKGRVLIDGvdlREVNVHSLREQI--GI--VS----QEPVLFDGTIYENIKMGN--EHAT 503
Cdd:COG1129 285 GLVGAGRTELARALFGADPADSGEIRLDG---KPVRIRSPRDAIraGIayVPedrkGEGLVLDLSIRENITLASldRLSR 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 504 HDQVVEACKMANANDFIKRL---PDGYGTRVGekgvQLSGGQKQRIAIARALVKNPKILLLDEATSALDTEAEREVQGAL 580
Cdd:COG1129 362 GGLLDRRRERALAEEYIKRLrikTPSPEQPVG----NLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLI 437
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 124244275 581 DQ-AQAGRTTIIVahrlST-----IRNVDRIFVFKAGNIV-----ESGSHEELM 623
Cdd:COG1129 438 RElAAEGKAVIVI----SSelpelLGLSDRILVMREGRIVgeldrEEATEEAIM 487
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
399-595 |
5.00e-18 |
|
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: 82.59 E-value: 5.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 399 ISFKDVHFRYPSRKdiHVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVlidgvdlrevnVHSLREQIG 478
Cdd:cd03223 1 IELENLSLATPDGR--VLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI-----------GMPEGEDLL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 479 IVSQEPVLFDGTIYEnikmgnehathdQVVEACKMAnandfikrlpdgygtrvgekgvqLSGGQKQRIAIARALVKNPKI 558
Cdd:cd03223 68 FLPQRPYLPLGTLRE------------QLIYPWDDV-----------------------LSGGEQQRLAFARLLLHKPKF 112
|
170 180 190
....*....|....*....|....*....|....*...
gi 124244275 559 LLLDEATSALDTEAEREVqgaLDQAQAGRTTII-VAHR 595
Cdd:cd03223 113 VFLDEATSALDEESEDRL---YQLLKELGITVIsVGHR 147
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
1028-1257 |
5.10e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 85.99 E-value: 5.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1028 ISIRNVFFNYP--TRKDTKVLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGMIMIDGDNI----RNLNISS 1101
Cdd:PRK13646 3 IRFDNVSYTYQkgTPYEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIthktKDKYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1102 LREQVCIVSQ--EPTLFDCTIGENICYG-TNRNVTYQEIVEAAkmanihnFILGLPDGYDTHVGEKGT-QLSGGQKQRIA 1177
Cdd:PRK13646 83 VRKRIGMVFQfpESQLFEDTVEREIIFGpKNFKMNLDEVKNYA-------HRLLMDLGFSRDVMSQSPfQMSGGQMRKIA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1178 IARALVRSPSVLLLDEATSALDTESEKIVQEALDA--AKQGRTCLVIAHRLSTI-QNSDVIAIVSEGKIVEKGTHDELIR 1254
Cdd:PRK13646 156 IVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSlqTDENKTIILVSHDMNEVaRYADEVIVMKEGSIVSQTSPKELFK 235
|
...
gi 124244275 1255 KSE 1257
Cdd:PRK13646 236 DKK 238
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
420-624 |
5.70e-18 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 84.98 E-value: 5.70e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 420 ISLELKAGDKIALVGSSGCGKSTivnLLQRFYD--PTKGRVLIDGVDLREVNVHSLREQIGIVSQE-PVLFDGTIYENIK 496
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKST---LLARMAGllPGSGSIQFAGQPLEAWSAAELARHRAYLSQQqTPPFAMPVFQYLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 497 M-----GNEHATHDQVVEACKMANANDFIKRlpdgygtRVGekgvQLSGGQKQRIAIARALVK-----NP--KILLLDEA 564
Cdd:PRK03695 92 LhqpdkTRTEAVASALNEVAEALGLDDKLGR-------SVN----QLSGGEWQRVRLAAVVLQvwpdiNPagQLLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 124244275 565 TSALDTeAErevQGALDQ-----AQAGRTTIIVAHRLS-TIRNVDRIFVFKAGNIVESGSHEELMS 624
Cdd:PRK03695 161 MNSLDV-AQ---QAALDRllselCQQGIAVVMSSHDLNhTLRHADRVWLLKQGKLLASGRRDEVLT 222
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
1045-1243 |
5.98e-18 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 85.11 E-value: 5.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1045 VLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGMIMIDgdnirNLNISSLREQVCIVSQEPTLFDC-TIGEN 1123
Cdd:PRK11247 27 VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAG-----TAPLAEAREDTRLMFQDARLLPWkKVIDN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1124 ICYGTNRNvtYQEIVEAAKMAnihnfiLGLPDgydtHVGEKGTQLSGGQKQRIAIARALVRSPSVLLLDEATSALDTESE 1203
Cdd:PRK11247 102 VGLGLKGQ--WRDAALQALAA------VGLAD----RANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTR 169
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 124244275 1204 KIVQEALDA--AKQGRTCLVIAHRLS-TIQNSDVIAIVSEGKI 1243
Cdd:PRK11247 170 IEMQDLIESlwQQHGFTVLLVTHDVSeAVAMADRVLLIEEGKI 212
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
413-611 |
6.66e-18 |
|
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: 88.73 E-value: 6.66e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 413 DIHVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFY--DPTKGRVLIDGVDLREVNVHSLREQ-IGIVSQEPVLF-D 488
Cdd:TIGR02633 13 GVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYphGTWDGEIYWSGSPLKASNIRDTERAgIVIIHQELTLVpE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 489 GTIYENIKMGNEhATH-------DQVVEACKMANANdfiKRLPDGYGTR-VGEKGvqlsGGQKQRIAIARALVKNPKILL 560
Cdd:TIGR02633 93 LSVAENIFLGNE-ITLpggrmayNAMYLRAKNLLRE---LQLDADNVTRpVGDYG----GGQQQLVEIAKALNKQARLLI 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 124244275 561 LDEATSALdTEAEREVQGAL--DQAQAGRTTIIVAHRLSTIRNV-DRIFVFKAG 611
Cdd:TIGR02633 165 LDEPSSSL-TEKETEILLDIirDLKAHGVACVYISHKLNEVKAVcDTICVIRDG 217
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
412-625 |
7.03e-18 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 88.71 E-value: 7.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 412 KDIHVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRF--YDPTKGRVL------------------------------ 459
Cdd:TIGR03269 11 DGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIyhvalcekcgyverpskvgepcpvcggtle 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 460 ---IDGVDLREVNVHSLREQIGIVSQEP-VLF-DGTIYENIKmgneHATHDQVVEACK-MANANDFIKRLPDGYgtRVGE 533
Cdd:TIGR03269 91 peeVDFWNLSDKLRRRIRKRIAIMLQRTfALYgDDTVLDNVL----EALEEIGYEGKEaVGRAVDLIEMVQLSH--RITH 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 534 KGVQLSGGQKQRIAIARALVKNPKILLLDEATSALDTEAEREVQGALDQA--QAGRTTIIVAHRLSTIRNV-DRIFVFKA 610
Cdd:TIGR03269 165 IARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAvkASGISMVLTSHWPEVIEDLsDKAIWLEN 244
|
250
....*....|....*
gi 124244275 611 GNIVESGSHEELMSK 625
Cdd:TIGR03269 245 GEIKEEGTPDEVVAV 259
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
414-594 |
7.23e-18 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 84.06 E-value: 7.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 414 IHVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDLREVNVH---SLR-EQIGIVSQE----PV 485
Cdd:PRK10584 23 LSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEaraKLRaKHVGFVFQSfmliPT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 486 LfdgTIYENIKM------GNEHATHDQVVEackmanandFIKRLpdGYGTRVGEKGVQLSGGQKQRIAIARALVKNPKIL 559
Cdd:PRK10584 103 L---NALENVELpallrgESSRQSRNGAKA---------LLEQL--GLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVL 168
|
170 180 190
....*....|....*....|....*....|....*...
gi 124244275 560 LLDEATSALDTEAEREVQG---ALDQAQAgRTTIIVAH 594
Cdd:PRK10584 169 FADEPTGNLDRQTGDKIADllfSLNREHG-TTLILVTH 205
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
408-628 |
7.87e-18 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 84.17 E-value: 7.87e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 408 YPSRKdihVLKGISLELKAGDKIALVGSSGCGKST----IVNLLQRfydpTKGRVLIDGVDLREVNVHS-LREQIGIVSQ 482
Cdd:PRK10895 13 YKGRR---VVEDVSLTVNSGEIVGLLGPNGAGKTTtfymVVGIVPR----DAGNIIIDDEDISLLPLHArARRGIGYLPQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 483 EPVLFDG-TIYENIkMGNEHATHDQVVEAcKMANANDF-----IKRLPDGYGTrvgekgvQLSGGQKQRIAIARALVKNP 556
Cdd:PRK10895 86 EASIFRRlSVYDNL-MAVLQIRDDLSAEQ-REDRANELmeefhIEHLRDSMGQ-------SLSGGERRRVEIARALAANP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124244275 557 KILLLDEATSALDTEAEREVQGALDQAQ-AGRTTIIVAHRL-STIRNVDRIFVFKAGNIVESGSHEELMSKQGI 628
Cdd:PRK10895 157 KFILLDEPFAGVDPISVIDIKRIIEHLRdSGLGVLITDHNVrETLAVCERAYIVSQGHLIAHGTPTEILQDEHV 230
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
406-624 |
8.84e-18 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 84.84 E-value: 8.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 406 FRYPS----RKDIHVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDLREVNVHSLREQIGIVS 481
Cdd:PRK15112 14 FRYRTgwfrRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIRMIF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 482 QEPV-----------LFDGTIYENIKMGNEhATHDQVVEACKManandfIKRLPDgygtRVGEKGVQLSGGQKQRIAIAR 550
Cdd:PRK15112 94 QDPStslnprqrisqILDFPLRLNTDLEPE-QREKQIIETLRQ------VGLLPD----HASYYPHMLAPGQKQRLGLAR 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 124244275 551 ALVKNPKILLLDEATSALDTEAEREVQGALDQAQA--GRTTIIVAHRLSTIRNV-DRIFVFKAGNIVESGSHEELMS 624
Cdd:PRK15112 163 ALILRPKVIIADEALASLDMSMRSQLINLMLELQEkqGISYIYVTQHLGMMKHIsDQVLVMHQGEVVERGSTADVLA 239
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1044-1253 |
9.98e-18 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 88.14 E-value: 9.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1044 KVLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGMIMIDGDNIRNLNISSLREQ-VCIVSQEPTLFD-CTIG 1121
Cdd:PRK10762 18 KALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQEAgIGIIHQELNLIPqLTIA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1122 ENICYG---TNR------NVTYQeivEAAKMANihnfILGLPDGYDTHVGEkgtqLSGGQKQRIAIARALVRSPSVLLLD 1192
Cdd:PRK10762 98 ENIFLGrefVNRfgridwKKMYA---EADKLLA----RLNLRFSSDKLVGE----LSIGEQQMVEIAKVLSFESKVIIMD 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 124244275 1193 EATSAL-DTESE---KIVQEaLDAakQGRTCLVIAHRLSTI-QNSDVIAIVSEGK-IVEKG----THDELI 1253
Cdd:PRK10762 167 EPTDALtDTETEslfRVIRE-LKS--QGRGIVYISHRLKEIfEICDDVTVFRDGQfIAEREvadlTEDSLI 234
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
1045-1233 |
1.03e-17 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 82.67 E-value: 1.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1045 VLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGMIMIDGDnirnLNISSLREQvcivSQEPTLFDCTIGENI 1124
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGG----ARVAYVPQR----SEVPDSLPLTVRDLV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1125 CYGT------NRNVTYQE--IVEAAKMAnihnfiLGLPDGYDTHVGEkgtqLSGGQKQRIAIARALVRSPSVLLLDEATS 1196
Cdd:NF040873 79 AMGRwarrglWRRLTRDDraAVDDALER------VGLADLAGRQLGE----LSGGQRQRALLAQGLAQEADLLLLDEPTT 148
|
170 180 190
....*....|....*....|....*....|....*...
gi 124244275 1197 ALDTESEKIVQEAL-DAAKQGRTCLVIAHRLSTIQNSD 1233
Cdd:NF040873 149 GLDAESRERIIALLaEEHARGATVVVVTHDLELVRRAD 186
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
1028-1252 |
1.15e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 85.14 E-value: 1.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1028 ISIRNV--FFNYPTRKDTKVLQGFTLDIKAGKTVALVGHSGCGKSTIM-----------GLLERFYNQDK---------- 1084
Cdd:PRK13651 3 IKVKNIvkIFNKKLPTELKALDNVSVEINQGEFIAIIGQTGSGKTTFIehlnalllpdtGTIEWIFKDEKnkkktkekek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1085 --GMIMIDGDNIRNL-NISSLREQVCIVSQ--EPTLFDCTIGENICYGTNRNVTYQEivEAAKMANIHNFILGLPDGYdt 1159
Cdd:PRK13651 83 vlEKLVIQKTRFKKIkKIKEIRRRVGVVFQfaEYQLFEQTIEKDIIFGPVSMGVSKE--EAKKRAAKYIELVGLDESY-- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1160 hVGEKGTQLSGGQKQRIAIARALVRSPSVLLLDEATSALDTESekiVQEALDA----AKQGRTCLVIAHRL-STIQNSDV 1234
Cdd:PRK13651 159 -LQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQG---VKEILEIfdnlNKQGKTIILVTHDLdNVLEWTKR 234
|
250
....*....|....*....
gi 124244275 1235 IAIVSEGKIVEKG-THDEL 1252
Cdd:PRK13651 235 TIFFKDGKIIKDGdTYDIL 253
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
402-617 |
1.25e-17 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 88.37 E-value: 1.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 402 KDVHFRYPSR--------KDIHVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDG--VD-LREVNV 470
Cdd:PRK10261 317 RNLVTRFPLRsgllnrvtREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGqrIDtLSPGKL 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 471 HSLREQIGIVSQEPvlfdgtiYENIKmgNEHATHDQVVEACKmanandfIKRLPDGYGT---------RVGEKGV----- 536
Cdd:PRK10261 397 QALRRDIQFIFQDP-------YASLD--PRQTVGDSIMEPLR-------VHGLLPGKAAaarvawlleRVGLLPEhawry 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 537 --QLSGGQKQRIAIARALVKNPKILLLDEATSALDTEAEREVQG-ALD-QAQAGRTTIIVAHRLSTIRNVD-RIFVFKAG 611
Cdd:PRK10261 461 phEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINlLLDlQRDFGIAYLFISHDMAVVERIShRVAVMYLG 540
|
....*.
gi 124244275 612 NIVESG 617
Cdd:PRK10261 541 QIVEIG 546
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1028-1252 |
1.40e-17 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 84.43 E-value: 1.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1028 ISIRNVFFnypTRKDTKVLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGMIMIDGDNIRNLNISSL---RE 1104
Cdd:PRK11831 8 VDMRGVSF---TRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLytvRK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1105 QVCIVSQEPTLF-DCTIGENICYGTNRNVTYQEIVeaakmanIHNFILGLPDGydthVGEKG------TQLSGGQKQRIA 1177
Cdd:PRK11831 85 RMSMLFQSGALFtDMNVFDNVAYPLREHTQLPAPL-------LHSTVMMKLEA----VGLRGaaklmpSELSGGMARRAA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 124244275 1178 IARALVRSPSVLLLDEATSALDTESEKIVQEALDAAKQ--GRTCLVIAHRLSTIQN-SDVIAIVSEGKIVEKGTHDEL 1252
Cdd:PRK11831 154 LARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSalGVTCVVVSHDVPEVLSiADHAYIVADKKIVAHGSAQAL 231
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
403-622 |
1.49e-17 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 87.99 E-value: 1.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 403 DVHFRYPSRKdIHVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDLREVN--VHSLREQ---- 476
Cdd:PRK10261 19 NIAFMQEQQK-IAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRSrqVIELSEQsaaq 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 477 --------IGIVSQEP------VLFDG-TIYENIKMGNEHATHDQVVEACKMANAndfiKRLPDGYgTRVGEKGVQLSGG 541
Cdd:PRK10261 98 mrhvrgadMAMIFQEPmtslnpVFTVGeQIAESIRLHQGASREEAMVEAKRMLDQ----VRIPEAQ-TILSRYPHQLSGG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 542 QKQRIAIARALVKNPKILLLDEATSALDTEAEREVQGALD--QAQAGRTTIIVAHRLSTIRNV-DRIFVFKAGNIVESGS 618
Cdd:PRK10261 173 MRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKvlQKEMSMGVIFITHDMGVVAEIaDRVLVMYQGEAVETGS 252
|
....
gi 124244275 619 HEEL 622
Cdd:PRK10261 253 VEQI 256
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1030-1202 |
1.52e-17 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 87.43 E-value: 1.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1030 IRNVFFNYPTRKdtkVLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGMIMIDgdniRNLNISSLreqvciv 1109
Cdd:COG0488 1 LENLSKSFGGRP---LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIP----KGLRIGYL------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1110 SQEPTLFD-CTIGENICYGTNRNVT----YQEIVEA--------AKMANIHNFI------------------LGLPDG-Y 1157
Cdd:COG0488 67 PQEPPLDDdLTVLDTVLDGDAELRAleaeLEELEAKlaepdedlERLAELQEEFealggweaearaeeilsgLGFPEEdL 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 124244275 1158 DTHVGEkgtqLSGGQKQRIAIARALVRSPSVLLLDEATSALDTES 1202
Cdd:COG0488 147 DRPVSE----LSGGWRRRVALARALLSEPDLLLLDEPTNHLDLES 187
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
125-323 |
1.61e-17 |
|
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: 84.41 E-value: 1.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 125 LVLGVLMFFTSYVqIACFESY-----AERLVHKLRQNYLKAILRQQIQWFDKQQTGNLTARLTDDLERVREGLGDKfalL 199
Cdd:cd18551 39 LALLVALFLLQAV-LSALSSYllgrtGERVVLDLRRRLWRRLLRLPVSFFDRRRSGDLVSRVTNDTTLLRELITSG---L 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 200 VQMFAAFL--AGYGVGFFY-SWSMTLVMMGFAPLIVLSGAKMSKSMATRTRVEQETYAVAGAIAEETFSSIRTVHSLNGH 276
Cdd:cd18551 115 PQLVTGVLtvVGAVVLMFLlDWVLTLVTLAVVPLAFLIILPLGRRIRKASKRAQDALGELSAALERALSAIRTVKASNAE 194
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 124244275 277 KRELDRFYNALEVGRQTGIVKYCYMGIGVGFSNLCMYSSYALAFWYG 323
Cdd:cd18551 195 ERETKRGGEAAERLYRAGLKAAKIEALIGPLMGLAVQLALLVVLGVG 241
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1044-1257 |
1.72e-17 |
|
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: 83.55 E-value: 1.72e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1044 KVLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGMIMIDGDNIRNLNISslreQVC---IVS--QEPTLF-D 1117
Cdd:COG0411 18 VAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPH----RIArlgIARtfQNPRLFpE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1118 CTIGENI----CYGTNRNV------------TYQEIVEAAkMANIHnfILGLPDGYDTHVGEkgtqLSGGQKQRIAIARA 1181
Cdd:COG0411 94 LTVLENVlvaaHARLGRGLlaallrlprarrEEREARERA-EELLE--RVGLADRADEPAGN----LSYGQQRRLEIARA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1182 LVRSPSVLLLDEATSAL-DTESEKIVQ--EALdAAKQGRTCLVIAHRLSTIQN-SDVIAIVSEGKIVEKGTHDElIRKSE 1257
Cdd:COG0411 167 LATEPKLLLLDEPAAGLnPEETEELAEliRRL-RDERGITILLIEHDMDLVMGlADRIVVLDFGRVIAEGTPAE-VRADP 244
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
1042-1261 |
2.26e-17 |
|
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: 81.80 E-value: 2.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1042 DTKVLQGFTLDIKAGKTVALVGHSGCGKST----IMGLLErfYNQDKGMIMIDGDNIRNLNISS-LREQVCIVSQEPtlf 1116
Cdd:cd03217 12 GKEILKGVNLTIKKGEVHALMGPNGSGKSTlaktIMGHPK--YEVTEGEILFKGEDITDLPPEErARLGIFLAFQYP--- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1117 dctigenicygtnrnvtyqEIVEAAKMANihnFILGLPDGydthvgekgtqLSGGQKQRIAIARALVRSPSVLLLDEATS 1196
Cdd:cd03217 87 -------------------PEIPGVKNAD---FLRYVNEG-----------FSGGEKKRNEILQLLLLEPDLAILDEPDS 133
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 124244275 1197 ALDTESEKIVQEALDA-AKQGRTCLVIAH--RLSTIQNSDVIAIVSEGKIVEKGThDELIRksEIYQK 1261
Cdd:cd03217 134 GLDIDALRLVAEVINKlREEGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVKSGD-KELAL--EIEKK 198
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
1041-1252 |
2.65e-17 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 84.76 E-value: 2.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1041 KDTKVLQGFTLDIKAGKTVALVGHSGCGKST----IMGLLErfynQDKGMIMIDGDNIRNLNISSLRE---------QVC 1107
Cdd:PRK15079 32 KTLKAVDGVTLRLYEGETLGVVGESGCGKSTfaraIIGLVK----ATDGEVAWLGKDLLGMKDDEWRAvrsdiqmifQDP 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1108 IVSQEPTLfdcTIGENIC-----YgtNRNVTYQEIVEAAK--MANI---HNFILGLPdgydtHvgekgtQLSGGQKQRIA 1177
Cdd:PRK15079 108 LASLNPRM---TIGEIIAeplrtY--HPKLSRQEVKDRVKamMLKVgllPNLINRYP-----H------EFSGGQCQRIG 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 124244275 1178 IARALVRSPSVLLLDEATSALDTESEKIVQEALDAAKQ--GRTCLVIAHRLSTIQN-SDVIAIVSEGKIVEKGTHDEL 1252
Cdd:PRK15079 172 IARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQRemGLSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEV 249
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
407-617 |
2.71e-17 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 83.05 E-value: 2.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 407 RYPSRKDIHvlkGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDLREVNVHSLREQI--------- 477
Cdd:PRK11701 15 LYGPRKGCR---DVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALSEAErrrllrtew 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 478 GIVSQEP-------VLFDGTIYENIkM--GNEHATHDQvveackmANANDFIKRL---PDgygtRVGEKGVQLSGGQKQR 545
Cdd:PRK11701 92 GFVHQHPrdglrmqVSAGGNIGERL-MavGARHYGDIR-------ATAGDWLERVeidAA----RIDDLPTTFSGGMQQR 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124244275 546 IAIARALVKNPKILLLDEATSALDTeaerEVQ-GALD-----QAQAGRTTIIVAHRLSTIRNV-DRIFVFKAGNIVESG 617
Cdd:PRK11701 160 LQIARNLVTHPRLVFMDEPTGGLDV----SVQaRLLDllrglVRELGLAVVIVTHDLAVARLLaHRLLVMKQGRVVESG 234
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1042-1250 |
2.78e-17 |
|
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: 86.80 E-value: 2.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1042 DTKVLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQD--KGMIMIDGDNIRNLNISSLREQ-VCIVSQEPTLF-D 1117
Cdd:TIGR02633 13 GVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGtwDGEIYWSGSPLKASNIRDTERAgIVIIHQELTLVpE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1118 CTIGENICYGTNRNVTYQEIVEAAKMANIHNFI--LGLPDGYDT-HVGEKGtqlsGGQKQRIAIARALVRSPSVLLLDEA 1194
Cdd:TIGR02633 93 LSVAENIFLGNEITLPGGRMAYNAMYLRAKNLLreLQLDADNVTrPVGDYG----GGQQQLVEIAKALNKQARLLILDEP 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 124244275 1195 TSAL-DTESEKIVQEALDAAKQGRTCLVIAHRLSTIQN-SDVIAIVSEGKIVekGTHD 1250
Cdd:TIGR02633 169 SSSLtEKETEILLDIIRDLKAHGVACVYISHKLNEVKAvCDTICVIRDGQHV--ATKD 224
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1044-1251 |
2.81e-17 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 82.23 E-value: 2.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1044 KVLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGMIMIDGDNI---RNLNISSLREQVCIVSQEP-TLFDCT 1119
Cdd:PRK10908 16 QALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDItrlKNREVPFLRRQIGMIFQDHhLLMDRT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1120 IGENicygtnrnVTYQEIVEAAKMANIHNFI------LGLPDGYDTHvgekGTQLSGGQKQRIAIARALVRSPSVLLLDE 1193
Cdd:PRK10908 96 VYDN--------VAIPLIIAGASGDDIRRRVsaaldkVGLLDKAKNF----PIQLSGGEQQRVGIARAVVNKPAVLLADE 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1194 ATSALDTE-SEKIVQEALDAAKQGRTCLVIAHRLSTIQNSDV-IAIVSEGKIVEkGTHDE 1251
Cdd:PRK10908 164 PTGNLDDAlSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYrMLTLSDGHLHG-GVGGE 222
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
1045-1252 |
3.91e-17 |
|
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: 81.80 E-value: 3.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1045 VLQGFTLDIKAGKTVALVGHSGCGKST----IMGLLerfyNQDKGMIMIDGDNIRNLNISSL-REQVCIVSQE----PTL 1115
Cdd:TIGR03410 15 ILRGVSLEVPKGEVTCVLGRNGVGKTTllktLMGLL----PVKSGSIRLDGEDITKLPPHERaRAGIAYVPQGreifPRL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1116 fdcTIGENICYG-TNRNVTYQEIVEaakmanihnFILGLPDGYDTHVGEKGTQLSGGQKQRIAIARALVRSPSVLLLDEA 1194
Cdd:TIGR03410 91 ---TVEENLLTGlAALPRRSRKIPD---------EIYELFPVLKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 124244275 1195 TSALDTESEKIVQEALD--AAKQGRTCLVIAHRLS-TIQNSDVIAIVSEGKIVEKGTHDEL 1252
Cdd:TIGR03410 159 TEGIQPSIIKDIGRVIRrlRAEGGMAILLVEQYLDfARELADRYYVMERGRVVASGAGDEL 219
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1050-1250 |
4.39e-17 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 85.85 E-value: 4.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1050 TLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGMIMIDGdniRNLNISS----LREQVCIVSQEPTLFDC-TIGENI 1124
Cdd:COG3845 25 SLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDG---KPVRIRSprdaIALGIGMVHQHFMLVPNlTVAENI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1125 CYGT--------NRNVTYQEIVEAAKManihnfiLGLPDGYDTHVGekgtQLSGGQKQRIAIARALVRSPSVLLLDEATS 1196
Cdd:COG3845 102 VLGLeptkggrlDRKAARARIRELSER-------YGLDVDPDAKVE----DLSVGEQQRVEILKALYRGARILILDEPTA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 124244275 1197 ALdTESEkiVQEALDA----AKQGRTCLVIAHRLSTI-QNSDVIAIVSEGKIVekGTHD 1250
Cdd:COG3845 171 VL-TPQE--ADELFEIlrrlAAEGKSIIFITHKLREVmAIADRVTVLRRGKVV--GTVD 224
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
1049-1272 |
4.77e-17 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 82.58 E-value: 4.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1049 FTLDikAGKTVALVGHSGCGKST----IMGLLERfynqDKGMIMIDGDNIRNLNISSLREQVCIVSQEP-TLFD--CTIG 1121
Cdd:COG4167 34 FTLE--AGQTLAIIGENGSGKSTlakmLAGIIEP----TSGEILINGHKLEYGDYKYRCKHIRMIFQDPnTSLNprLNIG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1122 E--NICYGTNRNVTYQE----IVEAAKMANIhnfilgLPDgydtHVGEKGTQLSGGQKQRIAIARALVRSPSVLLLDEAT 1195
Cdd:COG4167 108 QilEEPLRLNTDLTAEEreerIFATLRLVGL------LPE----HANFYPHMLSSGQKQRVALARALILQPKIIIADEAL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1196 SALD--TESEKI-----VQEaldaaKQGRTCLVIAHRLSTIQN-SDVIAIVSEGKIVEKGTHDELIR--KSEIyqkfceT 1265
Cdd:COG4167 178 AALDmsVRSQIInlmleLQE-----KLGISYIYVSQHLGIVKHiSDKVLVMHQGEVVEYGKTAEVFAnpQHEV------T 246
|
....*..
gi 124244275 1266 QRIVESQ 1272
Cdd:COG4167 247 KRLIESH 253
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
1042-1257 |
4.94e-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: 4.94e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1042 DTKVLQGFTLDIKAGKTVALVGHSGCGKST----IMGLLErfYNQDKGMIMIDGDNIRNL-------------------- 1097
Cdd:COG0396 12 GKEILKGVNLTIKPGEVHAIMGPNGSGKSTlakvLMGHPK--YEVTSGSILLDGEDILELspderaragiflafqypvei 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1098 ----NISSLREQVCIVSQEP-TLFDctigenicygtnrnvTYQEIVEAAKManihnfiLGLPDGY-DTHVGEKgtqLSGG 1171
Cdd:COG0396 90 pgvsVSNFLRTALNARRGEElSARE---------------FLKLLKEKMKE-------LGLDEDFlDRYVNEG---FSGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1172 QKQRIAIARALVRSPSVLLLDEATSALDTESEKIVQEALDA-AKQGRTCLVIAH--RLSTIQNSDVIAIVSEGKIVEKGT 1248
Cdd:COG0396 145 EKKRNEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKlRSPDRGILIITHyqRILDYIKPDFVHVLVDGRIVKSGG 224
|
....*....
gi 124244275 1249 HdELIRKSE 1257
Cdd:COG0396 225 K-ELALELE 232
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
1028-1243 |
7.14e-17 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 79.51 E-value: 7.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1028 ISIRNVFFNYPTrkDTKVLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGMImidgdnirnlnISSLREQVC 1107
Cdd:cd03223 1 IELENLSLATPD--GRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI-----------GMPEGEDLL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1108 IVSQEPTLFDCTIGENICYgtnrnvTYQEIveaakmanihnfilglpdgydthvgekgtqLSGGQKQRIAIARALVRSPS 1187
Cdd:cd03223 68 FLPQRPYLPLGTLREQLIY------PWDDV------------------------------LSGGEQQRLAFARLLLHKPK 111
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 124244275 1188 VLLLDEATSALDTESEKIVQEALDAAkqGRTCLVIAHRLSTIQ-NSDVIAIVSEGKI 1243
Cdd:cd03223 112 FVFLDEATSALDEESEDRLYQLLKEL--GITVISVGHRPSLWKfHDRVLDLDGEGGW 166
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
431-621 |
7.23e-17 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 83.77 E-value: 7.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 431 ALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDG---VDLRE-VNVHSLREQIGIVSQEPVLFDG-TIYENIKMGNEH---A 502
Cdd:PRK11144 28 AIFGRSGAGKTSLINAISGLTRPQKGRIVLNGrvlFDAEKgICLPPEKRRIGYVFQDARLFPHyKVRGNLRYGMAKsmvA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 503 THDQVVEackMANANDFIKRLPdgygtrvgekgVQLSGGQKQRIAIARALVKNPKILLLDEATSALDTEAEREVQGALDQ 582
Cdd:PRK11144 108 QFDKIVA---LLGIEPLLDRYP-----------GSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLER 173
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 124244275 583 -AQAGRTTII-VAHRLSTI-RNVDRIFVFKAGNIVESGSHEE 621
Cdd:PRK11144 174 lAREINIPILyVSHSLDEIlRLADRVVVLEQGKVKAFGPLEE 215
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
109-330 |
7.73e-17 |
|
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: 82.59 E-value: 7.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 109 SLDEFNSEVVKYCIYYLVLGVLMFFTSYVqIACFesyAERLVHKLRQNYLKAILRQQIQWFDKQQTGNLTARLTDDLERV 188
Cdd:cd18574 37 FIEDLKKPALKLLGLYLLQSLLTFAYISL-LSVV---GERVAARLRNDLFSSLLRQDIAFFDTHRTGELVNRLTADVQEF 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 189 REGlgdkFALLV-QMFAAFLAGYGVG---FFYSWSMTLVMMGFAPLIVLSGAKMSKSMATRTRVEQETYAVAGAIAEETF 264
Cdd:cd18574 113 KSS----FKQCVsQGLRSVTQTVGCVvslYLISPKLTLLLLVIVPVVVLVGTLYGSFLRKLSRRAQAQVAKATGVADEAL 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 124244275 265 SSIRTVHSLNGHKRELDRFYNALEVGRQTGIVKYCYMGIGVGFSNLCMYSSYALAFWYGSTLIIND 330
Cdd:cd18574 189 GNIRTVRAFAMEDRELELYEEEVEKAAKLNEKLGLGIGIFQGLSNLALNGIVLGVLYYGGSLVSRG 254
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
419-622 |
8.91e-17 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 81.57 E-value: 8.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 419 GISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDLREVNVHSLREQiGIVS--QEPVLF-DGTIYENI 495
Cdd:PRK11300 23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARM-GVVRtfQHVRLFrEMTVIENL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 496 KMgnehATHDQV----------------VEACKMANANDFIKRLpdGYGTRVGEKGVQLSGGQKQRIAIARALVKNPKIL 559
Cdd:PRK11300 102 LV----AQHQQLktglfsgllktpafrrAESEALDRAATWLERV--GLLEHANRQAGNLAYGQQRRLEIARCMVTQPEIL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 124244275 560 LLDEATSALDTEAEREVQGALDQ--AQAGRTTIIVAHRLSTIRNV-DRIFVFKAGNIVESGSHEEL 622
Cdd:PRK11300 176 MLDEPAAGLNPKETKELDELIAElrNEHNVTVLLIEHDMKLVMGIsDRIYVVNQGTPLANGTPEEI 241
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
410-594 |
9.26e-17 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 80.10 E-value: 9.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 410 SRKDIHVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDLREV------NVHSLREQIGIvsqE 483
Cdd:TIGR01189 9 SRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQrdepheNILYLGHLPGL---K 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 484 PVLfdgTIYENIKMGNE-HATHDQVV-EACKMANANDFiKRLPDGygtrvgekgvQLSGGQKQRIAIARALVKNPKILLL 561
Cdd:TIGR01189 86 PEL---SALENLHFWAAiHGGAQRTIeDALAAVGLTGF-EDLPAA----------QLSAGQQRRLALARLWLSRRPLWIL 151
|
170 180 190
....*....|....*....|....*....|....
gi 124244275 562 DEATSALDTEAEREVQGALDQ-AQAGRTTIIVAH 594
Cdd:TIGR01189 152 DEPTTALDKAGVALLAGLLRAhLARGGIVLLTTH 185
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
1032-1252 |
1.05e-16 |
|
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: 81.83 E-value: 1.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1032 NVFFNYPTRKDTKVLQGFTLDIKAGKTVALVGHSGCGKS----TIMGLLErfynQDKGMIMIDGdnirnlnisslreQVC 1107
Cdd:cd03291 39 NLFFSNLCLVGAPVLKNINLKIEKGEMLAITGSTGSGKTsllmLILGELE----PSEGKIKHSG-------------RIS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1108 IVSQEPTLFDCTIGENICYGTNRN-VTYQEIVEAAKManiHNFILGLPDGYDTHVGEKGTQLSGGQKQRIAIARALVRSP 1186
Cdd:cd03291 102 FSSQFSWIMPGTIKENIIFGVSYDeYRYKSVVKACQL---EEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 124244275 1187 SVLLLDEATSALDTESEK-IVQEALDAAKQGRTCLVIAHRLSTIQNSDVIAIVSEGKIVEKGTHDEL 1252
Cdd:cd03291 179 DLYLLDSPFGYLDVFTEKeIFESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSEL 245
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1005-1247 |
1.36e-16 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 84.76 E-value: 1.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1005 LIEHPTPIDSLSDSGIVKPITGNISIRNVFFNYptrkdtkVLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQdK 1084
Cdd:PRK15134 268 LPEPASPLLDVEQLQVAFPIRKGILKRTVDHNV-------VVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINS-Q 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1085 GMIMIDGDNIRNLNISSL---REQVCIVSQEPTlfdctigenicYGTNRNVTYQEIVEAAkmANIHNFIL---------- 1151
Cdd:PRK15134 340 GEIWFDGQPLHNLNRRQLlpvRHRIQVVFQDPN-----------SSLNPRLNVLQIIEEG--LRVHQPTLsaaqreqqvi 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1152 ------GL-PDGYDTHVGEkgtqLSGGQKQRIAIARALVRSPSVLLLDEATSALDTESEKIVQEALDAAKQGR--TCLVI 1222
Cdd:PRK15134 407 avmeevGLdPETRHRYPAE----FSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHqlAYLFI 482
|
250 260
....*....|....*....|....*..
gi 124244275 1223 AHRLSTIQN--SDVIaIVSEGKIVEKG 1247
Cdd:PRK15134 483 SHDLHVVRAlcHQVI-VLRQGEVVEQG 508
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
160-288 |
1.36e-16 |
|
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: 81.75 E-value: 1.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 160 AILRQQIQWFDKQQTGNLTARLTDDLERVREGLGDKFALLVQMFAAFLAGYGVGFFYSWSMTLVMMGFAPLIVL----SG 235
Cdd:cd18589 78 AVLRQEIAFFDSNQTGDIVSRVTTDTEDMSESLSENLSLLMWYLARGLFLFIFMLWLSPKLALLTALGLPLLLLvpkfVG 157
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 124244275 236 aKMSKSMATRTrveQETYAVAGAIAEETFSSIRTVHSLNGHKRELDRFYNALE 288
Cdd:cd18589 158 -KFQQSLAVQV---QKSLARANQVAVETFSAMKTVRSFANEEGEAQRYRQRLQ 206
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
405-617 |
1.62e-16 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 80.45 E-value: 1.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 405 HFRYPSRKDIHVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDLREvNVHSLREQIGIV---- 480
Cdd:cd03267 25 SLFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWK-RRKKFLRRIGVVfgqk 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 481 SQ--------EPVLFDGTIYeNIKMGNEHATHDQVVEACKMANANDFIKRlpdgygtrvgekgvQLSGGQKQRIAIARAL 552
Cdd:cd03267 104 TQlwwdlpviDSFYLLAAIY-DLPPARFKKRLDELSELLDLEELLDTPVR--------------QLSLGQRMRAEIAAAL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 124244275 553 VKNPKILLLDEATSALDTEAEREVQGALDQAQAGR-TTIIV-AHRLSTIRNV-DRIFVFKAGNIVESG 617
Cdd:cd03267 169 LHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERgTTVLLtSHYMKDIEALaRRVLVIDKGRLLYDG 236
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
417-616 |
1.77e-16 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 83.90 E-value: 1.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 417 LKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGvdlREVNVHSLREQ----IGIVSQEPVLFDG-TI 491
Cdd:PRK10762 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLG---KEVTFNGPKSSqeagIGIIHQELNLIPQlTI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 492 YENIKMGNEHATHDQVVEACKM-ANANDFIKRLPDGYG--TRVGEkgvqLSGGQKQRIAIARALVKNPKILLLDEATSAL 568
Cdd:PRK10762 97 AENIFLGREFVNRFGRIDWKKMyAEADKLLARLNLRFSsdKLVGE----LSIGEQQMVEIAKVLSFESKVIIMDEPTDAL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 124244275 569 -DTEAE------REVqgaldQAQaGRTTIIVAHRLSTIRNV-DRIFVFKAGN-IVES 616
Cdd:PRK10762 173 tDTETEslfrviREL-----KSQ-GRGIVYISHRLKEIFEIcDDVTVFRDGQfIAER 223
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
1041-1247 |
1.92e-16 |
|
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: 79.63 E-value: 1.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1041 KDTKVLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGMIMIDGDNIRnlniSSLREQVCIVSQEPTLF-DCT 1119
Cdd:cd03269 11 GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLD----IAARNRIGYLPEERGLYpKMK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1120 IGENICY-GTNRNVTYQEIveaakMANIHNFI--LGLPDgydtHVGEKGTQLSGGQKQRIAIARALVRSPSVLLLDEATS 1196
Cdd:cd03269 87 VIDQLVYlAQLKGLKKEEA-----RRRIDEWLerLELSE----YANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFS 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 124244275 1197 ALDTESEKIVQEALDA-AKQGRTCLVIAHRLSTIQN-SDVIAIVSEGKIVEKG 1247
Cdd:cd03269 158 GLDPVNVELLKDVIRElARAGKTVILSTHQMELVEElCDRVLLLNKGRAVLYG 210
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1045-1253 |
2.02e-16 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 83.95 E-value: 2.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1045 VLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGMIMIDGDNIRNLNiSSLREQVCI--VSQEPTLF-DCTIG 1121
Cdd:PRK15439 26 VLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLT-PAKAHQLGIylVPQEPLLFpNLSVK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1122 ENICYG-TNRNVTYQEIVEAAKMANIHnfilglpdgYDTHVgeKGTQLSGGQKQRIAIARALVRSPSVLLLDEATSALD- 1199
Cdd:PRK15439 105 ENILFGlPKRQASMQKMKQLLAALGCQ---------LDLDS--SAGSLEVADRQIVEILRGLMRDSRILILDEPTASLTp 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1200 TESEKIVQEALDAAKQGRTCLVIAHRLSTI-QNSDVIAIVSEGKIVEKG-----THDELI 1253
Cdd:PRK15439 174 AETERLFSRIRELLAQGVGIVFISHKLPEIrQLADRISVMRDGTIALSGktadlSTDDII 233
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
416-624 |
2.05e-16 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 83.99 E-value: 2.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 416 VLKGISLELKAGDKIALVGSSGCGKS-TIVNLLQRFYDP----TKGRVLIDGVDLREVNVHSLR----EQIGIVSQEPVL 486
Cdd:PRK15134 24 VVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFHGESLLHASEQTLRgvrgNKIAMIFQEPMV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 487 -------FDGTIYENIK----MGNEHATHD--QVVEACKMANANdfiKRLPDgYGTrvgekgvQLSGGQKQRIAIARALV 553
Cdd:PRK15134 104 slnplhtLEKQLYEVLSlhrgMRREAARGEilNCLDRVGIRQAA---KRLTD-YPH-------QLSGGERQRVMIAMALL 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124244275 554 KNPKILLLDEATSALDTEAE-------REVQGALDQAqagrtTIIVAHRLSTIRNV-DRIFVFKAGNIVESGSHEELMS 624
Cdd:PRK15134 173 TRPELLIADEPTTALDVSVQaqilqllRELQQELNMG-----LLFITHNLSIVRKLaDRVAVMQNGRCVEQNRAATLFS 246
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
1044-1256 |
2.62e-16 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 84.83 E-value: 2.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1044 KVLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGMIMIDgdnirnlnisslrEQVCIVSQEPTLFDCTIGEN 1123
Cdd:PTZ00243 674 VLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAE-------------RSIAYVPQQAWIMNATVRGN 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1124 ICYGTNRNVtyQEIVEAAKMANIHNFILGLPDGYDTHVGEKGTQLSGGQKQRIAIARALVRSPSVLLLDEATSALDTE-S 1202
Cdd:PTZ00243 741 ILFFDEEDA--ARLADAVRVSQLEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHvG 818
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 124244275 1203 EKIVQEALDAAKQGRTCLVIAHRLSTIQNSDVIAIVSEGKIVEKGTHDELIRKS 1256
Cdd:PTZ00243 819 ERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFMRTS 872
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1028-1258 |
3.31e-16 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 81.00 E-value: 3.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1028 ISIRNVFFNYptrKDTKVLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGMIMIDGDNIRNlNISSLREQVC 1107
Cdd:PRK13537 8 IDFRNVEKRY---GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPS-RARHARQRVG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1108 IVSQEPTLF-DCTIGENI-CYGTNRNVTYQEIveAAKMANIHNFIlGLPDGYDTHVGEkgtqLSGGQKQRIAIARALVRS 1185
Cdd:PRK13537 84 VVPQFDNLDpDFTVRENLlVFGRYFGLSAAAA--RALVPPLLEFA-KLENKADAKVGE----LSGGMKRRLTLARALVND 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 124244275 1186 PSVLLLDEATSALDTESEKIVQEALDA-AKQGRTCLVIAHRLSTIQN-SDVIAIVSEGKIVEKGTHDELIrKSEI 1258
Cdd:PRK13537 157 PDVLVLDEPTTGLDPQARHLMWERLRSlLARGKTILLTTHFMEEAERlCDRLCVIEEGRKIAEGAPHALI-ESEI 230
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1044-1254 |
3.37e-16 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 83.04 E-value: 3.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1044 KVLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGMIMIDGDNIRNLNI-SSLREQVCIVSQEPTLF-DCTIG 1121
Cdd:PRK11288 18 KALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTtAALAAGVAIIYQELHLVpEMTVA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1122 ENICYG--------TNRNVTYQEIVEAAKManihnfiLGLPDGYDTHVGEkgtqLSGGQKQRIAIARALVRSPSVLLLDE 1193
Cdd:PRK11288 98 ENLYLGqlphkggiVNRRLLNYEAREQLEH-------LGVDIDPDTPLKY----LSIGQRQMVEIAKALARNARVIAFDE 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 124244275 1194 ATSALDT-ESEKI--VQEALDAakQGRTCLVIAHRLSTI-QNSDVIAIVSEGKIVE------KGTHDELIR 1254
Cdd:PRK11288 167 PTSSLSArEIEQLfrVIRELRA--EGRVILYVSHRMEEIfALCDAITVFKDGRYVAtfddmaQVDRDQLVQ 235
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
756-989 |
5.31e-16 |
|
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: 80.07 E-value: 5.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 756 LMGItFFVGFFTSANCLGRC----GESLTMKLRFEAFKNLLRQDIAFYDDLRhgTGKLCTRFATDAPNV-RYVFTRLPVV 830
Cdd:cd18590 41 LMCL-FSLGSSLSAGLRGGLfmctLSRLNLRLRHQLFSSLVQQDIGFFEKTK--TGDLTSRLSTDTTLMsRSVALNANVL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 831 LASIVTICGALGIGFYYGWQLALILVVMVPLLVMGG--YFEMQMRFGKQIRDTQllEEAGKVASQAVEHIRTVHSLNRQE 908
Cdd:cd18590 118 LRSLVKTLGMLGFMLSLSWQLTLLTLIEMPLTAIAQkvYNTYHQKLSQAVQDSI--AKAGELAREAVSSIRTVRSFKAEE 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 909 QFHFTYCEYLREPFNTNLKHAHTYGAVFAFSQSLIFFMYAAAFYLGsifvnQQAMQPidvyrvffaisfcGQM-IGNTTS 987
Cdd:cd18590 196 EEACRYSEALERTYNLKDRRDTVRAVYLLVRRVLQLGVQVLMLYCG-----RQLIQS-------------GHLtTGSLVS 257
|
..
gi 124244275 988 FI 989
Cdd:cd18590 258 FI 259
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1027-1199 |
7.16e-16 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 80.84 E-value: 7.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1027 NISIRNVFFNYptrKDTKVLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGMIMIDgdNIRNLNISSLREQV 1106
Cdd:PRK11000 3 SVTLRNVTKAY---GDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIG--EKRMNDVPPAERGV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1107 CIVSQEPTLF-DCTIGENICYG-----TNRNVTYQEIVEAAKmanihnfILGLpdgydTHVGE-KGTQLSGGQKQRIAIA 1179
Cdd:PRK11000 78 GMVFQSYALYpHLSVAENMSFGlklagAKKEEINQRVNQVAE-------VLQL-----AHLLDrKPKALSGGQRQRVAIG 145
|
170 180
....*....|....*....|
gi 124244275 1180 RALVRSPSVLLLDEATSALD 1199
Cdd:PRK11000 146 RTLVAEPSVFLLDEPLSNLD 165
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1028-1256 |
7.80e-16 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 79.77 E-value: 7.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1028 ISIRNVffnypTRK--DTKVLQGFTLDIKAGKTVALVGHSGCGKST----IMGLLErfynQDKGMIMIDGDNIRNLNISS 1101
Cdd:COG4152 2 LELKGL-----TKRfgDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTtiriILGILA----PDSGEVLWDGEPLDPEDRRR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1102 ---LREqvcivsqEPTLF-DCTIGENICY-GTNRNVTYQEIVEAAK--MANihnfiLGLPDGYDTHVGEkgtqLSGGQKQ 1174
Cdd:COG4152 73 igyLPE-------ERGLYpKMKVGEQLVYlARLKGLSKAEAKRRADewLER-----LGLGDRANKKVEE----LSKGNQQ 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1175 RIAIARALVRSPSVLLLDEATSALDTES-EKIVQEALDAAKQGRTCLVIAHRLSTIQN-SDVIAIVSEGKIVEKGTHDEl 1252
Cdd:COG4152 137 KVQLIAALLHDPELLILDEPFSGLDPVNvELLKDVIRELAAKGTTVIFSSHQMELVEElCDRIVIINKGRKVLSGSVDE- 215
|
....
gi 124244275 1253 IRKS 1256
Cdd:COG4152 216 IRRQ 219
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1028-1258 |
8.16e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 79.08 E-value: 8.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1028 ISIRNVFFNYptRKDTKVLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGMIMIDGDNIRNLNISSLREQVC 1107
Cdd:PRK13652 4 IETRDLCYSY--SGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1108 IVSQEP--TLFDCTIGENICYGTNRNVTYQEIVEAAKMANIHnfILGLPDgYDTHVGEkgtQLSGGQKQRIAIARALVRS 1185
Cdd:PRK13652 82 LVFQNPddQIFSPTVEQDIAFGPINLGLDEETVAHRVSSALH--MLGLEE-LRDRVPH---HLSGGEKKRVAIAGVIAME 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 124244275 1186 PSVLLLDEATSALDTESEKIVQEALDA--AKQGRTCLVIAHRLSTI-QNSDVIAIVSEGKIVEKGTHDELIRKSEI 1258
Cdd:PRK13652 156 PQVLVLDEPTAGLDPQGVKELIDFLNDlpETYGMTVIFSTHQLDLVpEMADYIYVMDKGRIVAYGTVEEIFLQPDL 231
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1028-1255 |
9.59e-16 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 82.03 E-value: 9.59e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1028 ISIRNVFFNYPtrkDTKVLQGFTLDIKAGKTVALVGHSGCGKST----IMGLLErfynQDKGMIMIdGDNIRnlnISSLr 1103
Cdd:COG0488 316 LELEGLSKSYG---DKTLLDDLSLRIDRGDRIGLIGPNGAGKSTllklLAGELE----PDSGTVKL-GETVK---IGYF- 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1104 eqvcivSQEPTLFDctigenicygTNRNVtYQEIVEAAkmanihnfilglPDGYDTHV----------GEKGTQ----LS 1169
Cdd:COG0488 384 ------DQHQEELD----------PDKTV-LDELRDGA------------PGGTEQEVrgylgrflfsGDDAFKpvgvLS 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1170 GGQKQRIAIARALVRSPSVLLLDEATSALDTESEKIVQEALDAAKqGrTCLVIAH-R--LSTIQNSdvIAIVSEGKIVEK 1246
Cdd:COG0488 435 GGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDFP-G-TVLLVSHdRyfLDRVATR--ILEFEDGGVREY 510
|
250
....*....|
gi 124244275 1247 -GTHDELIRK 1255
Cdd:COG0488 511 pGGYDDYLEK 520
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
416-628 |
1.09e-15 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 78.49 E-value: 1.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 416 VLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDLREVNVHSLREQIGIVSQEPVL-FDGTIYEN 494
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTpGDITVQEL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 495 IKMGneHATHDQVVEACKMANANDFIKRLPDGYGTRVGEKGVQ-LSGGQKQRIAIARALVKNPKILLLDEATSALDTEAE 573
Cdd:PRK10253 102 VARG--RYPHQPLFTRWRKEDEEAVTKAMQATGITHLADQSVDtLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQ 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 124244275 574 ---REVQGALDQAQaGRTTIIVAHRLS-TIRNVDRIFVFKAGNIVESGSHEELMSKQGI 628
Cdd:PRK10253 180 idlLELLSELNREK-GYTLAAVLHDLNqACRYASHLIALREGKIVAQGAPKEIVTAELI 237
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
1044-1250 |
1.13e-15 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 81.37 E-value: 1.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1044 KVLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFY--NQDKGMIMIDGDNIRNLNIS-SLREQVCIVSQE----PTLf 1116
Cdd:NF040905 15 KALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYphGSYEGEILFDGEVCRFKDIRdSEALGIVIIHQElaliPYL- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1117 dcTIGENICYGT--------NRNVTYQEIVEAAKManihnfiLGLPDGYDTHVGEKGTqlsgGQKQRIAIARALVRSPSV 1188
Cdd:NF040905 94 --SIAENIFLGNerakrgviDWNETNRRARELLAK-------VGLDESPDTLVTDIGV----GKQQLVEIAKALSKDVKL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124244275 1189 LLLDEATSAL-DTESEKIVQEALDAAKQGRTCLVIAHRLSTI-QNSDVIAIVSEGKIVEkgTHD 1250
Cdd:NF040905 161 LILDEPTAALnEEDSAALLDLLLELKAQGITSIIISHKLNEIrRVADSITVLRDGRTIE--TLD 222
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
410-594 |
1.41e-15 |
|
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: 76.76 E-value: 1.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 410 SRKDIHVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDLREVNVHSLREQIGIVSQEPVLFDG 489
Cdd:cd03231 9 ERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 490 TIYENIKMGNEHATHDQVVEACKMANANDFiKRLPDGygtrvgekgvQLSGGQKQRIAIARALVKNPKILLLDEATSALD 569
Cdd:cd03231 89 SVLENLRFWHADHSDEQVEEALARVGLNGF-EDRPVA----------QLSAGQQRRVALARLLLSGRPLWILDEPTTALD 157
|
170 180
....*....|....*....|....*.
gi 124244275 570 TEAEREVQGALDQ-AQAGRTTIIVAH 594
Cdd:cd03231 158 KAGVARFAEAMAGhCARGGMVVLTTH 183
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
399-626 |
1.46e-15 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 79.08 E-value: 1.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 399 ISFKDVHFRYPSRKdihVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDLREvNVHSLREQIG 478
Cdd:PRK13537 8 IDFRNVEKRYGDKL---VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPS-RARHARQRVG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 479 IVSQ----EPvlfDGTIYENIKMGNEHATHDQVVEACKMANANDFiKRLPDGYGTRVGEkgvqLSGGQKQRIAIARALVK 554
Cdd:PRK13537 84 VVPQfdnlDP---DFTVRENLLVFGRYFGLSAAAARALVPPLLEF-AKLENKADAKVGE----LSGGMKRRLTLARALVN 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124244275 555 NPKILLLDEATSALDTEAEREVQGALDQAQA-GRTTIIVAHRLSTI-RNVDRIFVFKAGNIVESGSHEELMSKQ 626
Cdd:PRK13537 156 DPDVLVLDEPTTGLDPQARHLMWERLRSLLArGKTILLTTHFMEEAeRLCDRLCVIEEGRKIAEGAPHALIESE 229
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1041-1258 |
1.73e-15 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 77.63 E-value: 1.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1041 KDTKVLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGMIMIDGDNIRNLNI-SSLREQVCIVSQEPTLFD-C 1118
Cdd:PRK10895 14 KGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLhARARRGIGYLPQEASIFRrL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1119 TIGENI--CYGTNRNVTYQEIVEAAK--MANIHnfILGLPDGYdthvgekGTQLSGGQKQRIAIARALVRSPSVLLLDEA 1194
Cdd:PRK10895 94 SVYDNLmaVLQIRDDLSAEQREDRANelMEEFH--IEHLRDSM-------GQSLSGGERRRVEIARALAANPKFILLDEP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124244275 1195 TSALDTES----EKIVQEALDAakqGRTCLVIAHRL-STIQNSDVIAIVSEGKIVEKGTHDELIRKSEI 1258
Cdd:PRK10895 165 FAGVDPISvidiKRIIEHLRDS---GLGVLITDHNVrETLAVCERAYIVSQGHLIAHGTPTEILQDEHV 230
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
57-343 |
1.90e-15 |
|
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: 78.76 E-value: 1.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 57 LITGTVAAVIHGAgFPLLAIVLGGMT--TVFLRAQNSDFVVgvdnvnPEGLVPISLDEfnsevvkyciYYLVLGVLMFFT 134
Cdd:cd18565 1 LVLGLLASILNRL-FDLAPPLLIGVAidAVFNGEASFLPLV------PASLGPADPRG----------QLWLLGGLTVAA 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 135 -------SYVQIACFESYAERLVHKLRQNYLKAILRQQIQWFDKQQTGNLTARLTDDLERVREGLGDKFALLVQMFAAFL 207
Cdd:cd18565 64 flleslfQYLSGVLWRRFAQRVQHDLRTDTYDHVQRLDMAFFEDRQTGDLMSVLNNDVNQLERFLDDGANSIIRVVVTVL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 208 AGYGVGFFYSWSMTLVMMGFAPLIVLSGAKMSKSMATRTRVEQETYAVAGAIAEETFSSIRTVHSLNGHKRELDRF---- 283
Cdd:cd18565 144 GIGAILFYLNWQLALVALLPVPLIIAGTYWFQRRIEPRYRAVREAVGDLNARLENNLSGIAVIKAFTAEDFERERVadas 223
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124244275 284 -------YNALEVG-RQTGIVkycYMGIGVGFsnlcmyssyALAFWYGSTLIINDPTFDRGLI----FTVFF 343
Cdd:cd18565 224 eeyrdanWRAIRLRaAFFPVI---RLVAGAGF---------VATFVVGGYWVLDGPPLFTGTLtvgtLVTFL 283
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
431-618 |
2.01e-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: 81.98 E-value: 2.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 431 ALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDLrEVNVHSLREQIGIVSQEPVLFDG-TIYENIKMGNEHATHDQVVE 509
Cdd:TIGR01257 960 AFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-ETNLDAVRQSLGMCPQHNILFHHlTVAEHILFYAQLKGRSWEEA 1038
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 510 ACKMAnandfiKRLPD-GYGTRVGEKGVQLSGGQKQRIAIARALVKNPKILLLDEATSALDTEAEREVQGALDQAQAGRT 588
Cdd:TIGR01257 1039 QLEME------AMLEDtGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRT 1112
|
170 180 190
....*....|....*....|....*....|.
gi 124244275 589 TIIVAHRLSTIRNV-DRIFVFKAGNIVESGS 618
Cdd:TIGR01257 1113 IIMSTHHMDEADLLgDRIAIISQGRLYCSGT 1143
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
411-593 |
2.39e-15 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 76.07 E-value: 2.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 411 RKDIHVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDLREVNVhslREQIGIVSQ----EPVL 486
Cdd:PRK13539 12 RGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDV---AEACHYLGHrnamKPAL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 487 fdgTIYENIKM-GNEHATHDQVVEACKMANANDFIKRLPDGYgtrvgekgvqLSGGQKQRIAIARALVKNPKILLLDEAT 565
Cdd:PRK13539 89 ---TVAENLEFwAAFLGGEELDIAAALEAVGLAPLAHLPFGY----------LSAGQKRRVALARLLVSNRPIWILDEPT 155
|
170 180
....*....|....*....|....*...
gi 124244275 566 SALDTEAEREVQGALdQAQAGRTTIIVA 593
Cdd:PRK13539 156 AALDAAAVALFAELI-RAHLAQGGIVIA 182
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
885-1252 |
2.50e-15 |
|
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: 81.88 E-value: 2.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 885 EEAGKVA------SQAVEHIRTVHSLNRQEQFHfTYCEYLREpfnTNLKHAHTYGAVFAFSQSLIFFmyAAAFYLGSIFV 958
Cdd:TIGR01271 251 KRAGKISerlaitSEIIENIQSVKAYCWEEAME-KIIKNIRQ---DELKLTRKIAYLRYFYSSAFFF--SGFFVVFLSVV 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 959 NQQAMQPIDVYRVFFAISFCGQMIGNTTSFIPDVVKA---RLAA--SLLFYLI--EHPTPIDSLS-------------DS 1018
Cdd:TIGR01271 325 PYALIKGIILRRIFTTISYCIVLRMTVTRQFPGAIQTwydSLGAitKIQDFLCkeEYKTLEYNLTttevemvnvtaswDE 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1019 GI------VKPITGNISIRN----VFFNYPTRKDTKVLQGFTLDIKAGKTVALVGHSGCGKST----IMGLLErfynQDK 1084
Cdd:TIGR01271 405 GIgelfekIKQNNKARKQPNgddgLFFSNFSLYVTPVLKNISFKLEKGQLLAVAGSTGSGKSSllmmIMGELE----PSE 480
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1085 GMIMIDGdnirnlnisslreQVCIVSQEPTLFDCTIGENICYGtnrnVTYQEI--VEAAKMANIHNFILGLPDGYDTHVG 1162
Cdd:TIGR01271 481 GKIKHSG-------------RISFSPQTSWIMPGTIKDNIIFG----LSYDEYryTSVIKACQLEEDIALFPEKDKTVLG 543
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1163 EKGTQLSGGQKQRIAIARALVRSPSVLLLDEATSALDTESEK-IVQEALDAAKQGRTCLVIAHRLSTIQNSDVIAIVSEG 1241
Cdd:TIGR01271 544 EGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKeIFESCLCKLMSNKTRILVTSKLEHLKKADKILLLHEG 623
|
410
....*....|.
gi 124244275 1242 KIVEKGTHDEL 1252
Cdd:TIGR01271 624 VCYFYGTFSEL 634
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
148-330 |
6.54e-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: 76.97 E-value: 6.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 148 RLVHKLRQNYLKAILRQQIQWFDKQQTGNLTARLTDDLERVreglGDKFALLVQMF-AAFLAGYGVGFFY---SWSMTLV 223
Cdd:cd18784 66 RLNIRIRNLLFRSIVSQEIGFFDTVKTGDITSRLTSDTTTM----SDTVSLNLNIFlRSLVKAIGVIVFMfklSWQLSLV 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 224 MMGFAPLIVLSG---AKMSKSMATRTrveQETYAVAGAIAEETFSSIRTVHSLNGHKRELDRFYNALEVGRQTGIVKYCY 300
Cdd:cd18784 142 TLIGLPLIAIVSkvyGDYYKKLSKAV---QDSLAKANEVAEETISSIRTVRSFANEDGEANRYSEKLKDTYKLKIKEALA 218
|
170 180 190
....*....|....*....|....*....|
gi 124244275 301 MGIGVGFSNLCMYSSYALAFWYGSTLIIND 330
Cdd:cd18784 219 YGGYVWSNELTELALTVSTLYYGGHLVITG 248
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1046-1254 |
6.65e-15 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 79.06 E-value: 6.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1046 LQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGMIMIDGDNIRNLNIS-SLREQVCIVSQEPTLFD-CTIGEN 1123
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKlAAQLGIGIIYQELSVIDeLTVLEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1124 ICYGT--NRNVTYQEIVEAAKM---ANIHNFILGLPDGYDTHVGEkgtqLSGGQKQRIAIARALVRSPSVLLLDEATSAL 1198
Cdd:PRK09700 101 LYIGRhlTKKVCGVNIIDWREMrvrAAMMLLRVGLKVDLDEKVAN----LSISHKQMLEIAKTLMLDAKVIIMDEPTSSL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 124244275 1199 -DTESEKIVQEALDAAKQGRTCLVIAHRLSTIQN-SDVIAIVSEGKIVEKG-----THDELIR 1254
Cdd:PRK09700 177 tNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRiCDRYTVMKDGSSVCSGmvsdvSNDDIVR 239
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
115-283 |
7.57e-15 |
|
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: 76.67 E-value: 7.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 115 SEVVKYCIYYLVLGVLMFFTSYVQIACFESYAERLVHKLRQNYLKAILRQQIQWFDKQQTGNLTARLTDDLERVREGLGD 194
Cdd:cd18547 42 SGLLRILLLLLGLYLLSALFSYLQNRLMARVSQRTVYDLRKDLFEKLQRLPLSYFDTHSHGDIMSRVTNDVDNISQALSQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 195 KFALLVQMFAAFLAGYGVGFFYSWSMTLVMMGFAPLIVLSGAKMSKSMATRTRVEQETYAVAGAIAEETFSSIRTVHSLN 274
Cdd:cd18547 122 SLTQLISSILTIVGTLIMMLYISPLLTLIVLVTVPLSLLVTKFIAKRSQKYFRKQQKALGELNGYIEEMISGQKVVKAFN 201
|
....*....
gi 124244275 275 GHKRELDRF 283
Cdd:cd18547 202 REEEAIEEF 210
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
1045-1253 |
7.60e-15 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 76.18 E-value: 7.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1045 VLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGMIMIDGDNIRNLNISSLREQVCIVSQEPTlfdctigeni 1124
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNAT---------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1125 cygTNRNVTYQEIVEAAKMANIHNFILGLPDGYD-----------THVGEKGTQ-LSGGQKQRIAIARALVRSPSVLLLD 1192
Cdd:PRK10253 92 ---TPGDITVQELVARGRYPHQPLFTRWRKEDEEavtkamqatgiTHLADQSVDtLSGGQRQRAWIAMVLAQETAIMLLD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 124244275 1193 EATSALDTESEKIVQEALDA--AKQGRTCLVIAHRLSTI--QNSDVIAIvSEGKIVEKGTHDELI 1253
Cdd:PRK10253 169 EPTTWLDISHQIDLLELLSElnREKGYTLAAVLHDLNQAcrYASHLIAL-REGKIVAQGAPKEIV 232
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
1040-1252 |
1.03e-14 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 78.94 E-value: 1.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1040 RKDTK-VLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLErFYN----QDKGMIMIDGdniRNLNISSLREQVCIVSQE-- 1112
Cdd:TIGR00955 34 ERPRKhLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALA-FRSpkgvKGSGSVLLNG---MPIDAKEMRAISAYVQQDdl 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1113 --PTLfdcTIGENICYGTN----RNVTYQEiveaaKMANIHNFI--LGLPDGYDTHVGEKGTQ--LSGGQKQRIAIARAL 1182
Cdd:TIGR00955 110 fiPTL---TVREHLMFQAHlrmpRRVTKKE-----KRERVDEVLqaLGLRKCANTRIGVPGRVkgLSGGERKRLAFASEL 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 124244275 1183 VRSPSVLLLDEATSALDTES-EKIVQEALDAAKQGRTCLVIAHRLST--IQNSDVIAIVSEGKIVEKGTHDEL 1252
Cdd:TIGR00955 182 LTDPPLLFCDEPTSGLDSFMaYSVVQVLKGLAQKGKTIICTIHQPSSelFELFDKIILMAEGRVAYLGSPDQA 254
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
1029-1254 |
1.05e-14 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 75.59 E-value: 1.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1029 SIRNVFFNYPTRKdtkVLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGMIMIDGDNIRNLNISSLREQVCI 1108
Cdd:PRK10575 13 ALRNVSFRVPGRT---LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1109 VSQE-PTLFDCTIGENICYG-------------TNRnvtyQEIVEAAKMANIHNFILGLPDgydthvgekgtQLSGGQKQ 1174
Cdd:PRK10575 90 LPQQlPAAEGMTVRELVAIGrypwhgalgrfgaADR----EKVEEAISLVGLKPLAHRLVD-----------SLSGGERQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1175 RIAIARALVRSPSVLLLDEATSALDTESEKIVqealdaakqgrtcLVIAHRLSTIQNSDVIAIVSE-------------- 1240
Cdd:PRK10575 155 RAWIAMLVAQDSRCLLLDEPTSALDIAHQVDV-------------LALVHRLSQERGLTVIAVLHDinmaarycdylval 221
|
250
....*....|....*.
gi 124244275 1241 --GKIVEKGTHDELIR 1254
Cdd:PRK10575 222 rgGEMIAQGTPAELMR 237
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1045-1206 |
1.06e-14 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 74.82 E-value: 1.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1045 VLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGMIMIDGDNIRNLN---ISSLR-EQVCIVSQE----PTLf 1116
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDeeaRAKLRaKHVGFVFQSfmliPTL- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1117 dcTIGENI-----CYGTNRNVTYQEIVEAAKMANIHNFILGLPdgydthvgekgTQLSGGQKQRIAIARALVRSPSVLLL 1191
Cdd:PRK10584 104 --NALENVelpalLRGESSRQSRNGAKALLEQLGLGKRLDHLP-----------AQLSGGEQQRVALARAFNGRPDVLFA 170
|
170
....*....|....*.
gi 124244275 1192 DEATSALDTES-EKIV 1206
Cdd:PRK10584 171 DEPTGNLDRQTgDKIA 186
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
1028-1224 |
1.07e-14 |
|
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: 72.48 E-value: 1.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1028 ISIRNVFFNYPTRKdtkVLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGMIMIDGdnirnlnisslreqvc 1107
Cdd:cd03221 1 IELENLSKTYGGKL---LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGS---------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1108 ivsqeptlfdctiGENICYgtnrnvtyqeiveaakmanihnfilgLPdgydthvgekgtQLSGGQKQRIAIARALVRSPS 1187
Cdd:cd03221 62 -------------TVKIGY--------------------------FE------------QLSGGEKMRLALAKLLLENPN 90
|
170 180 190
....*....|....*....|....*....|....*..
gi 124244275 1188 VLLLDEATSALDTESEKIVQEALdAAKQGrTCLVIAH 1224
Cdd:cd03221 91 LLLLDEPTNHLDLESIEALEEAL-KEYPG-TVILVSH 125
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
417-622 |
1.16e-14 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 75.43 E-value: 1.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 417 LKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFY--DPTKG-RVLIDGVDLREV-----NVHSLREQIGIVSQEPVLFD 488
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgDKSAGsHIELLGRTVQREgrlarDIRKSRANTGYIFQQFNLVN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 489 G-TIYENIKMGNEHATH--DQVVEACKMANANDFIKRLpdgygTRVG------EKGVQLSGGQKQRIAIARALVKNPKIL 559
Cdd:PRK09984 100 RlSVLENVLIGALGSTPfwRTCFSWFTREQKQRALQAL-----TRVGmvhfahQRVSTLSGGQQQRVAIARALMQQAKVI 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 124244275 560 LLDEATSALDTEAEREVQGAL-DQAQA-GRTTIIVAHRLS-TIRNVDRIFVFKAGNIVESGSHEEL 622
Cdd:PRK09984 175 LADEPIASLDPESARIVMDTLrDINQNdGITVVVTLHQVDyALRYCERIVALRQGHVFYDGSSQQF 240
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
753-963 |
1.23e-14 |
|
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: 76.13 E-value: 1.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 753 MFVLMGITFFVGFFTSAN--CLGRCGESLTMKLRFEAFKNLLRQDIAFYDDLRhgTGKLCTRFATDAPNVRYVFT-RLPV 829
Cdd:cd18780 45 VLILLGVVLIGSIATFLRswLFTLAGERVVARLRKRLFSAIIAQEIAFFDVTR--TGELLNRLSSDTQVLQNAVTvNLSM 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 830 VLASIVTICGALGIGFYYGWQLALILVVMVPLLVMGG--YFEMQMRFGKQIRDTqlLEEAGKVASQAVEHIRTVHSLNRQ 907
Cdd:cd18780 123 LLRYLVQIIGGLVFMFTTSWKLTLVMLSVVPPLSIGAviYGKYVRKLSKKFQDA--LAAASTVAEESISNIRTVRSFAKE 200
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 124244275 908 EQFHFTYCEYLREPFNTNLKHAHTYGAVFAFSQSLIFFMYAAAFYLGSIFVNQQAM 963
Cdd:cd18780 201 TKEVSRYSEKINESYLLGKKLARASGGFNGFMGAAAQLAIVLVLWYGGRLVIDGEL 256
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1041-1253 |
1.25e-14 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 75.07 E-value: 1.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1041 KDTKVLQGFTLDIKAGKTVALVGHSGCGKST----IMGLLerfyNQDKGMIMIDGDNIRNLNISsLREQVCI--VSQEPT 1114
Cdd:COG1137 14 GKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTtfymIVGLV----KPDSGRIFLDGEDITHLPMH-KRARLGIgyLPQEAS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1115 LF-DCTIGENIcygtnRNV-TYQEIVEAAKMANIHNFI--LGLpdgydTHVGE-KGTQLSGGQKQRIAIARALVRSPSVL 1189
Cdd:COG1137 89 IFrKLTVEDNI-----LAVlELRKLSKKEREERLEELLeeFGI-----THLRKsKAYSLSGGERRRVEIARALATNPKFI 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 124244275 1190 LLDEATSALD----TESEKIVQealDAAKQG----------RTCLVIAHRlstiqnsdvIAIVSEGKIVEKGTHDELI 1253
Cdd:COG1137 159 LLDEPFAGVDpiavADIQKIIR---HLKERGigvlitdhnvRETLGICDR---------AYIISEGKVLAEGTPEEIL 224
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1043-1227 |
1.83e-14 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 74.47 E-value: 1.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1043 TKVLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGMIMIDGDNIRNLNISS---LREQVC--IVSQEPTLFD 1117
Cdd:PRK11629 22 TDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAkaeLRNQKLgfIYQFHHLLPD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1118 CTIGENICY-----GTNRNVTYQEIVEAAKMAnihnfilglpdGYDTHVGEKGTQLSGGQKQRIAIARALVRSPSVLLLD 1192
Cdd:PRK11629 102 FTALENVAMplligKKKPAEINSRALEMLAAV-----------GLEHRANHRPSELSGGERQRVAIARALVNNPRLVLAD 170
|
170 180 190
....*....|....*....|....*....|....*..
gi 124244275 1193 EATSALDTESEKIVQEALDA--AKQGRTCLVIAHRLS 1227
Cdd:PRK11629 171 EPTGNLDARNADSIFQLLGElnRLQGTAFLVVTHDLQ 207
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
418-622 |
2.09e-14 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 74.74 E-value: 2.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 418 KGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDP----TKGRVLIDGVdlrEVNVHSLR-EQIGIVSQ------EPVL 486
Cdd:PRK10418 20 HGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGK---PVAPCALRgRKIATIMQnprsafNPLH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 487 FDGT-IYENIKMGNEHATHDQVVEACKMANANDfIKRLPDGYGtrvgekgVQLSGGQKQRIAIARALVKNPKILLLDEAT 565
Cdd:PRK10418 97 TMHThARETCLALGKPADDATLTAALEAVGLEN-AARVLKLYP-------FEMSGGMLQRMMIALALLCEAPFIIADEPT 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 566 SALDTEAEREVQGALDQ--AQAGRTTIIVAHRLSTI-RNVDRIFVFKAGNIVESGSHEEL 622
Cdd:PRK10418 169 TDLDVVAQARILDLLESivQKRALGMLLVTHDMGVVaRLADDVAVMSHGRIVEQGDVETL 228
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1045-1252 |
2.21e-14 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 77.44 E-value: 2.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1045 VLQGFTLDIKAGKTVALVGHSGCGKS----TIMGLLER---FYNQdkGMIMIDGDNIRNLNISSLR----EQVCIVSQEP 1113
Cdd:PRK15134 24 VVNDVSLQIEAGETLALVGESGSGKSvtalSILRLLPSppvVYPS--GDIRFHGESLLHASEQTLRgvrgNKIAMIFQEP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1114 --TLFDCTIGENICY-------GTNRNVTYQEIVEAAKMANIHNFILGLPDGydTHvgekgtQLSGGQKQRIAIARALVR 1184
Cdd:PRK15134 102 mvSLNPLHTLEKQLYevlslhrGMRREAARGEILNCLDRVGIRQAAKRLTDY--PH------QLSGGERQRVMIAMALLT 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 124244275 1185 SPSVLLLDEATSALDTESEKIVQEALDAAKQ--GRTCLVIAHRLSTI-QNSDVIAIVSEGKIVEKGTHDEL 1252
Cdd:PRK15134 174 RPELLIADEPTTALDVSVQAQILQLLRELQQelNMGLLFITHNLSIVrKLADRVAVMQNGRCVEQNRAATL 244
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
1031-1247 |
2.69e-14 |
|
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: 73.72 E-value: 2.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1031 RNVFFNYPTRKDTKVLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGMIMIDGdnirnlNISSlreqvcivs 1110
Cdd:cd03220 23 LGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG------RVSS--------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1111 qeptLFDCTIG--------ENI-CYGTNRNVTYQEIveAAKMANIHNFIlGLPDGYDTHVGEkgtqLSGGQKQRIAIARA 1181
Cdd:cd03220 88 ----LLGLGGGfnpeltgrENIyLNGRLLGLSRKEI--DEKIDEIIEFS-ELGDFIDLPVKT----YSSGMKARLAFAIA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 124244275 1182 LVRSPSVLLLDEATSALDTESEKIVQEALDA-AKQGRTCLVIAHRLSTI-QNSDVIAIVSEGKIVEKG 1247
Cdd:cd03220 157 TALEPDILLIDEVLAVGDAAFQEKCQRRLRElLKQGKTVILVSHDPSSIkRLCDRALVLEKGKIRFDG 224
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1042-1259 |
2.80e-14 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 75.64 E-value: 2.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1042 DTKVLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGMIMIDGDNIRNlNISSLREQVCIVSQEPTL-FDCTI 1120
Cdd:PRK13536 53 DKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA-RARLARARIGVVPQFDNLdLEFTV 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1121 GEN-ICYGTNRNVTYQEIvEAAkMANIHNFILgLPDGYDTHVGEkgtqLSGGQKQRIAIARALVRSPSVLLLDEATSALD 1199
Cdd:PRK13536 132 RENlLVFGRYFGMSTREI-EAV-IPSLLEFAR-LESKADARVSD----LSGGMKRRLTLARALINDPQLLILDEPTTGLD 204
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 124244275 1200 TESEKIVQEALDA-AKQGRTCLVIAHRLSTIQN-SDVIAIVSEG-KIVEKGTH---DELIRKS--EIY 1259
Cdd:PRK13536 205 PHARHLIWERLRSlLARGKTILLTTHFMEEAERlCDRLCVLEAGrKIAEGRPHaliDEHIGCQviEIY 272
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1028-1264 |
2.86e-14 |
|
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: 77.15 E-value: 2.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1028 ISIRNVFFNYptrKDTKVLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERF--YNQDKGMIM----------------- 1088
Cdd:TIGR03269 1 IEVKNLTKKF---DGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIyhvalcekcgyverpsk 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1089 ----------------IDGDNIRNLNISSLREQVCIVSQ-------EPTLFDCTIG--ENICYGTNRNVtyQEIVEAAKM 1143
Cdd:TIGR03269 78 vgepcpvcggtlepeeVDFWNLSDKLRRRIRKRIAIMLQrtfalygDDTVLDNVLEalEEIGYEGKEAV--GRAVDLIEM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1144 ANIHNFIlglpdgydTHVGEkgtQLSGGQKQRIAIARALVRSPSVLLLDEATSALDTESEKIVQEALDAA--KQGRTCLV 1221
Cdd:TIGR03269 156 VQLSHRI--------THIAR---DLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAvkASGISMVL 224
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 124244275 1222 IAHRLSTIQN-SDVIAIVSEGKIVEKGTHDELIRK----SEIYQKFCE 1264
Cdd:TIGR03269 225 TSHWPEVIEDlSDKAIWLENGEIKEEGTPDEVVAVfmegVSEVEKECE 272
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
753-944 |
3.02e-14 |
|
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: 74.83 E-value: 3.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 753 MFVLMGITFFVGFFTSAN--CLGRCGESLTMKLRFEAFKNLLRQDIAFYDDLRhgTGKLCTRFATDAPNVRYVF-TRLPV 829
Cdd:cd18575 39 FLLLLAVALVLALASALRfyLVSWLGERVVADLRKAVFAHLLRLSPSFFETTR--TGEVLSRLTTDTTLIQTVVgSSLSI 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 830 VLASIVTICGALGIGFYYGWQLALILVVMVPLLVMGGYFemqmrFGKQIR----DTQ-LLEEAGKVASQAVEHIRTVHSL 904
Cdd:cd18575 117 ALRNLLLLIGGLVMLFITSPKLTLLVLLVIPLVVLPIIL-----FGRRVRrlsrASQdRLADLSAFAEETLSAIKTVQAF 191
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 124244275 905 NRQEQFHFTYCEYLREPFNTNLKHAHTYGAVFAFSQSLIF 944
Cdd:cd18575 192 TREDAERQRFATAVEAAFAAALRRIRARALLTALVIFLVF 231
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
708-964 |
3.33e-14 |
|
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: 74.73 E-value: 3.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 708 FIGGIFGAFIFGSVTPVFALVYAEIFNVYSLPADQMQANVYFWCGMFVLMGITFFVGFFTSANCLGRCGESLTMKLRFEA 787
Cdd:cd18544 1 FILALLLLLLATALELLGPLLIKRAIDDYIVPGQGDLQGLLLLALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 788 FKNLLRQDIAFYDdlRHGTGKLCTRFATDAPNVRYVFTR-LPVVLASIVTICGALGIGFYYGWQLALILVVMVPLLVMGG 866
Cdd:cd18544 81 FSHIQRLPLSFFD--RTPVGRLVTRVTNDTEALNELFTSgLVTLIGDLLLLIGILIAMFLLNWRLALISLLVLPLLLLAT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 867 YFemqmrFGKQIRDTQLL--EEAGKVASQAVEHI---RTVHSLNRQEQFHFTYCEYLREPFNTNLKHAHTYGAVFAFSQS 941
Cdd:cd18544 159 YL-----FRKKSRKAYREvrEKLSRLNAFLQESIsgmSVIQLFNREKREFEEFDEINQEYRKANLKSIKLFALFRPLVEL 233
|
250 260
....*....|....*....|...
gi 124244275 942 LIFFMYAAAFYLGSIFVNQQAMQ 964
Cdd:cd18544 234 LSSLALALVLWYGGGQVLSGAVT 256
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
420-624 |
3.45e-14 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 75.16 E-value: 3.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 420 ISLELKAGDKIALVGSSGCGKS----TIVNLLQrfydpTKGRVL-----IDGVDLREVNVHSLREQIG----IVSQEP-- 484
Cdd:PRK11022 26 ISYSVKQGEVVGIVGESGSGKSvsslAIMGLID-----YPGRVMaekleFNGQDLQRISEKERRNLVGaevaMIFQDPmt 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 485 -------VLFDgtIYENIKM---GNEHATHDQVVEACKMANANDFIKRLpDGYGTrvgekgvQLSGGQKQRIAIARALVK 554
Cdd:PRK11022 101 slnpcytVGFQ--IMEAIKVhqgGNKKTRRQRAIDLLNQVGIPDPASRL-DVYPH-------QLSGGMSQRVMIAMAIAC 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 124244275 555 NPKILLLDEATSALDTEAEREVQGALD--QAQAGRTTIIVAHRLSTIRNV-DRIFVFKAGNIVESGSHEELMS 624
Cdd:PRK11022 171 RPKLLIADEPTTALDVTIQAQIIELLLelQQKENMALVLITHDLALVAEAaHKIIVMYAGQVVETGKAHDIFR 243
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1039-1226 |
3.55e-14 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 74.28 E-value: 3.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1039 TRKDTKVLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDK---GMIMIDGDNIRNL-----NISSLREQV-CIV 1109
Cdd:PRK09984 13 TFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKsagSHIELLGRTVQREgrlarDIRKSRANTgYIF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1110 SQEPTLFDCTIGENI-------------CYGTNRNVTYQEIVEAAKMANIHNFilglpdgydthVGEKGTQLSGGQKQRI 1176
Cdd:PRK09984 93 QQFNLVNRLSVLENVligalgstpfwrtCFSWFTREQKQRALQALTRVGMVHF-----------AHQRVSTLSGGQQQRV 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 124244275 1177 AIARALVRSPSVLLLDEATSALDTESEKIVQEALDAAKQ--GRTCLVIAHRL 1226
Cdd:PRK09984 162 AIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQndGITVVVTLHQV 213
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1028-1233 |
5.05e-14 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 72.29 E-value: 5.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1028 ISIRNVFFNYptrKDTKVLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGMIMIDGDNIRNlNISSLREQVC 1107
Cdd:PRK13540 2 LDVIELDFDY---HDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKK-DLCTYQKQLC 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1108 IVSQE----PTLfdcTIGENICYGTNRNVTYQEIVEAAKMANIHNFIlGLPDGYdthvgekgtqLSGGQKQRIAIARALV 1183
Cdd:PRK13540 78 FVGHRsginPYL---TLRENCLYDIHFSPGAVGITELCRLFSLEHLI-DYPCGL----------LSSGQKRQVALLRLWM 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 124244275 1184 RSPSVLLLDEATSALDTES-EKIVQEALDAAKQGRTCLVIAHRLSTIQNSD 1233
Cdd:PRK13540 144 SKAKLWLLDEPLVALDELSlLTIITKIQEHRAKGGAVLLTSHQDLPLNKAD 194
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
403-633 |
5.13e-14 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 74.76 E-value: 5.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 403 DVHFRYPSrKDIHVLKGISLELKAGDKIALVGSSGCGKS----TIVNLLQRfYDPTKGRVLIDG---VDLREVNVHSLR- 474
Cdd:PRK09473 19 RVTFSTPD-GDVTAVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLAA-NGRIGGSATFNGreiLNLPEKELNKLRa 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 475 EQIGIVSQEP----------------VLFdgtiyENIKMGNEHATHDQV--VEACKMANANDFIKRLPDgygtrvgekgv 536
Cdd:PRK09473 97 EQISMIFQDPmtslnpymrvgeqlmeVLM-----LHKGMSKAEAFEESVrmLDAVKMPEARKRMKMYPH----------- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 537 QLSGGQKQRIAIARALVKNPKILLLDEATSALDTEAEREVQGALDQAQAGRTT--IIVAHRLSTIRNV-DRIFVFKAGNI 613
Cdd:PRK09473 161 EFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTaiIMITHDLGVVAGIcDKVLVMYAGRT 240
|
250 260
....*....|....*....|
gi 124244275 614 VESGSHEElmskqgIFYDMT 633
Cdd:PRK09473 241 MEYGNARD------VFYQPS 254
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
752-963 |
5.21e-14 |
|
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: 74.01 E-value: 5.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 752 GMFVLMGITFFVGFFTSANC---LGRCGESLTMKLRFEAFKNLLRQDIAFYDdlRHGTGKLCTRFATDAPNVRYVFTR-L 827
Cdd:cd18551 37 GLLALLVALFLLQAVLSALSsylLGRTGERVVLDLRRRLWRRLLRLPVSFFD--RRRSGDLVSRVTNDTTLLRELITSgL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 828 PVVLASIVTICGALGIGFYYGWQLALILVVMVPLLVMGGYFemqmrFGKQIRD--TQLLEEAGKVAS---QAVEHIRTVH 902
Cdd:cd18551 115 PQLVTGVLTVVGAVVLMFLLDWVLTLVTLAVVPLAFLIILP-----LGRRIRKasKRAQDALGELSAaleRALSAIRTVK 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 124244275 903 SLNRQEQFHFTYCEYLREPFNTNLKHAHTYGAVFAFSQSLIFFMYAAAFYLGSIFVNQQAM 963
Cdd:cd18551 190 ASNAEERETKRGGEAAERLYRAGLKAAKIEALIGPLMGLAVQLALLVVLGVGGARVASGAL 250
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
125-283 |
5.68e-14 |
|
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: 74.06 E-value: 5.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 125 LVLGVLMFFTSYV--QIACFESYaeRLVHKLRQNYLKAILRQQIQWFDKQQTGNLTARLTDDLERVREGLGdKFALLVQM 202
Cdd:cd18543 46 LALGVAEAVLSFLrrYLAGRLSL--GVEHDLRTDLFAHLQRLDGAFHDRWQSGQLLSRATSDLSLVQRFLA-FGPFLLGN 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 203 FAAFLAGYGVGFFYSWSMTLVMMGFAPLIVLSGAKMSKSMATRTRVEQETYAVAGAIAEETFSSIRTVHSLNGHKRELDR 282
Cdd:cd18543 123 LLTLVVGLVVMLVLSPPLALVALASLPPLVLVARRFRRRYFPASRRAQDQAGDLATVVEESVTGIRVVKAFGRERRELDR 202
|
.
gi 124244275 283 F 283
Cdd:cd18543 203 F 203
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
117-330 |
5.76e-14 |
|
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: 73.96 E-value: 5.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 117 VVKYCIYYLVLGVLMFFTSYVQIACFESYAERLVHKLRQNYLKAILRQQIQWFDKQQTGNLTARLTDDLERVREGLGDKF 196
Cdd:cd18544 40 LLLLALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRDLFSHIQRLPLSFFDRTPVGRLVTRVTNDTEALNELFTSGL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 197 ALLVQMFAAFLAGYGVGFFYSWSMTLVMMGFAPLIVLSGAKMSKSMATRTRVEQETYAVAGAIAEETFSSIRTVHSLNGH 276
Cdd:cd18544 120 VTLIGDLLLLIGILIAMFLLNWRLALISLLVLPLLLLATYLFRKKSRKAYREVREKLSRLNAFLQESISGMSVIQLFNRE 199
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 124244275 277 KRELDRFYNALEVGRQTGI--VKycYMGIGVGFSNLCMYSSYALAFWYGSTLIIND 330
Cdd:cd18544 200 KREFEEFDEINQEYRKANLksIK--LFALFRPLVELLSSLALALVLWYGGGQVLSG 253
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
749-977 |
5.94e-14 |
|
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: 74.06 E-value: 5.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 749 FWCGMFVLMGITFFVGFFTsancLGRCGESLTMKLRFEAFKNLLRQDIAFYDDLRhgTGKLCTRFATDAPNVRYVFTR-L 827
Cdd:cd18576 41 LLLGLFLLQAVFSFFRIYL----FARVGERVVADLRKDLYRHLQRLPLSFFHERR--VGELTSRLSNDVTQIQDTLTTtL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 828 PVVLASIVTICGALGIGFYYGWQLALILVVMVPLLVMGGYFemqmrFGKQIRD--TQLLE---EAGKVASQAVEHIRTVH 902
Cdd:cd18576 115 AEFLRQILTLIGGVVLLFFISWKLTLLMLATVPVVVLVAVL-----FGRRIRKlsKKVQDelaEANTIVEETLQGIRVVK 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 903 SLNRqEQFHFT-YCEYLREPFNTNLKHAHTYGAVFAFSQSLIFFMYAAAFYLGSIFVNQQAMQPID-----VYRVFFAIS 976
Cdd:cd18576 190 AFTR-EDYEIErYRKALERVVKLALKRARIRALFSSFIIFLLFGAIVAVLWYGGRLVLAGELTAGDlvaflLYTLFIAGS 268
|
.
gi 124244275 977 F 977
Cdd:cd18576 269 I 269
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
414-625 |
6.72e-14 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 74.56 E-value: 6.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 414 IHVLKGISLELKAGDKIALVGSSGCGKS----TIVNLLQRFYDPTKGRVLIDGVDLREVNVHSLRE----QIGIVSQEPV 485
Cdd:COG4170 20 VKAVDRVSLTLNEGEIRGLVGESGSGKSliakAICGITKDNWHVTADRFRWNGIDLLKLSPRERRKiigrEIAMIFQEPS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 486 lfdGTIYENIKMGnehathDQVVEAckmanandfikrLPDGYGT-------------------RVGEKG---------VQ 537
Cdd:COG4170 100 ---SCLDPSAKIG------DQLIEA------------IPSWTFKgkwwqrfkwrkkraiellhRVGIKDhkdimnsypHE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 538 LSGGQKQRIAIARALVKNPKILLLDEATSALDTEAEREVQGALDQ-AQAGRTTI-IVAHRLSTI-RNVDRIFVFKAGNIV 614
Cdd:COG4170 159 LTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARlNQLQGTSIlLISHDLESIsQWADTITVLYCGQTV 238
|
250
....*....|.
gi 124244275 615 ESGSHEELMSK 625
Cdd:COG4170 239 ESGPTEQILKS 249
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
744-963 |
7.11e-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: 7.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 744 QANVYFWCGMFVLMGITFFVGFFTSANCLGRCGESLTMKLRFEAFKNLLRQDIAFYDdlRHGTGKLCTRFATDAPNVRYV 823
Cdd:cd18541 36 ASQLLRYALLILLLALLIGIFRFLWRYLIFGASRRIEYDLRNDLFAHLLTLSPSFYQ--KNRTGDLMARATNDLNAVRMA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 824 FTrlPVVLA---SIVTICGALGIGFYYGWQLALILVVMVPLLVMGGYFemqmrFGKQIRD--TQLLEEAGKVASQAVEH- 897
Cdd:cd18541 114 LG--PGILYlvdALFLGVLVLVMMFTISPKLTLIALLPLPLLALLVYR-----LGKKIHKrfRKVQEAFSDLSDRVQESf 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 124244275 898 --IRTVHSLNRQEQFHFTYCEYLREPFNTNLKHAHTYGAVFAFSQSLIFFMYAAAFYLGSIFVNQQAM 963
Cdd:cd18541 187 sgIRVIKAFVQEEAEIERFDKLNEEYVEKNLRLARVDALFFPLIGLLIGLSFLIVLWYGGRLVIRGTI 254
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1044-1217 |
7.41e-14 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 72.60 E-value: 7.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1044 KVLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGMIMIDGDNIRNLNISS-LREQVCIVSQEPTLFD-CTIG 1121
Cdd:PRK11614 19 QALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKiMREAVAIVPEGRRVFSrMTVE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1122 ENICYG---TNRNvTYQEiveaaKMANIHNFilgLPDGYDTHVGEKGTqLSGGQKQRIAIARALVRSPSVLLLDEATSAL 1198
Cdd:PRK11614 99 ENLAMGgffAERD-QFQE-----RIKWVYEL---FPRLHERRIQRAGT-MSGGEQQMLAIGRALMSQPRLLLLDEPSLGL 168
|
170
....*....|....*....
gi 124244275 1199 dteSEKIVQEALDAAKQGR 1217
Cdd:PRK11614 169 ---APIIIQQIFDTIEQLR 184
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
405-622 |
8.66e-14 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 73.97 E-value: 8.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 405 HFRYPSRKDIHVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVD--LREvnvHSLREQIGIV-- 480
Cdd:COG4586 26 GLFRREYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVpfKRR---KEFARRIGVVfg 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 481 --SQ----EPVL--FD--GTIYEnIkmgnEHATHDQVVEAC-KMANANDFIKRlPdgygTRvgekgvQLSGGQKQRIAIA 549
Cdd:COG4586 103 qrSQlwwdLPAIdsFRllKAIYR-I----PDAEYKKRLDELvELLDLGELLDT-P----VR------QLSLGQRMRCELA 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 124244275 550 RALVKNPKILLLDEATSALDTEAEREVQGALDQAQAGR-TTIIVA-HRLSTIRNV-DRIFVFKAGNIVESGSHEEL 622
Cdd:COG4586 167 AALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERgTTILLTsHDMDDIEALcDRVIVIDHGRIIYDGSLEEL 242
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
754-963 |
9.30e-14 |
|
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: 73.23 E-value: 9.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 754 FVLMGITFFVGFFT--SANCLGRCGESLTMKLRFEAFKNLLRQDIAFYDdlRHGTGKLCTRFATDAPNVRYVF-TRLPVV 830
Cdd:cd18542 43 LLILGVALLRGVFRylQGYLAEKASQKVAYDLRNDLYDHLQRLSFSFHD--KARTGDLMSRCTSDVDTIRRFLaFGLVEL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 831 LASIVTICGALGIGFYYGWQLALILVVMVPLLVMGGYfemqmRFGKQIRDTQLL--EEAGKVASQAVEHI---RTVHSLN 905
Cdd:cd18542 121 VRAVLLFIGALIIMFSINWKLTLISLAIIPFIALFSY-----VFFKKVRPAFEEirEQEGELNTVLQENLtgvRVVKAFA 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124244275 906 RQ----EQFHftycEYLREPFNTNLKHAHTYGAVFAFSQSLIFFMYAAAFYLGSIFVNQQAM 963
Cdd:cd18542 196 REdyeiEKFD----KENEEYRDLNIKLAKLLAKYWPLMDFLSGLQIVLVLWVGGYLVINGEI 253
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1022-1254 |
9.84e-14 |
|
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: 75.61 E-value: 9.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1022 KPItgnISIRNVFFNYPT--RKDTKVLQGFTLDIKAGKTVALVGHSGCGKST----IMGLLERF---YNQDKGMIMIDGD 1092
Cdd:TIGR03269 277 EPI---IKVRNVSKRYISvdRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTlskiIAGVLEPTsgeVNVRVGDEWVDMT 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1093 NIRNLNISSLREQVCIVSQEPTLF-DCTIGENIcygtNRNVTYQEIVEAAKMANIHNF-ILGLPDGYDTHVGEKGT-QLS 1169
Cdd:TIGR03269 354 KPGPDGRGRAKRYIGILHQEYDLYpHRTVLDNL----TEAIGLELPDELARMKAVITLkMVGFDEEKAEEILDKYPdELS 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1170 GGQKQRIAIARALVRSPSVLLLDEATSALDTESEKIVQEALDAAKQ--GRTCLVIAHRLSTIQN-SDVIAIVSEGKIVEK 1246
Cdd:TIGR03269 430 EGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREemEQTFIIVSHDMDFVLDvCDRAALMRDGKIVKI 509
|
....*...
gi 124244275 1247 GTHDELIR 1254
Cdd:TIGR03269 510 GDPEEIVE 517
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
399-611 |
9.89e-14 |
|
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: 71.12 E-value: 9.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 399 ISFKDVHFRYPS-RKDIHVLKGISLELKAGDKIALVGSSGCGKSTIVNLL-QRFYDPT-KGRVLIDGVDLREvnvhSLRE 475
Cdd:cd03232 4 LTWKNLNYTVPVkGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLaGRKTAGViTGEILINGRPLDK----NFQR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 476 QIGIVSQEPVLFDG-TIYENIKMgnehathdqvvEACKMAnandfikrlpdgygtrvgekgvqLSGGQKQRIAIARALVK 554
Cdd:cd03232 80 STGYVEQQDVHSPNlTVREALRF-----------SALLRG-----------------------LSVEQRKRLTIGVELAA 125
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 555 NPKILLLDEATSALDTEAEREVQGALDQ-AQAGRTTIIVAHRLS--TIRNVDRIFVFKAG 611
Cdd:cd03232 126 KPSILFLDEPTSGLDSQAAYNIVRFLKKlADSGQAILCTIHQPSasIFEKFDRLLLLKRG 185
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
737-911 |
1.26e-13 |
|
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: 73.32 E-value: 1.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 737 SLPADQMQAnvyFWCGMFVLMGITFFVGFFTSAN--CLGRCGESLTMKLRFEAFKNLLRQDIAFYDdlRHGTGKLCTRFA 814
Cdd:cd18564 44 LLGPDPLAL---LLLAAAALVGIALLRGLASYAGtyLTALVGQRVVLDLRRDLFAHLQRLSLSFHD--RRRTGDLLSRLT 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 815 TDAPNVRYVFTRLPV-VLASIVTICGALGIGFYYGWQLALILVVMVPLLVMGGYfemqmRFGKQIRD--TQLLEEAGKVA 891
Cdd:cd18564 119 GDVGAIQDLLVSGVLpLLTNLLTLVGMLGVMFWLDWQLALIALAVAPLLLLAAR-----RFSRRIKEasREQRRREGALA 193
|
170 180
....*....|....*....|...
gi 124244275 892 SQAVE---HIRTVHSLNRQEQFH 911
Cdd:cd18564 194 SVAQEslsAIRVVQAFGREEHEE 216
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1028-1224 |
1.27e-13 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 72.42 E-value: 1.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1028 ISIRNVFFNYPTRKdtkVLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGMIMIDGDNIRNLNIsslrEQVC 1107
Cdd:PRK11248 2 LQISHLYADYGGKP---ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGA----ERGV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1108 IVSQEPTLFDCTIGENICYG--------TNRNVTYQEIVEAAKMANIHN-FILglpdgydthvgekgtQLSGGQKQRIAI 1178
Cdd:PRK11248 75 VFQNEGLLPWRNVQDNVAFGlqlagvekMQRLEIAHQMLKKVGLEGAEKrYIW---------------QLSGGQRQRVGI 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 124244275 1179 ARALVRSPSVLLLDEATSALDTESEKIVQEALDA--AKQGRTCLVIAH 1224
Cdd:PRK11248 140 ARALAANPQLLLLDEPFGALDAFTREQMQTLLLKlwQETGKQVLLITH 187
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
415-595 |
1.48e-13 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 71.53 E-value: 1.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 415 HVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFY--DPTKGRVLIDGVDL-REVnvhSLREQIGIvsqepvlfDGTI 491
Cdd:COG2401 44 YVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPDNQFgREA---SLIDAIGR--------KGDF 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 492 yenikmgnehathDQVVEACKMANAND--FIKRLPDgygtrvgekgvQLSGGQKQRIAIARALVKNPKILLLDEATSALD 569
Cdd:COG2401 113 -------------KDAVELLNAVGLSDavLWLRRFK-----------ELSTGQKFRFRLALLLAERPKLLVIDEFCSHLD 168
|
170 180
....*....|....*....|....*...
gi 124244275 570 TEAEREVQGALDQA--QAGRTTIIVAHR 595
Cdd:COG2401 169 RQTAKRVARNLQKLarRAGITLVVATHH 196
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1044-1243 |
1.87e-13 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 70.15 E-value: 1.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1044 KVLQGFTLDIKAGKTVALVGHSGCGKS----TIMGLLERfynqDKGMIMIDGDNIRNLNISSLREQ-VCIVSQE------ 1112
Cdd:cd03215 14 GAVRDVSFEVRAGEIVGIAGLVGNGQTelaeALFGLRPP----ASGEITLDGKPVTRRSPRDAIRAgIAYVPEDrkregl 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1113 -PTLfdcTIGENIcygtnrnvtyqeiveaakmanihnfILGLpdgydthvgekgtQLSGGQKQRIAIARALVRSPSVLLL 1191
Cdd:cd03215 90 vLDL---SVAENI-------------------------ALSS-------------LLSGGNQQKVVLARWLARDPRVLIL 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 124244275 1192 DEATSALDTES-EKIVQEALDAAKQGRTCLVIahrlST-----IQNSDVIAIVSEGKI 1243
Cdd:cd03215 129 DEPTRGVDVGAkAEIYRLIRELADAGKAVLLI----SSeldelLGLCDRILVMYEGRI 182
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
1056-1246 |
1.98e-13 |
|
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: 68.94 E-value: 1.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1056 GKTVALVGHSGCGKSTIMGLLERFYNQD-KGMIMIDGDNIRNLNISSLREqvcivsqeptlfdctigenicygtnrnvty 1134
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPgGGVIYIDGEDILEEVLDQLLL------------------------------ 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1135 qeiveaakmanihnfilglpdgydTHVGEKGTQLSGGQKQRIAIARALVRSPSVLLLDEATSALDTESEKIVQEALDA-- 1212
Cdd:smart00382 52 ------------------------IIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELrl 107
|
170 180 190
....*....|....*....|....*....|....*...
gi 124244275 1213 ----AKQGRTCLVIAHRLSTIQNSDVIAIVSEGKIVEK 1246
Cdd:smart00382 108 llllKSEKNLTVILTTNDEKDLGPALLRRRFDRRIVLL 145
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
148-293 |
2.54e-13 |
|
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: 71.99 E-value: 2.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 148 RLVHKLRQNYLKAILRQQIQWFDKQQTGNLTARLTDDLERVREGLGDKFALLVQMFAAFLAGYGVGFFYSWSMTLVMMGF 227
Cdd:cd18590 66 RLNLRLRHQLFSSLVQQDIGFFEKTKTGDLTSRLSTDTTLMSRSVALNANVLLRSLVKTLGMLGFMLSLSWQLTLLTLIE 145
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 124244275 228 APLIVLSGAKMSKSMATRTRVEQETYAVAGAIAEETFSSIRTVHSLNGHKRELDRFYNALEVGRQT 293
Cdd:cd18590 146 MPLTAIAQKVYNTYHQKLSQAVQDSIAKAGELAREAVSSIRTVRSFKAEEEEACRYSEALERTYNL 211
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
706-967 |
2.61e-13 |
|
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: 72.10 E-value: 2.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 706 GWFIGGIFGAFIFGSVTPVFALVYAEIFNVYsLPADQMQANVYFWCGMFVLMGITFFVGFFTSanclgRCGESLTMK--- 782
Cdd:cd18549 2 KLFFLDLFCAVLIAALDLVFPLIVRYIIDDL-LPSKNLRLILIIGAILLALYILRTLLNYFVT-----YWGHVMGARiet 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 783 -LRFEAFKNLLRQDIAFYDdlRHGTGKLCTRFATDAPNVRYVFTRLPV-VLASIVTICGALGIGFYYGWQLALILVVMVP 860
Cdd:cd18549 76 dMRRDLFEHLQKLSFSFFD--NNKTGQLMSRITNDLFDISELAHHGPEdLFISIITIIGSFIILLTINVPLTLIVFALLP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 861 LL-VMGGYFEMQMRFG-KQIRdtqllEEAGKVASQA---VEHIRTVHSlnrqeqfhFTYCEYLREPF---NTNLKHA--H 930
Cdd:cd18549 154 LMiIFTIYFNKKMKKAfRRVR-----EKIGEINAQLedsLSGIRVVKA--------FANEEYEIEKFdegNDRFLESkkK 220
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 124244275 931 TYGAVFAFSQSLIFF---MYAAAFYLGSIFVNQQAMQPID 967
Cdd:cd18549 221 AYKAMAYFFSGMNFFtnlLNLVVLVAGGYFIIKGEITLGD 260
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1057-1248 |
3.07e-13 |
|
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: 75.05 E-value: 3.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1057 KTVALVGHSGCGKSTIMGLLERFYNQDKGMIMIDGDNIRNlNISSLREQVCIVSQEPTLFD-CTIGENICYGTNRNVTYQ 1135
Cdd:TIGR01257 957 QITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET-NLDAVRQSLGMCPQHNILFHhLTVAEHILFYAQLKGRSW 1035
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1136 EIVEAAKMANIHNfilglpDGYDTHVGEKGTQLSGGQKQRIAIARALVRSPSVLLLDEATSALDTESEKIVQEALDAAKQ 1215
Cdd:TIGR01257 1036 EEAQLEMEAMLED------TGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRS 1109
|
170 180 190
....*....|....*....|....*....|....
gi 124244275 1216 GRTCLVIAHRLSTIQN-SDVIAIVSEGKIVEKGT 1248
Cdd:TIGR01257 1110 GRTIIMSTHHMDEADLlGDRIAIISQGRLYCSGT 1143
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
399-619 |
3.13e-13 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 70.98 E-value: 3.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 399 ISFKDVHFrypSRKDIHVLKGISLELKAGDKIALVGSSGCGKSTIVNLL--QRFYDPTKGRVLIDGVDLREVNVHSLR-E 475
Cdd:PRK09580 2 LSIKDLHV---SVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLagREDYEVTGGTVEFKGKDLLELSPEDRAgE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 476 QIGIVSQEPVLFDGT---IYENIKMGNEHATHDQvvEACKMANANDFIK------RLPDGYGTRvgEKGVQLSGGQKQRI 546
Cdd:PRK09580 79 GIFMAFQYPVEIPGVsnqFFLQTALNAVRSYRGQ--EPLDRFDFQDLMEekiallKMPEDLLTR--SVNVGFSGGEKKRN 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 124244275 547 AIARALVKNPKILLLDEATSALDTEAEREVQGALDQAQAG-RTTIIVAH--RLSTIRNVDRIFVFKAGNIVESGSH 619
Cdd:PRK09580 155 DILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGkRSFIIVTHyqRILDYIKPDYVHVLYQGRIVKSGDF 230
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1039-1208 |
3.22e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 69.90 E-value: 3.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1039 TRKDTKVLQGFTLDIKAGKTVALVGHSGCGKST----IMGLLERFynqdKGMIMIDGDNIRnlnISSLREQVCIVSQ--- 1111
Cdd:PRK13539 11 VRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTllrlIAGLLPPA----AGTIKLDGGDID---DPDVAEACHYLGHrna 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1112 -EPTLfdcTIGENI-----CYGTNRnvtyQEIVEAAKMANIHNfILGLPDGYdthvgekgtqLSGGQKQRIAIARALVRS 1185
Cdd:PRK13539 84 mKPAL---TVAENLefwaaFLGGEE----LDIAAALEAVGLAP-LAHLPFGY----------LSAGQKRRVALARLLVSN 145
|
170 180
....*....|....*....|...
gi 124244275 1186 PSVLLLDEATSALDTESEKIVQE 1208
Cdd:PRK13539 146 RPIWILDEPTAALDAAAVALFAE 168
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1029-1244 |
3.95e-13 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 73.52 E-value: 3.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1029 SIRNVffNYPTRKDTKVLQGFTLDIKAGKTVALVGHSGCGKS----TIMGLLERfynqDKGMIMIDGDNIRNLNISSLRE 1104
Cdd:COG3845 259 EVENL--SVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSelaeALAGLRPP----ASGSIRLDGEDITGLSPRERRR 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1105 Q-VCIVSQEPTLF----DCTIGENI--------CYGTNRNVTYQEIVEAAKMAnIHNF-ILglPDGYDTHVGekgtQLSG 1170
Cdd:COG3845 333 LgVAYIPEDRLGRglvpDMSVAENLilgryrrpPFSRGGFLDRKAIRAFAEEL-IEEFdVR--TPGPDTPAR----SLSG 405
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 124244275 1171 GQKQRIAIARALVRSPSVLLLDEATSALDTES-EKIVQEALDAAKQGRTCLVIAHRLSTIQN-SDVIAIVSEGKIV 1244
Cdd:COG3845 406 GNQQKVILARELSRDPKLLIAAQPTRGLDVGAiEFIHQRLLELRDAGAAVLLISEDLDEILAlSDRIAVMYEGRIV 481
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
407-614 |
6.10e-13 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 72.75 E-value: 6.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 407 RYPSRKDIHVLKGISLELKAGDKIALVGSSGCGKSTIVNLL--QRfyDPTKGRVLIDGVDLREVNVHSLREQ-IGIVSQE 483
Cdd:COG3845 264 SVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALagLR--PPASGSIRLDGEDITGLSPRERRRLgVAYIPED 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 484 P-----VLfDGTIYENIKMG-------------NEHATHdqvveackmANANDFIKRL---PDGYGTRVGekgvQLSGGQ 542
Cdd:COG3845 342 RlgrglVP-DMSVAENLILGryrrppfsrggflDRKAIR---------AFAEELIEEFdvrTPGPDTPAR----SLSGGN 407
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124244275 543 KQRIAIARALVKNPKILLLDEATSALDTEAEREVQGAL-DQAQAGRTTIIVAHRLSTIRNV-DRIFVFKAGNIV 614
Cdd:COG3845 408 QQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLlELRDAGAAVLLISEDLDEILALsDRIAVMYEGRIV 481
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
779-954 |
1.10e-12 |
|
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: 70.03 E-value: 1.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 779 LTMKLRFEAFKNLLRQDIAFYDDLRhgTGKLCTRFATDAPNVRYVFT-RLPVVLASIVTICGALGIGFYYGWQLALILVV 857
Cdd:cd18784 67 LNIRIRNLLFRSIVSQEIGFFDTVK--TGDITSRLTSDTTTMSDTVSlNLNIFLRSLVKAIGVIVFMFKLSWQLSLVTLI 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 858 MVPL--LVMGGYFEMQMRFGKQIRDTqlLEEAGKVASQAVEHIRTVHSLNRQEQFHFTYCEYLREPFNTNLKHAHTYGAv 935
Cdd:cd18784 145 GLPLiaIVSKVYGDYYKKLSKAVQDS--LAKANEVAEETISSIRTVRSFANEDGEANRYSEKLKDTYKLKIKEALAYGG- 221
|
170 180
....*....|....*....|
gi 124244275 936 FAFSQSLIFF-MYAAAFYLG 954
Cdd:cd18784 222 YVWSNELTELaLTVSTLYYG 241
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
427-600 |
1.38e-12 |
|
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: 66.63 E-value: 1.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 427 GDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVL-IDGVDLREVNVHSLREQIgivsqepvlfdgtiyenikmgnehathd 505
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIyIDGEDILEEVLDQLLLII---------------------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 506 qvveackmanandfikrlpdgygtrVGEKGVQLSGGQKQRIAIARALVKNPKILLLDEATSALDTEAEREVQGALD---- 581
Cdd:smart00382 54 -------------------------VGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElrll 108
|
170 180
....*....|....*....|..
gi 124244275 582 ---QAQAGRTTIIVAHRLSTIR 600
Cdd:smart00382 109 lllKSEKNLTVILTTNDEKDLG 130
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1040-1254 |
1.98e-12 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 71.42 E-value: 1.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1040 RKDTKVLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGMIMIDGDNI--RNLNISSLREQ------------ 1105
Cdd:PRK10261 26 QQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLrrRSRQVIELSEQsaaqmrhvrgad 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1106 VCIVSQEPT-----LFdcTIGENIC------YGTNRNvtyQEIVEAAKMANIhnfiLGLPDGyDTHVGEKGTQLSGGQKQ 1174
Cdd:PRK10261 106 MAMIFQEPMtslnpVF--TVGEQIAesirlhQGASRE---EAMVEAKRMLDQ----VRIPEA-QTILSRYPHQLSGGMRQ 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1175 RIAIARALVRSPSVLLLDEATSALDTESEKIVQEALDAAKQGRTCLV--IAHRLSTIQN-SDVIAIVSEGKIVEKGTHDE 1251
Cdd:PRK10261 176 RVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVifITHDMGVVAEiADRVLVMYQGEAVETGSVEQ 255
|
...
gi 124244275 1252 LIR 1254
Cdd:PRK10261 256 IFH 258
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
1040-1245 |
2.96e-12 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 67.68 E-value: 2.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1040 RKDTKVLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFY--NQDKGMIMIDGDNIrnlnisslreqvcivSQEPTLFD 1117
Cdd:COG2401 40 VVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPDNQF---------------GREASLID 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1118 CtIGenicygtnRNVTYQEIVEAAKMAnihnfilGLPDG--YDTHVGEkgtqLSGGQKQRIAIARALVRSPSVLLLDEAT 1195
Cdd:COG2401 105 A-IG--------RKGDFKDAVELLNAV-------GLSDAvlWLRRFKE----LSTGQKFRFRLALLLAERPKLLVIDEFC 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 124244275 1196 SALDTESEKIVQEAL-DAAKQ-GRTCLVIAHR---LSTIQnSDVIAIVSEGKIVE 1245
Cdd:COG2401 165 SHLDRQTAKRVARNLqKLARRaGITLVVATHHydvIDDLQ-PDLLIFVGYGGVPE 218
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1035-1253 |
4.88e-12 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 67.89 E-value: 4.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1035 FNYPT----RKDTKVLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGMIMIDGDNIRNLNISSLREQVCIVS 1110
Cdd:PRK15112 14 FRYRTgwfrRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIRMIF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1111 QEPT-----------LFDCTIGENicygTNRNVTYQE--IVEAAKMANIhnfilgLPDgydtHVGEKGTQLSGGQKQRIA 1177
Cdd:PRK15112 94 QDPStslnprqrisqILDFPLRLN----TDLEPEQREkqIIETLRQVGL------LPD----HASYYPHMLAPGQKQRLG 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124244275 1178 IARALVRSPSVLLLDEATSALD-TESEKIVQEALD-AAKQGRTCLVIAHRLSTIQN-SDVIAIVSEGKIVEKGTHDELI 1253
Cdd:PRK15112 160 LARALILRPKVIIADEALASLDmSMRSQLINLMLElQEKQGISYIYVTQHLGMMKHiSDQVLVMHQGEVVERGSTADVL 238
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
412-594 |
4.95e-12 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 66.37 E-value: 4.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 412 KDIHVL-KGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDLREVNVHSLRE------QIGIvsqEP 484
Cdd:PRK13538 11 RDERILfSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDllylghQPGI---KT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 485 VLfdgTIYENIKMgNEHATHDQVVEACKMANAndfikrlpdgygtRVGEKGV------QLSGGQKQRIAIARALVKNPKI 558
Cdd:PRK13538 88 EL---TALENLRF-YQRLHGPGDDEALWEALA-------------QVGLAGFedvpvrQLSAGQQRRVALARLWLTRAPL 150
|
170 180 190
....*....|....*....|....*....|....*..
gi 124244275 559 LLLDEATSALDTEAEREVQGALDQ-AQAGRTTIIVAH 594
Cdd:PRK13538 151 WILDEPFTAIDKQGVARLEALLAQhAEQGGMVILTTH 187
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
756-904 |
7.99e-12 |
|
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: 67.57 E-value: 7.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 756 LMGITFFVGFFTSANC--LGRCGESLTMKLRFEAFKNLLRQDIAFYDdlRHGTGKLCTRFATDAPNVRYVFtRLPVV--L 831
Cdd:cd18574 48 LLGLYLLQSLLTFAYIslLSVVGERVAARLRNDLFSSLLRQDIAFFD--THRTGELVNRLTADVQEFKSSF-KQCVSqgL 124
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124244275 832 ASIVTICGALGIGFYYGWQLALILVVMVPLLVMGGYFemqmrFGKQIRDT------QLLEEAGkVASQAVEHIRTVHSL 904
Cdd:cd18574 125 RSVTQTVGCVVSLYLISPKLTLLLLVIVPVVVLVGTL-----YGSFLRKLsrraqaQVAKATG-VADEALGNIRTVRAF 197
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
750-909 |
1.06e-11 |
|
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: 67.12 E-value: 1.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 750 WCGMFVLMGITFFVGFFTSANCLGRCGESLTMKLRFEAFKNLLRQDIAFYDDLRhgTGKLCTRFATDAPNVRYVFTRLPV 829
Cdd:cd18543 41 LVLLLLALGVAEAVLSFLRRYLAGRLSLGVEHDLRTDLFAHLQRLDGAFHDRWQ--SGQLLSRATSDLSLVQRFLAFGPF 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 830 VLASIVTICGALGIGFYYGWQLALILVVMVPLLVMGGYFeMQMRFGKQIRDTQllEEAGKVAS---QAVEHIRTVHSLNR 906
Cdd:cd18543 119 LLGNLLTLVVGLVVMLVLSPPLALVALASLPPLVLVARR-FRRRYFPASRRAQ--DQAGDLATvveESVTGIRVVKAFGR 195
|
...
gi 124244275 907 QEQ 909
Cdd:cd18543 196 ERR 198
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1029-1267 |
1.08e-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: 1.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1029 SIRNVFFNY-PTRKDTK-VLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGMIMIDGdnirnlNISSL---- 1102
Cdd:COG1134 23 SLKELLLRRrRTRREEFwALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG------RVSALlelg 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1103 ---------REQVcivsqeptLFDCTIgenicYGTNRNVT---YQEIVEaakMANIHNFIlglpdgyDTHVGekgtQLSG 1170
Cdd:COG1134 97 agfhpeltgRENI--------YLNGRL-----LGLSRKEIdekFDEIVE---FAELGDFI-------DQPVK----TYSS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1171 GQKQRIAIARALVRSPSVLLLDEATSALDTE-SEKIVQEALDAAKQGRTCLVIAHRLSTIQN-SDVIAIVSEGKIVEKGT 1248
Cdd:COG1134 150 GMRARLAFAVATAVDPDILLVDEVLAVGDAAfQKKCLARIRELRESGRTVIFVSHSMGAVRRlCDRAIWLEKGRLVMDGD 229
|
250
....*....|....*....
gi 124244275 1249 HDELIRKseiYQKFCETQR 1267
Cdd:COG1134 230 PEEVIAA---YEALLAGRE 245
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1053-1254 |
1.17e-11 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 67.46 E-value: 1.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1053 IKAGKTVALVGHSGCGKS----TIMGLLERfynqdKGMIM-----IDGDNIRNLNISSLRE----QVCIVSQEP--TLFD 1117
Cdd:PRK11022 30 VKQGEVVGIVGESGSGKSvsslAIMGLIDY-----PGRVMaekleFNGQDLQRISEKERRNlvgaEVAMIFQDPmtSLNP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1118 C-TIGENIC------YGTNRNVTYQEIVEAAKManihnfiLGLPDGyDTHVGEKGTQLSGGQKQRIAIARALVRSPSVLL 1190
Cdd:PRK11022 105 CyTVGFQIMeaikvhQGGNKKTRRQRAIDLLNQ-------VGIPDP-ASRLDVYPHQLSGGMSQRVMIAMAIACRPKLLI 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 124244275 1191 LDEATSALD-TESEKIVQEALDAAKQGRTCLV-IAHRLSTI-QNSDVIAIVSEGKIVEKGTHDELIR 1254
Cdd:PRK11022 177 ADEPTTALDvTIQAQIIELLLELQQKENMALVlITHDLALVaEAAHKIIVMYAGQVVETGKAHDIFR 243
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1048-1254 |
1.18e-11 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 66.55 E-value: 1.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1048 GFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGMIMIDGDNIRNL---NISslREQVCIVSQEPTLF-DCTIGEN 1123
Cdd:PRK11300 23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLpghQIA--RMGVVRTFQHVRLFrEMTVIEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1124 ICYGTNRNV------------TYQEiVEAAKMANIHNFI--LGLPDgydtHVGEKGTQLSGGQKQRIAIARALVRSPSVL 1189
Cdd:PRK11300 101 LLVAQHQQLktglfsgllktpAFRR-AESEALDRAATWLerVGLLE----HANRQAGNLAYGQQRRLEIARCMVTQPEIL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 124244275 1190 LLDEATSALDTESEKIVQEALDAAKQ--GRTCLVIAHRLSTIQN-SDVIAIVSEGKIVEKGTHDElIR 1254
Cdd:PRK11300 176 MLDEPAAGLNPKETKELDELIAELRNehNVTVLLIEHDMKLVMGiSDRIYVVNQGTPLANGTPEE-IR 242
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
408-606 |
1.24e-11 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 68.81 E-value: 1.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 408 YPSRKdiHVLKGISLELKAGDKIALVGSSGCGKSTivnLLQrfydptkgrvLIDGVDlREVNVHSLREQ---IGIVSQEP 484
Cdd:TIGR03719 14 VPPKK--EILKDISLSFFPGAKIGVLGLNGAGKST---LLR----------IMAGVD-KDFNGEARPQPgikVGYLPQEP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 485 VLFDG-TIYENI-------------------KMGNEHATHDQVVEacKMANANDFIK------------------RLPDG 526
Cdd:TIGR03719 78 QLDPTkTVRENVeegvaeikdaldrfneisaKYAEPDADFDKLAA--EQAELQEIIDaadawdldsqleiamdalRCPPW 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 527 yGTRVGEkgvqLSGGQKQRIAIARALVKNPKILLLDEATSALDTEAEREVQGALDQAQAgrTTIIVAHrlstirnvDRIF 606
Cdd:TIGR03719 156 -DADVTK----LSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPG--TVVAVTH--------DRYF 220
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
417-620 |
1.35e-11 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 66.44 E-value: 1.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 417 LKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDLREVNVHSLreqIGIVSQE-------PVLFDG 489
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNL---VAYVPQSeevdwsfPVLVED 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 490 TI----YENIKMGNEHATHDQ--VVEACKMANANDFIKRlpdgygtRVGEkgvqLSGGQKQRIAIARALVKNPKILLLDE 563
Cdd:PRK15056 100 VVmmgrYGHMGWLRRAKKRDRqiVTAALARVDMVEFRHR-------QIGE----LSGGQKKRVFLARAIAQQGQVILLDE 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 124244275 564 ATSALDTEAEREVQGALDQAQA-GRTTIIVAHRLSTIRNVDRIFVFKAGNIVESGSHE 620
Cdd:PRK15056 169 PFTGVDVKTEARIISLLRELRDeGKTMLVSTHNLGSVTEFCDYTVMVKGTVLASGPTE 226
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
1040-1216 |
1.39e-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: 65.07 E-value: 1.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1040 RKDTKVLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGMIMIDGDNIRNLNiSSLREQVCIVSQEPTL-FDC 1118
Cdd:TIGR01189 10 RGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQR-DEPHENILYLGHLPGLkPEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1119 TIGENICYgtnrnvtYQEIVEAAKMaNIHNFI--LGLPDGYDTHVGekgtQLSGGQKQRIAIARALVRSPSVLLLDEATS 1196
Cdd:TIGR01189 89 SALENLHF-------WAAIHGGAQR-TIEDALaaVGLTGFEDLPAA----QLSAGQQRRLALARLWLSRRPLWILDEPTT 156
|
170 180
....*....|....*....|..
gi 124244275 1197 ALDTESEKIVQEALDA--AKQG 1216
Cdd:TIGR01189 157 ALDKAGVALLAGLLRAhlARGG 178
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
420-621 |
1.50e-11 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 68.40 E-value: 1.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 420 ISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGvdlREVNVHSLREQI--GIV-SQEPVLFDG-----TI 491
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDG---KPIDIRSPRDAIraGIMlCPEDRKAEGiipvhSV 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 492 YENIKMG--NEHATHDQVVEACKMA-NANDFIKRL----PDGygtrvGEKGVQLSGGQKQRIAIARALVKNPKILLLDEA 564
Cdd:PRK11288 349 ADNINISarRHHLRAGCLINNRWEAeNADRFIRSLniktPSR-----EQLIMNLSGGNQQKAILGRWLSEDMKVILLDEP 423
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 124244275 565 TSALDTEAEREVQGAL-DQAQAGRTTIIVAHRLSTIRNV-DRIFVFKAGNIVESGSHEE 621
Cdd:PRK11288 424 TRGIDVGAKHEIYNVIyELAAQGVAVLFVSSDLPEVLGVaDRIVVMREGRIAGELAREQ 482
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
399-617 |
3.43e-11 |
|
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: 63.82 E-value: 3.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 399 ISFKDVHFRYPSRKDIH-VLKGISLELKAGDKIALVGSSGCGKST----IVNLLQRFYDPTkGRVLIDGVDLREvNVHSL 473
Cdd:cd03233 4 LSWRNISFTTGKGRSKIpILKDFSGVVKPGEMVLVLGRPGSGCSTllkaLANRTEGNVSVE-GDIHYNGIPYKE-FAEKY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 474 REQIGIVSQE----PVLfdgTIYENIKMgnehathdqvveACKMaNANDFIKrlpdgygtrvgekGVqlSGGQKQRIAIA 549
Cdd:cd03233 82 PGEIIYVSEEdvhfPTL---TVRETLDF------------ALRC-KGNEFVR-------------GI--SGGERKRVSIA 130
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124244275 550 RALVKNPKILLLDEATSALD-TEAEREVQGALDQAQAGRTTIIVAhrLS----TIRN-VDRIFVFKAGNIVESG 617
Cdd:cd03233 131 EALVSRASVLCWDNSTRGLDsSTALEILKCIRTMADVLKTTTFVS--LYqasdEIYDlFDKVLVLYEGRQIYYG 202
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
1049-1262 |
3.45e-11 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 64.95 E-value: 3.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1049 FTLDIKAGKTVALVGHSGCGKST----IMGLLErfynqDKGMIMIDGDNIRNLNISSLREQVCIVSQE-PTLFDCTIGEn 1123
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTllarMAGLLP-----GSGSIQFAGQPLEAWSAAELARHRAYLSQQqTPPFAMPVFQ- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1124 icY-------GTNRNVTYQEIVEAAKManihnfiLGLPDGYDTHVGekgtQLSGGQKQRIAIARALVR-SPSV------L 1189
Cdd:PRK03695 89 --YltlhqpdKTRTEAVASALNEVAEA-------LGLDDKLGRSVN----QLSGGEWQRVRLAAVVLQvWPDInpagqlL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1190 LLDEATSALDtesekIVQE-ALDA-----AKQGRTCLVIAHRLS-TIQNSDVIAIVSEGKIVEKGTHDELIRKSEIYQKF 1262
Cdd:PRK03695 156 LLDEPMNSLD-----VAQQaALDRllselCQQGIAVVMSSHDLNhTLRHADRVWLLKQGKLLASGRRDEVLTPENLAQVF 230
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
395-596 |
3.72e-11 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 64.75 E-value: 3.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 395 MKGDISFKDVHFRYPSRKdihVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDgvdlrevnvHSLR 474
Cdd:PRK09544 1 MTSLVSLENVSVSFGQRR---VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRN---------GKLR 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 475 eqIGIVSQEPVLfDGTIYENIK--MGNEHATHDQ-VVEACKMANANDFIkrlpdgygtrvgEKGVQ-LSGGQKQRIAIAR 550
Cdd:PRK09544 69 --IGYVPQKLYL-DTTLPLTVNrfLRLRPGTKKEdILPALKRVQAGHLI------------DAPMQkLSGGETQRVLLAR 133
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 124244275 551 ALVKNPKILLLDEATSALDTEAEREVQGALDQ--AQAGRTTIIVAHRL 596
Cdd:PRK09544 134 ALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQlrRELDCAVLMVSHDL 181
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
408-571 |
3.88e-11 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 67.45 E-value: 3.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 408 YPSRKdiHVLKGISLELKAGDKIALVGSSGCGKSTivnLLQrfydptkgrvLIDGVDlREVN---VHSLREQIGIVSQEP 484
Cdd:PRK11819 16 VPPKK--QILKDISLSFFPGAKIGVLGLNGAGKST---LLR----------IMAGVD-KEFEgeaRPAPGIKVGYLPQEP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 485 VLFDG-TIYENI-------------------KMGNEHATHDQVVEacKMANANDFIK------------------RLPDG 526
Cdd:PRK11819 80 QLDPEkTVRENVeegvaevkaaldrfneiyaAYAEPDADFDALAA--EQGELQEIIDaadawdldsqleiamdalRCPPW 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 124244275 527 yGTRVGekgvQLSGGQKQRIAIARALVKNPKILLLDEATSALDTE 571
Cdd:PRK11819 158 -DAKVT----KLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAE 197
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1049-1252 |
5.37e-11 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 65.52 E-value: 5.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1049 FTLDikAGKTVALVGHSGCGKS----TIMGLLERfYNQDKGMIMIDGDNIRNLN---ISSLR-EQVCIVSQEP-TLFD-- 1117
Cdd:PRK09473 37 FSLR--AGETLGIVGESGSGKSqtafALMGLLAA-NGRIGGSATFNGREILNLPekeLNKLRaEQISMIFQDPmTSLNpy 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1118 CTIGENIC------YGTNRNVTYQEIV---EAAKMANIHNFILGLPdgydtHvgekgtQLSGGQKQRIAIARALVRSPSV 1188
Cdd:PRK09473 114 MRVGEQLMevlmlhKGMSKAEAFEESVrmlDAVKMPEARKRMKMYP-----H------EFSGGMRQRVMIAMALLCRPKL 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 124244275 1189 LLLDEATSALDTESEKIVQEALDAAKQ--GRTCLVIAHRLSTIQNS-DVIAIVSEGKIVEKGTHDEL 1252
Cdd:PRK09473 183 LIADEPTTALDVTVQAQIMTLLNELKRefNTAIIMITHDLGVVAGIcDKVLVMYAGRTMEYGNARDV 249
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1044-1253 |
6.35e-11 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 66.29 E-value: 6.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1044 KVLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGMIMIDGDNIrnlNISSLREQ----VCIVSQEPTLF-DC 1118
Cdd:PRK10982 12 KALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEI---DFKSSKEAlengISMVHQELNLVlQR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1119 TIGENICYGtnRNVTYQEIVEAAKMANIHNFILGLPDgYDTHVGEKGTQLSGGQKQRIAIARALVRSPSVLLLDEATSAL 1198
Cdd:PRK10982 89 SVMDNMWLG--RYPTKGMFVDQDKMYRDTKAIFDELD-IDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 124244275 1199 dTESE-----KIVQEALDaakQGRTCLVIAHRLSTI-QNSDVIAIVSEGKIV-----EKGTHDELI 1253
Cdd:PRK10982 166 -TEKEvnhlfTIIRKLKE---RGCGIVYISHKMEEIfQLCDEITILRDGQWIatqplAGLTMDKII 227
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1037-1242 |
6.64e-11 |
|
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: 63.97 E-value: 6.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1037 YPTRKdtKVLQGFTLDIKAG-----KTVALVGHSGCGKSTIMGLLERFYNQDKGMIMIDGDNIrnlnisSLREQVCIVSQ 1111
Cdd:cd03237 3 YPTMK--KTLGEFTLEVEGGsisesEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTV------SYKPQYIKADY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1112 EPTLFDCTIGENICYGTNRnvtyQEIVEAAKManihnfiLGLPDGYDTHVgekgTQLSGGQKQRIAIARALVRSPSVLLL 1191
Cdd:cd03237 75 EGTVRDLLSSITKDFYTHP----YFKTEIAKP-------LQIEQILDREV----PELSGGELQRVAIAACLSKDADIYLL 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 124244275 1192 DEATSALDTESEKIVQEALD--AAKQGRTCLVIAHRLSTIqnsDVIA---IVSEGK 1242
Cdd:cd03237 140 DEPSAYLDVEQRLMASKVIRrfAENNEKTAFVVEHDIIMI---DYLAdrlIVFEGE 192
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
776-1245 |
7.59e-11 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 66.15 E-value: 7.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 776 GESLTMKLRFEAFKNLLRQDIAFYDDLrhGTGKLCTRFATDAPNVRYVFTRLP-VVLASIVTICGALgigfYYGW---QL 851
Cdd:PRK10522 76 GHHFVYRLRSEFIKRILDTHVERIEQL--GSASLLASLTSDVRNITIAFVRLPeLVQGIILTLGSAA----YLAWlspKM 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 852 ALILVVMVPLLVMGGYFEMqMRFGKQIRDTQLLEEAGKVASQAVEHIRTVHSLNRQEQFHFTYCEYLR--EPFNTNLKHA 929
Cdd:PRK10522 150 LLVTAIWMAVTIWGGFVLV-ARVYKHMATLRETEDKLYNDYQTVLEGRKELTLNRERAEYVFENEYEPdaQEYRHHIIRA 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 930 HTY-------------GAVfafsqSLIFFM----------YAAAFYLGSIFVNQqamqPIdvyrvffaisfcGQMIGNtt 986
Cdd:PRK10522 229 DTFhlsavnwsnimmlGAI-----GLVFYManslgwadtnVAATYSLTLLFLRT----PL------------LSAVGA-- 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 987 sfIPDVVKARLA------ASLLFYLIEHPTPIdslsdsgiVKPITGNISIRNVFFNYPTrkdtkvlQGFT-----LDIKA 1055
Cdd:PRK10522 286 --LPTLLSAQVAfnklnkLALAPYKAEFPRPQ--------AFPDWQTLELRNVTFAYQD-------NGFSvgpinLTIKR 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1056 GKTVALVGHSGCGKSTIMGLLERFYNQDKGMIMIDGDNIRNLNISSLREQVCIVSQEPTLFDCTIGENicyGTNRNVT-Y 1134
Cdd:PRK10522 349 GELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSAVFTDFHLFDQLLGPE---GKPANPAlV 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1135 QEIVEAAKMANihnfILGLPDGYDTHvgekgTQLSGGQKQRIAIARALVRSPSVLLLDEATSALDTESEKIV-QEALDAA 1213
Cdd:PRK10522 426 EKWLERLKMAH----KLELEDGRISN-----LKLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRREFyQVLLPLL 496
|
490 500 510
....*....|....*....|....*....|...
gi 124244275 1214 KQ-GRTCLVIAHRLSTIQNSDVIAIVSEGKIVE 1245
Cdd:PRK10522 497 QEmGKTIFAISHDDHYFIHADRLLEMRNGQLSE 529
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
773-965 |
8.70e-11 |
|
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: 64.43 E-value: 8.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 773 GRCGESLTMKLRFEAFKNLLRQDIAFYDdlRHGTGKLCTRFATDAPNVRYVF-TRLPVVLASIVTICGALGIGFYYGWQL 851
Cdd:cd18546 64 GRTGERLLYDLRLRVFAHLQRLSLDFHE--RETSGRIMTRMTSDIDALSELLqTGLVQLVVSLLTLVGIAVVLLVLDPRL 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 852 ALI-LVVMVPLLVMGGYFEMQMRFG-KQIRdtqllEEAGKVASQAVEH---IRTVHSLNRQEQFHFTYCEYLREPFNTNL 926
Cdd:cd18546 142 ALVaLAALPPLALATRWFRRRSSRAyRRAR-----ERIAAVNADLQETlagIRVVQAFRRERRNAERFAELSDDYRDARL 216
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 124244275 927 kHAHTYGAV-FAFSQSLIFFMYAAAFYLGSIFVNQQAMQP 965
Cdd:cd18546 217 -RAQRLVAIyFPGVELLGNLATAAVLLVGAWRVAAGTLTV 255
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
1040-1271 |
8.75e-11 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 64.08 E-value: 8.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1040 RKDTKVLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQD--------KGMIMIDGDNIRNLNISSLREQVCIVSQ 1111
Cdd:PRK13547 11 RRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarvTGDVTLNGEPLAAIDAPRLARLRAVLPQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1112 --EPTlFDCTIGENICYGTnrnvtYQEIVEAAKMA----NIHNFILGLPDGyDTHVGEKGTQLSGGQKQRIAIARAL--- 1182
Cdd:PRK13547 91 aaQPA-FAFSAREIVLLGR-----YPHARRAGALThrdgEIAWQALALAGA-TALVGRDVTTLSGGELARVQFARVLaql 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1183 ------VRSPSVLLLDEATSALD-TESEKIVQEALDAAKQGRT-CLVIAHRLS-TIQNSDVIAIVSEGKIVEKGTHDELI 1253
Cdd:PRK13547 164 wpphdaAQPPRYLLLDEPTAALDlAHQHRLLDTVRRLARDWNLgVLAIVHDPNlAARHADRIAMLADGAIVAHGAPADVL 243
|
250
....*....|....*...
gi 124244275 1254 RKSEIYQKFCETQRIVES 1271
Cdd:PRK13547 244 TPAHIARCYGFAVRLVDA 261
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1011-1244 |
1.11e-10 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 65.81 E-value: 1.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1011 PIDSLSDSGIVKPITGnisiRNVFFNYPTRKDT--------------KVLQGFTLDIKAGKTVALVGHSGCGKS----TI 1072
Cdd:COG1129 223 PVAELTEDELVRLMVG----RELEDLFPKRAAApgevvleveglsvgGVVRDVSFSVRAGEILGIAGLVGAGRTelarAL 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1073 MGLLERfynqDKGMIMIDGDNIRNLNIS-SLREQVCIVSQE-------PTLfdcTIGENIC------YGTNRNVTYQEIV 1138
Cdd:COG1129 299 FGADPA----DSGEIRLDGKPVRIRSPRdAIRAGIAYVPEDrkgeglvLDL---SIRENITlasldrLSRGGLLDRRRER 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1139 EAAKmanihNFI--LGL-PDGYDTHVGekgtQLSGGQKQRIAIARALVRSPSVLLLDEATSALD--TESE--KIVQEald 1211
Cdd:COG1129 372 ALAE-----EYIkrLRIkTPSPEQPVG----NLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDvgAKAEiyRLIRE--- 439
|
250 260 270
....*....|....*....|....*....|....*...
gi 124244275 1212 AAKQGRTCLVIahrlST-----IQNSDVIAIVSEGKIV 1244
Cdd:COG1129 440 LAAEGKAVIVI----SSelpelLGLSDRILVMREGRIV 473
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
115-330 |
1.14e-10 |
|
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: 64.01 E-value: 1.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 115 SEVVKYCIYYLVLGVLMFFTSYVQIACFESYAERLVHKLRQNYLKAILRQQIQWFDKQQTGNLTARLTDDLERVRE---- 190
Cdd:cd18549 39 RLILIIGAILLALYILRTLLNYFVTYWGHVMGARIETDMRRDLFEHLQKLSFSFFDNNKTGQLMSRITNDLFDISElahh 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 191 GLGDKFALLVQMFAAFlagyGVGFFYSWSMTLVMMGFAPLIVLSGAKMSKSMATRTRVEQETYAVAGAIAEETFSSIRTV 270
Cdd:cd18549 119 GPEDLFISIITIIGSF----IILLTINVPLTLIVFALLPLMIIFTIYFNKKMKKAFRRVREKIGEINAQLEDSLSGIRVV 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124244275 271 HSLNGHKRELDRF----YNALEVGRQTgivkYCYMGIGVGFSNLCMYSSYALAFWYGSTLIIND 330
Cdd:cd18549 195 KAFANEEYEIEKFdegnDRFLESKKKA----YKAMAYFFSGMNFFTNLLNLVVLVAGGYFIIKG 254
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
416-624 |
1.22e-10 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 66.06 E-value: 1.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 416 VLKGISLELKAGDKIALVGSSGCGKSTIVNLLQ-RFYDPT-KGRVLIDGvdlREVNVHSLReQIGIVSQEPVLFDG-TIY 492
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAgRIQGNNfTGTILANN---RKPTKQILK-RTGFVTQDDILYPHlTVR 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 493 ENIKMGNEHATHDQVVEACKMANANDFIKRL--PDGYGTRVGEKGVQ-LSGGQKQRIAIARALVKNPKILLLDEATSALD 569
Cdd:PLN03211 159 ETLVFCSLLRLPKSLTKQEKILVAESVISELglTKCENTIIGNSFIRgISGGERKRVSIAHEMLINPSLLILDEPTSGLD 238
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 124244275 570 -TEAEREVQGALDQAQAGRTTIIVAHRLST--IRNVDRIFVFKAGNIVESGSHEELMS 624
Cdd:PLN03211 239 aTAAYRLVLTLGSLAQKGKTIVTSMHQPSSrvYQMFDSVLVLSEGRCLFFGKGSDAMA 296
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
1030-1242 |
1.24e-10 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 65.67 E-value: 1.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1030 IRNVFFNYPTRKDTK-------VLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLE-RFY-NQDKGMIMIDGdniRNLNIS 1100
Cdd:PLN03211 61 IKRILGHKPKISDETrqiqertILNGVTGMASPGEILAVLGPSGSGKSTLLNALAgRIQgNNFTGTILANN---RKPTKQ 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1101 SLReQVCIVSQEPTLF-DCTIGENICYGT----NRNVTYQEIVEAAKMANIHnfiLGLPDGYDTHVGEKGTQ-LSGGQKQ 1174
Cdd:PLN03211 138 ILK-RTGFVTQDDILYpHLTVRETLVFCSllrlPKSLTKQEKILVAESVISE---LGLTKCENTIIGNSFIRgISGGERK 213
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 124244275 1175 RIAIARALVRSPSVLLLDEATSALD-TESEKIVQEALDAAKQGRTCLVIAHRLST--IQNSDVIAIVSEGK 1242
Cdd:PLN03211 214 RVSIAHEMLINPSLLILDEPTSGLDaTAAYRLVLTLGSLAQKGKTIVTSMHQPSSrvYQMFDSVLVLSEGR 284
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
752-879 |
1.39e-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: 350007 [Multi-domain] Cd Length: 296 Bit Score: 63.68 E-value: 1.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 752 GMFVLMGITFFVGFFTSaNCLGRCGESLTMKLRFEAFKNLLRQDIAFYDdlRHGTGKLCTRFATDAPNVRYVFTR-LPVV 830
Cdd:cd18563 48 GLAGAYVLSALLGILRG-RLLARLGERITADLRRDLYEHLQRLSLSFFD--KRQTGSLMSRVTSDTDRLQDFLSDgLPDF 124
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 124244275 831 LASIVTICGALGIGFYYGWQLALILVVMVPLLVMGGYFemqmrFGKQIR 879
Cdd:cd18563 125 LTNILMIIGIGVVLFSLNWKLALLVLIPVPLVVWGSYF-----FWKKIR 168
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
397-607 |
1.44e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 65.74 E-value: 1.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 397 GDISF--KDVHFRYPSRKdihVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIdGVDLREVNVHSLR 474
Cdd:PRK11147 316 GKIVFemENVNYQIDGKQ---LVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHC-GTKLEVAYFDQHR 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 475 EQIgivsqEPvlfDGTIYENIKMGNehathdQVVeackMANA---------NDFI---KRlpdgygTRVGEKGvqLSGGQ 542
Cdd:PRK11147 392 AEL-----DP---EKTVMDNLAEGK------QEV----MVNGrprhvlgylQDFLfhpKR------AMTPVKA--LSGGE 445
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 124244275 543 KQRIAIARALVKNPKILLLDEATSALDTEAEREVQGALDQAQAgrTTIIVAHrlstirnvDRIFV 607
Cdd:PRK11147 446 RNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELLDSYQG--TVLLVSH--------DRQFV 500
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1028-1202 |
2.63e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 64.59 E-value: 2.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1028 ISIRNVFFNYptrKDTKVLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGMIMIDGDnirnLNISSLReqvc 1107
Cdd:PRK11147 4 ISIHGAWLSF---SDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQD----LIVARLQ---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1108 ivsQEP------TLFDCT------IGE-------------------NIcygtNRNVTYQEIVEAAKMANIHNFI------ 1150
Cdd:PRK11147 73 ---QDPprnvegTVYDFVaegieeQAEylkryhdishlvetdpsekNL----NELAKLQEQLDHHNLWQLENRInevlaq 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 124244275 1151 LGL-PDgydthvgEKGTQLSGGQKQRIAIARALVRSPSVLLLDEATSALDTES 1202
Cdd:PRK11147 146 LGLdPD-------AALSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIET 191
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
416-628 |
3.09e-10 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 64.14 E-value: 3.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 416 VLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVlidgvdlrevnVHSLREQIGIVSQEPVL-FDG--TIY 492
Cdd:PRK15064 334 LFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV-----------KWSENANIGYYAQDHAYdFENdlTLF 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 493 ENIKMGNEHATHDQVVEAC--KMANANDFIKrlpdgygtrvgeKGVQ-LSGGQKQRIAIARALVKNPKILLLDEATSALD 569
Cdd:PRK15064 403 DWMSQWRQEGDDEQAVRGTlgRLLFSQDDIK------------KSVKvLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMD 470
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124244275 570 TEAEREVQGALDQAQAgrTTIIVAHrlstirnvDRIFV---------FKAGNIVE-SGSHEELMSKQGI 628
Cdd:PRK15064 471 MESIESLNMALEKYEG--TLIFVSH--------DREFVsslatriieITPDGVVDfSGTYEEYLRSQGI 529
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
420-626 |
4.12e-10 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 63.69 E-value: 4.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 420 ISLELKAGDKIALVGSSGCGKSTIVNLLQRFYdPTK--GRVLIDG--VDLREVnVHSLREQIGIVSQE-------PVLFD 488
Cdd:TIGR02633 279 VSFSLRRGEILGVAGLVGAGRTELVQALFGAY-PGKfeGNVFINGkpVDIRNP-AQAIRAGIAMVPEDrkrhgivPILGV 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 489 GtiyENIKMG--NEHATHDQVVEACKMANANDFIKRL------PDGYGTRvgekgvqLSGGQKQRIAIARALVKNPKILL 560
Cdd:TIGR02633 357 G---KNITLSvlKSFCFKMRIDAAAELQIIGSAIQRLkvktasPFLPIGR-------LSGGNQQKAVLAKMLLTNPRVLI 426
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 124244275 561 LDEATSALDTEAEREVQGALDQ-AQAGRTTIIVAHRLSTIRNV-DRIFVFKAGNIVESGSHEELMSKQ 626
Cdd:TIGR02633 427 LDEPTRGVDVGAKYEIYKLINQlAQEGVAIIVVSSELAEVLGLsDRVLVIGEGKLKGDFVNHALTQEQ 494
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
406-608 |
5.90e-10 |
|
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: 61.27 E-value: 5.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 406 FRYPSRKdiHVLKGISLELKAGD-----KIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDlrevnvhslreqigiV 480
Cdd:cd03237 1 YTYPTMK--KTLGEFTLEVEGGSiseseVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDT---------------V 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 481 SQEP----VLFDGTIYENI-KMGNEHATHDQVveackmanANDFIK--RLPDGYGTRVGEkgvqLSGGQKQRIAIARALV 553
Cdd:cd03237 64 SYKPqyikADYEGTVRDLLsSITKDFYTHPYF--------KTEIAKplQIEQILDREVPE----LSGGELQRVAIAACLS 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 554 KNPKILLLDEATSALDTE----AEREVQGALDQAQAgrTTIIVAHRLSTIRNV-DRIFVF 608
Cdd:cd03237 132 KDADIYLLDEPSAYLDVEqrlmASKVIRRFAENNEK--TAFVVEHDIIMIDYLaDRLIVF 189
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
1029-1247 |
6.34e-10 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 60.81 E-value: 6.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1029 SIRNVFfnYPTRKDTKVLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGMIMIDGdNIRNLNISSLREQVCI 1108
Cdd:cd03267 22 SLKSLF--KRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAG-LVPWKRRKKFLRRIGV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1109 V-SQEPTL-FDCTIGENicYGTNRNVtYQeIVEAAKMANIHNF--ILGLPDGYDTHVgekgTQLSGGQKQRIAIARALVR 1184
Cdd:cd03267 99 VfGQKTQLwWDLPVIDS--FYLLAAI-YD-LPPARFKKRLDELseLLDLEELLDTPV----RQLSLGQRMRAEIAAALLH 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 124244275 1185 SPSVLLLDEATSALDTESEKIVQEALDA--AKQGRTCLVIAHRLSTIQN-SDVIAIVSEGKIVEKG 1247
Cdd:cd03267 171 EPEILFLDEPTIGLDVVAQENIRNFLKEynRERGTTVLLTSHYMKDIEAlARRVLVIDKGRLLYDG 236
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
399-613 |
7.17e-10 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 63.34 E-value: 7.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 399 ISFKDVHFRYPSRKDIhvLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVL--------------IDGVD 464
Cdd:PLN03073 509 ISFSDASFGYPGGPLL--FKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFrsakvrmavfsqhhVDGLD 586
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 465 LrevnvhslreqigivSQEPVLFDGTIYENIKmgnehathDQVVEAckmanandfikrlpdgygtRVGEKGVQ------- 537
Cdd:PLN03073 587 L---------------SSNPLLYMMRCFPGVP--------EQKLRA-------------------HLGSFGVTgnlalqp 624
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 538 ---LSGGQKQRIAIARALVKNPKILLLDEATSALDTEA-EREVQGaLDQAQAGrtTIIVAHRLSTIR-NVDRIFVFKAGN 612
Cdd:PLN03073 625 mytLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAvEALIQG-LVLFQGG--VLMVSHDEHLISgSVDELWVVSEGK 701
|
.
gi 124244275 613 I 613
Cdd:PLN03073 702 V 702
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
417-623 |
7.79e-10 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 63.10 E-value: 7.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 417 LKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGvdlREVNVHSLREQI--GIVS-QEPVLFDG---- 489
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDG---HEVVTRSPQDGLanGIVYiSEDRKRDGlvlg 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 490 -TIYENI----------KMGN-EHATHDQVVEackmananDFIK----RLPdGYGTRVGEkgvqLSGGQKQRIAIARALV 553
Cdd:PRK10762 345 mSVKENMsltalryfsrAGGSlKHADEQQAVS--------DFIRlfniKTP-SMEQAIGL----LSGGNQQKVAIARGLM 411
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 124244275 554 KNPKILLLDEATSALDTEAEREVQGALDQAQA-GRTTIIVAHRLSTIRNV-DRIFVFKAGNI-----VESGSHEELM 623
Cdd:PRK10762 412 TRPKVLILDEPTRGVDVGAKKEIYQLINQFKAeGLSIILVSSEMPEVLGMsDRILVMHEGRIsgeftREQATQEKLM 488
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
712-910 |
1.18e-09 |
|
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: 60.88 E-value: 1.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 712 IFGAFIFGSVTPVFALVY----AEIFNVYSLPADQMQ----ANVYFWCGMFVLMGITFFVGFFTSANCLGRCGESLTMKL 783
Cdd:cd18547 1 LILVIILAIISTLLSVLGpyllGKAIDLIIEGLGGGGgvdfSGLLRILLLLLGLYLLSALFSYLQNRLMARVSQRTVYDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 784 RFEAFKNLLRQDIAFYDdlRHGTGKLCTRFATDAPNVRYVFTR-LPVVLASIVTICGALGIGFYYGWQLALILVVMVPLL 862
Cdd:cd18547 81 RKDLFEKLQRLPLSYFD--THSHGDIMSRVTNDVDNISQALSQsLTQLISSILTIVGTLIMMLYISPLLTLIVLVTVPLS 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 124244275 863 VMGGYFEM---QMRFGKQIRDTqlleeaGKVASQAVEHI---RTVHSLNRQEQF 910
Cdd:cd18547 159 LLVTKFIAkrsQKYFRKQQKAL------GELNGYIEEMIsgqKVVKAFNREEEA 206
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
125-330 |
1.31e-09 |
|
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: 60.92 E-value: 1.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 125 LVLGVLMFFTSYVQIacFESY-----AERLVHKLRQNYLKAILRQQIQWFDKQQTGNLTARLTDdLERVREGLGDKF-AL 198
Cdd:cd18570 46 IGLILLYLFQSLLSY--IRSYlllklSQKLDIRLILGYFKHLLKLPLSFFETRKTGEIISRFND-ANKIREAISSTTiSL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 199 LVQMFAAFLAGyGVGFFYSWSMTLVMMGFAPLIVLSGAKMSKSMATRTRVEQETYAVAGAIAEETFSSIRTVHSLNGHKR 278
Cdd:cd18570 123 FLDLLMVIISG-IILFFYNWKLFLITLLIIPLYILIILLFNKPFKKKNREVMESNAELNSYLIESLKGIETIKSLNAEEQ 201
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 124244275 279 ELD----RFYNALEVGRQTGIVKYCYMGIGVGFSNLCMyssyALAFWYGSTLIIND 330
Cdd:cd18570 202 FLKkiekKFSKLLKKSFKLGKLSNLQSSIKGLISLIGS----LLILWIGSYLVIKG 253
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
389-600 |
1.35e-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: 1.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 389 GILVDNMKGdISFKDVHFRYPSrkDIHVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQ--------RFYDPTKGRVLI 460
Cdd:TIGR00954 443 GIVEYQDNG-IKFENIPLVTPN--GDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGelwpvyggRLTKPAKGKLFY 519
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 461 dgVDLRE-VNVHSLREQIgivsqepvLFDGTIYENIKMGNEHATHDQVVEACKManaNDFIKRlpdgygtRVGEKGVQ-- 537
Cdd:TIGR00954 520 --VPQRPyMTLGTLRDQI--------IYPDSSEDMKRRGLSDKDLEQILDNVQL---THILER-------EGGWSAVQdw 579
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 124244275 538 ---LSGGQKQRIAIARALVKNPKILLLDEATSALDTeaerEVQGALDQA--QAGRTTIIVAHRLSTIR 600
Cdd:TIGR00954 580 mdvLSGGEKQRIAMARLFYHKPQFAILDECTSAVSV----DVEGYMYRLcrEFGITLFSVSHRKSLWK 643
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1040-1229 |
1.48e-09 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 60.28 E-value: 1.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1040 RKDTKVLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGMIMIDGDNIRNlnisSLREQ-VCIVSQE------ 1112
Cdd:PRK15056 17 RNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQ----ALQKNlVAYVPQSeevdws 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1113 -PTLFD--CTIGENICYGTNRNVTY--QEIVEAAkMANIhnfilGLPDGYDTHVGEkgtqLSGGQKQRIAIARALVRSPS 1187
Cdd:PRK15056 93 fPVLVEdvVMMGRYGHMGWLRRAKKrdRQIVTAA-LARV-----DMVEFRHRQIGE----LSGGQKKRVFLARAIAQQGQ 162
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 124244275 1188 VLLLDEATSALDTESE-KIVQEALDAAKQGRTCLVIAHRLSTI 1229
Cdd:PRK15056 163 VILLDEPFTGVDVKTEaRIISLLRELRDEGKTMLVSTHNLGSV 205
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
416-628 |
1.55e-09 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 60.23 E-value: 1.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 416 VLKGISLELKAGDKIALVGSSGCGKSTIVNLLQ-RFYDP-------TKGRVLIDGVDLREVNVHSLREQIGIVSQ----- 482
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAgDLTGGgaprgarVTGDVTLNGEPLAAIDAPRLARLRAVLPQaaqpa 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 483 ------EPVLFDGtiYENIKMGNEHATHDQVVEACKMANAndfikrlpdGYGTRVGEKGVQLSGGQKQRIAIARALVK-- 554
Cdd:PRK13547 96 fafsarEIVLLGR--YPHARRAGALTHRDGEIAWQALALA---------GATALVGRDVTTLSGGELARVQFARVLAQlw 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 555 -------NPKILLLDEATSALDTEAERE----VQGALDQAQAGRTTIIVAHRLSTiRNVDRIFVFKAGNIVESGSHEELM 623
Cdd:PRK13547 165 pphdaaqPPRYLLLDEPTAALDLAHQHRlldtVRRLARDWNLGVLAIVHDPNLAA-RHADRIAMLADGAIVAHGAPADVL 243
|
....*
gi 124244275 624 SKQGI 628
Cdd:PRK13547 244 TPAHI 248
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
124-283 |
2.14e-09 |
|
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: 60.24 E-value: 2.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 124 YLVLGVLMFFTSYvqiacFESYAE-RLVHKLRQNYLKAILRQQIQWFDKQQTGNLTARLTDDLERVREGLGDkfaLLVQM 202
Cdd:cd18778 50 YLLRALLNFLRIY-----LNHVAEqKVVADLRSDLYDKLQRLSLRYFDDRQTGDLMSRVINDVANVERLIAD---GIPQG 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 203 FAAFLAGYGVG---FFYSWSMTLVMMGFAPLIVLSGAKMSKSMATRTRVEQETYAVAGAIAEETFSSIRTVHSLNGHKRE 279
Cdd:cd18778 122 ITNVLTLVGVAiilFSINPKLALLTLIPIPFLALGAWLYSKKVRPRYRKVREALGELNALLQDNLSGIREIQAFGREEEE 201
|
....
gi 124244275 280 LDRF 283
Cdd:cd18778 202 AKRF 205
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
407-623 |
2.60e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 61.28 E-value: 2.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 407 RYPSRKDIhvlkgiSLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGvdlREVNVHSLREQI--------- 477
Cdd:PRK10982 260 RQPSIRDV------SFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHG---KKINNHNANEAInhgfalvte 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 478 -----GIVSQEPVLFDGTIyENIKmgnEHATHDQVVEACKMANAN----DFIKRLPDGYGTRVGekgvQLSGGQKQRIAI 548
Cdd:PRK10982 331 errstGIYAYLDIGFNSLI-SNIR---NYKNKVGLLDNSRMKSDTqwviDSMRVKTPGHRTQIG----SLSGGNQQKVII 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 549 ARALVKNPKILLLDEATSALDTEAEREV-QGALDQAQAGRTTIIVAHRLSTIRNV-DRIFVFKAG---NIVESG--SHEE 621
Cdd:PRK10982 403 GRWLLTQPEILMLDEPTRGIDVGAKFEIyQLIAELAKKDKGIIIISSEMPELLGItDRILVMSNGlvaGIVDTKttTQNE 482
|
..
gi 124244275 622 LM 623
Cdd:PRK10982 483 IL 484
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
147-283 |
3.08e-09 |
|
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: 59.83 E-value: 3.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 147 ERLVHKLRQNYLKAILRQQIQWFDKQQTGNLTARLTDDLERVREGLGDKFALLVQMFAAFLAGYGVGFFYSWSMTLVMMG 226
Cdd:cd18563 72 ERITADLRRDLYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDFLSDGLPDFLTNILMIIGIGVVLFSLNWKLALLVLI 151
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 124244275 227 FAPLIVLSGAKMSKSMATR-TRVEQETYAVAGAIAeETFSSIRTVHSLNGHKRELDRF 283
Cdd:cd18563 152 PVPLVVWGSYFFWKKIRRLfHRQWRRWSRLNSVLN-DTLPGIRVVKAFGQEKREIKRF 208
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
412-620 |
3.69e-09 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 58.88 E-value: 3.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 412 KDIHVLKGISLELKAGDKIALVGSSGCGKSTIVNLL--QRFYDPTKGRVLIDGVDLREVNVhSLREQIGI--VSQEPVLF 487
Cdd:CHL00131 18 NENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIagHPAYKILEGDILFKGESILDLEP-EERAHLGIflAFQYPIEI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 488 DGTIYENIKMGNEHATHDQ--------------VVEACKMANAND-FIKR-LPDGYgtrvgekgvqlSGGQKQRIAIARA 551
Cdd:CHL00131 97 PGVSNADFLRLAYNSKRKFqglpeldplefleiINEKLKLVGMDPsFLSRnVNEGF-----------SGGEKKRNEILQM 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124244275 552 LVKNPKILLLDEATSALDTEAEREVQGALDQ-AQAGRTTIIVAH--RLSTIRNVDRIFVFKAGNIVESGSHE 620
Cdd:CHL00131 166 ALLDSELAILDETDSGLDIDALKIIAEGINKlMTSENSIILITHyqRLLDYIKPDYVHVMQNGKIIKTGDAE 237
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
1048-1254 |
3.91e-09 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 58.94 E-value: 3.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1048 GFTLDIKAGKTVALVGHSGCGKS----TIMGLLERFYNQDKGMIMIDGdniRNLNISSLR-EQVCIVSQEP--------T 1114
Cdd:PRK10418 21 GVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDG---KPVAPCALRgRKIATIMQNPrsafnplhT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1115 LFDCTIGENICYG-TNRNVTYQEIVEAAKMANIHNfILGLpdgydthvgeKGTQLSGGQKQRIAIARALVRSPSVLLLDE 1193
Cdd:PRK10418 98 MHTHARETCLALGkPADDATLTAALEAVGLENAAR-VLKL----------YPFEMSGGMLQRMMIALALLCEAPFIIADE 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124244275 1194 ATSALDTESEKIVQEALDA--AKQGRTCLVIAHRLSTIQN-SDVIAIVSEGKIVEKGTHDELIR 1254
Cdd:PRK10418 167 PTTDLDVVAQARILDLLESivQKRALGMLLVTHDMGVVARlADDVAVMSHGRIVEQGDVETLFN 230
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
425-597 |
4.10e-09 |
|
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: 58.92 E-value: 4.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 425 KAGDKIALVGSSGCGKSTIVNLLQ--------RFYDPTKGRVLID---GVDLREVNVHSLREQIGI------VSQEPVLF 487
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAgklkpnlgKFDDPPDWDEILDefrGSELQNYFTKLLEGDVKVivkpqyVDLIPKAV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 488 DGTIYENIKMGNEHATHDQVVEACKMANandfikrlpdgygtrVGEKGV-QLSGGQKQRIAIARALVKNPKILLLDEATS 566
Cdd:cd03236 104 KGKVGELLKKKDERGKLDELVDQLELRH---------------VLDRNIdQLSGGELQRVAIAAALARDADFYFFDEPSS 168
|
170 180 190
....*....|....*....|....*....|....*
gi 124244275 567 ALDT----EAEREVQGAldqAQAGRTTIIVAHRLS 597
Cdd:cd03236 169 YLDIkqrlNAARLIREL---AEDDNYVLVVEHDLA 200
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
1060-1199 |
4.44e-09 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 59.89 E-value: 4.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1060 ALVGHSGCGKSTIMGLLERFYNQDKGMIMIDG----DNIRNLNISSLREQVCIVSQEPTLF-DCTIGENICYGTNRNVTY 1134
Cdd:PRK11144 28 AIFGRSGAGKTSLINAISGLTRPQKGRIVLNGrvlfDAEKGICLPPEKRRIGYVFQDARLFpHYKVRGNLRYGMAKSMVA 107
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 124244275 1135 Q--EIVEaakmanihnfILGLPDGYDTHVGekgtQLSGGQKQRIAIARALVRSPSVLLLDEATSALD 1199
Cdd:PRK11144 108 QfdKIVA----------LLGIEPLLDRYPG----SLSGGEKQRVAIGRALLTAPELLLMDEPLASLD 160
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
705-880 |
4.64e-09 |
|
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: 59.03 E-value: 4.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 705 VGWFIGGIFGAFIFGSVTPvfaLVYAEIFNVySLPADQMQANVYFWCGMFVLMGITFFVGFFTSAnCLGRCGESLTMKLR 784
Cdd:cd18550 1 LALVLLLILLSALLGLLPP---LLLREIIDD-ALPQGDLGLLVLLALGMVAVAVASALLGVVQTY-LSARIGQGVMYDLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 785 FEAFKNLLRQDIAFYDdlRHGTGKLCTRFATDAPNVRYVFTR-LPVVLASIVTICGALGIGFYYGWQLALILVVMVPLLV 863
Cdd:cd18550 76 VQLYAHLQRMSLAFFT--RTRTGEIQSRLNNDVGGAQSVVTGtLTSVVSNVVTLVATLVAMLALDWRLALLSLVLLPLFV 153
|
170
....*....|....*..
gi 124244275 864 MggyfeMQMRFGKQIRD 880
Cdd:cd18550 154 L-----PTRRVGRRRRK 165
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
414-597 |
4.98e-09 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 61.02 E-value: 4.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 414 IHVLKGISLELKAGDKIALVGSSGCGKSTIVNLL--QRFYDPTKGRVLIDGVDLRE---VNVHSLREQIGIVSQEPVLFD 488
Cdd:PLN03140 893 LQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLagRKTGGYIEGDIRISGFPKKQetfARISGYCEQNDIHSPQVTVRE 972
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 489 GTIYEN-----IKMGNEHATH--DQVVEACKMANANDFIKRLPDGYGtrvgekgvqLSGGQKQRIAIARALVKNPKILLL 561
Cdd:PLN03140 973 SLIYSAflrlpKEVSKEEKMMfvDEVMELVELDNLKDAIVGLPGVTG---------LSTEQRKRLTIAVELVANPSIIFM 1043
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 124244275 562 DEATSALDTEAE----REVQGALDqaqAGRTTIIVAHRLS 597
Cdd:PLN03140 1044 DEPTSGLDARAAaivmRTVRNTVD---TGRTVVCTIHQPS 1080
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
1044-1227 |
5.07e-09 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 61.02 E-value: 5.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1044 KVLQGFTLDIKAGKTVALVGHSGCGKSTIMGLL--ERFYNQDKGMIMIDGDNIRN---LNISSLREQVCIVSQEptlfdC 1118
Cdd:PLN03140 894 QLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLagRKTGGYIEGDIRISGFPKKQetfARISGYCEQNDIHSPQ-----V 968
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1119 TIGENICYGT----NRNVTYQE-------IVEAAKMANIHNFILGLPdgydthvGEKGtqLSGGQKQRIAIARALVRSPS 1187
Cdd:PLN03140 969 TVRESLIYSAflrlPKEVSKEEkmmfvdeVMELVELDNLKDAIVGLP-------GVTG--LSTEQRKRLTIAVELVANPS 1039
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 124244275 1188 VLLLDEATSALDTESEKIVQEAL-DAAKQGRTCLVIAHRLS 1227
Cdd:PLN03140 1040 IIFMDEPTSGLDARAAAIVMRTVrNTVDTGRTVVCTIHQPS 1080
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
1041-1257 |
5.99e-09 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 58.26 E-value: 5.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1041 KDTKVLQGFTLDIKAGKTVALVGHSGCGKSTIMGLL--ERFYNQDKGMIMIDGDNIRNLNISSLR-EQVCIVSQEPTLFD 1117
Cdd:PRK09580 12 EDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLagREDYEVTGGTVEFKGKDLLELSPEDRAgEGIFMAFQYPVEIP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1118 cTIGENICYGTNRNVT--YQEiVEAAKMANIHNFI------LGLPDGYDTHVGEKGtqLSGGQKQRIAIARALVRSPSVL 1189
Cdd:PRK09580 92 -GVSNQFFLQTALNAVrsYRG-QEPLDRFDFQDLMeekialLKMPEDLLTRSVNVG--FSGGEKKRNDILQMAVLEPELC 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 124244275 1190 LLDEATSALDTESEKIVQEALDAAKQG-RTCLVIAH--RLSTIQNSDVIAIVSEGKIVEKGTHdELIRKSE 1257
Cdd:PRK09580 168 ILDESDSGLDIDALKIVADGVNSLRDGkRSFIIVTHyqRILDYIKPDYVHVLYQGRIVKSGDF-TLVKQLE 237
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
1028-1244 |
7.21e-09 |
|
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: 57.27 E-value: 7.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1028 ISIRNVFFNYPTRKDT-KVLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLErfyNQDKGMIMIDGD----NIRNLNI-SS 1101
Cdd:cd03233 4 LSWRNISFTTGKGRSKiPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALA---NRTEGNVSVEGDihynGIPYKEFaEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1102 LREQVCIVSQE----PTLfdctigenicygtnrnvTYQEIVEAAKMANIHNFILGLpdgydthvgekgtqlSGGQKQRIA 1177
Cdd:cd03233 81 YPGEIIYVSEEdvhfPTL-----------------TVRETLDFALRCKGNEFVRGI---------------SGGERKRVS 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1178 IARALVRSPSVLLLDEATSALDTESekivqeALDAAKQGRTClviAH--RLSTI----QNS-------DVIAIVSEGKIV 1244
Cdd:cd03233 129 IAEALVSRASVLCWDNSTRGLDSST------ALEILKCIRTM---ADvlKTTTFvslyQASdeiydlfDKVLVLYEGRQI 199
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
1028-1228 |
7.88e-09 |
|
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: 56.87 E-value: 7.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1028 ISIRNVFFNYPTRKDTK-VLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQD--KGMIMIDGdniRNLNISSLRE 1104
Cdd:cd03232 4 LTWKNLNYTVPVKGGKRqLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGviTGEILING---RPLDKNFQRS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1105 qVCIVSQEPTLFDC-TIGENICYGtnrnvtyqeiveaakmANIhnfilglpdgydthvgeKGtqLSGGQKQRIAIARALV 1183
Cdd:cd03232 81 -TGYVEQQDVHSPNlTVREALRFS----------------ALL-----------------RG--LSVEQRKRLTIGVELA 124
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 124244275 1184 RSPSVLLLDEATSALDTESEKIVQEAL-DAAKQGRTCLVIAHRLST 1228
Cdd:cd03232 125 AKPSILFLDEPTSGLDSQAAYNIVRFLkKLADSGQAILCTIHQPSA 170
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
708-963 |
8.36e-09 |
|
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: 58.23 E-value: 8.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 708 FIGGIFGAFIFGSVTPVFALVYAEIFNVYsLPADQMQANVYFWCGMFVLMGITFFVGFFTSaNCLGRCGESLTMKLRFEA 787
Cdd:cd18570 4 LILILLLSLLITLLGIAGSFFFQILIDDI-IPSGDINLLNIISIGLILLYLFQSLLSYIRS-YLLLKLSQKLDIRLILGY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 788 FKNLLRQDIAFYDDLRhgTGKLCTRFaTDAPNVRYVFTRLPV-VLASIVTICGALGIGFYYGWQLALILVVMVPLlvmgg 866
Cdd:cd18570 82 FKHLLKLPLSFFETRK--TGEIISRF-NDANKIREAISSTTIsLFLDLLMVIISGIILFFYNWKLFLITLLIIPL----- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 867 YFEMQMRFGKQIRDTQ--LLEEAGKVASQAVEHIR---TVHSLNRQEQFHFTYCEYLREPFNTNLKHAHTYGAVFAFSQS 941
Cdd:cd18570 154 YILIILLFNKPFKKKNreVMESNAELNSYLIESLKgieTIKSLNAEEQFLKKIEKKFSKLLKKSFKLGKLSNLQSSIKGL 233
|
250 260
....*....|....*....|..
gi 124244275 942 LIFFMYAAAFYLGSIFVNQQAM 963
Cdd:cd18570 234 ISLIGSLLILWIGSYLVIKGQL 255
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
417-576 |
8.36e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 59.74 E-value: 8.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 417 LKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGvdlREVNVHSLREQ----IGIVSQE-PVLFDGTI 491
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQG---KEIDFKSSKEAlengISMVHQElNLVLQRSV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 492 YENIKMGnEHATHDQVVEACKMANANdfiKRLPDGYGTRVG--EKGVQLSGGQKQRIAIARALVKNPKILLLDEATSALd 569
Cdd:PRK10982 91 MDNMWLG-RYPTKGMFVDQDKMYRDT---KAIFDELDIDIDprAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSL- 165
|
....*..
gi 124244275 570 teAEREV 576
Cdd:PRK10982 166 --TEKEV 170
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
420-606 |
8.88e-09 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 59.52 E-value: 8.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 420 ISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDgvdlreVNvhslrEQIGIVSQEPVLF-DGTIYENIKMG 498
Cdd:PRK15064 20 ISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLD------PN-----ERLGKLRQDQFAFeEFTVLDTVIMG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 499 NEhathdqvvEACKMANANDFIKRLP--------------------DGYG--TRVGE--KGV------------QLSGGQ 542
Cdd:PRK15064 89 HT--------ELWEVKQERDRIYALPemseedgmkvadlevkfaemDGYTaeARAGEllLGVgipeeqhyglmsEVAPGW 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124244275 543 KQRIAIARALVKNPKILLLDEATSALDTEAEREVQGALDQAQAgrTTIIVAHrlstirnvDRIF 606
Cdd:PRK15064 161 KLRVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVLNERNS--TMIIISH--------DRHF 214
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
399-626 |
9.29e-09 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 57.85 E-value: 9.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 399 ISFKDVHFRYPSRKdihVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDLREVNVHSL---RE 475
Cdd:PRK11831 8 VDMRGVSFTRGNRC---IFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLytvRK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 476 QIGIVSQEPVLF-DGTIYENIKMGNEHATH--DQVVEACKMANANdfikrlpdgygtRVGEKGV------QLSGGQKQRI 546
Cdd:PRK11831 85 RMSMLFQSGALFtDMNVFDNVAYPLREHTQlpAPLLHSTVMMKLE------------AVGLRGAaklmpsELSGGMARRA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 547 AIARALVKNPKILLLDEA-------TSALDTEAEREVQGALdqaqaGRTTIIVAHRLSTIRNV-DRIFVFKAGNIVESGS 618
Cdd:PRK11831 153 ALARAIALEPDLIMFDEPfvgqdpiTMGVLVKLISELNSAL-----GVTCVVVSHDVPEVLSIaDHAYIVADKKIVAHGS 227
|
....*...
gi 124244275 619 HEELMSKQ 626
Cdd:PRK11831 228 AQALQANP 235
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
405-624 |
9.86e-09 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 59.42 E-value: 9.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 405 HFRYPSRKdihVLKGISLELKAGDKIALVGSSGCGKSTI-VNLLQRFYDP-TKGRVLIDGvdlREVNVHSLREQI--GI- 479
Cdd:NF040905 267 HPLHPERK---VVDDVSLNVRRGEIVGIAGLMGAGRTELaMSVFGRSYGRnISGTVFKDG---KEVDVSTVSDAIdaGLa 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 480 -VSQEP-----VLFDgTIYENIKMGN-----EHATHDQVVEackMANANDFIKRL----PDgygtrVGEKGVQLSGGQKQ 544
Cdd:NF040905 341 yVTEDRkgyglNLID-DIKRNITLANlgkvsRRGVIDENEE---IKVAEEYRKKMniktPS-----VFQKVGNLSGGNQQ 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 545 RIAIARALVKNPKILLLDEATSALDTEAEREVQGALDQ-AQAGRTTIIVAHRLSTIRNV-DRIFVFKAGNIV-----ESG 617
Cdd:NF040905 412 KVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINElAAEGKGVIVISSELPELLGMcDRIYVMNEGRITgelprEEA 491
|
....*..
gi 124244275 618 SHEELMS 624
Cdd:NF040905 492 SQERIMR 498
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1029-1255 |
1.00e-08 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 58.56 E-value: 1.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1029 SIRNVFFnyPTRKDTKVLQGFTLDIKAGKTVALVGHSGCGKSTIM----GLLErfynQDKGMIMIDG-----DNIRNL-N 1098
Cdd:COG4586 23 ALKGLFR--REYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIkmltGILV----PTSGEVRVLGyvpfkRRKEFArR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1099 ISSL---REQVcivsqeptLFDCTIGENicYGTNRNVtYqEIVEAAKMANIHNF--ILGLPDGYDTHVgekgTQLSGGQK 1173
Cdd:COG4586 97 IGVVfgqRSQL--------WWDLPAIDS--FRLLKAI-Y-RIPDAEYKKRLDELveLLDLGELLDTPV----RQLSLGQR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1174 QRIAIARALVRSPSVLLLDEATSALDTESEKIVQEALDA--AKQGRTCLVIAHRLSTIQN-SDVIAIVSEGKIVEKGTHD 1250
Cdd:COG4586 161 MRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEynRERGTTILLTSHDMDDIEAlCDRVIVIDHGRIIYDGSLE 240
|
....*
gi 124244275 1251 ELIRK 1255
Cdd:COG4586 241 ELKER 245
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
124-283 |
1.44e-08 |
|
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: 57.48 E-value: 1.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 124 YLVLGVLMFFTSYVQIACFESYAERLVHKLRQNYLKAILRQQIQWFDKQQTGNLTARLTDDLERVRE----GLGDKFALL 199
Cdd:cd18545 46 FLALNLVNWVASRLRIYLMAKVGQRILYDLRQDLFSHLQKLSFSFFDSRPVGKILSRVINDVNSLSDllsnGLINLIPDL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 200 VQMFAAFlagyGVGFFYSWSMTLVMMGFAPLIVLSGAKMSKSMATRTRVEQETYAVAGAIAEETFSSIRTVHSLNGHKRE 279
Cdd:cd18545 126 LTLVGIV----IIMFSLNVRLALVTLAVLPLLVLVVFLLRRRARKAWQRVRKKISNLNAYLHESISGIRVIQSFAREDEN 201
|
....
gi 124244275 280 LDRF 283
Cdd:cd18545 202 EEIF 205
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
403-587 |
1.60e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 56.11 E-value: 1.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 403 DVHFRYpsrKDIHVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDLREvNVHSLREQIGIVSQ 482
Cdd:PRK13540 6 ELDFDY---HDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKK-DLCTYQKQLCFVGH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 483 E----PVLfdgTIYENIKMG-NEHATHDQVVEACKMANANDFIKrLPDGYgtrvgekgvqLSGGQKQRIAIARALVKNPK 557
Cdd:PRK13540 82 RsginPYL---TLRENCLYDiHFSPGAVGITELCRLFSLEHLID-YPCGL----------LSSGQKRQVALLRLWMSKAK 147
|
170 180 190
....*....|....*....|....*....|
gi 124244275 558 ILLLDEATSALDteaEREVQGALDQAQAGR 587
Cdd:PRK13540 148 LWLLDEPLVALD---ELSLLTIITKIQEHR 174
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1135-1202 |
1.74e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 58.59 E-value: 1.74e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124244275 1135 QEIVEAAKMANIHNFI------LGLPDGyDTHVgekgTQLSGGQKQRIAIARALVRSPSVLLLDEATSALDTES 1202
Cdd:PRK11819 130 QEIIDAADAWDLDSQLeiamdaLRCPPW-DAKV----TKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES 198
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
747-990 |
2.32e-08 |
|
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: 57.02 E-value: 2.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 747 VYFWCGMFVLMGITFFVGFFTSANCLGRCGESLTMKLRFEAFKNLLRQDIAFYDDLrhGTGKLCTRFATDAPNV-RYVFT 825
Cdd:cd18548 38 ILRTGLLMLLLALLGLIAGILAGYFAAKASQGFGRDLRKDLFEKIQSFSFAEIDKF--GTSSLITRLTNDVTQVqNFVMM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 826 RLPVVLASIVTICGALGIGFYYGWQLALILVVMVPLLVMGGYFEMQM---RFGKQirdTQLLEEAGKVASQAVEHIRTVH 902
Cdd:cd18548 116 LLRMLVRAPIMLIGAIIMAFRINPKLALILLVAIPILALVVFLIMKKaipLFKKV---QKKLDRLNRVVRENLTGIRVIR 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 903 SLNRQeqfhftycEYLREPF---NTNLKHAHTY-GAVFAFSQSLIFF-MYA---AAFYLGSIFVNQQAMQPIDV-----Y 969
Cdd:cd18548 193 AFNRE--------DYEEERFdkaNDDLTDTSLKaGRLMALLNPLMMLiMNLaivAILWFGGHLINAGSLQVGDLvafinY 264
|
250 260
....*....|....*....|...
gi 124244275 970 --RVFFAISfcgqMIGNTTSFIP 990
Cdd:cd18548 265 lmQILMSLM----MLSMVFVMLP 283
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
738-958 |
2.45e-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: 350009 [Multi-domain] Cd Length: 313 Bit Score: 57.19 E-value: 2.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 738 LPADQMQanvYFWcgmfVLMGITFFVGFFTS------ANCLGRCGESLTMKLRFEAFKNLLRQDIAFYDDlrHGTGKLCT 811
Cdd:cd18565 45 GPADPRG---QLW----LLGGLTVAAFLLESlfqylsGVLWRRFAQRVQHDLRTDTYDHVQRLDMAFFED--RQTGDLMS 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 812 ----------RFATDAPN--VRYVftrlpvvlasiVTICGALGIGFYYGWQLALILVVMVPLLVMGGYfemqmRFGKQI- 878
Cdd:cd18565 116 vlnndvnqleRFLDDGANsiIRVV-----------VTVLGIGAILFYLNWQLALVALLPVPLIIAGTY-----WFQRRIe 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 879 -RDTQLLEEAGKVASQ---AVEHIRTVHSLNRqEQFhftycEYLR------EPFNTNLKHAHTYGAVFAFSQSLIFFMYA 948
Cdd:cd18565 180 pRYRAVREAVGDLNARlenNLSGIAVIKAFTA-EDF-----ERERvadaseEYRDANWRAIRLRAAFFPVIRLVAGAGFV 253
|
250
....*....|
gi 124244275 949 AAFYLGSIFV 958
Cdd:cd18565 254 ATFVVGGYWV 263
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
708-908 |
2.86e-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: 56.78 E-value: 2.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 708 FIGGIFGAFIFGSVTPVFALVYAEIFNvySLPADQMQANVYFWCGMfVLMGITFF--VGFFTSANCLGRCGESLTMKLRF 785
Cdd:cd18778 1 LILTLLCALLSTLLGLVPPWLIRELVD--LVTIGSKSLGLLLGLAL-LLLGAYLLraLLNFLRIYLNHVAEQKVVADLRS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 786 EAFKNLLRQDIAFYDDlrHGTGKLCTRFATDAPNVRYVFTR-LPVVLASIVTICGALGIGFYYGWQLALILVVMVPLLVM 864
Cdd:cd18778 78 DLYDKLQRLSLRYFDD--RQTGDLMSRVINDVANVERLIADgIPQGITNVLTLVGVAIILFSINPKLALLTLIPIPFLAL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 124244275 865 GGyfemqMRFGKQIRDT--QLLEEAGKVASQAVEH---IRTVHSLNRQE 908
Cdd:cd18778 156 GA-----WLYSKKVRPRyrKVREALGELNALLQDNlsgIREIQAFGREE 199
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1135-1202 |
2.94e-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: 2.94e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124244275 1135 QEIVEAAKMANIHNFI------LGLPDGyDTHVgekgTQLSGGQKQRIAIARALVRSPSVLLLDEATSALDTES 1202
Cdd:TIGR03719 128 QEIIDAADAWDLDSQLeiamdaLRCPPW-DADV----TKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAES 196
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1043-1242 |
3.03e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 57.90 E-value: 3.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1043 TKVLQGFTLDIKAGK-----TVALVGHSGCGKSTIMGLLERFYNQDKGMIMIDgdnirnLNISsLREQVCIVSQEPTLFD 1117
Cdd:PRK13409 347 TKKLGDFSLEVEGGEiyegeVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE------LKIS-YKPQYIKPDYDGTVED 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1118 C--TIGENIcygtNRNVTYQEIVEAakmanihnfiLGLPDGYDTHVGEkgtqLSGGQKQRIAIARALVRSPSVLLLDEAT 1195
Cdd:PRK13409 420 LlrSITDDL----GSSYYKSEIIKP----------LQLERLLDKNVKD----LSGGELQRVAIAACLSRDADLYLLDEPS 481
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 124244275 1196 SALDTESEKIVQEALD--AAKQGRTCLVIAHRLSTIqnsDVIA---IVSEGK 1242
Cdd:PRK13409 482 AHLDVEQRLAVAKAIRriAEEREATALVVDHDIYMI---DYISdrlMVFEGE 530
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
409-613 |
3.13e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 57.63 E-value: 3.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 409 PSRKDIHvlkGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYdPTK--GRVLIDGvdlREVNVHSLREQI--------- 477
Cdd:PRK13549 273 PHIKRVD---DVSFSLRRGEILGIAGLVGAGRTELVQCLFGAY-PGRweGEIFIDG---KPVKIRNPQQAIaqgiamvpe 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 478 -----GIVSQEPVLfdgtiyENIKMGN--EHATHDQVVEACKMANANDFIKRL------PDgygTRVGekgvQLSGGQKQ 544
Cdd:PRK13549 346 drkrdGIVPVMGVG------KNITLAAldRFTGGSRIDDAAELKTILESIQRLkvktasPE---LAIA----RLSGGNQQ 412
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 124244275 545 RIAIARALVKNPKILLLDEATSALDTEAEREVQGALDQ-AQAGRTTIIVAHRLSTIRNV-DRIFVFKAGNI 613
Cdd:PRK13549 413 KAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQlVQQGVAIIVISSELPEVLGLsDRVLVMHEGKL 483
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
1046-1248 |
3.44e-08 |
|
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: 56.08 E-value: 3.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1046 LQGFTLDIKAGKTVALVGHSGCGKSTIM------GLLERFYNQD---KGMIMIDGdnIRNLnisslrEQVCIVSQEPT-- 1114
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLIndtlypALARRLHLKKeqpGNHDRIEG--LEHI------DKVIVIDQSPIgr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1115 -----------LFDcTIGE---NICYGTNRN-----VTYQ----------EIVEAAK----MANIHNFILGLPD---GYd 1158
Cdd:cd03271 83 tprsnpatytgVFD-EIRElfcEVCKGKRYNretleVRYKgksiadvldmTVEEALEffenIPKIARKLQTLCDvglGY- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1159 THVGEKGTQLSGGQKQRIAIARALVR---SPSVLLLDEATSALDTESEKIVQEALDA-AKQGRTCLVIAHRLSTIQNSD- 1233
Cdd:cd03271 161 IKLGQPATTLSGGEAQRIKLAKELSKrstGKTLYILDEPTTGLHFHDVKKLLEVLQRlVDKGNTVVVIEHNLDVIKCADw 240
|
250 260
....*....|....*....|
gi 124244275 1234 VIAIVSE-----GKIVEKGT 1248
Cdd:cd03271 241 IIDLGPEggdggGQVVASGT 260
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
1044-1227 |
3.80e-08 |
|
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: 57.84 E-value: 3.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1044 KVLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGMIMIDGDNirnlnisslreQVCIVSQEPTLFDCTIGEN 1123
Cdd:TIGR00954 466 VLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAKG-----------KLFYVPQRPYMTLGTLRDQ 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1124 ICYGTN------RNVTYQEIVEAAKMANIHNfILGLPDGYDThVGEKGTQLSGGQKQRIAIARALVRSPSVLLLDEATSA 1197
Cdd:TIGR00954 535 IIYPDSsedmkrRGLSDKDLEQILDNVQLTH-ILEREGGWSA-VQDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSA 612
|
170 180 190
....*....|....*....|....*....|
gi 124244275 1198 LDTESEKIVQEAldAAKQGRTCLVIAHRLS 1227
Cdd:TIGR00954 613 VSVDVEGYMYRL--CREFGITLFSVSHRKS 640
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
115-329 |
4.14e-08 |
|
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: 56.25 E-value: 4.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 115 SEVVKYCIYYLVLGVLMFFTSYVQIACFESYAERLVHKLRQNYLKAILRQQIQWFDKQQTGNLTARLTDDLERVREGlgd 194
Cdd:cd18548 36 SYILRTGLLMLLLALLGLIAGILAGYFAAKASQGFGRDLRKDLFEKIQSFSFAEIDKFGTSSLITRLTNDVTQVQNF--- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 195 kFALLVQMF--AAFLAGYGV--GFFYSWSMTLVMMGFAPLIVLSGAKMSKSMATRTRVEQETYAVAGAIAEETFSSIRTV 270
Cdd:cd18548 113 -VMMLLRMLvrAPIMLIGAIimAFRINPKLALILLVAIPILALVVFLIMKKAIPLFKKVQKKLDRLNRVVRENLTGIRVI 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 124244275 271 HSLNGHKRELDRFYNALEVGRQTGIVKYCYMGIGVGFSNLCMYSSYALAFWYGSTLIIN 329
Cdd:cd18548 192 RAFNREDYEEERFDKANDDLTDTSLKAGRLMALLNPLMMLIMNLAIVAILWFGGHLINA 250
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
1031-1229 |
4.18e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 58.20 E-value: 4.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1031 RNVFFNYPTRKDTKVL----QGFtldIKAGKTVALVGHSGCGKSTIMGLL-ERfynQDKGMIMiDGD---NIRNLNISSL 1102
Cdd:TIGR00956 763 RNLTYEVKIKKEKRVIlnnvDGW---VKPGTLTALMGASGAGKTTLLNVLaER---VTTGVIT-GGDrlvNGRPLDSSFQ 835
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1103 REQVCIVSQEPTLFDCTIGENICYgTNRNVTYQEIVEAAKMANIHNFI--LGLPDGYDTHVGEKGTQLSGGQKQRIAIAR 1180
Cdd:TIGR00956 836 RSIGYVQQQDLHLPTSTVRESLRF-SAYLRQPKSVSKSEKMEYVEEVIklLEMESYADAVVGVPGEGLNVEQRKRLTIGV 914
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 124244275 1181 ALVRSPSVLL-LDEATSALDTESE-KIVQEALDAAKQGRTCLVIAHRLSTI 1229
Cdd:TIGR00956 915 ELVAKPKLLLfLDEPTSGLDSQTAwSICKLMRKLADHGQAILCTIHQPSAI 965
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
1039-1224 |
4.21e-08 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 55.24 E-value: 4.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1039 TRKDTKVLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGMIMIDGDNIRNLNISslrEQVCIVSQEPTL-FD 1117
Cdd:PRK13543 20 SRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRS---RFMAYLGHLPGLkAD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1118 CTIGENICYgtnrnVTYQEIVEAAKMANIHNFILGLPDGYDTHVgekgTQLSGGQKQRIAIARaLVRSPSVL-LLDEATS 1196
Cdd:PRK13543 97 LSTLENLHF-----LCGLHGRRAKQMPGSALAIVGLAGYEDTLV----RQLSAGQKKRLALAR-LWLSPAPLwLLDEPYA 166
|
170 180
....*....|....*....|....*....
gi 124244275 1197 ALDTESEKIVQEALDA-AKQGRTCLVIAH 1224
Cdd:PRK13543 167 NLDLEGITLVNRMISAhLRGGGAALVTTH 195
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
1053-1251 |
4.59e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 57.81 E-value: 4.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1053 IKAGKTVALVGHSGCGKST----IMGLLERFYNQDKGMIMIDG---DNIRNlnisSLREQVCIVSQEPTLF-DCTIGENI 1124
Cdd:TIGR00956 84 IKPGELTVVLGRPGSGCSTllktIASNTDGFHIGVEGVITYDGitpEEIKK----HYRGDVVYNAETDVHFpHLTVGETL 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1125 -----CYG-TNRNVTYQEIVEAAKMANIHNFILGLPDGYDTHVGE---KGtqLSGGQKQRIAIARALVRSPSVLLLDEAT 1195
Cdd:TIGR00956 160 dfaarCKTpQNRPDGVSREEYAKHIADVYMATYGLSHTRNTKVGNdfvRG--VSGGERKRVSIAEASLGGAKIQCWDNAT 237
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 124244275 1196 SALDTESekivqeALDAAKQGRTCLVIAHRLSTI---QNS-------DVIAIVSEGKIVEKGTHDE 1251
Cdd:TIGR00956 238 RGLDSAT------ALEFIRALKTSANILDTTPLVaiyQCSqdayelfDKVIVLYEGYQIYFGPADK 297
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
416-600 |
5.88e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 57.10 E-value: 5.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 416 VLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRV-LIDGVDLREVNVHSLreqigivsqEPVLFDGTIYEN 494
Cdd:PRK10636 327 ILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIgLAKGIKLGYFAQHQL---------EFLRADESPLQH 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 495 IKMGNEHATHDQVveackmanaNDFIkrlpDGYG---TRVGEKGVQLSGGQKQRIAIARALVKNPKILLLDEATSALD-- 569
Cdd:PRK10636 398 LARLAPQELEQKL---------RDYL----GGFGfqgDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDld 464
|
170 180 190
....*....|....*....|....*....|....*.
gi 124244275 570 -----TEAEREVQGALdqaqagrttIIVAHRLSTIR 600
Cdd:PRK10636 465 mrqalTEALIDFEGAL---------VVVSHDRHLLR 491
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
1040-1241 |
6.85e-08 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 54.42 E-value: 6.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1040 RKDTKVLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGMIMIDGDNIRNLNISSLREQVCIVSQEPTLFDCT 1119
Cdd:cd03231 10 RDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1120 IGENICYGTNRNVTYQeIVEAAKMANIHNFilglpdgYDTHVGekgtQLSGGQKQRIAIARALVRSPSVLLLDEATSALD 1199
Cdd:cd03231 90 VLENLRFWHADHSDEQ-VEEALARVGLNGF-------EDRPVA----QLSAGQQRRVALARLLLSGRPLWILDEPTTALD 157
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 124244275 1200 TESEKIVQEALDAAKQGRTCLVIAHRLSTIQNSDVIAIVSEG 1241
Cdd:cd03231 158 KAGVARFAEAMAGHCARGGMVVLTTHQDLGLSEAGARELDLG 199
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1041-1248 |
6.95e-08 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 55.03 E-value: 6.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1041 KDTKVLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERF--YNQDKGMIMIDGDNIRNLNiSSLREQVCI---------- 1108
Cdd:CHL00131 18 NENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHpaYKILEGDILFKGESILDLE-PEERAHLGIflafqypiei 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1109 --VSQEPTLfdctigeNICYGTNRNVTYQEIVEAAKMANIHNFILGLpdgydthVGEKGTQL--------SGGQKQRIAI 1178
Cdd:CHL00131 97 pgVSNADFL-------RLAYNSKRKFQGLPELDPLEFLEIINEKLKL-------VGMDPSFLsrnvnegfSGGEKKRNEI 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 124244275 1179 ARALVRSPSVLLLDEATSALDTESEKIVQEALDA-AKQGRTCLVIAH--RLSTIQNSDVIAIVSEGKIVEKGT 1248
Cdd:CHL00131 163 LQMALLDSELAILDETDSGLDIDALKIIAEGINKlMTSENSIILITHyqRLLDYIKPDYVHVMQNGKIIKTGD 235
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
748-908 |
7.89e-08 |
|
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: 55.55 E-value: 7.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 748 YFWCGMFVLMGITFFVGFFTSANCLGRCGESLTMKLRFEAFKNLLRQDIAFYDdlRHGTGKLCTRFATDAPNVRYVFTR- 826
Cdd:cd18545 40 LIIALLFLALNLVNWVASRLRIYLMAKVGQRILYDLRQDLFSHLQKLSFSFFD--SRPVGKILSRVINDVNSLSDLLSNg 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 827 LPVVLASIVTICGALGIGFYYGWQLALILVVMVPLLVMGGYFemqmrFGKQIRdtqlleEAGKVASQA-----------V 895
Cdd:cd18545 118 LINLIPDLLTLVGIVIIMFSLNVRLALVTLAVLPLLVLVVFL-----LRRRAR------KAWQRVRKKisnlnaylhesI 186
|
170
....*....|...
gi 124244275 896 EHIRTVHSLNRQE 908
Cdd:cd18545 187 SGIRVIQSFARED 199
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
121-330 |
7.93e-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: 55.57 E-value: 7.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 121 CIYYLVLGVLMFFTSYVQIACFESYAERLVHKLRQNYLKAILRQQIQWFDKQQTGNLTARLTDDLERVREGLGDKFALLV 200
Cdd:cd18546 42 AAAYLAVVLAGWVAQRAQTRLTGRTGERLLYDLRLRVFAHLQRLSLDFHERETSGRIMTRMTSDIDALSELLQTGLVQLV 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 201 QMFAAFLAGYGVGFFYSWSMTLVMMGFAPLIVLsgakmsksmATR--TRVEQETYAVA-GAIAE------ETFSSIRTVH 271
Cdd:cd18546 122 VSLLTLVGIAVVLLVLDPRLALVALAALPPLAL---------ATRwfRRRSSRAYRRArERIAAvnadlqETLAGIRVVQ 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 124244275 272 SLNGHKRELDRFYNALEVGRQTGIVKYCYMGIGVGFSNLCMYSSYALAFWYGSTLIIND 330
Cdd:cd18546 193 AFRRERRNAERFAELSDDYRDARLRAQRLVAIYFPGVELLGNLATAAVLLVGAWRVAAG 251
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
400-611 |
8.95e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 57.04 E-value: 8.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 400 SFKDVHFRYPSRKDIHV-LKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDP---TKGRVLIDGVDLREvnvhSLRE 475
Cdd:TIGR00956 761 HWRNLTYEVKIKKEKRViLNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTTgviTGGDRLVNGRPLDS----SFQR 836
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 476 QIGIVSQEPV-LFDGTIYE--------------NIKMGNEHAthDQVVEACKMANANDFIkrlpdgygtrVGEKGVQLSG 540
Cdd:TIGR00956 837 SIGYVQQQDLhLPTSTVREslrfsaylrqpksvSKSEKMEYV--EEVIKLLEMESYADAV----------VGVPGEGLNV 904
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 124244275 541 GQKQRIAIARALVKNPKILL-LDEATSALDTEAEREVQGALDQ-AQAGRTTIIVAHRLSTI--RNVDRIFVFKAG 611
Cdd:TIGR00956 905 EQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKlADHGQAILCTIHQPSAIlfEEFDRLLLLQKG 979
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
117-331 |
9.69e-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: 349994 [Multi-domain] Cd Length: 294 Bit Score: 55.18 E-value: 9.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 117 VVKYCIYYLVLGVLMFFTSYVQIACFESYAERLVHKLRQNYLKAILRQQIQWFDKQQTGNLTARLTDDLERVREGLGDKF 196
Cdd:cd18550 38 LVLLALGMVAVAVASALLGVVQTYLSARIGQGVMYDLRVQLYAHLQRMSLAFFTRTRTGEIQSRLNNDVGGAQSVVTGTL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 197 ALLVQMFAAFLAGYGVGFFYSWSMTLVMMGFAPLIVLSGAKMSKSMATRTRVEQETYAVAGAIAEETFS--SIRTVHSLN 274
Cdd:cd18550 118 TSVVSNVVTLVATLVAMLALDWRLALLSLVLLPLFVLPTRRVGRRRRKLTREQQEKLAELNSIMQETLSvsGALLVKLFG 197
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 124244275 275 GHKRELDRFYNA------LEVgRQTGIVKYCYMGIGVGFSnlcmySSYALAFWYGSTLIINDP 331
Cdd:cd18550 198 REDDEAARFARRsrelrdLGV-RQALAGRWFFAALGLFTA-----IGPALVYWVGGLLVIGGG 254
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
402-625 |
1.34e-07 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 54.44 E-value: 1.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 402 KDVHFRYPSRKDIHVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGvdlrEVNVHSLreQIGIVS 481
Cdd:PRK13546 25 KDALIPKHKNKTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG----EVSVIAI--SAGLSG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 482 QEpvlfdgTIYENIK-----MGNEHATHDQVV-EACKMANANDFIKRLPDGYgtrvgekgvqlSGGQKQRIAIARALVKN 555
Cdd:PRK13546 99 QL------TGIENIEfkmlcMGFKRKEIKAMTpKIIEFSELGEFIYQPVKKY-----------SSGMRAKLGFSINITVN 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124244275 556 PKILLLDEATSALD-TEAEREVQGALDQAQAGRTTIIVAHRLSTIRN-VDRIFVFKAGNIVESGSHEELMSK 625
Cdd:PRK13546 162 PDILVIDEALSVGDqTFAQKCLDKIYEFKEQNKTIFFVSHNLGQVRQfCTKIAWIEGGKLKDYGELDDVLPK 233
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
420-624 |
1.35e-07 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 55.19 E-value: 1.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 420 ISLELKAGDKIALVGSSGCGKSTIVNLL----QRFYDPTKGRVLIDGVDLREVNVHSLREQIG----IVSQEPV------ 485
Cdd:PRK15093 26 VSMTLTEGEIRGLVGESGSGKSLIAKAIcgvtKDNWRVTADRMRFDDIDLLRLSPRERRKLVGhnvsMIFQEPQscldps 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 486 --------------LFDGTIYENIKMGNEHAThdQVVEACKMANANDFIKRLPdgygtrvgekgVQLSGGQKQRIAIARA 551
Cdd:PRK15093 106 ervgrqlmqnipgwTYKGRWWQRFGWRKRRAI--ELLHRVGIKDHKDAMRSFP-----------YELTEGECQKVMIAIA 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 124244275 552 LVKNPKILLLDEATSALDTEAEREVQGALDQA-QAGRTTI-IVAHRLSTIRN-VDRIFVFKAGNIVESGSHEELMS 624
Cdd:PRK15093 173 LANQPRLLIADEPTNAMEPTTQAQIFRLLTRLnQNNNTTIlLISHDLQMLSQwADKINVLYCGQTVETAPSKELVT 248
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
1021-1242 |
1.42e-07 |
|
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: 55.95 E-value: 1.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1021 VKPITGNISiRNVFFNYPtrKDTKVLQGFTLDIKAGK-----TVALVGHSGCGKSTIMGLLerfynqdKGMIMID-GDNI 1094
Cdd:COG1245 329 VHAPRREKE-EETLVEYP--DLTKSYGGFSLEVEGGEiregeVLGIVGPNGIGKTTFAKIL-------AGVLKPDeGEVD 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1095 RNLNISsLREQVCIVSQEPTLFDC---TIGENIcygtNRNVTYQEIVEAakmanihnfiLGLPDGYDTHVGEkgtqLSGG 1171
Cdd:COG1245 399 EDLKIS-YKPQYISPDYDGTVEEFlrsANTDDF----GSSYYKTEIIKP----------LGLEKLLDKNVKD----LSGG 459
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 124244275 1172 QKQRIAIARALVRSPSVLLLDEATSALDTESEKIVQEALD--AAKQGRTCLVIAHRLSTIqnsDVIA---IVSEGK 1242
Cdd:COG1245 460 ELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRrfAENRGKTAMVVDHDIYLI---DYISdrlMVFEGE 532
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
125-329 |
1.47e-07 |
|
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: 54.52 E-value: 1.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 125 LVLGVLMFFTSYVQI--ACFESY-----AERLVHKLRQNYLKAILRQQIQWFDKQQTGNLTARLtDDLERVREGLGDKfA 197
Cdd:cd18782 42 YVIGVVMLVAALLEAvlTALRTYlftdtANRIDLELGGTIIDHLLRLPLGFFDKRPVGELSTRI-SELDTIRGFLTGT-A 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 198 LLVQMFAAFLAGY-GVGFFYSWSMTLVMMGFAPLIVLSGAKMSKSMATRTRVEQETYAVAGAIAEETFSSIRTVHSLNG- 275
Cdd:cd18782 120 LTTLLDVLFSVIYiAVLFSYSPLLTLVVLATVPLQLLLTFLFGPILRRQIRRRAEASAKTQSYLVESLTGIQTVKAQNAe 199
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 124244275 276 --HKRELDRFYNA-LEVGRQTGIVKYCYMGIGVGFSNLcmysSYALAFWYGSTLIIN 329
Cdd:cd18782 200 lkARWRWQNRYARsLGEGFKLTVLGTTSGSLSQFLNKL----SSLLVLWVGAYLVLR 252
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
392-628 |
2.09e-07 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 55.18 E-value: 2.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 392 VDNMKGDISFKdvhFRYPSRKDIHVLKGISLELKAGDKIALVGSSGCGKSTIVNLLqrF-YDPTK-GRVLIDGVDLREVN 469
Cdd:PRK09700 257 VSNLAHETVFE---VRNVTSRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCL--FgVDKRAgGEIRLNGKDISPRS 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 470 -VHSLREQIGIVSQ---EPVLFDG-TIYENI------KMGNEHATHDQVVEACKMANANDFIKRLPDGYGTrVGEKGVQL 538
Cdd:PRK09700 332 pLDAVKKGMAYITEsrrDNGFFPNfSIAQNMaisrslKDGGYKGAMGLFHEVDEQRTAENQRELLALKCHS-VNQNITEL 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 539 SGGQKQRIAIARALVKNPKILLLDEATSALDTEAEREVQGALDQ-AQAGRTTIIVAHRLSTIRNV-DRIFVFKAGNIVES 616
Cdd:PRK09700 411 SGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQlADDGKVILMVSSELPEIITVcDRIAVFCEGRLTQI 490
|
250
....*....|..
gi 124244275 617 GSHEELMSKQGI 628
Cdd:PRK09700 491 LTNRDDMSEEEI 502
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1047-1243 |
3.25e-07 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 54.67 E-value: 3.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1047 QGF---TLDIKAGKTVALVGHSGCGKSTimgLLERFYN---QDKGMIMIDGDNIRNLNISSlREQVCIV-----SQEPTL 1115
Cdd:PRK15439 277 EGFrniSLEVRAGEILGLAGVVGAGRTE---LAETLYGlrpARGGRIMLNGKEINALSTAQ-RLARGLVylpedRQSSGL 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1116 F-DCTIGENICYGTNRNVTY--QEIVEAAKMANIHNfILGLPDgydTHVGEKGTQLSGGQKQRIAIARALVRSPSVLLLD 1192
Cdd:PRK15439 353 YlDAPLAWNVCALTHNRRGFwiKPARENAVLERYRR-ALNIKF---NHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVD 428
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 124244275 1193 EATSALDTESEK-IVQEALDAAKQGRTCLVIAHRLSTI-QNSDVIAIVSEGKI 1243
Cdd:PRK15439 429 EPTRGVDVSARNdIYQLIRSIAAQNVAVLFISSDLEEIeQMADRVLVMHQGEI 481
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
424-596 |
3.45e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 54.43 E-value: 3.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 424 LKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVL----IDGV--------------DLREVNVHSLReQIGIVSQEPV 485
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSGELIPNLGDYEeepsWDEVlkrfrgtelqnyfkKLYNGEIKVVH-KPQYVDLIPK 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 486 LFDGTIYENIKMGNEHATHDQVVEACKMANANDfikrlpdgygtrvgeKGV-QLSGGQKQRIAIARALVKNPKILLLDEA 564
Cdd:PRK13409 175 VFKGKVRELLKKVDERGKLDEVVERLGLENILD---------------RDIsELSGGELQRVAIAAALLRDADFYFFDEP 239
|
170 180 190
....*....|....*....|....*....|...
gi 124244275 565 TSALDTEaER-EVQGALDQAQAGRTTIIVAHRL 596
Cdd:PRK13409 240 TSYLDIR-QRlNVARLIRELAEGKYVLVVEHDL 271
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1030-1252 |
4.52e-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: 54.06 E-value: 4.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1030 IRNVFFNYPTRKDTKVLQGFTLDIKAGKTVALVGHSGCGKS-TIMGLLERFYNQDKGMIMIDGD--NIRNLnISSLREQV 1106
Cdd:TIGR02633 260 ARNLTCWDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTeLVQALFGAYPGKFEGNVFINGKpvDIRNP-AQAIRAGI 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1107 CIVSQEPT----LFDCTIGENICYGT-NRNVTYQEIVEAAKMANIHNFILGLpdgydtHVGEKG-----TQLSGGQKQRI 1176
Cdd:TIGR02633 339 AMVPEDRKrhgiVPILGVGKNITLSVlKSFCFKMRIDAAAELQIIGSAIQRL------KVKTASpflpiGRLSGGNQQKA 412
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 124244275 1177 AIARALVRSPSVLLLDEATSALDTESEKIVQEALDA-AKQGRTCLVIAHRLSTIQN-SDVIAIVSEGKIVEKGTHDEL 1252
Cdd:TIGR02633 413 VLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQlAQEGVAIIVVSSELAEVLGlSDRVLVIGEGKLKGDFVNHAL 490
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
422-601 |
4.91e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 54.19 E-value: 4.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 422 LELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDgvdlREVNVHSLrEQigivsQEPVLFDGTIYENIKMGNE- 500
Cdd:PRK11147 24 LHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYE----QDLIVARL-QQ-----DPPRNVEGTVYDFVAEGIEe 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 501 --------HATHDQVVEAC------KMANA----------------NDFIKRL---PDgygTRVGEkgvqLSGGQKQRIA 547
Cdd:PRK11147 94 qaeylkryHDISHLVETDPseknlnELAKLqeqldhhnlwqlenriNEVLAQLgldPD---AALSS----LSGGWLRKAA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 124244275 548 IARALVKNPKILLLDEATSALDTEAEREVQGALDQAQAgrTTIIVAHRLSTIRN 601
Cdd:PRK11147 167 LGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQG--SIIFISHDRSFIRN 218
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1054-1238 |
5.16e-07 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 52.37 E-value: 5.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1054 KAGKTVALVGHSGCGKSTIMGLLE--------RFYNQDKGMIMID---GDNIRNLNISSLREQV-CI-----VSQEPTLF 1116
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAgklkpnlgKFDDPPDWDEILDefrGSELQNYFTKLLEGDVkVIvkpqyVDLIPKAV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1117 DCTIGENIcYGTNRNVTYQEIVEAakmanihnfiLGLPDGYDTHVgekgTQLSGGQKQRIAIARALVRSPSVLLLDEATS 1196
Cdd:cd03236 104 KGKVGELL-KKKDERGKLDELVDQ----------LELRHVLDRNI----DQLSGGELQRVAIAAALARDADFYFFDEPSS 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 124244275 1197 ALDTESE----KIVQEaldAAKQGRTCLVIAHRLSTIQN-SDVIAIV 1238
Cdd:cd03236 169 YLDIKQRlnaaRLIRE---LAEDDNYVLVVEHDLAVLDYlSDYIHCL 212
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
786-995 |
5.17e-07 |
|
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: 52.86 E-value: 5.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 786 EAFKNLLRQDIAFYDdlRHGTGKLCTRFATDAPNVRYVFT-RLPVVLASIVTICGALGIGFYYGWQLALILVVMVPLLVM 864
Cdd:cd18589 74 LVFAAVLRQEIAFFD--SNQTGDIVSRVTTDTEDMSESLSeNLSLLMWYLARGLFLFIFMLWLSPKLALLTALGLPLLLL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 865 GGYF--EMQMRFGKQIRDTqlLEEAGKVASQAVEHIRTVHSLNRQEQFHFTYCEYLREPFNTNLKHAHTYgAVFAFSQSL 942
Cdd:cd18589 152 VPKFvgKFQQSLAVQVQKS--LARANQVAVETFSAMKTVRSFANEEGEAQRYRQRLQKTYRLNKKEAAAY-AVSMWTSSF 228
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 124244275 943 I-FFMYAAAFYLGSIFVNQQAMQPID-VYRVFFAISFcGQMIGNTTSFIPDVVKA 995
Cdd:cd18589 229 SgLALKVGILYYGGQLVTAGTVSSGDlVTFVLYELQF-TSAVEVLLSYYPSVMKA 282
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
536-608 |
6.41e-07 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 51.03 E-value: 6.41e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 124244275 536 VQLSGGQKQRIAIARALVKNPKILLLDEATSALDTEAEREVQGALDQ--AQAGRTTIIVAHRLSTIRNV-DRIFVF 608
Cdd:cd03222 70 IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRlsEEGKKTALVVEHDLAVLDYLsDRIHVF 145
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
1054-1238 |
7.79e-07 |
|
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: 53.25 E-value: 7.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1054 KAGKTVALVGHSGCGKSTIMGLL---------------------ERFynqdKGMIMIDG-DNIRNLNIS-SLREQVciVS 1110
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILsgelkpnlgdydeepswdevlKRF----RGTELQDYfKKLANGEIKvAHKPQY--VD 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1111 QEPTLFDCTIGEnICYGTNRNVTYQEIVEAAKMANIhnfilglpdgYDTHVGEkgtqLSGGQKQRIAIARALVRSPSVLL 1190
Cdd:COG1245 171 LIPKVFKGTVRE-LLEKVDERGKLDELAEKLGLENI----------LDRDISE----LSGGELQRVAIAAALLRDADFYF 235
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 124244275 1191 LDEATSALD----TESEKIVQEaldAAKQGRTCLVIAHRLSTIQN-SDVIAIV 1238
Cdd:COG1245 236 FDEPSSYLDiyqrLNVARLIRE---LAEEGKYVLVVEHDLAILDYlADYVHIL 285
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1033-1199 |
8.23e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 53.25 E-value: 8.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1033 VFFNYPTRKDTKVL-QGFTLDIKAGKTVALVGHSGCGKSTIMGLLerfynqdKGMIMIDGDNIRNLNISSLreqvCIVSQ 1111
Cdd:PRK10636 3 VFSSLQIRRGVRVLlDNATATINPGQKVGLVGKNGCGKSTLLALL-------KNEISADGGSYTFPGNWQL----AWVNQ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1112 EPTLFDCTIGENICYGTNRnvtYQEIVEAAKMANIHN------FILGLPDGYDT------------HVGEKGTQL----- 1168
Cdd:PRK10636 72 ETPALPQPALEYVIDGDRE---YRQLEAQLHDANERNdghaiaTIHGKLDAIDAwtirsraasllhGLGFSNEQLerpvs 148
|
170 180 190
....*....|....*....|....*....|...
gi 124244275 1169 --SGGQKQRIAIARALVRSPSVLLLDEATSALD 1199
Cdd:PRK10636 149 dfSGGWRMRLNLAQALICRSDLLLLDEPTNHLD 181
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1053-1248 |
8.71e-07 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 53.86 E-value: 8.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1053 IKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGMIMIDGDNIRNlNISSLREQVCIVSQEPTLFDCTIGEN--ICYGTNR 1130
Cdd:TIGR01257 1962 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT-NISDVHQNMGYCPQFDAIDDLLTGREhlYLYARLR 2040
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1131 NVTYQEIveaAKMANIHNFILGLPDGYDTHVGekgtQLSGGQKQRIAIARALVRSPSVLLLDEATSALDTESEKIVQEAL 1210
Cdd:TIGR01257 2041 GVPAEEI---EKVANWSIQSLGLSLYADRLAG----TYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTI 2113
|
170 180 190
....*....|....*....|....*....|....*....
gi 124244275 1211 -DAAKQGRTCLVIAHRLSTIQnsdviAIVSEGKIVEKGT 1248
Cdd:TIGR01257 2114 vSIIREGRAVVLTSHSMEECE-----ALCTRLAIMVKGA 2147
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
378-619 |
8.84e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 53.27 E-value: 8.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 378 SHPK-----IDPYsLEGILVD-NM---KGDISFK----------DVHFRYPS-RKDihvLKGISLELKAGDK-----IAL 432
Cdd:PRK13409 295 SKPKgvrvgINEY-LKGYLPEeNMrirPEPIEFEerpprdeserETLVEYPDlTKK---LGDFSLEVEGGEIyegevIGI 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 433 VGSSGCGKSTIVNLLQRFYDPTKGRVLIDgvdlrevnvhsLReqigiVSQEP----VLFDGTIYENIKMGNEhATHDQVV 508
Cdd:PRK13409 371 VGPNGIGKTTFAKLLAGVLKPDEGEVDPE-----------LK-----ISYKPqyikPDYDGTVEDLLRSITD-DLGSSYY 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 509 EackmanaNDFIKRL--PDGYGTRVGEkgvqLSGGQKQRIAIARALVKNPKILLLDEATSALDTEAEREVQGALDQAQAG 586
Cdd:PRK13409 434 K-------SEIIKPLqlERLLDKNVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEE 502
|
250 260 270
....*....|....*....|....*....|....*.
gi 124244275 587 R--TTIIVAHRLSTIRNV-DRIFVFKAgnivESGSH 619
Cdd:PRK13409 503 ReaTALVVDHDIYMIDYIsDRLMVFEG----EPGKH 534
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
423-609 |
9.24e-07 |
|
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: 53.25 E-value: 9.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 423 ELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVlidGVDLRevnvhslreqigiVSQEP----VLFDGTIYENIKMG 498
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV---DEDLK-------------ISYKPqyisPDYDGTVEEFLRSA 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 499 NEHATHDQVVEackmanaNDFIKRLpdgyG-TRVGEKGV-QLSGGQKQRIAIARALVKNPKILLLDEATSALDTEAEREV 576
Cdd:COG1245 426 NTDDFGSSYYK-------TEIIKPL----GlEKLLDKNVkDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAV 494
|
170 180 190
....*....|....*....|....*....|....*.
gi 124244275 577 QGALDQ--AQAGRTTIIVAHRLSTIRNV-DRIFVFK 609
Cdd:COG1245 495 AKAIRRfaENRGKTAMVVDHDIYLIDYIsDRLMVFE 530
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
1162-1253 |
9.49e-07 |
|
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: 53.48 E-value: 9.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1162 GEKGTQLSGGQKQRIAIARALVR---SPSVLLLDEATSALDTESEK----IVQEALDaakQGRTCLVIAHRLSTIQNSD- 1233
Cdd:TIGR00630 824 GQPATTLSGGEAQRIKLAKELSKrstGRTLYILDEPTTGLHFDDIKklleVLQRLVD---KGNTVVVIEHNLDVIKTADy 900
|
90 100
....*....|....*....|....*
gi 124244275 1234 VIAIVSE-----GKIVEKGTHDELI 1253
Cdd:TIGR00630 901 IIDLGPEggdggGTVVASGTPEEVA 925
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
420-613 |
1.03e-06 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 52.75 E-value: 1.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 420 ISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDLREVNVHSlREQIGIV-----SQEPVLF-DGTIYE 493
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQ-RLARGLVylpedRQSSGLYlDAPLAW 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 494 N------------IKMGNEHATHDQVVEA--CKMANANDFIKRlpdgygtrvgekgvqLSGGQKQRIAIARALVKNPKIL 559
Cdd:PRK15439 361 NvcalthnrrgfwIKPARENAVLERYRRAlnIKFNHAEQAART---------------LSGGNQQKVLIAKCLEASPQLL 425
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 124244275 560 LLDEATSALDTEAEREV-QGALDQAQAGRTTIIVAHRLSTIRNV-DRIFVFKAGNI 613
Cdd:PRK15439 426 IVDEPTRGVDVSARNDIyQLIRSIAAQNVAVLFISSDLEEIEQMaDRVLVMHQGEI 481
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1028-1226 |
1.10e-06 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 51.27 E-value: 1.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1028 ISIRNVFFNYPTRKdtkVLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGMIMIDGdnirNLNISSLREQVC 1107
Cdd:PRK09544 5 VSLENVSVSFGQRR---VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNG----KLRIGYVPQKLY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1108 IvsqEPTLfDCTIGENICYgtNRNVTYQEIVEAAKMANIhnfilglpdgydTHVGEKGTQ-LSGGQKQRIAIARALVRSP 1186
Cdd:PRK09544 78 L---DTTL-PLTVNRFLRL--RPGTKKEDILPALKRVQA------------GHLIDAPMQkLSGGETQRVLLARALLNRP 139
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 124244275 1187 SVLLLDEATSALDTESEKIVQEALDAAKQGRTC--LVIAHRL 1226
Cdd:PRK09544 140 QLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCavLMVSHDL 181
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
415-617 |
1.21e-06 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 50.01 E-value: 1.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 415 HVLKGISLELKAGDKIALVGSSGCGKSTIVNllQRFYDPTKGRVlidgVDLREVNvhslreqigivSQEPVLFDGTIYEN 494
Cdd:cd03238 9 HNLQNLDVSIPLNVLVVVTGVSGSGKSTLVN--EGLYASGKARL----ISFLPKF-----------SRNKLIFIDQLQFL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 495 IKMGNEHATHDQvveacKMANandfikrlpdgygtrvgekgvqLSGGQKQRIAIARALVKNPK--ILLLDEATSALDTEA 572
Cdd:cd03238 72 IDVGLGYLTLGQ-----KLST----------------------LSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQD 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 124244275 573 EREVQGALDQ-AQAGRTTIIVAHRLSTIRNVDRIFVF------KAGNIVESG 617
Cdd:cd03238 125 INQLLEVIKGlIDLGNTVILIEHNLDVLSSADWIIDFgpgsgkSGGKVVFSG 176
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
424-598 |
1.49e-06 |
|
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: 52.48 E-value: 1.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 424 LKAGDKIALVGSSGCGKSTIVNLL---------------------QRFydptKG-------RVLIDGvdlrEVNVhSLRE 475
Cdd:COG1245 96 PKKGKVTGILGPNGIGKSTALKILsgelkpnlgdydeepswdevlKRF----RGtelqdyfKKLANG----EIKV-AHKP 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 476 QIgiVSQEPVLFDGTIYENIKMGNEHATHDQVVEACKMANandFIKRlpdgygtRVGEkgvqLSGGQKQRIAIARALVKN 555
Cdd:COG1245 167 QY--VDLIPKVFKGTVRELLEKVDERGKLDELAEKLGLEN---ILDR-------DISE----LSGGELQRVAIAAALLRD 230
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 124244275 556 PKILLLDEATSALDTEAEREVQGAL-DQAQAGRTTIIVAHRLST 598
Cdd:COG1245 231 ADFYFFDEPSSYLDIYQRLNVARLIrELAEEGKYVLVVEHDLAI 274
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
122-329 |
1.55e-06 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; This group represents 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: 350010 [Multi-domain] Cd Length: 294 Bit Score: 51.43 E-value: 1.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 122 IYYLVLGVLMFFTSYVqiacFESYAERLVHKLRQNYLKAILRQQIQWFDKQQTGNLTARLTdDLERVREGLGDKfALLVQ 201
Cdd:cd18566 50 IAILLESLLRLLRSYI----LAWIGARFDHRLSNAAFEHLLSLPLSFFEREPSGAHLERLN-SLEQIREFLTGQ-ALLAL 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 202 MFAAFLAGY-GVGFFYSWSMTLVMMGFAPLIVLSGAKMSKSMATRTRVEQETYAVAGAIAEETFSSIRTVHSLNGHKREL 280
Cdd:cd18566 124 LDLPFVLIFlGLIWYLGGKLVLVPLVLLGLFVLVAILLGPILRRALKERSRADERRQNFLIETLTGIHTIKAMAMEPQML 203
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 124244275 281 DRF--------YNALEVGRQTGIVkycymgigVGFSNLCMYSSYALAFWYGSTLIIN 329
Cdd:cd18566 204 RRYerlqanaaYAGFKVAKINAVA--------QTLGQLFSQVSMVAVVAFGALLVIN 252
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
1046-1235 |
1.77e-06 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 49.63 E-value: 1.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1046 LQGFTLDIKAGKTVALVGHSGCGKSTImgLLERFYNQDKGMIMIDgdnirnlnisslreqvcivsqePTLFDctigenic 1125
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTL--VNEGLYASGKARLISF----------------------LPKFS-------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1126 ygtnrnvtYQEIVEAAKMANIHNfiLGLpdGYDThVGEKGTQLSGGQKQRIAIARALVRSP--SVLLLDEATSALDTES- 1202
Cdd:cd03238 59 --------RNKLIFIDQLQFLID--VGL--GYLT-LGQKLSTLSGGELQRVKLASELFSEPpgTLFILDEPSTGLHQQDi 125
|
170 180 190
....*....|....*....|....*....|...
gi 124244275 1203 EKIVQEALDAAKQGRTCLVIAHRLSTIQNSDVI 1235
Cdd:cd03238 126 NQLLEVIKGLIDLGNTVILIEHNLDVLSSADWI 158
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1156-1259 |
1.83e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 52.04 E-value: 1.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1156 GYDTHVGekgtQLSGGQKQRIAIARALVRSPSVLLLDEATSALDTESE-KIVQEALDAAKQGRTCLVIAHRLSTIQN-SD 1233
Cdd:PRK10982 384 GHRTQIG----SLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKfEIYQLIAELAKKDKGIIIISSEMPELLGiTD 459
|
90 100 110
....*....|....*....|....*....|.
gi 124244275 1234 VIAIVSEGK---IVE--KGTHDELIRKSEIY 1259
Cdd:PRK10982 460 RILVMSNGLvagIVDtkTTTQNEILRLASLH 490
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
421-624 |
1.85e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 51.94 E-value: 1.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 421 SLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLidgVDLREVNVHSLREQIGIVSQE------PVLFDG----- 489
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQ---SQFSHITRLSFEQLQKLVSDEwqrnntDMLSPGeddtg 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 490 -TIYENIKMGNEHAthdqvvEACKMANANDFIKRLPDgygtrvgEKGVQLSGGQKQRIAIARALVKNPKILLLDEATSAL 568
Cdd:PRK10938 100 rTTAEIIQDEVKDP------ARCEQLAQQFGITALLD-------RRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 124244275 569 DTEAEREVQGALDQ-AQAGRTTIIVAHRLSTIRN-VDRIFVFKAGNIVESGSHEELMS 624
Cdd:PRK10938 167 DVASRQQLAELLASlHQSGITLVLVLNRFDEIPDfVQFAGVLADCTLAETGEREEILQ 224
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
526-622 |
2.63e-06 |
|
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: 51.94 E-value: 2.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 526 GYgTRVGEKGVQLSGGQKQRIAIARALVK---NPKILLLDEATSALDTEAERE----VQGALDQaqaGRTTIIVAHRLST 598
Cdd:TIGR00630 819 GY-IRLGQPATTLSGGEAQRIKLAKELSKrstGRTLYILDEPTTGLHFDDIKKllevLQRLVDK---GNTVVVIEHNLDV 894
|
90 100 110
....*....|....*....|....*....|
gi 124244275 599 IRNVDRIFVF------KAGNIVESGSHEEL 622
Cdd:TIGR00630 895 IKTADYIIDLgpeggdGGGTVVASGTPEEV 924
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
1028-1199 |
3.24e-06 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 51.66 E-value: 3.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1028 ISIRNVFFNYptrKDTKVLQGFTLDIKAGKTVALVGHSGCGKSTIMGLL--ERFYNQdkGMIMIDGDNIRNlniSSLREQ 1105
Cdd:NF033858 2 ARLEGVSHRY---GKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIagARKIQQ--GRVEVLGGDMAD---ARHRRA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1106 VC--I--VSQ------EPTLfdcTIGENI-----CYGTNRNVTYQEIVEAAKMANIHNFiLGLPDGydthvgekgtQLSG 1170
Cdd:NF033858 74 VCprIayMPQglgknlYPTL---SVFENLdffgrLFGQDAAERRRRIDELLRATGLAPF-ADRPAG----------KLSG 139
|
170 180
....*....|....*....|....*....
gi 124244275 1171 GQKQRIAIARALVRSPSVLLLDEATSALD 1199
Cdd:NF033858 140 GMKQKLGLCCALIHDPDLLILDEPTTGVD 168
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1053-1238 |
3.72e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 51.35 E-value: 3.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1053 IKAGKTVALVGHSGCGKSTIMGLL---------------------ERFynqdKGMIMidGDNIRNLNISSLREQVCI--V 1109
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILsgelipnlgdyeeepswdevlKRF----RGTEL--QNYFKKLYNGEIKVVHKPqyV 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1110 SQEPTLFDCTIGEnICYGTNRNVTYQEIVEAAKMANIhnfilglpdgYDTHVGEkgtqLSGGQKQRIAIARALVRSPSVL 1189
Cdd:PRK13409 170 DLIPKVFKGKVRE-LLKKVDERGKLDEVVERLGLENI----------LDRDISE----LSGGELQRVAIAAALLRDADFY 234
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 124244275 1190 LLDEATSALDtesekiVQEALDAAK------QGRTCLVIAHRLSTIQN-SDVIAIV 1238
Cdd:PRK13409 235 FFDEPTSYLD------IRQRLNVARlirelaEGKYVLVVEHDLAVLDYlADNVHIA 284
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1044-1228 |
4.87e-06 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 50.70 E-value: 4.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1044 KVL-QGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGMIMIdGDNIrnlnisslreQVCIVSQEPTLFDctige 1122
Cdd:TIGR03719 335 KLLiDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETV----------KLAYVDQSRDALD----- 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1123 nicygTNRNVtYQEIVEAAKMANIHNFILGlPDGYDTHVGEKGT-------QLSGGQKQRIAIARALVRSPSVLLLDEAT 1195
Cdd:TIGR03719 399 -----PNKTV-WEEISGGLDIIKLGKREIP-SRAYVGRFNFKGSdqqkkvgQLSGGERNRVHLAKTLKSGGNVLLLDEPT 471
|
170 180 190
....*....|....*....|....*....|....*....
gi 124244275 1196 SALDTESEKIVQEALDAAkqGRTCLVIAH------RLST 1228
Cdd:TIGR03719 472 NDLDVETLRALEEALLNF--AGCAVVISHdrwfldRIAT 508
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
1004-1243 |
5.23e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 51.01 E-value: 5.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1004 YLIEHPTPIDslsdsgivKPITGNISIRNVFFNYPtrKDTKVLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLER----- 1078
Cdd:PLN03073 493 YKFEFPTPDD--------RPGPPIISFSDASFGYP--GGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGelqps 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1079 ----FYNQDKGMIMIDGDNIRNLNISSlreqvcivsqEPTLF--DCtigenicygtnrnvtYQEIVEAAKMANIHNF--- 1149
Cdd:PLN03073 563 sgtvFRSAKVRMAVFSQHHVDGLDLSS----------NPLLYmmRC---------------FPGVPEQKLRAHLGSFgvt 617
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1150 -ILGLPDGYdthvgekgtQLSGGQKQRIAIARALVRSPSVLLLDEATSALDTESEKIVQEALdAAKQGRTCLViAHRLST 1228
Cdd:PLN03073 618 gNLALQPMY---------TLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGL-VLFQGGVLMV-SHDEHL 686
|
250
....*....|....*.
gi 124244275 1229 IQNS-DVIAIVSEGKI 1243
Cdd:PLN03073 687 ISGSvDELWVVSEGKV 702
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
402-629 |
6.75e-06 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 50.27 E-value: 6.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 402 KDVHFRYPSRKDIHVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDLREVNVHSLREQI-GIV 480
Cdd:PRK13545 25 KDLFFRSKDGEYHYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIAISSGLNGQLtGIE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 481 SQE-PVLFDGTIYENIKmgnehATHDQVVEackMANANDFIKRLPDGYgtrvgekgvqlSGGQKQRIAIARALVKNPKIL 559
Cdd:PRK13545 105 NIElKGLMMGLTKEKIK-----EIIPEIIE---FADIGKFIYQPVKTY-----------SSGMKSRLGFAISVHINPDIL 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 124244275 560 LLDEATSALDTEAEREVQGALDQ-AQAGRTTIIVAHRLSTIRNvdriFVFKA-----GNIVESGSHEELMSKQGIF 629
Cdd:PRK13545 166 VIDEALSVGDQTFTKKCLDKMNEfKEQGKTIFFISHSLSQVKS----FCTKAlwlhyGQVKEYGDIKEVVDHYDEF 237
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1030-1232 |
9.10e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 49.95 E-value: 9.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1030 IRNVFFNYPtrkDTKVLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLerfynqdKGMIMIDGDNIR---NLNISSLREQV 1106
Cdd:PRK11147 322 MENVNYQID---GKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLM-------LGQLQADSGRIHcgtKLEVAYFDQHR 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1107 CIVSQEPTLFDctigeNICYGTnrnvtyQEIveaakMAN-IHNFILGL-------PDGYDTHVgekgTQLSGGQKQRIAI 1178
Cdd:PRK11147 392 AELDPEKTVMD-----NLAEGK------QEV-----MVNgRPRHVLGYlqdflfhPKRAMTPV----KALSGGERNRLLL 451
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 124244275 1179 ARALVRSPSVLLLDEATSALDTESEKIVQEALDAAkQGrTCLVIAHRLSTIQNS 1232
Cdd:PRK11147 452 ARLFLKPSNLLILDEPTNDLDVETLELLEELLDSY-QG-TVLLVSHDRQFVDNT 503
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
1168-1242 |
9.28e-06 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 47.57 E-value: 9.28e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 124244275 1168 LSGGQKQRIAIARALVRSPSVLLLDEATSALDTESEKIVQEALD--AAKQGRTCLVIAHRLSTIQNSDVIAIVSEGK 1242
Cdd:cd03222 72 LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRrlSEEGKKTALVVEHDLAVLDYLSDRIHVFEGE 148
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
399-606 |
1.55e-05 |
|
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: 49.16 E-value: 1.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 399 ISFKDVHFRYPSRKdihVLKGISLELKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLI-DGVdlrevnvhslreQI 477
Cdd:TIGR03719 323 IEAENLTKAFGDKL---LIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIgETV------------KL 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 478 GIVSQEPVLFDG--TIYENIKMGNEHAthdqvveacKMANAnDFIKRlpdGYGTRVGEKGV-------QLSGGQKQRIAI 548
Cdd:TIGR03719 388 AYVDQSRDALDPnkTVWEEISGGLDII---------KLGKR-EIPSR---AYVGRFNFKGSdqqkkvgQLSGGERNRVHL 454
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 124244275 549 ARALVKNPKILLLDEATSALDTEAEREVQGALDqAQAGrTTIIVAHrlstirnvDRIF 606
Cdd:TIGR03719 455 AKTLKSGGNVLLLDEPTNDLDVETLRALEEALL-NFAG-CAVVISH--------DRWF 502
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
1028-1233 |
1.68e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 48.86 E-value: 1.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1028 ISIRNVFFNYptrKDTKVLQGFTLDIKAGKTVALVGHSGCGKSTIMGLlerfynqdkgmimIDGDNIRNLnisslreqvc 1107
Cdd:PRK10938 261 IVLNNGVVSY---NDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSL-------------ITGDHPQGY---------- 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1108 ivSQEPTLF-----------DctIGENICYGTN------------RNV----------TYQEIVEAA-KMANIHNFILGL 1153
Cdd:PRK10938 315 --SNDLTLFgrrrgsgetiwD--IKKHIGYVSSslhldyrvstsvRNVilsgffdsigIYQAVSDRQqKLAQQWLDILGI 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1154 pdgyDTHVGEKGTQ-LSGGQkQRIA-IARALVRSPSVLLLDEATSALDTESEKIVQEALDA-AKQGRTCLV--------- 1221
Cdd:PRK10938 391 ----DKRTADAPFHsLSWGQ-QRLAlIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVlISEGETQLLfvshhaeda 465
|
250
....*....|....*
gi 124244275 1222 ---IAHRLSTIQNSD 1233
Cdd:PRK10938 466 pacITHRLEFVPDGD 480
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
122-330 |
1.86e-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: 1.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 122 IYYLVLGVLMFFTSYVQIACFESY-----AERLVHKLRQNYLKAILRQQIQWFDKQQTGNLTARLTDDlERVREGL-GDK 195
Cdd:cd18568 41 LNLILIGLLIVGIFQILLSAVRQYlldyfANRIDLSLLSDFYKHLLSLPLSFFASRKVGDIITRFQEN-QKIRRFLtRSA 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 196 FALLVQMFAAFLAGyGVGFFYSWSMTLVMMGFAPLIVLSGAKMSKSMatrTRVEQETYAvAGAIAE----ETFSSIRTVH 271
Cdd:cd18568 120 LTTILDLLMVFIYL-GLMFYYNLQLTLIVLAFIPLYVLLTLLSSPKL---KRNSREIFQ-ANAEQQsflvEALTGIATIK 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124244275 272 SLNG----HKRELDRFYNALEVGRQTGIvkycyMGIGVGF-SNLCMYSSYALAFWYGSTLIIND 330
Cdd:cd18568 195 ALAAerpiRWRWENKFAKALNTRFRGQK-----LSIVLQLiSSLINHLGTIAVLWYGAYLVISG 253
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1022-1258 |
2.05e-05 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 48.63 E-value: 2.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1022 KPITGNISIRNVF-FNYPTRKDTKVLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLerfYNQDK---GMIMIDGDNIRNL 1097
Cdd:PRK09700 254 KENVSNLAHETVFeVRNVTSRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCL---FGVDKragGEIRLNGKDISPR 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1098 N-ISSLREQVCIVSQ---EPTLF-DCTIGENIC-------------YGTNRNVTYQEIVEAA------KMANIHNFIlgl 1153
Cdd:PRK09700 331 SpLDAVKKGMAYITEsrrDNGFFpNFSIAQNMAisrslkdggykgaMGLFHEVDEQRTAENQrellalKCHSVNQNI--- 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1154 pdgydthvgekgTQLSGGQKQRIAIARALVRSPSVLLLDEATSALD----TESEKIVQEaldAAKQGRTCLVIAHRLSTI 1229
Cdd:PRK09700 408 ------------TELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDvgakAEIYKVMRQ---LADDGKVILMVSSELPEI 472
|
250 260 270
....*....|....*....|....*....|
gi 124244275 1230 QN-SDVIAIVSEGKIVEKGTHDELIRKSEI 1258
Cdd:PRK09700 473 ITvCDRIAVFCEGRLTQILTNRDDMSEEEI 502
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1029-1250 |
2.18e-05 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 47.61 E-value: 2.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1029 SIRNVFFNYPTRKDtkvLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGMIMIDGDNIRNLNISSL------ 1102
Cdd:PRK11701 8 SVRGLTKLYGPRKG---CRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALseaerr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1103 ---REQVCIVSQEPTlfD---------CTIGENICYGTNRNvtYQEIVEAAK--MANIH---NFILGLPdgydthvgekg 1165
Cdd:PRK11701 85 rllRTEWGFVHQHPR--DglrmqvsagGNIGERLMAVGARH--YGDIRATAGdwLERVEidaARIDDLP----------- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1166 TQLSGGQKQRIAIARALVRSPSVLLLDEATSALDTEsekiVQ-EALD-----AAKQGRTCLVIAHRLSTIQN-SDVIAIV 1238
Cdd:PRK11701 150 TTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVS----VQaRLLDllrglVRELGLAVVIVTHDLAVARLlAHRLLVM 225
|
250
....*....|..
gi 124244275 1239 SEGKIVEKGTHD 1250
Cdd:PRK11701 226 KQGRVVESGLTD 237
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
1162-1255 |
2.25e-05 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 48.19 E-value: 2.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1162 GEKGTQLSGGQKQRIAIARALVRSPSVLLLDEATSALDTESE-KIVQEALDAAKQGRTCLVIAHRLSTI-QNSDVIAIVS 1239
Cdd:NF000106 139 GRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRnEVWDEVRSMVRDGATVLLTTQYMEEAeQLAHELTVID 218
|
90
....*....|....*.
gi 124244275 1240 EGKIVEKGTHDELIRK 1255
Cdd:NF000106 219 RGRVIADGKVDELKTK 234
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
416-593 |
2.59e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 48.95 E-value: 2.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 416 VLKGISLELKAGDKIALVGSSGCGKST----IVNLLQRFYDPTKGRVLIDGVDLREVNVHSLREQIGIVSQE---PVLfd 488
Cdd:TIGR00956 76 ILKPMDGLIKPGELTVVLGRPGSGCSTllktIASNTDGFHIGVEGVITYDGITPEEIKKHYRGDVVYNAETDvhfPHL-- 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 489 gTIYEN----IKM---GNEHATHDQVVEACKMANANDFIKRLPDGYGTRVGEKGVQ-LSGGQKQRIAIARALVKNPKILL 560
Cdd:TIGR00956 154 -TVGETldfaARCktpQNRPDGVSREEYAKHIADVYMATYGLSHTRNTKVGNDFVRgVSGGERKRVSIAEASLGGAKIQC 232
|
170 180 190
....*....|....*....|....*....|....
gi 124244275 561 LDEATSALDTEAEREVQGAL-DQAQAGRTTIIVA 593
Cdd:TIGR00956 233 WDNATRGLDSATALEFIRALkTSANILDTTPLVA 266
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18783 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
161-273 |
2.62e-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: 350056 [Multi-domain] Cd Length: 294 Bit Score: 47.51 E-value: 2.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 161 ILRQQIQWFDKQQTGNLTARLTDdLERVREGLG--------DKFALLVqmFAAFLagygvgFFYSWSMTLVMMGFAPLIV 232
Cdd:cd18783 85 LLSLPIDFFERTPAGVLTKHMQQ-IERIRQFLTgqlfgtllDATSLLV--FLPVL------FFYSPTLALVVLAFSALIA 155
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 124244275 233 LSGAKMSKSMATRTRVEQETYAVAGAIAEETFSSIRTVHSL 273
Cdd:cd18783 156 LIILAFLPPFRRRLQALYRAEGERQAFLVETVHGIRTVKSL 196
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
424-633 |
2.83e-05 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 48.86 E-value: 2.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 424 LKAGDKIALVGSSGCGKSTIVNLLQRFYDPTKGRVLIDGVDLReVNVHSLREQIGIVSQepvlFDGTiyENIKMGNEH-- 501
Cdd:TIGR01257 1962 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIL-TNISDVHQNMGYCPQ----FDAI--DDLLTGREHly 2034
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 502 ------ATHDQVVEacKMANANdfIKRLpdGYGTRVGEKGVQLSGGQKQRIAIARALVKNPKILLLDEATSALDTEAERE 575
Cdd:TIGR01257 2035 lyarlrGVPAEEIE--KVANWS--IQSL--GLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRM 2108
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 576 VQGAL-DQAQAGRTTIIVAHRLSTIRNV-DRIFVFKAGNIVESGSHEELMSKQGIFYDMT 633
Cdd:TIGR01257 2109 LWNTIvSIIREGRAVVLTSHSMEECEALcTRLAIMVKGAFQCLGTIQHLKSKFGDGYIVT 2168
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
1167-1238 |
2.94e-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: 2.94e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 124244275 1167 QLSGGQKQRIAIARAL----VRSPSVLLLDEATSALDTESEKIVQEAL-DAAKQGRTCLVIAHRLSTIQNSDVIAIV 1238
Cdd:cd03227 77 QLSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAIlEHLVKGAQVIVITHLPELAELADKLIHI 153
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
1063-1237 |
3.08e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 46.40 E-value: 3.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1063 GHSGCGKSTIMGLLERFYNQDKGMIMIdgdniRNLNISSLREQVC--IVSQEPTLFDCTIGENIcygtnrnVTYQEIVEA 1140
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGNIYY-----KNCNINNIAKPYCtyIGHNLGLKLEMTVFENL-------KFWSEIYNS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1141 AKM--ANIHNFILglpdgyDTHVGEKGTQLSGGQKQRIAIARALVRSPSVLLLDEATSALDTESEKIVQEALD-AAKQGR 1217
Cdd:PRK13541 101 AETlyAAIHYFKL------HDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLIVmKANSGG 174
|
170 180
....*....|....*....|
gi 124244275 1218 TCLVIAHRLSTIQNSDVIAI 1237
Cdd:PRK13541 175 IVLLSSHLESSIKSAQILQL 194
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1040-1216 |
4.98e-05 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 45.95 E-value: 4.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1040 RKDTKVLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGMIMIDGDNIRnlnisSLREQvcivsqeptlfdct 1119
Cdd:PRK13538 11 RDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIR-----RQRDE-------------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1120 IGENICY-----GTNRNVTYQEiveaakmaNIHnFILGLPDGYDT--------HVGEKGT------QLSGGQKQRIAIAR 1180
Cdd:PRK13538 72 YHQDLLYlghqpGIKTELTALE--------NLR-FYQRLHGPGDDealwealaQVGLAGFedvpvrQLSAGQQRRVALAR 142
|
170 180 190
....*....|....*....|....*....|....*..
gi 124244275 1181 ALVRSPSVLLLDEATSALDTESEKIVQEALDA-AKQG 1216
Cdd:PRK13538 143 LWLTRAPLWILDEPFTAIDKQGVARLEALLAQhAEQG 179
|
|
| ABC_6TM_AarD_CydD |
cd18584 |
Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH ... |
115-233 |
5.84e-05 |
|
Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH transporter, and a homolog AarD; The CydD protein, together with the CydC protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. Mutations in AarD, a homolog from Providencia stuartii, also show phenotypic characteristic consistent with a defect in the cytochrome d oxidase. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs).
Pssm-ID: 350028 [Multi-domain] Cd Length: 290 Bit Score: 46.63 E-value: 5.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 115 SEVVKYCIYYLVLGVLMFFTSYVQIACFESYAERLVHKLRQNYLKAILRQQIQWFDKQQTGNLTARLTDDLervrEGLGD 194
Cdd:cd18584 34 AALLPLLLLLLAALLLRALLAWAQERLAARAAARVKAELRRRLLARLLALGPALLRRQSSGELATLLTEGV----DALDG 109
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 124244275 195 KFAL-LVQMFAA------FLAgygVGFFYSWSMTLVMMGFAPLIVL 233
Cdd:cd18584 110 YFARyLPQLVLAaivpllILV---AVFPLDWVSALILLVTAPLIPL 152
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
1042-1260 |
7.34e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 46.93 E-value: 7.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1042 DTKVLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLERFYNQDKGMIMIDGDNIRNLnisSLREQVCIVSQE--------- 1112
Cdd:PRK10938 15 DTKTLQLPSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRL---SFEQLQKLVSDEwqrnntdml 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1113 -PTLFDC--TIGENICYGTNRNVTYQEIveAAKManihnfilglpdGYDTHVGEKGTQLSGGQKQRIAIARALVRSPSVL 1189
Cdd:PRK10938 92 sPGEDDTgrTTAEIIQDEVKDPARCEQL--AQQF------------GITALLDRRFKYLSTGETRKTLLCQALMSEPDLL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 124244275 1190 LLDEATSALDTESEKIVQEALDA-AKQGRTCLVIAHRLSTIQN-SDVIAIVSEGKIVEKGTHDELIRKSEIYQ 1260
Cdd:PRK10938 158 ILDEPFDGLDVASRQQLAELLASlHQSGITLVLVLNRFDEIPDfVQFAGVLADCTLAETGEREEILQQALVAQ 230
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1168-1243 |
7.43e-05 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 46.92 E-value: 7.43e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 124244275 1168 LSGGQKQRIAIARALVRSPSVLLLDEATSALDTESEKIVQEALDAAKQ-GRTCLVIAHRLSTIQN-SDVIAIVSEGKI 1243
Cdd:PRK10762 396 LSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAeGLSIILVSSEMPEVLGmSDRILVMHEGRI 473
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
1167-1257 |
9.05e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 46.78 E-value: 9.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1167 QLSGGQKQRIAIARALVRSPSVLLLDEATSALDTESEKIVQEALdaAKQGRTCLVIAHR---LSTIQnSDVIAIVSEGKI 1243
Cdd:PLN03073 344 TFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYL--LKWPKTFIVVSHArefLNTVV-TDILHLHGQKLV 420
|
90
....*....|....
gi 124244275 1244 VEKGTHDELIRKSE 1257
Cdd:PLN03073 421 TYKGDYDTFERTRE 434
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1167-1253 |
9.06e-05 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 46.33 E-value: 9.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1167 QLSGGQKQRIAIARALVRSPSVLLLDEATSALDTESEKIVQEALDAAKQ--GRTCLVIAHRLSTI-QNSDVIAIVSEGKI 1243
Cdd:PRK15093 158 ELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQnnNTTILLISHDLQMLsQWADKINVLYCGQT 237
|
90
....*....|
gi 124244275 1244 VEKGTHDELI 1253
Cdd:PRK15093 238 VETAPSKELV 247
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
413-605 |
1.02e-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: 45.68 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 413 DIHVLKGISLELKAGDKIALVGSSGCGKSTIVNllqrfydPTKGRVLIDGVDLREVNVHSLREQIGI--------VSQEP 484
Cdd:cd03271 7 RENNLKNIDVDIPLGVLTCVTGVSGSGKSSLIN-------DTLYPALARRLHLKKEQPGNHDRIEGLehidkvivIDQSP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 485 V-------------LFD-----------GTIY--ENIKMGNEHATHDQVVEackM--ANANDFIKRLPD----------- 525
Cdd:cd03271 80 IgrtprsnpatytgVFDeirelfcevckGKRYnrETLEVRYKGKSIADVLD---MtvEEALEFFENIPKiarklqtlcdv 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 526 --GYgTRVGEKGVQLSGGQKQRIAIARALVK---NPKILLLDEATSALDTEAEREVQGALDQ-AQAGRTTIIVAHRLSTI 599
Cdd:cd03271 157 glGY-IKLGQPATTLSGGEAQRIKLAKELSKrstGKTLYILDEPTTGLHFHDVKKLLEVLQRlVDKGNTVVVIEHNLDVI 235
|
....*.
gi 124244275 600 RNVDRI 605
Cdd:cd03271 236 KCADWI 241
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
537-594 |
1.26e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 46.39 E-value: 1.26e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 124244275 537 QLSGGQKQRIAIARALVKNPKILLLDEATSALDTEAEREVQGALdqAQAGRTTIIVAH 594
Cdd:PLN03073 344 TFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYL--LKWPKTFIVVSH 399
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
514-627 |
1.47e-04 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 45.50 E-value: 1.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 514 ANANDFIKRLpdGYGTRVGEKGVQLSGGQKQRIAIARALVKNPKILLLDEATSALDTEAEREVQGAL-DQAQAGRTTIIV 592
Cdd:NF000106 123 ARADELLERF--SLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVrSMVRDGATVLLT 200
|
90 100 110
....*....|....*....|....*....|....*.
gi 124244275 593 AHRLSTIRNV-DRIFVFKAGNIVESGSHEELMSKQG 627
Cdd:NF000106 201 TQYMEEAEQLaHELTVIDRGRVIADGKVDELKTKVG 236
|
|
| ABC_6TM_CyaB_HlyB_like |
cd18588 |
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ... |
161-329 |
1.49e-04 |
|
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunits of T1SS, such as CyaG and HlyB. 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). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. Additionally, CyaB is part of the three T1SS complex proteins for adenylate cyclase toxin CyaA, which is a primary virulence factor in Bordetella pertussis: CyaB (an ABC transporter) CyaD (a membrane fusion protein), and CyaE (an outer membrane protein).
Pssm-ID: 350032 [Multi-domain] Cd Length: 294 Bit Score: 45.18 E-value: 1.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 161 ILRQQIQWFDKQQTGNLTARLTDdLERVREGL-GDKFALLVQMFAA--FLAgygVGFFYSWSMTLVMMGFAPLIVLSGAK 237
Cdd:cd18588 85 LLRLPLSYFESRQVGDTVARVRE-LESIRQFLtGSALTLVLDLVFSvvFLA---VMFYYSPTLTLIVLASLPLYALLSLL 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 238 MSKSMatRTRVEQ--ETYAVAGAIAEETFSSIRTVHSL----NGHKRELDRFYNALEVGRQTGIVKYCYMGIGVGFSNLC 311
Cdd:cd18588 161 VTPIL--RRRLEEkfQRGAENQSFLVETVTGIETVKSLavepQFQRRWEELLARYVKASFKTANLSNLASQIVQLIQKLT 238
|
170
....*....|....*...
gi 124244275 312 MyssyALAFWYGSTLIIN 329
Cdd:cd18588 239 T----LAILWFGAYLVMD 252
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
120-233 |
1.85e-04 |
|
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: 44.80 E-value: 1.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 120 YCIYYLVLGVLMFFTSYVQIACFESYAERLVHKLRQNYLKAILRQQIQWFDKQQTGNLTARLTDDLERVREGLGDKFALL 199
Cdd:cd18580 41 LGVYAALLVLASVLLVLLRWLLFVLAGLRASRRLHDKLLRSVLRAPMSFFDTTPSGRILNRFSKDIGLIDEELPLALLDF 120
|
90 100 110
....*....|....*....|....*....|....
gi 124244275 200 VQMFAAFLAGYGVGFFYSWSMTLVMmgfAPLIVL 233
Cdd:cd18580 121 LQSLFSVLGSLIVIAIVSPYFLIVL---PPLLVV 151
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
707-964 |
1.99e-04 |
|
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: 44.78 E-value: 1.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 707 WFIGGIFGAFIFGSVTPVFALVYAEIFNVYSLPADQmqANVYFWCGMFVLMGITFFVGFFTSANCLGRCGESLTMKLRFE 786
Cdd:cd18540 3 LLILLIILMLLVALLDAVFPLLTKYAIDHFITPGTL--DGLTGFILLYLGLILIQALSVFLFIRLAGKIEMGVSYDLRKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 787 AFKNLLRQDIAFYDdlRHGTGKLCTRFATDApnvryvfTRLPVVLA--------SIVTICGALGIGFYYGWQLALILVVM 858
Cdd:cd18540 81 AFEHLQTLSFSYFD--KTPVGWIMARVTSDT-------QRLGEIISwglvdlvwGITYMIGILIVMLILNWKLALIVLAV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 859 VPLLVM-GGYFEMQM-RFGKQIRdtqlleeagKVASQAV----EHI---RTVHSLNRQEQfhfTYCEYLRepFNTNLKHA 929
Cdd:cd18540 152 VPVLAVvSIYFQKKIlKAYRKVR---------KINSRITgafnEGItgaKTTKTLVREEK---NLREFKE--LTEEMRRA 217
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 124244275 930 HTYGAVF-AFSQSLIFFM----YAAAFYLGSIFVNQQAMQ 964
Cdd:cd18540 218 SVRAARLsALFLPIVLFLgsiaTALVLWYGGILVLAGAIT 257
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
1152-1259 |
2.72e-04 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 45.45 E-value: 2.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1152 GLpdGYdTHVGEKGTQLSGGQKQRIAIARALVRSP---SVLLLDEATSALDTES----EKIVQEALDaakQGRTCLVIAH 1224
Cdd:PRK00349 818 GL--GY-IKLGQPATTLSGGEAQRVKLAKELSKRStgkTLYILDEPTTGLHFEDirklLEVLHRLVD---KGNTVVVIEH 891
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 124244275 1225 RLSTIQNSD-VIAIVSE-----GKIVEKGTHDELIRKSEIY 1259
Cdd:PRK00349 892 NLDVIKTADwIIDLGPEggdggGEIVATGTPEEVAKVEASY 932
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1166-1243 |
2.92e-04 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 44.92 E-value: 2.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1166 TQLSGGQKQRIAIARALVRSPSVLLLDEATSALDT----ESEKIVQEaldAAKQGRTCLVIAHRLSTIQN-SDVIAIVSE 1240
Cdd:PRK13549 404 ARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVgakyEIYKLINQ---LVQQGVAIIVISSELPEVLGlSDRVLVMHE 480
|
...
gi 124244275 1241 GKI 1243
Cdd:PRK13549 481 GKL 483
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1044-1251 |
3.46e-04 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 44.90 E-value: 3.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1044 KVLQGFTLDIKAGKTVALVGHSGCGKSTIMGLLerfYNQDK---GMIMIDGdniRNLNISSLREQV------C------- 1107
Cdd:PRK11288 267 GLREPISFSVRAGEIVGLFGLVGAGRSELMKLL---YGATRrtaGQVYLDG---KPIDIRSPRDAIragimlCpedrkae 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1108 -IVSQEptlfdcTIGENICYGTNRN-VTYQEIVEAAKMA-NIHNFILGL----PDGyDTHVGekgtQLSGGQKQRIAIAR 1180
Cdd:PRK11288 341 gIIPVH------SVADNINISARRHhLRAGCLINNRWEAeNADRFIRSLniktPSR-EQLIM----NLSGGNQQKAILGR 409
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124244275 1181 ALVRSPSVLLLDEATSALD--TESEkIVQEALDAAKQGRTCLVIAHRLSTIQN-SDVIAIVSEGKIVEKGTHDE 1251
Cdd:PRK11288 410 WLSEDMKVILLDEPTRGIDvgAKHE-IYNVIYELAAQGVAVLFVSSDLPEVLGvADRIVVMREGRIAGELAREQ 482
|
|
| APS_kinase |
pfam01583 |
Adenylylsulphate kinase; Enzyme that catalyzes the phosphorylation of adenylylsulphate to 3 ... |
1056-1098 |
4.12e-04 |
|
Adenylylsulphate kinase; Enzyme that catalyzes the phosphorylation of adenylylsulphate to 3'-phosphoadenylylsulfate. This domain contains an ATP binding P-loop motif.
Pssm-ID: 396247 [Multi-domain] Cd Length: 154 Bit Score: 42.30 E-value: 4.12e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 124244275 1056 GKTVALVGHSGCGKSTIMGLLER-FYNQDKGMIMIDGDNIR-NLN 1098
Cdd:pfam01583 2 GCTIWLTGLSGAGKSTIANALERkLFEQGRSVYVLDGDNVRhGLN 46
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
434-601 |
4.35e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 42.94 E-value: 4.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 434 GSSGCGKSTIVNLLQRFYDPTKGRVLIdgvdlREVNVHSLREQIG--IVSQEPVLFDGTIYENIKMGNE-HATHDQVVEA 510
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGNIYY-----KNCNINNIAKPYCtyIGHNLGLKLEMTVFENLKFWSEiYNSAETLYAA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 511 CKMANANDFIKrlpdgygtrvgEKGVQLSGGQKQRIAIARALVKNPKILLLDEATSALDTEAEREVQGALD-QAQAGRTT 589
Cdd:PRK13541 108 IHYFKLHDLLD-----------EKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLIVmKANSGGIV 176
|
170
....*....|..
gi 124244275 590 IIVAHRLSTIRN 601
Cdd:PRK13541 177 LLSSHLESSIKS 188
|
|
| ABC_6TM_VMR1_D2_like |
cd18604 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
117-240 |
4.54e-04 |
|
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; This group includes the six-transmembrane domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1, all of which are ABC transporters of the MRP (multidrug resistance-associated protein) subfamily (ABCC). Yeast ABCC (also termed MRP/CFTR) subfamily includes six members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, Vmr1p, and Yor1p), of which three members (Ycf1p, Bpt1P and Yor1p) are not included here. While Yor1p, an oligomycin resistance ABC transporter, 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. Ybt1p is originally identified as a bile acid transporter and regulates membrane fusion through Ca2+ transport modulation. Ybt1p also plays a part in ade2 pigment transport. Moreover, Ybt1p has been recently shown to translocate phosphatidylcholine from the outer leaflet of the vacuole to the inner leaflet for degradation and choline recycling. Vmr1p, a vacuolar membrane protein, participates in the export of numerous growth inhibitors from the cell, such as cycloheximide, 2,4-dinitrophenole, cadmium and other toxic metals. Nft1p is not well-characterized, but it is proposed to be regulate Ycf1p, which is involved in heavy metal detoxification.
Pssm-ID: 350048 [Multi-domain] Cd Length: 297 Bit Score: 43.61 E-value: 4.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 117 VVKYCIYYLVLGVLMFFTSYVQIACFESYAERLVHKLRQNYLKAILRQQIQWFDKQQTGNLTARLTDDLERVREGLGDKF 196
Cdd:cd18604 42 VLYYLGIYALISLLSVLLGTLRYLLFFFGSLRASRKLHERLLHSVLRAPLRWLDTTPVGRILNRFSKDIETIDSELADSL 121
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 124244275 197 ALLVQMFAAFLAGYGVGFFYSWsmtlVMMGFAPLIVLSGAKMSK 240
Cdd:cd18604 122 SSLLESTLSLLVILIAIVVVSP----AFLLPAVVLAALYVYIGR 161
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
778-963 |
5.06e-04 |
|
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: 43.70 E-value: 5.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 778 SLTMKLRFeaFKNLLRQDIAFYDdlRHGTGKLCTRFATDApNVRYVFTR--LPVVLASIVTICgALGIGFYYGWQLALIL 855
Cdd:cd18568 74 DLSLLSDF--YKHLLSLPLSFFA--SRKVGDIITRFQENQ-KIRRFLTRsaLTTILDLLMVFI-YLGLMFYYNLQLTLIV 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 856 VVMVPLLVMggyfeMQMRFGKQIR--DTQLLEEAGKVASQAVE---HIRTVHSLNRQEQFHFTYCEYLREPFNTNLKHAH 930
Cdd:cd18568 148 LAFIPLYVL-----LTLLSSPKLKrnSREIFQANAEQQSFLVEaltGIATIKALAAERPIRWRWENKFAKALNTRFRGQK 222
|
170 180 190
....*....|....*....|....*....|...
gi 124244275 931 TYGAVFAFSQSLIFFMYAAAFYLGSIFVNQQAM 963
Cdd:cd18568 223 LSIVLQLISSLINHLGTIAVLWYGAYLVISGQL 255
|
|
| ABC_6TM_CvaB_RaxB_like |
cd18567 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ... |
751-989 |
6.02e-04 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 secretion systems, CvaB and RaxB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the peptidase-containing ABC transporter subunit of T1SS (Type 1 secretion systems), such as Escherichia coli colicin V secretion/processing ATP-binding protein CvaB and putative ABC transporter RaxB. These ABC-transporter proteins carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion. RaxB is part of the T1SS RaxABC, which is responsible for the type 1-dependent secretion of the bacterial quorum-sensing molecule AvrXa21. Both CvaB and RaxB belong to a subgroup of T1SS ABC transporters that contain a C39 peptidase domain. T1SS are found in pathogenic Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium.
Pssm-ID: 350011 [Multi-domain] Cd Length: 294 Bit Score: 43.22 E-value: 6.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 751 CGMFVLMGITFFVGFFTSaNCLGRCGESLTMKLRFEAFKNLLRQDIAFYDdLRHgTGKLCTRFATDAPNVRYVFTRLPVV 830
Cdd:cd18567 46 IGFGLLLLLQALLSALRS-WLVLYLSTSLNLQWTSNLFRHLLRLPLSYFE-KRH-LGDIVSRFGSLDEIQQTLTTGFVEA 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 831 LASIVTICGALGIGFYYGWQLALIlvvmvPLLVMGGYFEMQMRFGKQIRD--TQLLEEAGKVASQAVEHIRTVHSL---N 905
Cdd:cd18567 123 LLDGLMAILTLVMMFLYSPKLALI-----VLAAVALYALLRLALYPPLRRatEEQIVASAKEQSHFLETIRGIQTIklfG 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 906 RQEQFHFTYCEYLREPFNTNLKHAHtYGAVFAFSQSLIF-FMYAAAFYLGSIFVNQQAMQpidvyrV--FFA-ISFCGQM 981
Cdd:cd18567 198 REAEREARWLNLLVDAINADIRLQR-LQILFSAANGLLFgLENILVIYLGALLVLDGEFT------VgmLFAfLAYKDQF 270
|
....*...
gi 124244275 982 IGNTTSFI 989
Cdd:cd18567 271 SSRASSLI 278
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
399-569 |
6.50e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 43.85 E-value: 6.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 399 ISFKDVHFRYPSRKdihVLKGISLELKAGDKIALVGSSGCGKSTIVNLL-----QRFY-DPTK-GRVLIDGVDLREVNVH 471
Cdd:PRK10938 261 IVLNNGVVSYNDRP---ILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLItgdhpQGYSnDLTLfGRRRGSGETIWDIKKH 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 472 slreqIGIVSQEPVL----------------FDGT-IYenikmgnehathdQVVEACKMANANDFIKRLpdGYGTRVGEK 534
Cdd:PRK10938 338 -----IGYVSSSLHLdyrvstsvrnvilsgfFDSIgIY-------------QAVSDRQQKLAQQWLDIL--GIDKRTADA 397
|
170 180 190
....*....|....*....|....*....|....*..
gi 124244275 535 GVQ-LSGGQkQRIA-IARALVKNPKILLLDEATSALD 569
Cdd:PRK10938 398 PFHsLSWGQ-QRLAlIVRALVKHPTLLILDEPLQGLD 433
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
1168-1241 |
8.93e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 43.66 E-value: 8.93e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124244275 1168 LSGGQKQRIAIARAL---VRSPSVLLLDEATSALDTES-EKIVQEALDAAKQGRTCLVIAHRLSTIQNSD-VIAIVSEG 1241
Cdd:PRK00635 810 LSGGEIQRLKLAYELlapSKKPTLYVLDEPTTGLHTHDiKALIYVLQSLTHQGHTVVIIEHNMHVVKVADyVLELGPEG 888
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
754-951 |
1.09e-03 |
|
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: 42.58 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 754 FVLMGITFFVGFFTSANC--LGRCGESLTMKLRFEAFKNLLRQDIAFYDdlRHGTGKLCTRFAtDAPNVR--YVFTRLPV 829
Cdd:cd18782 46 VVMLVAALLEAVLTALRTylFTDTANRIDLELGGTIIDHLLRLPLGFFD--KRPVGELSTRIS-ELDTIRgfLTGTALTT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 830 VLASIVTIcGALGIGFYYGWQLALILVVMVPLLVmGGYFEMQMRFGKQIRDTqlLEEAGKVASQAVEH---IRTVHSLNR 906
Cdd:cd18782 123 LLDVLFSV-IYIAVLFSYSPLLTLVVLATVPLQL-LLTFLFGPILRRQIRRR--AEASAKTQSYLVESltgIQTVKAQNA 198
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 124244275 907 QE----QFHFTYCEYLREPFNTNLKHAHTYGAVFAFSQ-SLIFFMYAAAF 951
Cdd:cd18782 199 ELkarwRWQNRYARSLGEGFKLTVLGTTSGSLSQFLNKlSSLLVLWVGAY 248
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
536-606 |
1.25e-03 |
|
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: 40.81 E-value: 1.25e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 124244275 536 VQLSGGQKQRIAIARAL----VKNPKILLLDEATSALDTEAEREVQGAL-DQAQAGRTTIIVAHRLSTIRNVDRIF 606
Cdd:cd03227 76 LQLSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAIlEHLVKGAQVIVITHLPELAELADKLI 151
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
538-678 |
1.33e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 43.28 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 538 LSGGQKQRIAIARAL---VKNPKILLLDEATSALDT-EAEREVQGALDQAQAGRTTIIVAHRLSTIRNVDRIFVF----- 608
Cdd:PRK00635 810 LSGGEIQRLKLAYELlapSKKPTLYVLDEPTTGLHThDIKALIYVLQSLTHQGHTVVIIEHNMHVVKVADYVLELgpegg 889
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 124244275 609 -KAGNIVESGSHEELMSKQgifydmTQAQVVRQQQQEAGKDIEDTISESAHSHLSRksstrsAISIATSIH 678
Cdd:PRK00635 890 nLGGYLLASCSPEELIHLH------TPTAKALRPYLSSPQELPYLPDPSPKPPVPA------DITIKNAYQ 948
|
|
| PRK13850 |
PRK13850 |
type IV secretion system protein VirD4; Provisional |
299-374 |
2.38e-03 |
|
type IV secretion system protein VirD4; Provisional
Pssm-ID: 237531 [Multi-domain] Cd Length: 670 Bit Score: 42.17 E-value: 2.38e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 124244275 299 CYMGIGVGFSNLCMYSSYALAFWYGSTLIIN--DPTFDRGLIFTVFFAVLSGSTSLGGALPHLASFGTARGAASTVLR 374
Cdd:PRK13850 28 LYVTFRHGFNGEAMMTFDVFAFWYETPLYLGyaTPVFYRGLAIVVSTSVVVLLSQLIVSLRNREHHGTARWAEEGEMR 105
|
|
| CysC |
COG0529 |
Adenylylsulfate kinase or related kinase [Inorganic ion transport and metabolism]; ... |
1056-1098 |
3.10e-03 |
|
Adenylylsulfate kinase or related kinase [Inorganic ion transport and metabolism]; Adenylylsulfate kinase or related kinase is part of the Pathway/BioSystem: Cysteine biosynthesis
Pssm-ID: 440295 [Multi-domain] Cd Length: 189 Bit Score: 40.07 E-value: 3.10e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 124244275 1056 GKTVALVGHSGCGKSTIMGLLE-RFYNQDKGMIMIDGDNIR-NLN 1098
Cdd:COG0529 16 GFVVWFTGLSGSGKSTLANALErRLFERGRHVYLLDGDNVRhGLN 60
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
1150-1253 |
3.53e-03 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 41.76 E-value: 3.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1150 ILGLPDGYDTHVGEKGTQ-LSGGQKQRIAIARALVRSPSVLLLDEATSALDTESE-KIVQealdaakqgrtCL--VIAHR 1225
Cdd:PLN03140 318 ILGLDICKDTIVGDEMIRgISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTyQIVK-----------CLqqIVHLT 386
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 124244275 1226 LSTIQNS------------DVIAIVSEGKIVEKGTHDELI 1253
Cdd:PLN03140 387 EATVLMSllqpapetfdlfDDIILLSEGQIVYQGPRDHIL 426
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1167-1212 |
5.35e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 40.87 E-value: 5.35e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 124244275 1167 QLSGGQKQRIAIARALVRSPSVLLLDEATSALDTESEKIVQEALDA 1212
Cdd:PRK11819 445 VLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVETLRALEEALLE 490
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
1161-1244 |
5.37e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 40.93 E-value: 5.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1161 VGEKGTQLSGGQKQRIAIARALVRSPSVLLLDEATSALDT----ESEKIVQEaldAAKQGRTCLVIAHRL-STIQNSDVI 1235
Cdd:NF040905 398 VFQKVGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVgakyEIYTIINE---LAAEGKGVIVISSELpELLGMCDRI 474
|
....*....
gi 124244275 1236 AIVSEGKIV 1244
Cdd:NF040905 475 YVMNEGRIT 483
|
|
| APSK |
cd02027 |
Adenosine 5'-phosphosulfate kinase (APSK) catalyzes the phosphorylation of adenosine 5 ... |
1058-1098 |
6.64e-03 |
|
Adenosine 5'-phosphosulfate kinase (APSK) catalyzes the phosphorylation of adenosine 5'-phosphosulfate to form 3'-phosphoadenosine 5'-phosphosulfate (PAPS). The end-product PAPS is a biologically "activated" sulfate form important for the assimilation of inorganic sulfate.
Pssm-ID: 238985 [Multi-domain] Cd Length: 149 Bit Score: 38.61 E-value: 6.64e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 124244275 1058 TVALVGHSGCGKSTIMGLLERfYNQDKGM--IMIDGDNIR-NLN 1098
Cdd:cd02027 1 VIWLTGLSGSGKSTIARALEE-KLFQRGRpvYVLDGDNVRhGLN 43
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1161-1210 |
7.10e-03 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 40.54 E-value: 7.10e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 124244275 1161 VGEKGTQLSGGQKQRIAIARALVRSPSVLLLDEATSALDTESEKIVQEAL 1210
Cdd:PRK10636 424 VTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEAL 473
|
|
| ABC_6TM_AarD_CydDC_like |
cd18561 |
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and ... |
146-324 |
8.04e-03 |
|
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and similar proteins; The CydD protein, together with the CydC protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. Mutations in AarD, a homolog from Providencia stuartii, also show phenotypic characteristic consistent with a defect in the cytochrome d oxidase. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs).
Pssm-ID: 350005 [Multi-domain] Cd Length: 289 Bit Score: 39.96 E-value: 8.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 146 AERLVHKLRQNYLKAILRQQIQWFDKQQTGNLTARLTDDLERVREGLGDkfaLLVQMFAAFLAGYGVG---FFYSWSMTL 222
Cdd:cd18561 64 AQRVKQHLRRRLFAKLLKLGPGYLEGERTGELQTTVVDGVEALEAYYGR---YLPQLLVALLGPLLILiylFFLDPLVAL 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 223 VMMGFAPLIVLSGAKMSKSMATRTRVEQETYAVAGAIAEETFSSIRTVHSLNGHKRELDRFYNALEVGRQTGIVKYCYMG 302
Cdd:cd18561 141 ILLVFALLIPLSPALWDRLAKDTGRRHWAAYGRLSAQFLDSLQGMTTLKAFGASKRRGNELAARAEDLRQATMKVLAVSL 220
|
170 180
....*....|....*....|..
gi 124244275 303 IGVGFSNLCMYSSYALAFWYGS 324
Cdd:cd18561 221 LSSGIMGLATALGTALALGVGA 242
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
1166-1254 |
8.52e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 40.39 E-value: 8.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1166 TQLSGGQKQRIAIARALVRS---PSVLLLDEATSALDTESEKIVQEALDA-AKQGRTCLVIAHRLSTIQNSD-VIAIVSE 1240
Cdd:COG0178 825 TTLSGGEAQRVKLASELSKRstgKTLYILDEPTTGLHFHDIRKLLEVLHRlVDKGNTVVVIEHNLDVIKTADwIIDLGPE 904
|
90
....*....|....*....
gi 124244275 1241 -----GKIVEKGTHDELIR 1254
Cdd:COG0178 905 ggdggGEIVAEGTPEEVAK 923
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
1168-1258 |
8.94e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 40.26 E-value: 8.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124244275 1168 LSGGQKQRIAIARALVRSPSVLLLDEATSALDTESEKIVQEALDAAKQgrTCLVIAH-R--LSTIQNSdVIAIVSEGKIV 1244
Cdd:PRK15064 439 LSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESIESLNMALEKYEG--TLIFVSHdRefVSSLATR-IIEITPDGVVD 515
|
90
....*....|....
gi 124244275 1245 EKGTHDELIRKSEI 1258
Cdd:PRK15064 516 FSGTYEEYLRSQGI 529
|
|
| PRK01889 |
PRK01889 |
GTPase RsgA; Reviewed |
424-447 |
9.15e-03 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234988 [Multi-domain] Cd Length: 356 Bit Score: 39.92 E-value: 9.15e-03
10 20
....*....|....*....|....
gi 124244275 424 LKAGDKIALVGSSGCGKSTIVNLL 447
Cdd:PRK01889 192 LSGGKTVALLGSSGVGKSTLVNAL 215
|
|
| |
