|
Name |
Accession |
Description |
Interval |
E-value |
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
36-612 |
1.57e-176 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 533.20 E-value: 1.57e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 36 LMTLGILASMINGATVPLMSLVLGEISDHLINGCLVQTnrtkyqncsqtqeklnedIIVLTLYYIGIGAAALIFGYVQIS 115
Cdd:COG1132 22 LLILALLLLLLSALLELLLPLLLGRIIDALLAGGDLSA------------------LLLLLLLLLGLALLRALLSYLQRY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 116 FWVITAARQTTRIRKQFFHSILAQDISWFDGSDICELNTRMTGDINKLCDGIGDKIPLMFQNISGFSIGLVISLIKSWKL 195
Cdd:COG1132 84 LLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDWRL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 196 SLVVLSTSPLIMASSALCSRMIISLTSKELDAYSKAGAVAEEALSSIQTVTAFGAQEKEIQRYTQHLKDAKDAGIKRATA 275
Cdd:COG1132 164 ALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAARL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 276 SKLSLGAVYFFMNGAYGLAFWYGTSLIFGGEPgyTIGTILAVFFSVIHSSYCIGSVAPHLETFTVARGAAFNIFQVIDKK 355
Cdd:COG1132 244 SALFFPLMELLGNLGLALVLLVGGLLVLSGSL--TVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEP 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 356 PNIDNFSTAGFVPEcIEGNIEFKNVSFSYPsrPSAKVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCIT 435
Cdd:COG1132 322 PEIPDPPGAVPLPP-VRGEIEFENVSFSYP--GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRIL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 436 VDENDIRAQNVRHYREQIGVVRQEPVLFGTTIGNNIKFGREGVGEKEMEQAAREANAYDFIMAFPKKFNTLVGEKGAQMS 515
Cdd:COG1132 399 IDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLS 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 516 GGQKQRIAIARALVRNPKILILDEATSALDTESESLVQTALEKASKGRTTIVVAHRLSTIRGADLIVTMKDGMVVEKGTH 595
Cdd:COG1132 479 GGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTH 558
|
570
....*....|....*..
gi 568980685 596 AELMAKQGLYYSLAMAQ 612
Cdd:COG1132 559 EELLARGGLYARLYRLQ 575
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
36-1238 |
1.16e-174 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 555.79 E-value: 1.16e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 36 LMTLGILASMINGATVPLMSLVLGEISDHLingclvqtnrtkyqncsqtqeKLNEDI--IVLTLYYIGIGAAALIFgyvq 113
Cdd:PTZ00265 61 LLGVSFVCATISGGTLPFFVSVFGVIMKNM---------------------NLGENVndIIFSLVLIGIFQFILSF---- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 114 ISFWVITAArqTTRIRK----QFFHSILAQDISWFDGSDICELNTRMTGDINKLCDGIGDKIPLMFQNISGFsIGLVI-S 188
Cdd:PTZ00265 116 ISSFCMDVV--TTKILKtlklEFLKSVFYQDGQFHDNNPGSKLTSDLDFYLEQVNAGIGTKFITIFTYASAF-LGLYIwS 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 189 LIKSWKLSLVVLSTSPLIMASSALCSRMIISLTSKELDAYSKAGAVAEEALSSIQTVTAFGAQEKEIQRYTQHLKDAKDA 268
Cdd:PTZ00265 193 LFKNARLTLCITCVFPLIYICGVICNKKVKINKKTSLLYNNNTMSIIEEALVGIRTVVSYCGEKTILKKFNLSEKLYSKY 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 269 GIKRATASKLSLGAVYFFMNGAYGLAFWYGTSLIFGG----EPG--YTIGTILAVFFSVIHSSYCIGSVAPHLETFTVAR 342
Cdd:PTZ00265 273 ILKANFMESLHIGMINGFILASYAFGFWYGTRIIISDlsnqQPNndFHGGSVISILLGVLISMFMLTIILPNITEYMKSL 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 343 GAAFNIFQVIDKKPNIDNFSTAGFVPECieGNIEFKNVSFSYPSRPSAKVLKGLNLKIKAGETVALVGPSGSGKSTTVQL 422
Cdd:PTZ00265 353 EATNSLYEIINRKPLVENNDDGKKLKDI--KKIQFKNVRFHYDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKL 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 423 LQRLYDPEDGCITV-DENDIRAQNVRHYREQIGVVRQEPVLFGTTIGNNIKFG--------------------------- 474
Cdd:PTZ00265 431 IERLYDPTEGDIIInDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKYSlyslkdlealsnyynedgndsqenknk 510
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 475 ------------------------------REGVGEKEMEQAAREANAYDFIMAFPKKFNTLVGEKGAQMSGGQKQRIAI 524
Cdd:PTZ00265 511 rnscrakcagdlndmsnttdsneliemrknYQTIKDSEVVDVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISI 590
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 525 ARALVRNPKILILDEATSALDTESESLVQTALE--KASKGRTTIVVAHRLSTIRGADLIVTM------------------ 584
Cdd:PTZ00265 591 ARAIIRNPKILILDEATSSLDNKSEYLVQKTINnlKGNENRITIIIAHRLSTIRYANTIFVLsnrergstvdvdiigedp 670
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 585 ------------KDG-----------------MVVEKGTHAELMA-KQGLYYSLAMAQDI-----------KKVD----- 618
Cdd:PTZ00265 671 tkdnkennnknnKDDnnnnnnnnnnkinnagsYIIEQGTHDALMKnKNGIYYTMINNQKVsskkssnndndKDSDmkssa 750
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 619 ----------EQMESRTCSTAGNASYGSLCDVNSAKAPCTDQLEEA-----VHHQKTSLP---EVSLLKIFKLSKSewpf 680
Cdd:PTZ00265 751 ykdsergydpDEMNGNSKHENESASNKKSCKMSDENASENNAGGKLpflrnLFKRKPKAPnnlRIVYREIFSYKKD---- 826
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 681 VVLGTLASALNGSVHPVFSIIFGKLV-TMFEDKNkatLKQDAELYSMMLVVLGIVALVTYLMQGLFYGRAEENLAMRLRH 759
Cdd:PTZ00265 827 VTIIALSILVAGGLYPVFALLYAKYVsTLFDFAN---LEANSNKYSLYILVIAIAMFISETLKNYYNNVIGEKVEKTMKR 903
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 760 SAFKAMLYQDMAWYDDKENNTGALTTTLAVDVAQIQGAATSRLGIVTQDVSNMSLSILISF----IYGWEMTLLILSFAP 835
Cdd:PTZ00265 904 RLFENILYQEISFFDQDKHAPGLLSAHINRDVHLLKTGLVNNIVIFTHFIVLFLVSMVMSFyfcpIVAAVLTGTYFIFMR 983
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 836 VLAVTGMI--------QTAAMAGFA---NRDKQALKRAGKIATEAVENIRTVVSLTRERAFEQMYEETLQTQHRNALKRA 904
Cdd:PTZ00265 984 VFAIRARLtankdvekKEINQPGTVfayNSDDEIFKDPSFLIQEAFYNMNTVIIYGLEDYFCNLIEKAIDYSNKGQKRKT 1063
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 905 HITGCCYAVSHAFVHFAHAAGFRFGAYLIQAGRMMPEG-MFIVFTAIAYGAMAiGETLVWAPEYSKAKAGASHLFALLKN 983
Cdd:PTZ00265 1064 LVNSMLWGFSQSAQLFINSFAYWFGSFLIRRGTILVDDfMKSLFTFLFTGSYA-GKLMSLKGDSENAKLSFEKYYPLIIR 1142
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 984 KPTINSCSQSG---EKPDTCEGNLEFREVSFVYPCRPEVPVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYD--- 1057
Cdd:PTZ00265 1143 KSNIDVRDNGGiriKNKNDIKGKIEIMDVNFRYISRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDlkn 1222
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1058 ----------------------------PMK-----------------------GQVLLDGVDVKELNVQWLRSQTAIVS 1086
Cdd:PTZ00265 1223 dhhivfknehtndmtneqdyqgdeeqnvGMKnvnefsltkeggsgedstvfknsGKILLDGVDICDYNLKDLRNLFSIVS 1302
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1087 QEPVLFNCSIAENIAYGDNSrmVPLEEIKEVADAANIHSFIEGLPRKYNTLVGLRGVQLSGGQKQRLAIARALLRKPKIL 1166
Cdd:PTZ00265 1303 QEPMLFNMSIYENIKFGKED--ATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKIL 1380
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1167 LLDEATSALDNESEKVVQQAL----DKArrGKTCLVVAHRLSTIQNADMIVVLQN----GS-IKEQGTHQELLRNGDTYF 1237
Cdd:PTZ00265 1381 LLDEATSSLDSNSEKLIEKTIvdikDKA--DKTIITIAHRIASIKRSDKIVVFNNpdrtGSfVQAHGTHEELLSVQDGVY 1458
|
.
gi 568980685 1238 K 1238
Cdd:PTZ00265 1459 K 1459
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
666-1243 |
1.84e-158 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 486.21 E-value: 1.84e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 666 SLLKIFKLSKSEWPFVVLGTLASALNGSVHPVFSIIFGKLV-TMFEDKNKATLKqdaeLYSMMLVVLGIVALVTYLMQGL 744
Cdd:COG1132 8 LLRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIdALLAGGDLSALL----LLLLLLLGLALLRALLSYLQRY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 745 FYGRAEENLAMRLRHSAFKAMLYQDMAWYDDkeNNTGALTTTLAVDVAQIQGAATSRLGIVTQDVSNMSLSILISFIYGW 824
Cdd:COG1132 84 LLARLAQRVVADLRRDLFEHLLRLPLSFFDR--RRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDW 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 825 EMTLLILSFAPVLAVTGMIQTAAMAGFANRDKQALKRAGKIATEAVENIRTVVSLTRERAFEQMYEETLQTQHRNALKRA 904
Cdd:COG1132 162 RLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 905 HITGCCYAVSHAFVHFAHAAGFRFGAYLIQAGRMMPeGMFIVFtaIAYGAMAIG--ETLVW-APEYSKAKAGASHLFALL 981
Cdd:COG1132 242 RLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTV-GDLVAF--ILYLLRLFGplRQLANvLNQLQRALASAERIFELL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 982 KNKPTINSCSQSGEKPDTcEGNLEFREVSFVYPcrPEVPVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKG 1061
Cdd:COG1132 319 DEPPEIPDPPGAVPLPPV-RGEIEFENVSFSYP--GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSG 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1062 QVLLDGVDVKELNVQWLRSQTAIVSQEPVLFNCSIAENIAYGDNSrmVPLEEIKEVADAANIHSFIEGLPRKYNTLVGLR 1141
Cdd:COG1132 396 RILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPD--ATDEEVEEAAKAAQAHEFIEALPDGYDTVVGER 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1142 GVQLSGGQKQRLAIARALLRKPKILLLDEATSALDNESEKVVQQALDKARRGKTCLVVAHRLSTIQNADMIVVLQNGSIK 1221
Cdd:COG1132 474 GVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIV 553
|
570 580
....*....|....*....|..
gi 568980685 1222 EQGTHQELLRNGDTYFKLVAAH 1243
Cdd:COG1132 554 EQGTHEELLARGGLYARLYRLQ 575
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
1005-1240 |
2.34e-144 |
|
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: 435.82 E-value: 2.34e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1005 EFREVSFVYPCRPEVPVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVKELNVQWLRSQTAI 1084
Cdd:cd03249 2 EFKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1085 VSQEPVLFNCSIAENIAYGDNSRmvPLEEIKEVADAANIHSFIEGLPRKYNTLVGLRGVQLSGGQKQRLAIARALLRKPK 1164
Cdd:cd03249 82 VSQEPVLFDGTIAENIRYGKPDA--TDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPK 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568980685 1165 ILLLDEATSALDNESEKVVQQALDKARRGKTCLVVAHRLSTIQNADMIVVLQNGSIKEQGTHQELLRNGDTYFKLV 1240
Cdd:cd03249 160 ILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLV 235
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
375-612 |
2.27e-141 |
|
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: 427.73 E-value: 2.27e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 375 IEFKNVSFSYPSRPSAKVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDIRAQNVRHYREQIG 454
Cdd:cd03249 1 IEFKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 455 VVRQEPVLFGTTIGNNIKFGREGVGEKEMEQAAREANAYDFIMAFPKKFNTLVGEKGAQMSGGQKQRIAIARALVRNPKI 534
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKI 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568980685 535 LILDEATSALDTESESLVQTALEKASKGRTTIVVAHRLSTIRGADLIVTMKDGMVVEKGTHAELMAKQGLYYSLAMAQ 612
Cdd:cd03249 161 LLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKAQ 238
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
96-612 |
5.00e-141 |
|
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: 445.05 E-value: 5.00e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 96 TLYYIGIGAAAL-----IFGYVQISFWVITAARQTTRIRKQFFHSILAQDISWFDGSDICELNTRMtGDINKLCDGIGDK 170
Cdd:COG2274 194 TLWVLAIGLLLAllfegLLRLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRF-RDVESIREFLTGS 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 171 IPLMFQNISGFSIGLVISLIKSWKLSLVVLSTSPLIMASSALCSRMIISLTSKELDAYSKAGAVAEEALSSIQTVTAFGA 250
Cdd:COG2274 273 LLTALLDLLFVLIFLIVLFFYSPPLALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGA 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 251 QEKEIQRYTQHLKDAKDAGIKRATASKLSLGAVYFFMNGAYGLAFWYGTSLIFGGEpgYTIGTILAvfFSVIhSSYCIGS 330
Cdd:COG2274 353 ESRFRRRWENLLAKYLNARFKLRRLSNLLSTLSGLLQQLATVALLWLGAYLVIDGQ--LTLGQLIA--FNIL-SGRFLAP 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 331 VAP---HLETFTVARGAAFNIFQVIDKKPNIDNFSTAGFVPEcIEGNIEFKNVSFSYPSRpSAKVLKGLNLKIKAGETVA 407
Cdd:COG2274 428 VAQligLLQRFQDAKIALERLDDILDLPPEREEGRSKLSLPR-LKGDIELENVSFRYPGD-SPPVLDNISLTIKPGERVA 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 408 LVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDIRAQNVRHYREQIGVVRQEPVLFGTTIGNNIKFGREGVGEKEMEQAA 487
Cdd:COG2274 506 IVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPDATDEEIIEAA 585
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 488 REANAYDFIMAFPKKFNTLVGEKGAQMSGGQKQRIAIARALVRNPKILILDEATSALDTESESLVQTALEKASKGRTTIV 567
Cdd:COG2274 586 RLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVII 665
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 568980685 568 VAHRLSTIRGADLIVTMKDGMVVEKGTHAELMAKQGLYYSLAMAQ 612
Cdd:COG2274 666 IAHRLSTIRLADRIIVLDKGRIVEDGTHEELLARKGLYAELVQQQ 710
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
86-608 |
2.94e-139 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 440.31 E-value: 2.94e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 86 EKLNEDIIVLTLYYIgigaAALIFGYVQISFWVITAARQTTRIRKQFFHSILAQDISWFDGSDICELNTRMTGDINKLCD 165
Cdd:TIGR00958 198 PALASAIFFMCLLSI----ASSVSAGLRGGSFNYTMARINLRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSR 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 166 GIGDKIPLMFQNIsGFSIGLVISLIK-SWKLSLVVLSTSPLIMASSALCSRMIISLTSKELDAYSKAGAVAEEALSSIQT 244
Cdd:TIGR00958 274 SLSLNVNVLLRNL-VMLLGLLGFMLWlSPRLTMVTLINLPLVFLAEKVFGKRYQLLSEELQEAVAKANQVAEEALSGMRT 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 245 VTAFGAQEKEIQRYTQHLKDAKDAGIKRATASKLSLGAVYFFMNGAYGLAFWYGTSLIFGGEpgYTIGTILAVF---FSV 321
Cdd:TIGR00958 353 VRSFAAEEGEASRFKEALEETLQLNKRKALAYAGYLWTTSVLGMLIQVLVLYYGGQLVLTGK--VSSGNLVSFLlyqEQL 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 322 IHSSYCIGSVAPHLETftvARGAAFNIFQVIDKKPNIDNfsTAGFVPECIEGNIEFKNVSFSYPSRPSAKVLKGLNLKIK 401
Cdd:TIGR00958 431 GEAVRVLSYVYSGMMQ---AVGASEKVFEYLDRKPNIPL--TGTLAPLNLEGLIEFQDVSFSYPNRPDVPVLKGLTFTLH 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 402 AGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDIRAQNVRHYREQIGVVRQEPVLFGTTIGNNIKFGREGVGEK 481
Cdd:TIGR00958 506 PGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTPDE 585
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 482 EMEQAAREANAYDFIMAFPKKFNTLVGEKGAQMSGGQKQRIAIARALVRNPKILILDEATSALDTESESLVQTAleKASK 561
Cdd:TIGR00958 586 EIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQES--RSRA 663
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 568980685 562 GRTTIVVAHRLSTIRGADLIVTMKDGMVVEKGTHAELMAKQGLYYSL 608
Cdd:TIGR00958 664 SRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQGCYKHL 710
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
667-1241 |
9.21e-128 |
|
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: 409.61 E-value: 9.21e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 667 LLKIFKLSKSEWPFVVLGTLASALNGSVHPVFS--IIfgklvtmfedkNKATLKQDAELysmmLVVLGIVALVTYLMQGL 744
Cdd:COG2274 147 FLRLLRRYRRLLLQVLLASLLINLLALATPLFTqvVI-----------DRVLPNQDLST----LWVLAIGLLLALLFEGL 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 745 FYG-------RAEENLAMRLRHSAFKAMLYQDMAWYDDKenNTGALTTTLAvDVAQIQGAATSRLGIVTQDVSNMSLSIL 817
Cdd:COG2274 212 LRLlrsylllRLGQRIDLRLSSRFFRHLLRLPLSFFESR--SVGDLASRFR-DVESIREFLTGSLLTALLDLLFVLIFLI 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 818 ISFIYGWEMTLLILSFAPVLAVTGMIqtaAMAGFANRDKQALKRAGKIAT---EAVENIRTVVSLTRERAFEQMYEETLQ 894
Cdd:COG2274 289 VLFFYSPPLALVVLLLIPLYVLLGLL---FQPRLRRLSREESEASAKRQSllvETLRGIETIKALGAESRFRRRWENLLA 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 895 TQHRNALKRAHITGCCYAVSHAFVHFAHAAGFRFGAYLIQAGRMMPeGMFIVFTAIAYGAMA----IGETLVwapEYSKA 970
Cdd:COG2274 366 KYLNARFKLRRLSNLLSTLSGLLQQLATVALLWLGAYLVIDGQLTL-GQLIAFNILSGRFLApvaqLIGLLQ---RFQDA 441
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 971 KAGASHLFALLkNKPTINSCSQSGEKPDTCEGNLEFREVSFVYPcRPEVPVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQ 1050
Cdd:COG2274 442 KIALERLDDIL-DLPPEREEGRSKLSLPRLKGDIELENVSFRYP-GDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLK 519
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1051 LLQRFYDPMKGQVLLDGVDVKELNVQWLRSQTAIVSQEPVLFNCSIAENIAYGDNSrmVPLEEIKEVADAANIHSFIEGL 1130
Cdd:COG2274 520 LLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPD--ATDEEIIEAARLAGLHDFIEAL 597
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1131 PRKYNTLVGLRGVQLSGGQKQRLAIARALLRKPKILLLDEATSALDNESEKVVQQALDKARRGKTCLVVAHRLSTIQNAD 1210
Cdd:COG2274 598 PMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLAD 677
|
570 580 590
....*....|....*....|....*....|.
gi 568980685 1211 MIVVLQNGSIKEQGTHQELLRNGDTYFKLVA 1241
Cdd:COG2274 678 RIIVLDKGRIVEDGTHEELLARKGLYAELVQ 708
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
88-612 |
3.17e-126 |
|
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: 401.00 E-value: 3.17e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 88 LNEDIIVLTLYYIGIGAAALIFGY-VQISFWVIT--AARQTTRIRKQFFHSILAQDISWFDGSDICELNTRMTGDINKLC 164
Cdd:TIGR02204 50 SKDSSGLLNRYFAFLLVVALVLALgTAARFYLVTwlGERVVADIRRAVFAHLISLSPSFFDKNRSGEVVSRLTTDTTLLQ 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 165 DGIGDKIPLMFQNISGFSIGLVISLIKSWKLSLVVLSTSPLIMASSALCSRMIISLTSKELDAYSKAGAVAEEALSSIQT 244
Cdd:TIGR02204 130 SVIGSSLSMALRNALMCIGGLIMMFITSPKLTSLVLLAVPLVLLPILLFGRRVRKLSRESQDRIADAGSYAGETLGAIRT 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 245 VTAFGAQEKEIQRYTQHLKDAKDAGIKRATASKLSLGAVYFFMNGAYGLAFWYGTSLIFGGEpgYTIGTILA-VFFSVIH 323
Cdd:TIGR02204 210 VQAFGHEDAERSRFGGAVEKAYEAARQRIRTRALLTAIVIVLVFGAIVGVLWVGAHDVIAGK--MSAGTLGQfVFYAVMV 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 324 SSyCIGSVAPHLETFTVARGAAFNIFQVIDKKPNIDNFSTAGFVPECIEGNIEFKNVSFSYPSRPSAKVLKGLNLKIKAG 403
Cdd:TIGR02204 288 AG-SIGTLSEVWGELQRAAGAAERLIELLQAEPDIKAPAHPKTLPVPLRGEIEFEQVNFAYPARPDQPALDGLNLTVRPG 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 404 ETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDIRAQNVRHYREQIGVVRQEPVLFGTTIGNNIKFGREGVGEKEM 483
Cdd:TIGR02204 367 ETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDLRQLDPAELRARMALVPQDPVLFAASVMENIRYGRPDATDEEV 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 484 EQAAREANAYDFIMAFPKKFNTLVGEKGAQMSGGQKQRIAIARALVRNPKILILDEATSALDTESESLVQTALEKASKGR 563
Cdd:TIGR02204 447 EAAARAAHAHEFISALPEGYDTYLGERGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDAESEQLVQQALETLMKGR 526
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 568980685 564 TTIVVAHRLSTIRGADLIVTMKDGMVVEKGTHAELMAKQGLYYSLAMAQ 612
Cdd:TIGR02204 527 TTLIIAHRLATVLKADRIVVMDQGRIVAQGTHAELIAKGGLYARLARLQ 575
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
671-987 |
3.39e-121 |
|
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: 377.56 E-value: 3.39e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 671 FKLSKSEWPFVVLGTLASALNGSVHPVFSIIFGKLVTMFEDKNKATLKQDAELYSMMLVVLGIVALVTYLMQGLFYGRAE 750
Cdd:cd18578 1 LKLNKPEWPLLLLGLIGAIIAGAVFPVFAILFSKLISVFSLPDDDELRSEANFWALMFLVLAIVAGIAYFLQGYLFGIAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 751 ENLAMRLRHSAFKAMLYQDMAWYDDKENNTGALTTTLAVDVAQIQGAATSRLGIVTQDVSNMSLSILISFIYGWEMTLLI 830
Cdd:cd18578 81 ERLTRRLRKLAFRAILRQDIAWFDDPENSTGALTSRLSTDASDVRGLVGDRLGLILQAIVTLVAGLIIAFVYGWKLALVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 831 LSFAPVLAVTGMIQTAAMAGFANRDKQALKRAGKIATEAVENIRTVVSLTRERAFEQMYEETLQTQHRNALKRAHITGCC 910
Cdd:cd18578 161 LATVPLLLLAGYLRMRLLSGFEEKNKKAYEESSKIASEAVSNIRTVASLTLEDYFLEKYEEALEEPLKKGLRRALISGLG 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568980685 911 YAVSHAFVHFAHAAGFRFGAYLIQAGRMMPEGMFIVFTAIAYGAMAIGETLVWAPEYSKAKAGASHLFALLKNKPTI 987
Cdd:cd18578 241 FGLSQSLTFFAYALAFWYGGRLVANGEYTFEQFFIVFMALIFGAQSAGQAFSFAPDIAKAKAAAARIFRLLDRKPEI 317
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
724-1241 |
9.13e-118 |
|
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: 378.27 E-value: 9.13e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 724 YSMMLVVLGIVALVTYlMQGLFYGRAEENLAMRLRHSAFKAMLYQDMAWYDdkENNTGALTTTLAVDVAQIQGAATSRLG 803
Cdd:TIGR02204 61 FAFLLVVALVLALGTA-ARFYLVTWLGERVVADIRRAVFAHLISLSPSFFD--KNRSGEVVSRLTTDTTLLQSVIGSSLS 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 804 IVTQDVSNMSLSILISFIYGWEMTLLILSFAPVLAvtgmiqtAAMAGFAnRDKQALKR--------AGKIATEAVENIRT 875
Cdd:TIGR02204 138 MALRNALMCIGGLIMMFITSPKLTSLVLLAVPLVL-------LPILLFG-RRVRKLSResqdriadAGSYAGETLGAIRT 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 876 VVSLTRERAFEQMYEETLQTQHRNALKRAHITGCCYAVSHAFVHFAHAAGFRFGAYLIQAGRMMPE--GMFIVFTAIAYG 953
Cdd:TIGR02204 210 VQAFGHEDAERSRFGGAVEKAYEAARQRIRTRALLTAIVIVLVFGAIVGVLWVGAHDVIAGKMSAGtlGQFVFYAVMVAG 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 954 AM-AIGEtlVWApEYSKAKAGASHLFALLKNKPTINSCSQSGEKPDTCEGNLEFREVSFVYPCRPEVPVLQNMSLSIEKG 1032
Cdd:TIGR02204 290 SIgTLSE--VWG-ELQRAAGAAERLIELLQAEPDIKAPAHPKTLPVPLRGEIEFEQVNFAYPARPDQPALDGLNLTVRPG 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1033 KTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVKELNVQWLRSQTAIVSQEPVLFNCSIAENIAYG--DNSRmvp 1110
Cdd:TIGR02204 367 ETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDLRQLDPAELRARMALVPQDPVLFAASVMENIRYGrpDATD--- 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1111 lEEIKEVADAANIHSFIEGLPRKYNTLVGLRGVQLSGGQKQRLAIARALLRKPKILLLDEATSALDNESEKVVQQALDKA 1190
Cdd:TIGR02204 444 -EEVEAAARAAHAHEFISALPEGYDTYLGERGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDAESEQLVQQALETL 522
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 568980685 1191 RRGKTCLVVAHRLSTIQNADMIVVLQNGSIKEQGTHQELLRNGDTYFKLVA 1241
Cdd:TIGR02204 523 MKGRTTLIIAHRLATVLKADRIVVMDQGRIVAQGTHAELIAKGGLYARLAR 573
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
667-1240 |
3.34e-115 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 375.98 E-value: 3.34e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 667 LLKIFKLSKSEWPFVVLGTL---ASALNGSVHPVFSiifGKLV-TMFEDKNKATLKQDaeLYSMMLvvLGIVALVTYLMQ 742
Cdd:TIGR00958 149 LFRLLGLSGRDWPWLISAFVfltLSSLGEMFIPFYT---GRVIdTLGGDKGPPALASA--IFFMCL--LSIASSVSAGLR 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 743 GLFYGRAEENLAMRLRHSAFKAMLYQDMAWYDdkENNTGALTTTLAVDVAQIQGAATSRLGIVTQDVSnMSLSILISFIY 822
Cdd:TIGR00958 222 GGSFNYTMARINLRIREDLFRSLLRQDLGFFD--ENKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLV-MLLGLLGFMLW 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 823 G-WEMTLLILSFAPVLAVTGMIQTAAMAGFANRDKQALKRAGKIATEAVENIRTVVSLTRE----RAFEQMYEETLQTQH 897
Cdd:TIGR00958 299 LsPRLTMVTLINLPLVFLAEKVFGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFAAEegeaSRFKEALEETLQLNK 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 898 RNALKRAHITgccyAVSHAFVHFAHAAGFRFGAYLIQAGRMMPEGM--FIVFTaiaygaMAIGETL-----VWaPEYSKA 970
Cdd:TIGR00958 379 RKALAYAGYL----WTTSVLGMLIQVLVLYYGGQLVLTGKVSSGNLvsFLLYQ------EQLGEAVrvlsyVY-SGMMQA 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 971 KAGASHLFALLKNKPtinSCSQSGE-KPDTCEGNLEFREVSFVYPCRPEVPVLQNMSLSIEKGKTVAFVGSSGCGKSTCV 1049
Cdd:TIGR00958 448 VGASEKVFEYLDRKP---NIPLTGTlAPLNLEGLIEFQDVSFSYPNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVA 524
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1050 QLLQRFYDPMKGQVLLDGVDVKELNVQWLRSQTAIVSQEPVLFNCSIAENIAYGDNSrmVPLEEIKEVADAANIHSFIEG 1129
Cdd:TIGR00958 525 ALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTD--TPDEEIMAAAKAANAHDFIME 602
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1130 LPRKYNTLVGLRGVQLSGGQKQRLAIARALLRKPKILLLDEATSALDNESEKVVQQalDKARRGKTCLVVAHRLSTIQNA 1209
Cdd:TIGR00958 603 FPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQE--SRSRASRTVLLIAHRLSTVERA 680
|
570 580 590
....*....|....*....|....*....|.
gi 568980685 1210 DMIVVLQNGSIKEQGTHQELLRNGDTYFKLV 1240
Cdd:TIGR00958 681 DQILVLKKGSVVEMGTHKQLMEDQGCYKHLV 711
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
36-608 |
3.12e-114 |
|
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: 368.66 E-value: 3.12e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 36 LMTLGILASMINGATVPLMSLVLGEISDHLINGclvqTNRTKyqncsqtqeklnedIIVLTLYYIGIGAAALIFGYVQIS 115
Cdd:TIGR02203 15 GLVLAGVAMILVAATESTLAALLKPLLDDGFGG----RDRSV--------------LWWVPLVVIGLAVLRGICSFVSTY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 116 F--WVitaARQTTR-IRKQFFHSILAQDISWFDGSDICELNTRMTGDINKLCDGIGDKIPLMFQNiSGFSIGLVISLI-K 191
Cdd:TIGR02203 77 LlsWV---SNKVVRdIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLVRE-TLTVIGLFIVLLyY 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 192 SWKLSLVVLSTSPLIMASSALCSRMIISLTSKELDAYSKAGAVAEEALSSIQTVTAFGAQEKEIQRYTQHLKDAKDAGIK 271
Cdd:TIGR02203 153 SWQLTLIVVVMLPVLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFDAVSNRNRRLAMK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 272 RATASKLSLGAVYFFmnGAYGLAFWYGTSLIFGGEPGYTIGTILAVFFSVIHSSYCIGSVAPHLETFTVARGAAFNIFQV 351
Cdd:TIGR02203 233 MTSAGSISSPITQLI--ASLALAVVLFIALFQAQAGSLTAGDFTAFITAMIALIRPLKSLTNVNAPMQRGLAAAESLFTL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 352 IDKKPNIDnfsTAGFVPECIEGNIEFKNVSFSYPSRpSAKVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPED 431
Cdd:TIGR02203 311 LDSPPEKD---TGTRAIERARGDVEFRNVTFRYPGR-DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDS 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 432 GCITVDENDIRAQNVRHYREQIGVVRQEPVLFGTTIGNNIKFGR-EGVGEKEMEQAAREANAYDFIMAFPKKFNTLVGEK 510
Cdd:TIGR02203 387 GQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRtEQADRAEIERALAAAYAQDFVDKLPLGLDTPIGEN 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 511 GAQMSGGQKQRIAIARALVRNPKILILDEATSALDTESESLVQTALEKASKGRTTIVVAHRLSTIRGADLIVTMKDGMVV 590
Cdd:TIGR02203 467 GVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIV 546
|
570
....*....|....*...
gi 568980685 591 EKGTHAELMAKQGLYYSL 608
Cdd:TIGR02203 547 ERGTHNELLARNGLYAQL 564
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
37-348 |
7.51e-113 |
|
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: 354.86 E-value: 7.51e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 37 MTLGILASMINGATVPLMSLVLGEISDHLINgclvqtnrtkYQNCSQTQEKLNEDIIVLTLYYIGIGAAALIFGYVQISF 116
Cdd:cd18577 1 LIIGLLAAIAAGAALPLMTIVFGDLFDAFTD----------FGSGESSPDEFLDDVNKYALYFVYLGIGSFVLSYIQTAC 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 117 WVITAARQTTRIRKQFFHSILAQDISWFDGSDICELNTRMTGDINKLCDGIGDKIPLMFQNISGFSIGLVISLIKSWKLS 196
Cdd:cd18577 71 WTITGERQARRIRKRYLKALLRQDIAWFDKNGAGELTSRLTSDTNLIQDGIGEKLGLLIQSLSTFIAGFIIAFIYSWKLT 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 197 LVVLSTSPLIMASSALCSRMIISLTSKELDAYSKAGAVAEEALSSIQTVTAFGAQEKEIQRYTQHLKDAKDAGIKRATAS 276
Cdd:cd18577 151 LVLLATLPLIAIVGGIMGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKALEKARKAGIKKGLVS 230
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568980685 277 KLSLGAVYFFMNGAYGLAFWYGTSLIFGGEpgYTIGTILAVFFSVIHSSYCIGSVAPHLETFTVARGAAFNI 348
Cdd:cd18577 231 GLGLGLLFFIIFAMYALAFWYGSRLVRDGE--ISPGDVLTVFFAVLIGAFSLGQIAPNLQAFAKARAAAAKI 300
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
226-612 |
4.33e-110 |
|
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: 358.36 E-value: 4.33e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 226 DAYSKAGAVAEEALSSIQTVTAFGAQEKEIQRYTQHLKDAKDAGIKrataSKLSLGAVYF----FMNGAYGLAFWYGTSL 301
Cdd:COG5265 212 EADSEANTRAVDSLLNYETVKYFGNEAREARRYDEALARYERAAVK----SQTSLALLNFgqalIIALGLTAMMLMAAQG 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 302 IFGGEpgYTIGTILAVffsvihSSYCIGSVAPhLETFTVA----RGAAFNI---FQVIDKKPNIDNFSTAGFVPeCIEGN 374
Cdd:COG5265 288 VVAGT--MTVGDFVLV------NAYLIQLYIP-LNFLGFVyreiRQALADMermFDLLDQPPEVADAPDAPPLV-VGGGE 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 375 IEFKNVSFSY-PSRPsakVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDIRAQNVRHYREQI 453
Cdd:COG5265 358 VRFENVSFGYdPERP---ILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAI 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 454 GVVRQEPVLFGTTIGNNIKFGREGVGEKEMEQAAREANAYDFIMAFPKKFNTLVGEKGAQMSGGQKQRIAIARALVRNPK 533
Cdd:COG5265 435 GIVPQDTVLFNDTIAYNIAYGRPDASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPP 514
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568980685 534 ILILDEATSALDTESESLVQTALEKASKGRTTIVVAHRLSTIRGADLIVTMKDGMVVEKGTHAELMAKQGLYYSLAMAQ 612
Cdd:COG5265 515 ILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLYAQMWARQ 593
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
375-608 |
5.58e-110 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 344.21 E-value: 5.58e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 375 IEFKNVSFSYPSRPSAkVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDIRAQNVRHYREQIG 454
Cdd:cd03251 1 VEFKNVTFRYPGDGPP-VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 455 VVRQEPVLFGTTIGNNIKFGREGVGEKEMEQAAREANAYDFIMAFPKKFNTLVGEKGAQMSGGQKQRIAIARALVRNPKI 534
Cdd:cd03251 80 LVSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568980685 535 LILDEATSALDTESESLVQTALEKASKGRTTIVVAHRLSTIRGADLIVTMKDGMVVEKGTHAELMAKQGLYYSL 608
Cdd:cd03251 160 LILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKL 233
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
375-612 |
3.19e-108 |
|
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: 339.59 E-value: 3.19e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 375 IEFKNVSFSYPsrPSAKVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDIRAQNVRHYREQIG 454
Cdd:cd03253 1 IEFENVTFAYD--PGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 455 VVRQEPVLFGTTIGNNIKFGREGVGEKEMEQAAREANAYDFIMAFPKKFNTLVGEKGAQMSGGQKQRIAIARALVRNPKI 534
Cdd:cd03253 79 VVPQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPI 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568980685 535 LILDEATSALDTESESLVQTALEKASKGRTTIVVAHRLSTIRGADLIVTMKDGMVVEKGTHAELMAKQGLYYSLAMAQ 612
Cdd:cd03253 159 LLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMWKAQ 236
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
675-1233 |
3.63e-108 |
|
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: 352.10 E-value: 3.63e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 675 KSEWPFVVLGTLASALNGSVHPVFSIIFGKLVtmfedkNKATLKQDAE-LYSMMLVVLGIVAL--VTYLMQGLFYGRAEE 751
Cdd:TIGR02203 10 RPYKAGLVLAGVAMILVAATESTLAALLKPLL------DDGFGGRDRSvLWWVPLVVIGLAVLrgICSFVSTYLLSWVSN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 752 NLAMRLRHSAFKAMLYQDMAWYDdkENNTGALTTTLAVDVAQIQGAATSRLGIVTQDVSNMSLSILISFIYGWEMTLLIL 831
Cdd:TIGR02203 84 KVVRDIRVRMFEKLLGLPVSFFD--RQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIVLLYYSWQLTLIVV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 832 SFAPVLAVTGMIQTAAMAGFANRDKQALKRAGKIATEAVENIRTVVSLTRERAFEQMYEETLQTQHRNALKRAHITGCCY 911
Cdd:TIGR02203 162 VMLPVLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFDAVSNRNRRLAMKMTSAGSISS 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 912 AVSHAFVHFAHAAGFRFGAYLIQAGRMMPEGMFIVFTAIAYGAMAIGETLVWAPEYSKAKAGASHLFALLKNKPTInscs 991
Cdd:TIGR02203 242 PITQLIASLALAVVLFIALFQAQAGSLTAGDFTAFITAMIALIRPLKSLTNVNAPMQRGLAAAESLFTLLDSPPEK---- 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 992 QSGEKP-DTCEGNLEFREVSFVYPCRpEVPVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDV 1070
Cdd:TIGR02203 318 DTGTRAiERARGDVEFRNVTFRYPGR-DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDL 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1071 KELNVQWLRSQTAIVSQEPVLFNCSIAENIAYGDnSRMVPLEEIKEVADAANIHSFIEGLPRKYNTLVGLRGVQLSGGQK 1150
Cdd:TIGR02203 397 ADYTLASLRRQVALVSQDVVLFNDTIANNIAYGR-TEQADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQR 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1151 QRLAIARALLRKPKILLLDEATSALDNESEKVVQQALDKARRGKTCLVVAHRLSTIQNADMIVVLQNGSIKEQGTHQELL 1230
Cdd:TIGR02203 476 QRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHNELL 555
|
....
gi 568980685 1231 -RNG 1233
Cdd:TIGR02203 556 aRNG 559
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
1004-1239 |
2.63e-105 |
|
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: 331.89 E-value: 2.63e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1004 LEFREVSFVYPCRPEvPVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVKELNVQWLRSQTA 1083
Cdd:cd03251 1 VEFKNVTFRYPGDGP-PVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1084 IVSQEPVLFNCSIAENIAYGDnsRMVPLEEIKEVADAANIHSFIEGLPRKYNTLVGLRGVQLSGGQKQRLAIARALLRKP 1163
Cdd:cd03251 80 LVSQDVFLFNDTVAENIAYGR--PGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568980685 1164 KILLLDEATSALDNESEKVVQQALDKARRGKTCLVVAHRLSTIQNADMIVVLQNGSIKEQGTHQELLRNGDTYFKL 1239
Cdd:cd03251 158 PILILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKL 233
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
976-1239 |
4.78e-101 |
|
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: 334.10 E-value: 4.78e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 976 HLFALLKNKPTINscsqsgEKPD-----TCEGNLEFREVSFVYpcRPEVPVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQ 1050
Cdd:COG5265 331 RMFDLLDQPPEVA------DAPDapplvVGGGEVRFENVSFGY--DPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLAR 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1051 LLQRFYDPMKGQVLLDGVDVKELNVQWLRSQTAIVSQEPVLFNCSIAENIAYG--DNSRmvplEEIKEVADAANIHSFIE 1128
Cdd:COG5265 403 LLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAYGrpDASE----EEVEAAARAAQIHDFIE 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1129 GLPRKYNTLVGLRGVQLSGGQKQRLAIARALLRKPKILLLDEATSALDNESEKVVQQALDKARRGKTCLVVAHRLSTIQN 1208
Cdd:COG5265 479 SLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVD 558
|
250 260 270
....*....|....*....|....*....|.
gi 568980685 1209 ADMIVVLQNGSIKEQGTHQELLRNGDTYFKL 1239
Cdd:COG5265 559 ADEILVLEAGRIVERGTHAELLAQGGLYAQM 589
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
1004-1239 |
6.88e-99 |
|
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: 314.55 E-value: 6.88e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1004 LEFREVSFVYPcrPEVPVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVKELNVQWLRSQTA 1083
Cdd:cd03253 1 IEFENVTFAYD--PGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1084 IVSQEPVLFNCSIAENIAYGDNSrmVPLEEIKEVADAANIHSFIEGLPRKYNTLVGLRGVQLSGGQKQRLAIARALLRKP 1163
Cdd:cd03253 79 VVPQDTVLFNDTIGYNIRYGRPD--ATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568980685 1164 KILLLDEATSALDNESEKVVQQALDKARRGKTCLVVAHRLSTIQNADMIVVLQNGSIKEQGTHQELLRNGDTYFKL 1239
Cdd:cd03253 157 PILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEM 232
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
373-603 |
3.09e-98 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 312.24 E-value: 3.09e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 373 GNIEFKNVSFSYpsRPSAKVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDIRAQNVRHYREQ 452
Cdd:cd03254 1 GEIEFENVNFSY--DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 453 IGVVRQEPVLFGTTIGNNIKFGREGVGEKEMEQAAREANAYDFIMAFPKKFNTLVGEKGAQMSGGQKQRIAIARALVRNP 532
Cdd:cd03254 79 IGVVLQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568980685 533 KILILDEATSALDTESESLVQTALEKASKGRTTIVVAHRLSTIRGADLIVTMKDGMVVEKGTHAELMAKQG 603
Cdd:cd03254 159 KILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
37-603 |
2.20e-97 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 322.48 E-value: 2.20e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 37 MTLGILASMINGATVPLMSLVLGEISDHLINGclvqtnrtkyqncsqtqeklNEDIIVLTLYYIGIGAAAL---IFGYVQ 113
Cdd:COG4988 19 LALAVLLGLLSGLLIIAQAWLLASLLAGLIIG--------------------GAPLSALLPLLGLLLAVLLlraLLAWLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 114 ISFWVITAARQTTRIRKQFFHSILAQDISWFDGSDICELNTRMTGDINKLCDGIGDKIPLMFQN-ISGFSIGLVISLIkS 192
Cdd:COG4988 79 ERAAFRAAARVKRRLRRRLLEKLLALGPAWLRGKSTGELATLLTEGVEALDGYFARYLPQLFLAaLVPLLILVAVFPL-D 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 193 WKLSLVVLSTSPLIMASsalcsrMII------SLTSKELDAYSKAGAVAEEALSSIQTVTAFGAQEkeiqRYTQHLKDAK 266
Cdd:COG4988 158 WLSGLILLVTAPLIPLF------MILvgkgaaKASRRQWRALARLSGHFLDRLRGLTTLKLFGRAK----AEAERIAEAS 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 267 DAgIKRATASKL-----SLGAVYFFMNGAYGLAFWY-GTSLIFGG---EPGYTIgTILAV-FFsvihssycigsvAP--H 334
Cdd:COG4988 228 ED-FRKRTMKVLrvaflSSAVLEFFASLSIALVAVYiGFRLLGGSltlFAALFV-LLLAPeFF------------LPlrD 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 335 LETF----TVARGAAFNIFQVIDKKPNIDNFSTAGfVPECIEGNIEFKNVSFSYPSRPsaKVLKGLNLKIKAGETVALVG 410
Cdd:COG4988 294 LGSFyharANGIAAAEKIFALLDAPEPAAPAGTAP-LPAAGPPSIELEDVSFSYPGGR--PALDGLSLTIPPGERVALVG 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 411 PSGSGKSTTVQLLQRLYDPEDGCITVDENDIRAQNVRHYREQIGVVRQEPVLFGTTIGNNIKFGREGVGEKEMEQAAREA 490
Cdd:COG4988 371 PSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPDASDEELEAALEAA 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 491 NAYDFIMAFPKKFNTLVGEKGAQMSGGQKQRIAIARALVRNPKILILDEATSALDTESESLVQTALEKASKGRTTIVVAH 570
Cdd:COG4988 451 GLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITH 530
|
570 580 590
....*....|....*....|....*....|...
gi 568980685 571 RLSTIRGADLIVTMKDGMVVEKGTHAELMAKQG 603
Cdd:COG4988 531 RLALLAQADRILVLDDGRIVEQGTHEELLAKNG 563
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
183-608 |
4.82e-96 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 319.66 E-value: 4.82e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 183 IGLVISLI-KSWKLSLVVLSTSPLIMASSALCSRMIISLTSKELDAYSKAGAVAEEALSSIQTVTAFGAQEKEIQRYTQH 261
Cdd:PRK11176 154 IGLFIMMFyYSWQLSLILIVIAPIVSIAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKV 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 262 LKDAKDAGIKRATASKLSLGAVYFFMNGAygLAF-WYGTSLifggePG----YTIGTILAVFFSVIhssyciGSVAPhLE 336
Cdd:PRK11176 234 SNRMRQQGMKMVSASSISDPIIQLIASLA--LAFvLYAASF-----PSvmdtLTAGTITVVFSSMI------ALMRP-LK 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 337 TFT-----VARG--AAFNIFQVIDKKPNIDnfsTAGFVPECIEGNIEFKNVSFSYPSR--PSakvLKGLNLKIKAGETVA 407
Cdd:PRK11176 300 SLTnvnaqFQRGmaACQTLFAILDLEQEKD---EGKRVIERAKGDIEFRNVTFTYPGKevPA---LRNINFKIPAGKTVA 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 408 LVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDIRAQNVRHYREQIGVVRQEPVLFGTTIGNNIKFGREGVGEKE-MEQA 486
Cdd:PRK11176 374 LVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYARTEQYSREqIEEA 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 487 AREANAYDFIMAFPKKFNTLVGEKGAQMSGGQKQRIAIARALVRNPKILILDEATSALDTESESLVQTALEKASKGRTTI 566
Cdd:PRK11176 454 ARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSL 533
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 568980685 567 VVAHRLSTIRGADLIVTMKDGMVVEKGTHAELMAKQGLYYSL 608
Cdd:PRK11176 534 VIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQNGVYAQL 575
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
187-630 |
2.25e-95 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 317.67 E-value: 2.25e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 187 ISLIKSWKLSLVVLstspLIMASSALCSRMIISLTsKELDA-----YSKAGAVAEEALSSIQTVTAFGAQEKEIQ---RY 258
Cdd:PRK13657 150 LALFMNWRLSLVLV----VLGIVYTLITTLVMRKT-KDGQAaveehYHDLFAHVSDAIGNVSVVQSYNRIEAETQalrDI 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 259 TQHLKDAKD---------AGIKRAtASKLSLGAVyffmngayglaFWYGTSLIFGGEpgYTIGTILA-VFFS-------- 320
Cdd:PRK13657 225 ADNLLAAQMpvlswwalaSVLNRA-ASTITMLAI-----------LVLGAALVQKGQ--LRVGEVVAfVGFAtlligrld 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 321 -VIHSSYCIGSVAPHLETFtvargaafniFQVIDKKPNIDNFSTAGFVPEcIEGNIEFKNVSFSYPSRPSAkvLKGLNLK 399
Cdd:PRK13657 291 qVVAFINQVFMAAPKLEEF----------FEVEDAVPDVRDPPGAIDLGR-VKGAVEFDDVSFSYDNSRQG--VEDVSFE 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 400 IKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDIRAQNVRHYREQIGVVRQEPVLFGTTIGNNIKFGREGVG 479
Cdd:PRK13657 358 AKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRPDAT 437
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 480 EKEMEQAAREANAYDFIMAFPKKFNTLVGEKGAQMSGGQKQRIAIARALVRNPKILILDEATSALDTESESLVQTALEKA 559
Cdd:PRK13657 438 DEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDEL 517
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568980685 560 SKGRTTIVVAHRLSTIRGADLIVTMKDGMVVEKGTHAELMAKQGLYYSLAMAQDIKKVDEQMESRTCSTAG 630
Cdd:PRK13657 518 MKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVARGGRFAALLRAQGMLQEDERRKQPAAEGAN 588
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
123-608 |
1.20e-93 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 312.47 E-value: 1.20e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 123 RQTTRIRKQFFHSILAQDISW---FDGSDIceLNtRMTGDINKLcdgigdkiplmfQN-------------ISGFSIGLV 186
Cdd:COG4987 85 RLLADLRVRLYRRLEPLAPAGlarLRSGDL--LN-RLVADVDAL------------DNlylrvllpllvalLVILAAVAF 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 187 ISLIkSWKLSLVVLstspLIMASSALCSRMIISLTSKELDAYSKA--GAVAEEALSSIQ---TVTAFGAQEKEIQRYTQH 261
Cdd:COG4987 150 LAFF-SPALALVLA----LGLLLAGLLLPLLAARLGRRAGRRLAAarAALRARLTDLLQgaaELAAYGALDRALARLDAA 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 262 LKDAKDAGIKRATASKLSLGAVYFFMNGAYGLAFWYGTSLIFGGEPGytiGTILAVFFSVIHSSycIGSVAP------HL 335
Cdd:COG4987 225 EARLAAAQRRLARLSALAQALLQLAAGLAVVAVLWLAAPLVAAGALS---GPLLALLVLAALAL--FEALAPlpaaaqHL 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 336 ETftvARGAAFNIFQVIDKKPNIDNFSTAGFVPEciEGNIEFKNVSFSYPSRPSAkVLKGLNLKIKAGETVALVGPSGSG 415
Cdd:COG4987 300 GR---VRAAARRLNELLDAPPAVTEPAEPAPAPG--GPSLELEDVSFRYPGAGRP-VLDGLSLTLPPGERVAIVGPSGSG 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 416 KSTTVQLLQRLYDPEDGCITVDENDIRAQNVRHYREQIGVVRQEPVLFGTTIGNNIKFGREGVGEKEMEQAAREANAYDF 495
Cdd:COG4987 374 KSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPDATDEELWAALERVGLGDW 453
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 496 IMAFPKKFNTLVGEKGAQMSGGQKQRIAIARALVRNPKILILDEATSALDTESESLVQTALEKASKGRTTIVVAHRLSTI 575
Cdd:COG4987 454 LAALPDGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGL 533
|
490 500 510
....*....|....*....|....*....|...
gi 568980685 576 RGADLIVTMKDGMVVEKGTHAELMAKQGLYYSL 608
Cdd:COG4987 534 ERMDRILVLEDGRIVEQGTHEELLAQNGRYRQL 566
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
1002-1230 |
1.42e-93 |
|
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: 299.53 E-value: 1.42e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1002 GNLEFREVSFVYpcRPEVPVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVKELNVQWLRSQ 1081
Cdd:cd03254 1 GEIEFENVNFSY--DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1082 TAIVSQEPVLFNCSIAENIAYGDNSrmVPLEEIKEVADAANIHSFIEGLPRKYNTLVGLRGVQLSGGQKQRLAIARALLR 1161
Cdd:cd03254 79 IGVVLQDTFLFSGTIMENIRLGRPN--ATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLR 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568980685 1162 KPKILLLDEATSALDNESEKVVQQALDKARRGKTCLVVAHRLSTIQNADMIVVLQNGSIKEQGTHQELL 1230
Cdd:cd03254 157 DPKILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELL 225
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
752-1239 |
1.42e-91 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 307.33 E-value: 1.42e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 752 NLAMRLRHSAFKAMLYQDMAWYDdkENNTGALTTTLAVDVAQIQGAATSRL-GIVTQDVSNMSLSILIsFIYGWEMTLLI 830
Cdd:PRK11176 95 KVVMTMRRRLFGHMMGMPVSFFD--KQSTGTLLSRITYDSEQVASSSSGALiTVVREGASIIGLFIMM-FYYSWQLSLIL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 831 LSFAPVLAVTgmIQTAAMAgFANRDKQALKRAGKIATEAVENI---RTVVSLTRERAFEQMYEETLQTQHRNALKRAHIT 907
Cdd:PRK11176 172 IVIAPIVSIA--IRVVSKR-FRNISKNMQNTMGQVTTSAEQMLkghKEVLIFGGQEVETKRFDKVSNRMRQQGMKMVSAS 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 908 gccyAVSHAFVHFAHAAGFRFGAYLIQAGRMMPE---GMF-IVFTAIaYGAMAIGETL--VWApEYSKAKAGASHLFALL 981
Cdd:PRK11176 249 ----SISDPIIQLIASLALAFVLYAASFPSVMDTltaGTItVVFSSM-IALMRPLKSLtnVNA-QFQRGMAACQTLFAIL 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 982 KNKPTINSCSQSGEKPdtcEGNLEFREVSFVYPCRpEVPVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKG 1061
Cdd:PRK11176 323 DLEQEKDEGKRVIERA---KGDIEFRNVTFTYPGK-EVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEG 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1062 QVLLDGVDVKELNVQWLRSQTAIVSQEPVLFNCSIAENIAYGDN---SRmvplEEIKEVADAANIHSFIEGLPRKYNTLV 1138
Cdd:PRK11176 399 EILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYARTeqySR----EQIEEAARMAYAMDFINKMDNGLDTVI 474
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1139 GLRGVQLSGGQKQRLAIARALLRKPKILLLDEATSALDNESEKVVQQALDKARRGKTCLVVAHRLSTIQNADMIVVLQNG 1218
Cdd:PRK11176 475 GENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDG 554
|
490 500
....*....|....*....|.
gi 568980685 1219 SIKEQGTHQELLRNGDTYFKL 1239
Cdd:PRK11176 555 EIVERGTHAELLAQNGVYAQL 575
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
997-1220 |
2.45e-89 |
|
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: 287.83 E-value: 2.45e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 997 PDTCEGNLEFREVSFVYPCRPEVPVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVKELNVQ 1076
Cdd:cd03248 5 PDHLKGIVKFQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1077 WLRSQTAIVSQEPVLFNCSIAENIAYGDNSrmVPLEEIKEVADAANIHSFIEGLPRKYNTLVGLRGVQLSGGQKQRLAIA 1156
Cdd:cd03248 85 YLHSKVSLVGQEPVLFARSLQDNIAYGLQS--CSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568980685 1157 RALLRKPKILLLDEATSALDNESEKVVQQALDKARRGKTCLVVAHRLSTIQNADMIVVLQNGSI 1220
Cdd:cd03248 163 RALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
970-1233 |
3.91e-88 |
|
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: 297.05 E-value: 3.91e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 970 AKAGASHLFALLkNKPTINSCSQSGEKPDTCEGNLEFREVSFVYPcrPEVPVLQNMSLSIEKGKTVAFVGSSGCGKSTCV 1049
Cdd:COG4988 304 GIAAAEKIFALL-DAPEPAAPAGTAPLPAAGPPSIELEDVSFSYP--GGRPALDGLSLTIPPGERVALVGPSGAGKSTLL 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1050 QLLQRFYDPMKGQVLLDGVDVKELNVQWLRSQTAIVSQEPVLFNCSIAENIAYGDnsRMVPLEEIKEVADAANIHSFIEG 1129
Cdd:COG4988 381 NLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGR--PDASDEELEAALEAAGLDEFVAA 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1130 LPRKYNTLVGLRGVQLSGGQKQRLAIARALLRKPKILLLDEATSALDNESEKVVQQALDKARRGKTCLVVAHRLSTIQNA 1209
Cdd:COG4988 459 LPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQA 538
|
250 260
....*....|....*....|....
gi 568980685 1210 DMIVVLQNGSIKEQGTHQELLRNG 1233
Cdd:COG4988 539 DRILVLDDGRIVEQGTHEELLAKN 562
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
375-612 |
2.31e-87 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 282.84 E-value: 2.31e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 375 IEFKNVSFSYpsRP-SAKVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDIRAQNVRHYREQI 453
Cdd:cd03252 1 ITFEHVRFRY--KPdGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 454 GVVRQEPVLFGTTIGNNIKFGREGVGEKEMEQAAREANAYDFIMAFPKKFNTLVGEKGAQMSGGQKQRIAIARALVRNPK 533
Cdd:cd03252 79 GVVLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568980685 534 ILILDEATSALDTESESLVQTALEKASKGRTTIVVAHRLSTIRGADLIVTMKDGMVVEKGTHAELMAKQGLYYSLAMAQ 612
Cdd:cd03252 159 ILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQLQ 237
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
816-1241 |
3.47e-87 |
|
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: 294.37 E-value: 3.47e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 816 ILISFIYGWemtlLILSFAPVLAVTGMIQTAAMAGFANRDKQALKRA-GKIATEAVENIRTVVSLT---RERAFEQMYEE 891
Cdd:COG4987 148 AFLAFFSPA----LALVLALGLLLAGLLLPLLAARLGRRAGRRLAAArAALRARLTDLLQGAAELAaygALDRALARLDA 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 892 TLQTQHRNALKRAHITGCCYAVSHAFVHFAHAAGFRFGAYLIQAGRMMPegmfIVFTAIAYGAMAIGEtlVWAP------ 965
Cdd:COG4987 224 AEARLAAAQRRLARLSALAQALLQLAAGLAVVAVLWLAAPLVAAGALSG----PLLALLVLAALALFE--ALAPlpaaaq 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 966 EYSKAKAGASHLFALLKNKPTINSCSQSGEKPDtcEGNLEFREVSFVYPCRPEvPVLQNMSLSIEKGKTVAFVGSSGCGK 1045
Cdd:COG4987 298 HLGRVRAAARRLNELLDAPPAVTEPAEPAPAPG--GPSLELEDVSFRYPGAGR-PVLDGLSLTLPPGERVAIVGPSGSGK 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1046 STCVQLLQRFYDPMKGQVLLDGVDVKELNVQWLRSQTAIVSQEPVLFNCSIAENIAYGDNSrmVPLEEIKEVADAANIHS 1125
Cdd:COG4987 375 STLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPD--ATDEELWAALERVGLGD 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1126 FIEGLPRKYNTLVGLRGVQLSGGQKQRLAIARALLRKPKILLLDEATSALDNESEKVVQQALDKARRGKTCLVVAHRLST 1205
Cdd:COG4987 453 WLAALPDGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAG 532
|
410 420 430
....*....|....*....|....*....|....*.
gi 568980685 1206 IQNADMIVVLQNGSIKEQGTHQELLRNGDTYFKLVA 1241
Cdd:COG4987 533 LERMDRILVLEDGRIVEQGTHEELLAQNGRYRQLYQ 568
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
37-348 |
1.17e-86 |
|
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: 284.17 E-value: 1.17e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 37 MTLGILASMINGATVPLMSLVLGEISDHLINGCLVQTNRTKYQNCSQTQ--EKLNEDIIVLTLYYIGIGAAALIFGYVQI 114
Cdd:cd18558 1 MVVGILCAIIHGGLLPAFMVIFGDMTDSFTNGGMTNITGNSSGLNSSAGpfEKLEEEMTLYAYYYLIIGAIVLITAYIQG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 115 SFWVITAARQTTRIRKQFFHSILAQDISWFDGSDICELNTRMTGDINKLCDGIGDKIPLMFQNISGFSIGLVISLIKSWK 194
Cdd:cd18558 81 SFWGLAAGRQTKKIRYKFFHAIMRQEIGWFDVNDTGELNTRLADDVSKINEGIGDKIGVIFQNIATFGTGFIIGFIRGWK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 195 LSLVVLSTSPLIMASSALCSRMIISLTSKELDAYSKAGAVAEEALSSIQTVTAFGAQEKEIQRYTQHLKDAKDAGIKRAT 274
Cdd:cd18558 161 LTLVILAISPVLGLSAVVWAKILSGFTDKEKKAYAKAGAVAEEVLEAFRTVIAFGGQQKEETRYAQNLEIAKRNGIKKAI 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568980685 275 ASKLSLGAVYFFMNGAYGLAFWYGTSLIFGGEpgYTIGTILAVFFSVIHSSYCIGSVAPHLETFTVARGAAFNI 348
Cdd:cd18558 241 TFNISMGAAFLLIYASYALAFWYGTYLVTQQE--YSIGEVLTVFFSVLIGAFSAGQQVPSIEAFANARGAAYHI 312
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
94-612 |
2.91e-84 |
|
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: 290.11 E-value: 2.91e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 94 VLTLYYIGIGAAALIFGYVQISFWVITAARQTTRIRKQFFHSILAQDISWFDGSDICELNTRMTgdinklcdgigdKIPL 173
Cdd:TIGR01846 180 VLALAMLAVAIFEPALGGLRTYLFAHLTSRIDVELGARLYRHLLGLPLGYFESRRVGDTVARVR------------ELEQ 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 174 MFQNISGFSIGLVISLI-----------KSWKLSLVVLSTSPLIMASSALCSRMIISLTSKELDAYSKAGAVAEEALSSI 242
Cdd:TIGR01846 248 IRNFLTGSALTVVLDLLfvvvflavmffYSPTLTGVVIGSLVCYALLSVFVGPILRKRVEDKFERSAAATSFLVESVTGI 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 243 QTVTAFGAQEKEIQRYTQHLKDAKDAGIKRATASKLSLGAVYFFMNGAYGLAFWYGTSLIFGGEpgYTIGTILAVFFSVI 322
Cdd:TIGR01846 328 ETIKATATEPQFQNRWDRQLAAYVAASFRVTNLGNIAGQAIELIQKLTFAILLWFGAHLVIGGA--LSPGQLVAFNMLAG 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 323 HSSYCIGSVAPHLETFTVARGAAFNIFQVIDKkPNIDNFSTAGFVPEcIEGNIEFKNVSFSYpsRP-SAKVLKGLNLKIK 401
Cdd:TIGR01846 406 RVTQPVLRLAQLWQDFQQTGIALERLGDILNS-PTEPRSAGLAALPE-LRGAITFENIRFRY--APdSPEVLSNLNLDIK 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 402 AGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDIRAQNVRHYREQIGVVRQEPVLFGTTIGNNIKFGREGVGEK 481
Cdd:TIGR01846 482 PGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAWLRRQMGVVLQENVLFSRSIRDNIALCNPGAPFE 561
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 482 EMEQAAREANAYDFIMAFPKKFNTLVGEKGAQMSGGQKQRIAIARALVRNPKILILDEATSALDTESESLVQTALEKASK 561
Cdd:TIGR01846 562 HVIHAAKLAGAHDFISELPQGYNTEVGEKGANLSGGQRQRIAIARALVGNPRILIFDEATSALDYESEALIMRNMREICR 641
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 568980685 562 GRTTIVVAHRLSTIRGADLIVTMKDGMVVEKGTHAELMAKQGLYYSLAMAQ 612
Cdd:TIGR01846 642 GRTVIIIAHRLSTVRACDRIIVLEKGQIAESGRHEELLALQGLYARLWQQQ 692
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
1004-1241 |
1.30e-83 |
|
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: 272.44 E-value: 1.30e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1004 LEFREVSFVYpcRPEVP-VLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVKELNVQWLRSQT 1082
Cdd:cd03252 1 ITFEHVRFRY--KPDGPvILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1083 AIVSQEPVLFNCSIAENIAYGDNSrmVPLEEIKEVADAANIHSFIEGLPRKYNTLVGLRGVQLSGGQKQRLAIARALLRK 1162
Cdd:cd03252 79 GVVLQENVLFNRSIRDNIALADPG--MSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHN 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568980685 1163 PKILLLDEATSALDNESEKVVQQALDKARRGKTCLVVAHRLSTIQNADMIVVLQNGSIKEQGTHQELLRNGDTYFKLVA 1241
Cdd:cd03252 157 PRILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQ 235
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
368-589 |
8.62e-83 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 269.73 E-value: 8.62e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 368 PECIEGNIEFKNVSFSYPSRPSAKVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDIRAQNVR 447
Cdd:cd03248 5 PDHLKGIVKFQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 448 HYREQIGVVRQEPVLFGTTIGNNIKFGREGVGEKEMEQAAREANAYDFIMAFPKKFNTLVGEKGAQMSGGQKQRIAIARA 527
Cdd:cd03248 85 YLHSKVSLVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568980685 528 LVRNPKILILDEATSALDTESESLVQTALEKASKGRTTIVVAHRLSTIRGADLIVTMKDGMV 589
Cdd:cd03248 165 LIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
375-587 |
3.89e-82 |
|
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: 265.79 E-value: 3.89e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 375 IEFKNVSFSYPSRPsAKVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDIRAQNVRHYREQIG 454
Cdd:cd03228 1 IEFKNVSFSYPGRP-KPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 455 VVRQEPVLFGTTIGNNIkfgregvgekemeqaareanaydfimafpkkfntlvgekgaqMSGGQKQRIAIARALVRNPKI 534
Cdd:cd03228 80 YVPQDPFLFSGTIRENI------------------------------------------LSGGQRQRIAIARALLRDPPI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 568980685 535 LILDEATSALDTESESLVQTALEKASKGRTTIVVAHRLSTIRGADLIVTMKDG 587
Cdd:cd03228 118 LILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDG 170
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
1004-1218 |
1.88e-81 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 263.86 E-value: 1.88e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1004 LEFREVSFVYPCRPEvPVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVKELNVQWLRSQTA 1083
Cdd:cd03228 1 IEFKNVSFSYPGRPK-PVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1084 IVSQEPVLFNCSIAENIaygdnsrmvpleeikevadaanihsfieglprkyntlvglrgvqLSGGQKQRLAIARALLRKP 1163
Cdd:cd03228 80 YVPQDPFLFSGTIRENI--------------------------------------------LSGGQRQRIAIARALLRDP 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 568980685 1164 KILLLDEATSALDNESEKVVQQALDKARRGKTCLVVAHRLSTIQNADMIVVLQNG 1218
Cdd:cd03228 116 PILILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDG 170
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
926-1242 |
1.33e-77 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 267.98 E-value: 1.33e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 926 FRFGAYLIQAGrMMPEGMFIVFTAIAygAMAIG--ETLV-WAPEYSKAKAGASHLFALLKNKPTINscsqsgEKPDTCE- 1001
Cdd:PRK13657 258 LVLGAALVQKG-QLRVGEVVAFVGFA--TLLIGrlDQVVaFINQVFMAAPKLEEFFEVEDAVPDVR------DPPGAIDl 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1002 ----GNLEFREVSFVYPCRPevPVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVKELNVQW 1077
Cdd:PRK13657 329 grvkGAVEFDDVSFSYDNSR--QGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRAS 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1078 LRSQTAIVSQEPVLFNCSIAENIAYGDNSrmVPLEEIKEVADAANIHSFIEGLPRKYNTLVGLRGVQLSGGQKQRLAIAR 1157
Cdd:PRK13657 407 LRRNIAVVFQDAGLFNRSIEDNIRVGRPD--ATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIAR 484
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1158 ALLRKPKILLLDEATSALDNESEKVVQQALDKARRGKTCLVVAHRLSTIQNADMIVVLQNGSIKEQGTHQELLRNGDTYF 1237
Cdd:PRK13657 485 ALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVARGGRFA 564
|
....*
gi 568980685 1238 KLVAA 1242
Cdd:PRK13657 565 ALLRA 569
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
666-1241 |
8.06e-76 |
|
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: 266.42 E-value: 8.06e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 666 SLLKIFKLSKSEWPFVVLGTLASALNGSVHPVFSIIFgklVTMFedknkaTLKQDAELYSMMLVVLGIVALVTY---LMQ 742
Cdd:TIGR03796 144 ALWRRLRGSRGALLYLLLAGLLLVLPGLVIPAFSQIF---VDEI------LVQGRQDWLRPLLLGMGLTALLQGvltWLQ 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 743 GLFYGRAEENLAMRLRHSAFKAMLYQDMAWYDDKENNTGALTTTLAVDVAQIQGA--ATSRLGIVTqdvsnMSLSILISF 820
Cdd:TIGR03796 215 LYYLRRLEIKLAVGMSARFLWHILRLPVRFFAQRHAGDIASRVQLNDQVAEFLSGqlATTALDAVM-----LVFYALLML 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 821 IYGWEMTLLILSFAPVLAVTgMIQTAAMAGFANRdkQALKRAGKIATEAVENIRTVVSL----TRERAFEQ---MYEETL 893
Cdd:TIGR03796 290 LYDPVLTLIGIAFAAINVLA-LQLVSRRRVDANR--RLQQDAGKLTGVAISGLQSIETLkasgLESDFFSRwagYQAKLL 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 894 QTQHRNALKRAHITgccyAVSHAFVHFAHAAGFRFGAYLIQAGRMMPeGMFIVFTAIAYGAMAIGETLV-WAPEYSKAKA 972
Cdd:TIGR03796 367 NAQQELGVLTQILG----VLPTLLTSLNSALILVVGGLRVMEGQLTI-GMLVAFQSLMSSFLEPVNNLVgFGGTLQELEG 441
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 973 GASHLFALLKNKP------TINSCSQSGEKPdTCEGNLEFREVSFVYPcRPEVPVLQNMSLSIEKGKTVAFVGSSGCGKS 1046
Cdd:TIGR03796 442 DLNRLDDVLRNPVdplleePEGSAATSEPPR-RLSGYVELRNITFGYS-PLEPPLIENFSLTLQPGQRVALVGGSGSGKS 519
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1047 TCVQLLQRFYDPMKGQVLLDGVDVKELNVQWLRSQTAIVSQEPVLFNCSIAENIAYGDNSrmVPLEEIKEVADAANIHSF 1126
Cdd:TIGR03796 520 TIAKLVAGLYQPWSGEILFDGIPREEIPREVLANSVAMVDQDIFLFEGTVRDNLTLWDPT--IPDADLVRACKDAAIHDV 597
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1127 IEGLPRKYNTLVGLRGVQLSGGQKQRLAIARALLRKPKILLLDEATSALDNESEKVVQQALdkARRGKTCLVVAHRLSTI 1206
Cdd:TIGR03796 598 ITSRPGGYDAELAEGGANLSGGQRQRLEIARALVRNPSILILDEATSALDPETEKIIDDNL--RRRGCTCIIVAHRLSTI 675
|
570 580 590
....*....|....*....|....*....|....*
gi 568980685 1207 QNADMIVVLQNGSIKEQGTHQELLRNGDTYFKLVA 1241
Cdd:TIGR03796 676 RDCDEIIVLERGKVVQRGTHEELWAVGGAYARLIR 710
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
123-608 |
1.09e-72 |
|
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: 257.56 E-value: 1.09e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 123 RQTTRIRKQFFHSILAQDISWFDGSDICELNTRMTGDiNKLCDGIGDKIPLMFQNISGFSIGLVISLIKSWKLSLVVLST 202
Cdd:TIGR03796 224 KLAVGMSARFLWHILRLPVRFFAQRHAGDIASRVQLN-DQVAEFLSGQLATTALDAVMLVFYALLMLLYDPVLTLIGIAF 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 203 SPLIMASSALCSRMIISLTSKELDAYSKAGAVAEEALSSIQTVTAFGAQEKEIQR----YTQHLKDAKDAGIKRATaskl 278
Cdd:TIGR03796 303 AAINVLALQLVSRRRVDANRRLQQDAGKLTGVAISGLQSIETLKASGLESDFFSRwagyQAKLLNAQQELGVLTQI---- 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 279 sLGAVYFFMNG-AYGLAFWYGTSLIFGGEpgYTIG------TILAVFFSVIHSSYCIGSVAPHLETftvargaafNIFQV 351
Cdd:TIGR03796 379 -LGVLPTLLTSlNSALILVVGGLRVMEGQ--LTIGmlvafqSLMSSFLEPVNNLVGFGGTLQELEG---------DLNRL 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 352 ID-----KKPNIDNFSTAGFVPEC---IEGNIEFKNVSFSYpSRPSAKVLKGLNLKIKAGETVALVGPSGSGKSTTVQLL 423
Cdd:TIGR03796 447 DDvlrnpVDPLLEEPEGSAATSEPprrLSGYVELRNITFGY-SPLEPPLIENFSLTLQPGQRVALVGGSGSGKSTIAKLV 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 424 QRLYDPEDGCITVDenDIRAQNVRHYR--EQIGVVRQEPVLFGTTIGNNIKFGREGVGEKEMEQAAREANAYDFIMAFPK 501
Cdd:TIGR03796 526 AGLYQPWSGEILFD--GIPREEIPREVlaNSVAMVDQDIFLFEGTVRDNLTLWDPTIPDADLVRACKDAAIHDVITSRPG 603
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 502 KFNTLVGEKGAQMSGGQKQRIAIARALVRNPKILILDEATSALDTESESLVQTALEKasKGRTTIVVAHRLSTIRGADLI 581
Cdd:TIGR03796 604 GYDAELAEGGANLSGGQRQRLEIARALVRNPSILILDEATSALDPETEKIIDDNLRR--RGCTCIIVAHRLSTIRDCDEI 681
|
490 500
....*....|....*....|....*..
gi 568980685 582 VTMKDGMVVEKGTHAELMAKQGLYYSL 608
Cdd:TIGR03796 682 IVLERGKVVQRGTHEELWAVGGAYARL 708
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
682-977 |
4.97e-71 |
|
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: 240.26 E-value: 4.97e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 682 VLGTLASALNGSVHPVFSIIFGKLVTMFEDKNK-----------------ATLKQDAELYSMMLVVLGIVALVTYLMQGL 744
Cdd:cd18558 2 VVGILCAIIHGGLLPAFMVIFGDMTDSFTNGGMtnitgnssglnssagpfEKLEEEMTLYAYYYLIIGAIVLITAYIQGS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 745 FYGRAEENLAMRLRHSAFKAMLYQDMAWYDdkENNTGALTTTLAVDVAQIQGAATSRLGIVTQDVSNMSLSILISFIYGW 824
Cdd:cd18558 82 FWGLAAGRQTKKIRYKFFHAIMRQEIGWFD--VNDTGELNTRLADDVSKINEGIGDKIGVIFQNIATFGTGFIIGFIRGW 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 825 EMTLLILSFAPVLAVTGMIQTAAMAGFANRDKQALKRAGKIATEAVENIRTVVSLTRERAFEQMYEETLQTQHRNALKRA 904
Cdd:cd18558 160 KLTLVILAISPVLGLSAVVWAKILSGFTDKEKKAYAKAGAVAEEVLEAFRTVIAFGGQQKEETRYAQNLEIAKRNGIKKA 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568980685 905 HITGCCYAVSHAFVHFAHAAGFRFGAYLIQAGRM-MPEGMFIVFTAIAYGAMAIGETLVWAPeYSKAKAGASHL 977
Cdd:cd18558 240 ITFNISMGAAFLLIYASYALAFWYGTYLVTQQEYsIGEVLTVFFSVLIGAFSAGQQVPSIEA-FANARGAAYHI 312
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
193-625 |
4.95e-70 |
|
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: 246.34 E-value: 4.95e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 193 WKLSLVVLstspLIMASSALCSRMIISLTsKELDA-----YSKAGAVAEEALSSIQTVTAFG---AQEKEIQRYTQHLKD 264
Cdd:TIGR01192 156 WRLSIVLM----VLGILYILIAKLVMQRT-KNGQAavehhYHNVFKHVSDSISNVSVVHSYNrieAETSALKQFTNNLLS 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 265 AK---------DAGIKRaTASKLSLGAVYFFmngayglafwyGTSLIFGGEPGytIGTILAVffsVIHSSYCIGSVaPHL 335
Cdd:TIGR01192 231 AQypvldwwalASGLNR-MASTISMMCILVI-----------GTVLVIKGELS--VGEVIAF---IGFANLLIGRL-DQM 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 336 ETFTV----ARGAAFNIFQVIDKKPNIDNFSTAGFVPEcIEGNIEFKNVSFSYPSrpSAKVLKGLNLKIKAGETVALVGP 411
Cdd:TIGR01192 293 SGFITqifeARAKLEDFFDLEDSVFQREEPADAPELPN-VKGAVEFRHITFEFAN--SSQGVFDVSFEAKAGQTVAIVGP 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 412 SGSGKSTTVQLLQRLYDPEDGCITVDENDIRAQNVRHYREQIGVVRQEPVLFGTTIGNNIKFGREGVGEKEMEQAAREAN 491
Cdd:TIGR01192 370 TGAGKTTLINLLQRVYDPTVGQILIDGIDINTVTRESLRKSIATVFQDAGLFNRSIRENIRLGREGATDEEVYEAAKAAA 449
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 492 AYDFIMAFPKKFNTLVGEKGAQMSGGQKQRIAIARALVRNPKILILDEATSALDTESESLVQTALEKASKGRTTIVVAHR 571
Cdd:TIGR01192 450 AHDFILKRSNGYDTLVGERGNRLSGGERQRLAIARAILKNAPILVLDEATSALDVETEARVKNAIDALRKNRTTFIIAHR 529
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 568980685 572 LSTIRGADLIVTMKDGMVVEKGTHAELMAKQGLYYSLAMAQDIKKVDEQMESRT 625
Cdd:TIGR01192 530 LSTVRNADLVLFLDQGRLIEKGSFQELIQKDGRFYKLLRRSGLLTNQPATKPLR 583
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
661-1241 |
5.90e-69 |
|
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: 246.02 E-value: 5.90e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 661 SLPEVSL----LKIFKLSKSEWPFVVLG--TLASALNGSVHPvfsIIFGKLVtmfedkNKATLKQDAELysmmLVVLGIV 734
Cdd:TIGR03797 115 PLPDKALglrdLLRFALRGARRDLLAILamGLLGTLLGMLVP---IATGILI------GTAIPDADRSL----LVQIALA 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 735 ALVTYLMQGLFygRAEENLAMrLR-HSAFKAMLyqDMAWYDD---------KENNTGALTTTlAVDVAQIQGAATSRLGI 804
Cdd:TIGR03797 182 LLAAAVGAAAF--QLAQSLAV-LRlETRMDASL--QAAVWDRllrlpvsffRQYSTGDLASR-AMGISQIRRILSGSTLT 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 805 VTQDVSNMSLSILISFIYGWEMTL----LILSFAPVLAVTGMIQTaamagfaNRDKQALKRAGKIATEAVENIRTVVSL- 879
Cdd:TIGR03797 256 TLLSGIFALLNLGLMFYYSWKLALvavaLALVAIAVTLVLGLLQV-------RKERRLLELSGKISGLTVQLINGISKLr 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 880 ---TRERAFEQMYEETLQtQHRNALKRAHITGCCYAVSHAFVHFAHAAGFRFGAYLIQAGRMMPeGMFIVFTAiAYG--- 953
Cdd:TIGR03797 329 vagAENRAFARWAKLFSR-QRKLELSAQRIENLLTVFNAVLPVLTSAALFAAAISLLGGAGLSL-GSFLAFNT-AFGsfs 405
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 954 ------AMAIGETLVWAPEYSKAKAgashlfaLLKNKPTINScsqSGEKPDTCEGNLEFREVSFVYpcRPEVP-VLQNMS 1026
Cdd:TIGR03797 406 gavtqlSNTLISILAVIPLWERAKP-------ILEALPEVDE---AKTDPGKLSGAIEVDRVTFRY--RPDGPlILDDVS 473
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1027 LSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVKELNVQWLRSQTAIVSQEPVLFNCSIAENIAYGDns 1106
Cdd:TIGR03797 474 LQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLDVQAVRRQLGVVLQNGRLMSGSIFENIAGGA-- 551
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1107 rMVPLEEIKEVADAANIHSFIEGLPRKYNTLVGLRGVQLSGGQKQRLAIARALLRKPKILLLDEATSALDNESEKVVQQA 1186
Cdd:TIGR03797 552 -PLTLDEAWEAARMAGLAEDIRAMPMGMHTVISEGGGTLSGGQRQRLLIARALVRKPRILLFDEATSALDNRTQAIVSES 630
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*
gi 568980685 1187 LDKARrgKTCLVVAHRLSTIQNADMIVVLQNGSIKEQGTHQELLRNGDTYFKLVA 1241
Cdd:TIGR03797 631 LERLK--VTRIVIAHRLSTIRNADRIYVLDAGRVVQQGTYDELMAREGLFAQLAR 683
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
36-358 |
5.98e-69 |
|
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: 234.27 E-value: 5.98e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 36 LMTLGILASMINGATVPLMSLVLGEISDHLINgclvqtnrtkyqncsQTQEKLNEDIIVLTLYYIGIGAAALIFGYVQIS 115
Cdd:cd18578 10 LLLLGLIGAIIAGAVFPVFAILFSKLISVFSL---------------PDDDELRSEANFWALMFLVLAIVAGIAYFLQGY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 116 FWVITAARQTTRIRKQFFHSILAQDISWFD------GSdiceLNTRMTGDINKLCDGIGDKIPLMFQNISGFSIGLVISL 189
Cdd:cd18578 75 LFGIAGERLTRRLRKLAFRAILRQDIAWFDdpenstGA----LTSRLSTDASDVRGLVGDRLGLILQAIVTLVAGLIIAF 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 190 IKSWKLSLVVLSTSPLIMASSALCSRMIISLTSKELDAYSKAGAVAEEALSSIQTVTAFGAQEKEIQRYTQHLKDAKDAG 269
Cdd:cd18578 151 VYGWKLALVGLATVPLLLLAGYLRMRLLSGFEEKNKKAYEESSKIASEAVSNIRTVASLTLEDYFLEKYEEALEEPLKKG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 270 IKRATASKLSLGAVYFFMNGAYGLAFWYGTSLIFGGEpgYTIGTILAVFFSVIHSSYCIGSVAPHLETFTVARGAAFNIF 349
Cdd:cd18578 231 LRRALISGLGFGLSQSLTFFAYALAFWYGGRLVANGE--YTFEQFFIVFMALIFGAQSAGQAFSFAPDIAKAKAAAARIF 308
|
....*....
gi 568980685 350 QVIDKKPNI 358
Cdd:cd18578 309 RLLDRKPEI 317
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
1002-1224 |
1.68e-67 |
|
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: 226.70 E-value: 1.68e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1002 GNLEFREVSFVYPcRPEVPVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVKELNVQWLRSQ 1081
Cdd:cd03245 1 GRIEFRNVSFSYP-NQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1082 TAIVSQEPVLFNCSIAENIAYGDNSrmVPLEEIKEVADAANIHSFIEGLPRKYNTLVGLRGVQLSGGQKQRLAIARALLR 1161
Cdd:cd03245 80 IGYVPQDVTLFYGTLRDNITLGAPL--ADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLN 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568980685 1162 KPKILLLDEATSALDNESEKVVQQALDKARRGKTCLVVAHRLSTIQNADMIVVLQNGSIKEQG 1224
Cdd:cd03245 158 DPPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
657-1225 |
2.62e-66 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 246.86 E-value: 2.62e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 657 HQKTSLPEVSLLKIFK-LSKSEWPFVVLGTLASALNGSVHPVFSIIFGKLVtmfedKNkATLKQDAELYSMMLVVLGIVA 735
Cdd:PTZ00265 37 YKKIKTQKIPFFLPFKcLPASHRKLLGVSFVCATISGGTLPFFVSVFGVIM-----KN-MNLGENVNDIIFSLVLIGIFQ 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 736 LVTYLMQGLFYGRAEENLAMRLRHSAFKAMLYQDMAWYDdkeNNTGA-LTTTLAVDVAQIQ-GAATSRLGIVTQDVSNMS 813
Cdd:PTZ00265 111 FILSFISSFCMDVVTTKILKTLKLEFLKSVFYQDGQFHD---NNPGSkLTSDLDFYLEQVNaGIGTKFITIFTYASAFLG 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 814 LSILiSFIYGWEMTLLILSFAPVLAVTGMIQTAAMAgfANRDKQAL--KRAGKIATEAVENIRTVVSLTRERAFEQMY-- 889
Cdd:PTZ00265 188 LYIW-SLFKNARLTLCITCVFPLIYICGVICNKKVK--INKKTSLLynNNTMSIIEEALVGIRTVVSYCGEKTILKKFnl 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 890 EETLQTQH---RNALKRAHItgccyAVSHAFVHFAHAAGFRFGAYLI--QAGRMMPEGMF------IVFTAIAYGAMAIG 958
Cdd:PTZ00265 265 SEKLYSKYilkANFMESLHI-----GMINGFILASYAFGFWYGTRIIisDLSNQQPNNDFhggsviSILLGVLISMFMLT 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 959 ETLVWAPEYSKAKAGASHLFALLKNKPTINScSQSGEK-PDTceGNLEFREVSFVYPCRPEVPVLQNMSLSIEKGKTVAF 1037
Cdd:PTZ00265 340 IILPNITEYMKSLEATNSLYEIINRKPLVEN-NDDGKKlKDI--KKIQFKNVRFHYDTRKDVEIYKDLNFTLTEGKTYAF 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1038 VGSSGCGKSTCVQLLQRFYDPMKGQVLL-DGVDVKELNVQWLRSQTAIVSQEPVLFNCSIAENIAY-------------- 1102
Cdd:PTZ00265 417 VGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKYslyslkdlealsny 496
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1103 ----------GDNSR-------------------------------MVPLEEIKEVADAANIHSFIEGLPRKYNTLVGLR 1141
Cdd:PTZ00265 497 ynedgndsqeNKNKRnscrakcagdlndmsnttdsneliemrknyqTIKDSEVVDVSKKVLIHDFVSALPDKYETLVGSN 576
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1142 GVQLSGGQKQRLAIARALLRKPKILLLDEATSALDNESEKVVQQALD--KARRGKTCLVVAHRLSTIQNADMIVVLQNgs 1219
Cdd:PTZ00265 577 ASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINnlKGNENRITIIIAHRLSTIRYANTIFVLSN-- 654
|
....*.
gi 568980685 1220 iKEQGT 1225
Cdd:PTZ00265 655 -RERGS 659
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
373-594 |
4.89e-66 |
|
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: 222.37 E-value: 4.89e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 373 GNIEFKNVSFSYpsRPSAK-VLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDIRAQNVRHYRE 451
Cdd:cd03244 1 GDIEFKNVSLRY--RPNLPpVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 452 QIGVVRQEPVLFGTTIGNNIK-FGRegVGEKEMEQAAREANAYDFIMAFPKKFNTLVGEKGAQMSGGQKQRIAIARALVR 530
Cdd:cd03244 79 RISIIPQDPVLFSGTIRSNLDpFGE--YSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLR 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568980685 531 NPKILILDEATSALDTESESLVQTALEKASKGRTTIVVAHRLSTIRGADLIVTMKDGMVVEKGT 594
Cdd:cd03244 157 KSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
37-322 |
1.44e-65 |
|
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: 223.29 E-value: 1.44e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 37 MTLGILASMINGATVPLMSLVLGEISDHLIngclvQTNRTKYQncsqtqeklneDIIVLTLYYIGIGAAALIFGYVQISF 116
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLL-----PDGDPETQ-----------ALNVYSLALLLLGLAQFILSFLQSYL 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 117 WVITAARQTTRIRKQFFHSILAQDISWFDGSDICELNTRMTGDINKLCDGIGDKIPLMFQNISGFSIGLVISLIKSWKLS 196
Cdd:pfam00664 65 LNHTGERLSRRLRRKLFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLT 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 197 LVVLSTSPLIMASSALCSRMIISLTSKELDAYSKAGAVAEEALSSIQTVTAFGAQEKEIQRYTQHLKDAKDAGIKRATAS 276
Cdd:pfam00664 145 LVLLAVLPLYILVSAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVAN 224
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 568980685 277 KLSLGAVYFFMNGAYGLAFWYGTSLIFGGEpgYTIGTILA--VFFSVI 322
Cdd:pfam00664 225 GLSFGITQFIGYLSYALALWFGAYLVISGE--LSVGDLVAflSLFAQL 270
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
375-1240 |
1.48e-65 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 244.50 E-value: 1.48e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 375 IEFKNVSFSYPSRPSAKVLKGLNLKIKAGETVALVGPSGSGKSTTVQ-LLQRLYDPEDGCITVdendiraqnvrhyREQI 453
Cdd:PLN03232 615 ISIKNGYFSWDSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISaMLGELSHAETSSVVI-------------RGSV 681
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 454 GVVRQEPVLFGTTIGNNIKFGREGVGEKEMEQAAREANAYDFIMaFPKKFNTLVGEKGAQMSGGQKQRIAIARALVRNPK 533
Cdd:PLN03232 682 AYVPQVSWIFNATVRENILFGSDFESERYWRAIDVTALQHDLDL-LPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSD 760
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 534 ILILDEATSALDTE-SESLVQTALEKASKGRTTIVVAHRLSTIRGADLIVTMKDGMVVEKGTHAELmAKQGLYYSLAMaQ 612
Cdd:PLN03232 761 IYIFDDPLSALDAHvAHQVFDSCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAEL-SKSGSLFKKLM-E 838
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 613 DIKKVDEQMESRTCS-TAGNASYGSLCDVNSAKAPCTDQLEEA----VHHQKTSLPEVS---LLKIFKLSKSEWpfVVLG 684
Cdd:PLN03232 839 NAGKMDATQEVNTNDeNILKLGPTVTIDVSERNLGSTKQGKRGrsvlVKQEERETGIISwnvLMRYNKAVGGLW--VVMI 916
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 685 TLASALNGSVHPVFSIIFGKLVTmfedkNKATLKQ-DAELYSMMLVVLGIVALVTYLMQGLFYGRAEENLAMRLRHSAFK 763
Cdd:PLN03232 917 LLVCYLTTEVLRVSSSTWLSIWT-----DQSTPKSySPGFYIVVYALLGFGQVAVTFTNSFWLISSSLHAAKRLHDAMLN 991
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 764 AMLYQDMAWYDdkENNTGALTTTLAVDVAQIQ----GAATSRLGIVTQDVSNMSLSILISFIYGWE-MTLLILSFA---- 834
Cdd:PLN03232 992 SILRAPMLFFH--TNPTGRVINRFSKDIGDIDrnvaNLMNMFMNQLWQLLSTFALIGTVSTISLWAiMPLLILFYAayly 1069
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 835 -----------------PVLAVTGmiqtAAMAGFAN-RDKQALKRAGKIATEAVEN-IR-TVVSLTRERAFeqmyeetlq 894
Cdd:PLN03232 1070 yqstsrevrrldsvtrsPIYAQFG----EALNGLSSiRAYKAYDRMAKINGKSMDNnIRfTLANTSSNRWL--------- 1136
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 895 tqhrnALKRAHITGCCYAVSHAFvhfahaAGFRFGAYLIQAGRMMPEGMFIVFTaiaygaMAIGETLvwapeySKAKAGA 974
Cdd:PLN03232 1137 -----TIRLETLGGVMIWLTATF------AVLRNGNAENQAGFASTMGLLLSYT------LNITTLL------SGVLRQA 1193
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 975 ShlfallKNKPTINSCSQSG-------EKPDTCEGN-----------LEFREVSFVYpcRPEVP-VLQNMSLSIEKGKTV 1035
Cdd:PLN03232 1194 S------KAENSLNSVERVGnyidlpsEATAIIENNrpvsgwpsrgsIKFEDVHLRY--RPGLPpVLHGLSFFVSPSEKV 1265
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1036 AFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVKELNVQWLRSQTAIVSQEPVLFNCSIAENIAygdnsrmvPLEE-- 1113
Cdd:PLN03232 1266 GVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNID--------PFSEhn 1337
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1114 ---IKEVADAANIHSFIEGLPRKYNTLVGLRGVQLSGGQKQRLAIARALLRKPKILLLDEATSALDNESEKVVQQALDKA 1190
Cdd:PLN03232 1338 dadLWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREE 1417
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|.
gi 568980685 1191 RRGKTCLVVAHRLSTIQNADMIVVLQNGSIKEQGTHQELL-RNGDTYFKLV 1240
Cdd:PLN03232 1418 FKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLsRDTSAFFRMV 1468
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
102-584 |
2.61e-64 |
|
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: 228.33 E-value: 2.61e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 102 IGAAALIF------GYVQISFWVITAARQTTRIRKQFFHSILAQDISWFDGSDICELNTRMTGDINKLCDGIGDKIP-LM 174
Cdd:TIGR02857 47 LGALALVLllrallGWLQERAAARAAAAVKSQLRERLLEAVAALGPRWLQGRPSGELATLALEGVEALDGYFARYLPqLV 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 175 FQNISGFSIGLVISLIkSWKLSLVVLSTSPLIMASSALCSRMIISLTSKELDAYSKAGAVAEEALSSIQTVTAFGAQEKE 254
Cdd:TIGR02857 127 LAVIVPLAILAAVFPQ-DWISGLILLLTAPLIPIFMILIGWAAQAAARKQWAALSRLSGHFLDRLRGLPTLKLFGRAKAQ 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 255 IQRytqhLKDAKDAgIKRATASKL-----SLGAVYFFMN-GAYGLAFWYGTSLIFGG---EPGYTIgTILAVFF------ 319
Cdd:TIGR02857 206 AAA----IRRSSEE-YRERTMRVLriaflSSAVLELFATlSVALVAVYIGFRLLAGDldlATGLFV-LLLAPEFylplrq 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 320 --SVIHSSycigsvaphletfTVARGAAFNIFQVIDKKPNIdnFSTAGFVPECIEGNIEFKNVSFSYPSRPsaKVLKGLN 397
Cdd:TIGR02857 280 lgAQYHAR-------------ADGVAAAEALFAVLDAAPRP--LAGKAPVTAAPASSLEFSGVSVAYPGRR--PALRPVS 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 398 LKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDIRAQNVRHYREQIGVVRQEPVLFGTTIGNNIKFGREG 477
Cdd:TIGR02857 343 FTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLARPD 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 478 VGEKEMEQAAREANAYDFIMAFPKKFNTLVGEKGAQMSGGQKQRIAIARALVRNPKILILDEATSALDTESESLVQTALE 557
Cdd:TIGR02857 423 ASDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALR 502
|
490 500
....*....|....*....|....*..
gi 568980685 558 KASKGRTTIVVAHRLSTIRGADLIVTM 584
Cdd:TIGR02857 503 ALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
373-593 |
3.33e-64 |
|
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: 217.07 E-value: 3.33e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 373 GNIEFKNVSFSYPSRPsAKVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDIRAQNVRHYREQ 452
Cdd:cd03245 1 GRIEFRNVSFSYPNQE-IPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 453 IGVVRQEPVLFGTTIGNNIKFGREGVGEKEMEQAAREANAYDFIMAFPKKFNTLVGEKGAQMSGGQKQRIAIARALVRNP 532
Cdd:cd03245 80 IGYVPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568980685 533 KILILDEATSALDTESESLVQTALEKASKGRTTIVVAHRLSTIRGADLIVTMKDGMVVEKG 593
Cdd:cd03245 160 PILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
1002-1225 |
4.01e-64 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 216.98 E-value: 4.01e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1002 GNLEFREVSFVYpcRPE-VPVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVKELNVQWLRS 1080
Cdd:cd03244 1 GDIEFKNVSLRY--RPNlPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1081 QTAIVSQEPVLFNCSIAENIA----YGDnsrmvplEEIKEVADAANIHSFIEGLPRKYNTLVGLRGVQLSGGQKQRLAIA 1156
Cdd:cd03244 79 RISIIPQDPVLFSGTIRSNLDpfgeYSD-------EELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568980685 1157 RALLRKPKILLLDEATSALDNESEKVVQQALDKARRGKTCLVVAHRLSTIQNADMIVVLQNGSIKEQGT 1225
Cdd:cd03244 152 RALLRKSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
682-977 |
1.52e-63 |
|
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: 218.50 E-value: 1.52e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 682 VLGTLASALNGSVHPVFSIIFGKLVTMF-----EDKNKATLKQDAELYSMMLVVLGIVALVTYLMQGLFYGRAEENLAMR 756
Cdd:cd18577 2 IIGLLAAIAAGAALPLMTIVFGDLFDAFtdfgsGESSPDEFLDDVNKYALYFVYLGIGSFVLSYIQTACWTITGERQARR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 757 LRHSAFKAMLYQDMAWYDdkENNTGALTTTLAVDVAQIQGAATSRLGIVTQDVSNMSLSILISFIYGWEMTLLILSFAPV 836
Cdd:cd18577 82 IRKRYLKALLRQDIAWFD--KNGAGELTSRLTSDTNLIQDGIGEKLGLLIQSLSTFIAGFIIAFIYSWKLTLVLLATLPL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 837 LAVTGMIQTAAMAGFANRDKQALKRAGKIATEAVENIRTVVSLTRERAFEQMYEETLQTQHRNALKRAHITGCCYAVSHA 916
Cdd:cd18577 160 IAIVGGIMGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKALEKARKAGIKKGLVSGLGLGLLFF 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568980685 917 FVHFAHAAGFRFGAYLIQAGRMMPEGMFIVFTAIAYGAMAIGETLVWAPEYSKAKAGASHL 977
Cdd:cd18577 240 IIFAMYALAFWYGSRLVRDGEISPGDVLTVFFAVLIGAFSLGQIAPNLQAFAKARAAAAKI 300
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
181-612 |
5.41e-63 |
|
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: 228.30 E-value: 5.41e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 181 FSIGLVisLIKSWKLSLVVLSTSPLIMASSALCSRMiisLTSKELDAYSKAGAVAEEALSSIQTVT----------AFG- 249
Cdd:TIGR03797 265 LNLGLM--FYYSWKLALVAVALALVAIAVTLVLGLL---QVRKERRLLELSGKISGLTVQLINGISklrvagaenrAFAr 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 250 -----AQEKEIQRYTQHLKDAKDagikratasklSLGAVY--FFMngayGLAFWYGTSLifGGEPGYTIGTILAvfFSVI 322
Cdd:TIGR03797 340 waklfSRQRKLELSAQRIENLLT-----------VFNAVLpvLTS----AALFAAAISL--LGGAGLSLGSFLA--FNTA 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 323 HSSYcIGSVAPHLETFTVARgAAFNIFQ----VIDKKPNIDnfsTAGFVPECIEGNIEFKNVSFSYpSRPSAKVLKGLNL 398
Cdd:TIGR03797 401 FGSF-SGAVTQLSNTLISIL-AVIPLWErakpILEALPEVD---EAKTDPGKLSGAIEVDRVTFRY-RPDGPLILDDVSL 474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 399 KIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDIRAQNVRHYREQIGVVRQEPVLFGTTIGNNIKfGREGV 478
Cdd:TIGR03797 475 QIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLDVQAVRRQLGVVLQNGRLMSGSIFENIA-GGAPL 553
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 479 GEKEMEQAAREANAYDFIMAFPKKFNTLVGEKGAQMSGGQKQRIAIARALVRNPKILILDEATSALDTESESLVQTALEK 558
Cdd:TIGR03797 554 TLDEAWEAARMAGLAEDIRAMPMGMHTVISEGGGTLSGGQRQRLLIARALVRKPRILLFDEATSALDNRTQAIVSESLER 633
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 568980685 559 ASKGRttIVVAHRLSTIRGADLIVTMKDGMVVEKGTHAELMAKQGLYYSLAMAQ 612
Cdd:TIGR03797 634 LKVTR--IVIAHRLSTIRNADRIYVLDAGRVVQQGTYDELMAREGLFAQLARRQ 685
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
970-1215 |
8.63e-63 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 223.70 E-value: 8.63e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 970 AKAGASHLFALLKNKPTInsCSQSGEKPDTCEGNLEFREVSFVYPCRPevPVLQNMSLSIEKGKTVAFVGSSGCGKSTCV 1049
Cdd:TIGR02857 290 GVAAAEALFAVLDAAPRP--LAGKAPVTAAPASSLEFSGVSVAYPGRR--PALRPVSFTVPPGERVALVGPSGAGKSTLL 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1050 QLLQRFYDPMKGQVLLDGVDVKELNVQWLRSQTAIVSQEPVLFNCSIAENIAYGDNSrmVPLEEIKEVADAANIHSFIEG 1129
Cdd:TIGR02857 366 NLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLARPD--ASDAEIREALERAGLDEFVAA 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1130 LPRKYNTLVGLRGVQLSGGQKQRLAIARALLRKPKILLLDEATSALDNESEKVVQQALDKARRGKTCLVVAHRLSTIQNA 1209
Cdd:TIGR02857 444 LPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALA 523
|
....*.
gi 568980685 1210 DMIVVL 1215
Cdd:TIGR02857 524 DRIVVL 529
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
728-1231 |
2.70e-62 |
|
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: 223.47 E-value: 2.70e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 728 LVVLGIVALVTYLMQGLF-------YGRAEENLAMRLRHSAFKAMLyqdmawyDDKENNTGALTTTLAVDVAQIQGAATS 800
Cdd:COG4618 59 LLMLTLLALGLYAVMGLLdavrsriLVRVGARLDRRLGPRVFDAAF-------RAALRGGGGAAAQALRDLDTLRQFLTG 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 801 R--------------LGIVTqdvsnmslsiLISFIYGWemtlLILSFAPVLAVTGMIQTAAMAGFANRDKQALKRAGKIA 866
Cdd:COG4618 132 PglfalfdlpwapifLAVLF----------LFHPLLGL----LALVGALVLVALALLNERLTRKPLKEANEAAIRANAFA 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 867 TEAVENIRTVVSL-----TRERaFEQMYEETLQTQHRnALKRAHITGccyAVSHAFVHFAHAAGFRFGAYL-----IQAG 936
Cdd:COG4618 198 EAALRNAEVIEAMgmlpaLRRR-WQRANARALALQAR-ASDRAGGFS---ALSKFLRLLLQSAVLGLGAYLviqgeITPG 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 937 rMMPEGMFIVFTAIAYGAMAIGetlVWAPeYSKAKAGASHLFALLKNKPtinscsqsgEKPDTC-----EGNLEFREVSF 1011
Cdd:COG4618 273 -AMIAASILMGRALAPIEQAIG---GWKQ-FVSARQAYRRLNELLAAVP---------AEPERMplprpKGRLSVENLTV 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1012 VYPCRpEVPVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVKelnvQWLRSQ--TAI--VSQ 1087
Cdd:COG4618 339 VPPGS-KRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLS----QWDREElgRHIgyLPQ 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1088 EPVLFNCSIAENIAygdnsRM--VPLEEIKEVADAANIHSFIEGLPRKYNTLVGLRGVQLSGGQKQRLAIARALLRKPKI 1165
Cdd:COG4618 414 DVELFDGTIAENIA-----RFgdADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRL 488
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568980685 1166 LLLDEATSALDNESEKVVQQALDKAR-RGKTCLVVAHRLSTIQNADMIVVLQNGSIKEQGTHQELLR 1231
Cdd:COG4618 489 VVLDEPNSNLDDEGEAALAAAIRALKaRGATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLA 555
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
117-605 |
8.41e-61 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 219.20 E-value: 8.41e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 117 WVITAARQ-TTRIRKQFFHSILAQDISWFDGSDICELNTRMTGDINKLCDGIGDKI-PLMFQNISGFSIGLVISLIKSWK 194
Cdd:PRK10789 59 LLFGASYQlAVELREDFYRQLSRQHPEFYLRHRTGDLMARATNDVDRVVFAAGEGVlTLVDSLVMGCAVLIVMSTQISWQ 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 195 LSLVVLSTSPlIMAssalcsrMIISLTSKELD--------AYSKAGAVAEEALSSIQTVTAFGAQEKEIQRYTQhlkDAK 266
Cdd:PRK10789 139 LTLLALLPMP-VMA-------IMIKRYGDQLHerfklaqaAFSSLNDRTQESLTSIRMIKAFGLEDRQSALFAA---DAE 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 267 DAGIKR------------------ATASKLSL-GAVYFFMNGAYGLafwyGTSLIFGGEPGYTIGTILAV--FFSVihss 325
Cdd:PRK10789 208 DTGKKNmrvaridarfdptiyiaiGMANLLAIgGGSWMVVNGSLTL----GQLTSFVMYLGLMIWPMLALawMFNI---- 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 326 ycigsvaphletftVARG-AAFN-IFQVIDKKPNIDNFSTAgfVPEcIEGNIEFKNVSFSYPSRpSAKVLKGLNLKIKAG 403
Cdd:PRK10789 280 --------------VERGsAAYSrIRAMLAEAPVVKDGSEP--VPE-GRGELDVNIRQFTYPQT-DHPALENVNFTLKPG 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 404 ETVALVGPSGSGKSTTVQLLQRLYDpedgcitVDENDIRAQNVR-------HYREQIGVVRQEPVLFGTTIGNNIKFGRE 476
Cdd:PRK10789 342 QMLGICGPTGSGKSTLLSLIQRHFD-------VSEGDIRFHDIPltklqldSWRSRLAVVSQTPFLFSDTVANNIALGRP 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 477 GVGEKEMEQAAREANAYDFIMAFPKKFNTLVGEKGAQMSGGQKQRIAIARALVRNPKILILDEATSALDTESESLVQTAL 556
Cdd:PRK10789 415 DATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNL 494
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 568980685 557 EKASKGRTTIVVAHRLSTIRGADLIVTMKDGMVVEKGTHAELMAKQGLY 605
Cdd:PRK10789 495 RQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSGWY 543
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
727-1230 |
3.97e-59 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 214.19 E-value: 3.97e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 727 MLVVLGIVALVTYLMQGLFYGrAEENLAMRLRHSAFKAMLYQDMAWYddKENNTGALTTTLAVDVAQIQGAATSrlGIVT 806
Cdd:PRK10789 42 MVLIAVVVYLLRYVWRVLLFG-ASYQLAVELREDFYRQLSRQHPEFY--LRHRTGDLMARATNDVDRVVFAAGE--GVLT 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 807 Q-DVSNMSLSILI--SFIYGWEMTLLILSFAPVLAVtgMIQ----------TAAMAGFANRDKQAlkragkiaTEAVENI 873
Cdd:PRK10789 117 LvDSLVMGCAVLIvmSTQISWQLTLLALLPMPVMAI--MIKrygdqlherfKLAQAAFSSLNDRT--------QESLTSI 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 874 RTVVSLTRE----RAFEQMYEETLQTQHRNALKRAHITGCCYaVSHAFVHFAHAAGfrfGAYLIQAGRMMpEGMFIVFta 949
Cdd:PRK10789 187 RMIKAFGLEdrqsALFAADAEDTGKKNMRVARIDARFDPTIY-IAIGMANLLAIGG---GSWMVVNGSLT-LGQLTSF-- 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 950 IAYGAMAIGETLVWAPEYS---KAKAGASHLFALLKNKPTINSCSQSgeKPDTcEGNLEFREVSFVYPcRPEVPVLQNMS 1026
Cdd:PRK10789 260 VMYLGLMIWPMLALAWMFNiveRGSAAYSRIRAMLAEAPVVKDGSEP--VPEG-RGELDVNIRQFTYP-QTDHPALENVN 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1027 LSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVKELNVQWLRSQTAIVSQEPVLFNCSIAENIAYG--D 1104
Cdd:PRK10789 336 FTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNIALGrpD 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1105 NSRmvplEEIKEVADAANIHSFIEGLPRKYNTLVGLRGVQLSGGQKQRLAIARALLRKPKILLLDEATSALDNESEKVVQ 1184
Cdd:PRK10789 416 ATQ----QEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQIL 491
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 568980685 1185 QALDKARRGKTCLVVAHRLSTIQNADMIVVLQNGSIKEQGTHQELL 1230
Cdd:PRK10789 492 HNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLA 537
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
344-608 |
8.46e-58 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 210.45 E-value: 8.46e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 344 AAFNIFQVIDKKPNIDnFSTAGfVPECIEGNIEFKNVSFSYPSRPSaKVLKGLNLKIKAGETVALVGPSGSGKSTTVQLL 423
Cdd:PRK11160 310 SARRINEITEQKPEVT-FPTTS-TAAADQVSLTLNNVSFTYPDQPQ-PVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLL 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 424 QRLYDPEDGCITVDENDIRAQNVRHYREQIGVVRQEPVLFGTTIGNNIKFGREGVGEKEMEQAAREANaYDFIMAFPKKF 503
Cdd:PRK11160 387 TRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLLAAPNASDEALIEVLQQVG-LEKLLEDDKGL 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 504 NTLVGEKGAQMSGGQKQRIAIARALVRNPKILILDEATSALDTESESLVQTALEKASKGRTTIVVAHRLSTIRGADLIVT 583
Cdd:PRK11160 466 NAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRICV 545
|
250 260
....*....|....*....|....*
gi 568980685 584 MKDGMVVEKGTHAELMAKQGLYYSL 608
Cdd:PRK11160 546 MDNGQIIEQGTHQELLAQQGRYYQL 570
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
24-605 |
9.96e-58 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 219.52 E-value: 9.96e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 24 EIFRFADnlDIVLMTLGIlasMINGATVPLMSLVLGEISDHLINGCLVQTNRTKYqncsqtqeklnediivlTLYYIGIG 103
Cdd:PTZ00265 819 EIFSYKK--DVTIIALSI---LVAGGLYPVFALLYAKYVSTLFDFANLEANSNKY-----------------SLYILVIA 876
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 104 AAALIFGYVQISFWVITAARQTTRIRKQFFHSILAQDISWFDGSDICE--LNTRMTGDINKLCDGIGDKIPLMFQNISGF 181
Cdd:PTZ00265 877 IAMFISETLKNYYNNVIGEKVEKTMKRRLFENILYQEISFFDQDKHAPglLSAHINRDVHLLKTGLVNNIVIFTHFIVLF 956
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 182 SIGLVISLIKSWKLSLVVLSTSPLIMASSALCSRMIIS--LTSKELDAYSKAGA-------------VAEEALSSIQTVT 246
Cdd:PTZ00265 957 LVSMVMSFYFCPIVAAVLTGTYFIFMRVFAIRARLTANkdVEKKEINQPGTVFAynsddeifkdpsfLIQEAFYNMNTVI 1036
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 247 AFGAqEKEIQRYTQHLKDAKDAGIKRATASKLSL----GAVYFFMNGaygLAFWYGTSLIfggepgyTIGTILAV-FFSV 321
Cdd:PTZ00265 1037 IYGL-EDYFCNLIEKAIDYSNKGQKRKTLVNSMLwgfsQSAQLFINS---FAYWFGSFLI-------RRGTILVDdFMKS 1105
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 322 IHSSYCIGSVAPHLETFtvaRGAAFNI-------FQVIDKKPNIDNFSTAGFV---PECIEGNIEFKNVSFSYPSRPSAK 391
Cdd:PTZ00265 1106 LFTFLFTGSYAGKLMSL---KGDSENAklsfekyYPLIIRKSNIDVRDNGGIRiknKNDIKGKIEIMDVNFRYISRPNVP 1182
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 392 VLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPED---------------------------------------- 431
Cdd:PTZ00265 1183 IYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLKNdhhivfknehtndmtneqdyqgdeeqnvgmknvnefsltk 1262
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 432 --------------GCITVDENDIRAQNVRHYREQIGVVRQEPVLFGTTIGNNIKFGREGVGEKEMEQAAREANAYDFIM 497
Cdd:PTZ00265 1263 eggsgedstvfknsGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKEDATREDVKRACKFAAIDEFIE 1342
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 498 AFPKKFNTLVGEKGAQMSGGQKQRIAIARALVRNPKILILDEATSALDTESESLVQTALE--KASKGRTTIVVAHRLSTI 575
Cdd:PTZ00265 1343 SLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVdiKDKADKTIITIAHRIASI 1422
|
650 660 670
....*....|....*....|....*....|....*.
gi 568980685 576 RGADLIVTM----KDGMVVE-KGTHAELMAKQ-GLY 605
Cdd:PTZ00265 1423 KRSDKIVVFnnpdRTGSFVQaHGTHEELLSVQdGVY 1458
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
372-1230 |
9.94e-57 |
|
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: 216.35 E-value: 9.94e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 372 EGN-IEFKNVSFSYpSRPSAKVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCItvdendiraqnvrHYR 450
Cdd:TIGR00957 633 EGNsITVHNATFTW-ARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHV-------------HMK 698
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 451 EQIGVVRQEPVLFGTTIGNNIKFGREGvgEKEMEQAAREANAY--DFIMaFPKKFNTLVGEKGAQMSGGQKQRIAIARAL 528
Cdd:TIGR00957 699 GSVAYVPQQAWIQNDSLRENILFGKAL--NEKYYQQVLEACALlpDLEI-LPSGDRTEIGEKGVNLSGGQKQRVSLARAV 775
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 529 VRNPKILILDEATSALDTE-SESLVQTAL--EKASKGRTTIVVAHRLSTIRGADLIVTMKDGMVVEKGTHAELMAKQGLY 605
Cdd:TIGR00957 776 YSNADIYLFDDPLSAVDAHvGKHIFEHVIgpEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAF 855
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 606 YSL----AMAQDIKKVDE--------------QME-----------------SRTCSTAGNAS--YGSLCDVNSAKAPCT 648
Cdd:TIGR00957 856 AEFlrtyAPDEQQGHLEDswtalvsgegkeakLIEngmlvtdvvgkqlqrqlSASSSDSGDQSrhHGSSAELQKAEAKEE 935
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 649 D-QLEEAvhhQKTSLPEVSLLKIFKLSKSEWPFVVLGTLASALNGSVHPVFSIIFGKLVT--MFEDKNKATLKQDAELYS 725
Cdd:TIGR00957 936 TwKLMEA---DKAQTGQVELSVYWDYMKAIGLFITFLSIFLFVCNHVSALASNYWLSLWTddPMVNGTQNNTSLRLSVYG 1012
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 726 MMLVVLGIvALVTYLMQ----GLFYGRAeenLAMRLRHSAFKAmlyqDMAWYDdkENNTGALTTTLAVDvaqiqgaatsr 801
Cdd:TIGR00957 1013 ALGILQGF-AVFGYSMAvsigGIQASRV---LHQDLLHNKLRS----PMSFFE--RTPSGNLVNRFSKE----------- 1071
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 802 LGIVTQDVSNMSLSILISFIYGWEMTLLILSFAPVLAVT----GMIQTAAMAGFANRDKQaLKRAGKIA--------TEA 869
Cdd:TIGR00957 1072 LDTVDSMIPPVIKMFMGSLFNVIGALIVILLATPIAAVIipplGLLYFFVQRFYVASSRQ-LKRLESVSrspvyshfNET 1150
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 870 VENIRTVVSLTRERAFEQMYEETLQTQHRNALK----------RAHITGCC-------YAV------SHAFVHFAHAAGF 926
Cdd:TIGR00957 1151 LLGVSVIRAFEEQERFIHQSDLKVDENQKAYYPsivanrwlavRLECVGNCivlfaalFAVisrhslSAGLVGLSVSYSL 1230
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 927 RFGAYLIQAGRMMPEgMFIVFTAIaygamaigETLvwaPEYSKAKAGAShlFALLKNKPTiNSCSQSGEkpdtcegnLEF 1006
Cdd:TIGR00957 1231 QVTFYLNWLVRMSSE-METNIVAV--------ERL---KEYSETEKEAP--WQIQETAPP-SGWPPRGR--------VEF 1287
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1007 REVSFVYpcRPEVP-VLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVKELNVQWLRSQTAIV 1085
Cdd:TIGR00957 1288 RNYCLRY--REDLDlVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITII 1365
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1086 SQEPVLFNCSIAENI----AYGDnsrmvplEEIKEVADAANIHSFIEGLPRKYNTLVGLRGVQLSGGQKQRLAIARALLR 1161
Cdd:TIGR00957 1366 PQDPVLFSGSLRMNLdpfsQYSD-------EEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLR 1438
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568980685 1162 KPKILLLDEATSALDNESEKVVQQALDKARRGKTCLVVAHRLSTIQNADMIVVLQNGSIKEQGTHQELL 1230
Cdd:TIGR00957 1439 KTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLL 1507
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
984-1239 |
2.27e-56 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 206.21 E-value: 2.27e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 984 KPTINSCSQSGEKPDtcEGNLEFREVSFVYPCRPEvPVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQV 1063
Cdd:PRK11160 321 KPEVTFPTTSTAAAD--QVSLTLNNVSFTYPDQPQ-PVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEI 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1064 LLDGVDVKELNVQWLRSQTAIVSQEPVLFNCSIAENIAYGDNSrmVPLEEIKEVADAANIHSFIEGlPRKYNTLVGLRGV 1143
Cdd:PRK11160 398 LLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLLAAPN--ASDEALIEVLQQVGLEKLLED-DKGLNAWLGEGGR 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1144 QLSGGQKQRLAIARALLRKPKILLLDEATSALDNESEKVVQQALDKARRGKTCLVVAHRLSTIQNADMIVVLQNGSIKEQ 1223
Cdd:PRK11160 475 QLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQ 554
|
250
....*....|....*.
gi 568980685 1224 GTHQELLRNGDTYFKL 1239
Cdd:PRK11160 555 GTHQELLAQQGRYYQL 570
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
195-572 |
1.49e-55 |
|
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: 202.59 E-value: 1.49e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 195 LSLVVLSTSPLIMASSALCSRMIISLTSKELDAYSKA------GAVAEEALSSIQ---TVTAFGAQEKEIQRYTQHLKDA 265
Cdd:TIGR02868 147 AIAVLSVPAALILAAGLLLAGFVAPLVSLRAARAAEQalarlrGELAAQLTDALDgaaELVASGALPAALAQVEEADREL 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 266 KDAGIKRATASKLSLGAVYFFMNGAYGLAFWYGtslIFGGEPGYTIGTILAVF----FSVIHSSYCIGSVAPHLETftvA 341
Cdd:TIGR02868 227 TRAERRAAAATALGAALTLLAAGLAVLGALWAG---GPAVADGRLAPVTLAVLvllpLAAFEAFAALPAAAQQLTR---V 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 342 RGAAFNIFQVIDKKPNIDNFSTAGFVPECIEG-NIEFKNVSFSYPsrPSAKVLKGLNLKIKAGETVALVGPSGSGKSTTV 420
Cdd:TIGR02868 301 RAAAERIVEVLDAAGPVAEGSAPAAGAVGLGKpTLELRDLSAGYP--GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLL 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 421 QLLQRLYDPEDGCITVDENDIRAQNVRHYREQIGVVRQEPVLFGTTIGNNIKFGREGVGEKEMEQAAREANAYDFIMAFP 500
Cdd:TIGR02868 379 ATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPDATDEELWAALERVGLADWLRALP 458
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568980685 501 KKFNTLVGEKGAQMSGGQKQRIAIARALVRNPKILILDEATSALDTESESLVQTALEKASKGRTTIVVAHRL 572
Cdd:TIGR02868 459 DGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
1002-1239 |
1.16e-54 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 201.49 E-value: 1.16e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1002 GNLEFREVSFVYpcRPEVPVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVKELNVQWLRSQ 1081
Cdd:PRK10790 339 GRIDIDNVSFAY--RDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQG 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1082 TAIVSQEPVLFNCSIAENIAYGdnsRMVPLEEIKEVADAANIHSFIEGLPRKYNTLVGLRGVQLSGGQKQRLAIARALLR 1161
Cdd:PRK10790 417 VAMVQQDPVVLADTFLANVTLG---RDISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQ 493
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568980685 1162 KPKILLLDEATSALDNESEKVVQQALDKARRGKTCLVVAHRLSTIQNADMIVVLQNGSIKEQGTHQELLRNGDTYFKL 1239
Cdd:PRK10790 494 TPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQGRYWQM 571
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
728-1230 |
3.60e-54 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 199.11 E-value: 3.60e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 728 LVVLGIVALVTYLMQGLFYG-------RAEENLAMRLRHSAFKAMLYQDMawyddkENNTGALTTTLAvDVAQIQGAATS 800
Cdd:TIGR01842 45 LLMLTVLALGLYLFLGLLDAlrsfvlvRIGEKLDGALNQPIFAASFSATL------RRGSGDGLQALR-DLDQLRQFLTG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 801 RLGIVTQDVSNMSLSILISFIYGWEMTLLILSFAPVLAVTGMIQTAAMAGFANRDKQALKRAGKIATEAVENIRTVVSLT 880
Cdd:TIGR01842 118 PGLFAFFDAPWMPIYLLVCFLLHPWIGILALGGAVVLVGLALLNNRATKKPLKEATEASIRANNLADSALRNAEVIEAMG 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 881 RERAFEQMYEETLQ---TQHRNALKRAHITGccyAVSHAFVHFAHAAGFRFGAYLIQAGRMMPeGMFIVFTAIAYGAMAI 957
Cdd:TIGR01842 198 MMGNLTKRWGRFHSkylSAQSAASDRAGMLS---NLSKYFRIVLQSLVLGLGAYLAIDGEITP-GMMIAGSILVGRALAP 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 958 GETLV--WApEYSKAKAGASHLFALLKNKPTiNSCSQSGEKPdtcEGNLEFREVSFVYPcRPEVPVLQNMSLSIEKGKTV 1035
Cdd:TIGR01842 274 IDGAIggWK-QFSGARQAYKRLNELLANYPS-RDPAMPLPEP---EGHLSVENVTIVPP-GGKKPTLRGISFSLQAGEAL 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1036 AFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVKELNVQWLRSQTAIVSQEPVLFNCSIAENIA-YGDNsrmVPLEEI 1114
Cdd:TIGR01842 348 AIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKHIGYLPQDVELFPGTVAENIArFGEN---ADPEKI 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1115 KEVADAANIHSFIEGLPRKYNTLVGLRGVQLSGGQKQRLAIARALLRKPKILLLDEATSALDNESEKVVQQALDKAR-RG 1193
Cdd:TIGR01842 425 IEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALKaRG 504
|
490 500 510
....*....|....*....|....*....|....*..
gi 568980685 1194 KTCLVVAHRLSTIQNADMIVVLQNGSIKEQGTHQELL 1230
Cdd:TIGR01842 505 ITVVVITHRPSLLGCVDKILVLQDGRIARFGERDEVL 541
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
372-601 |
4.23e-54 |
|
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: 199.20 E-value: 4.23e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 372 EGNIEFKNVSFSYPSRPSAkVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDIRAQNVRHYRE 451
Cdd:COG4618 328 KGRLSVENLTVVPPGSKRP-ILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGR 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 452 QIGVVRQEPVLFGTTIGNNI-KFG---REGVGEkemeqAAREANAYDFIMAFPKKFNTLVGEKGAQMSGGQKQRIAIARA 527
Cdd:COG4618 407 HIGYLPQDVELFDGTIAENIaRFGdadPEKVVA-----AAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARA 481
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568980685 528 LVRNPKILILDEATSALDTESESLVQTALEKA-SKGRTTIVVAHRLSTIRGADLIVTMKDGMVVEKGTHAELMAK 601
Cdd:COG4618 482 LYGDPRLVVLDEPNSNLDDEGEAALAAAIRALkARGATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
388-608 |
5.55e-54 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 199.30 E-value: 5.55e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 388 PSAKVLKG-LNLKIKAGETVALVGPSGSGKSTTVQLLqrL-YDPEDGCITVDENDIRAQNVRHYREQIGVVRQEPVLFGT 465
Cdd:PRK11174 360 PDGKTLAGpLNFTLPAGQRIALVGPSGAGKTSLLNAL--LgFLPYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHG 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 466 TIGNNIKFGREGVGEKEMEQAAREANAYDFIMAFPKKFNTLVGEKGAQMSGGQKQRIAIARALVRNPKILILDEATSALD 545
Cdd:PRK11174 438 TLRDNVLLGNPDASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLD 517
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568980685 546 TESESLVQTALEKASKGRTTIVVAHRLSTIRGADLIVTMKDGMVVEKGTHAELMAKQGLYYSL 608
Cdd:PRK11174 518 AHSEQLVMQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATL 580
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
87-608 |
1.09e-53 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 201.12 E-value: 1.09e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 87 KLNEDIIVLTLYYIGIGAAALIFGYVQISFWVITAARQTTRIRKQFFHSILAQDISWFDGSDICELNTRMTgDINKLCDG 166
Cdd:TIGR01193 190 KMMGTLGIISIGLIIAYIIQQILSYIQIFLLNVLGQRLSIDIILSYIKHLFELPMSFFSTRRTGEIVSRFT-DASSIIDA 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 167 IGDKIPLMFQNISGFSIGLVISLIKSWKLSLVVLSTSPLIMASSALCSRMIISLTSKELDAYSKAGAVAEEALSSIQTVT 246
Cdd:TIGR01193 269 LASTILSLFLDMWILVIVGLFLVRQNMLLFLLSLLSIPVYAVIIILFKRTFNKLNHDAMQANAVLNSSIIEDLNGIETIK 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 247 AFGAQEKEIQRYT--------QHLKDAKDAGIKRA--TASKLSLGAVyffmngayglAFWYGTSLIFGGEpgYTIGTILA 316
Cdd:TIGR01193 349 SLTSEAERYSKIDsefgdylnKSFKYQKADQGQQAikAVTKLILNVV----------ILWTGAYLVMRGK--LTLGQLIT 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 317 vfFSVIHSSYC-----IGSVAPHLETFTVARGAAFNIFQV---IDKKPNIDNFSTagfvpecIEGNIEFKNVSFSYPSrp 388
Cdd:TIGR01193 417 --FNALLSYFLtplenIINLQPKLQAARVANNRLNEVYLVdseFINKKKRTELNN-------LNGDIVINDVSYSYGY-- 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 389 SAKVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDIRAQNVRHYREQIGVVRQEPVLFGTTIG 468
Cdd:TIGR01193 486 GSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSIL 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 469 NNIKFG-REGVGEKEMEQAAREANAYDFIMAFPKKFNTLVGEKGAQMSGGQKQRIAIARALVRNPKILILDEATSALDTE 547
Cdd:TIGR01193 566 ENLLLGaKENVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTI 645
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568980685 548 SESLVQTALEKAsKGRTTIVVAHRLSTIRGADLIVTMKDGMVVEKGTHAELMAKQGLYYSL 608
Cdd:TIGR01193 646 TEKKIVNNLLNL-QDKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYASL 705
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
373-612 |
1.35e-53 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 198.40 E-value: 1.35e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 373 GNIEFKNVSFSYpsRPSAKVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDIRAQNVRHYREQ 452
Cdd:PRK10790 339 GRIDIDNVSFAY--RDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQG 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 453 IGVVRQEPVLFGTTIGNNIKFGREgVGEKEMEQAAREANAYDFIMAFPKKFNTLVGEKGAQMSGGQKQRIAIARALVRNP 532
Cdd:PRK10790 417 VAMVQQDPVVLADTFLANVTLGRD-ISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTP 495
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 533 KILILDEATSALDTESESLVQTALEKASKGRTTIVVAHRLSTIRGADLIVTMKDGMVVEKGTHAELMAKQGLYYSLAMAQ 612
Cdd:PRK10790 496 QILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQGRYWQMYQLQ 575
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
375-602 |
6.57e-53 |
|
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: 185.23 E-value: 6.57e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 375 IEFKNVSFSYPsrPSAKVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDIRAQNVRHYREQIG 454
Cdd:COG1122 1 IELENLSFSYP--GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 455 VVRQEPV--LFGTTIGNNIKFGRE--GVGEKEMEQAAREA----NAYDFIMAFPkkfntlvgekgAQMSGGQKQRIAIAR 526
Cdd:COG1122 79 LVFQNPDdqLFAPTVEEDVAFGPEnlGLPREEIRERVEEAlelvGLEHLADRPP-----------HELSGGQKQRVAIAG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568980685 527 ALVRNPKILILDEATSALDTESESLVQTALEK-ASKGRTTIVVAHRLSTIRG-ADLIVTMKDGMVVEKGTHAELMAKQ 602
Cdd:COG1122 148 VLAMEPEVLVLDEPTAGLDPRGRRELLELLKRlNKEGKTVIIVTHDLDLVAElADRVIVLDDGRIVADGTPREVFSDY 225
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
375-1237 |
1.56e-52 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 203.05 E-value: 1.56e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 375 IEFKNVSFSYPSRPSAKVLKGLNLKIKAGETVALVGPSGSGKSTTVQ-LLQRLYDPEDGCITVdendiraqnvrhyREQI 453
Cdd:PLN03130 615 ISIKNGYFSWDSKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISaMLGELPPRSDASVVI-------------RGTV 681
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 454 GVVRQEPVLFGTTIGNNIKFGREGVGEKeMEQAAREANAYDFIMAFPKKFNTLVGEKGAQMSGGQKQRIAIARALVRNPK 533
Cdd:PLN03130 682 AYVPQVSWIFNATVRDNILFGSPFDPER-YERAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSD 760
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 534 ILILDEATSALDTE-SESLVQTALEKASKGRTTIVVAHRLSTIRGADLIVTMKDGMVVEKGTHAELMAKQGLYYSLAmaQ 612
Cdd:PLN03130 761 VYIFDDPLSALDAHvGRQVFDKCIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSNNGPLFQKLM--E 838
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 613 DIKKVDEQMESRTCSTAGNASYGSLCDVNsakapcTDQLEEAVHHQKTSLPEVSLLkiFKLSKSEWPFV---VLGTLASA 689
Cdd:PLN03130 839 NAGKMEEYVEENGEEEDDQTSSKPVANGN------ANNLKKDSSSKKKSKEGKSVL--IKQEERETGVVswkVLERYKNA 910
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 690 LNGSVhpVFSIIFGKLVT-----------MFEDKNKATLKQDAELYSMM---LVVLGIVaLVT-----YLMQGLFYGrae 750
Cdd:PLN03130 911 LGGAW--VVMILFLCYVLtevfrvssstwLSEWTDQGTPKTHGPLFYNLiyaLLSFGQV-LVTllnsyWLIMSSLYA--- 984
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 751 enlAMRLRHSAFKAMLYQDMAWYddKENNTGALTTTLAVDVAQIQGA----ATSRLGIVTQDVSNMSLSILISFIYGWE- 825
Cdd:PLN03130 985 ---AKRLHDAMLGSILRAPMSFF--HTNPLGRIINRFAKDLGDIDRNvavfVNMFLGQIFQLLSTFVLIGIVSTISLWAi 1059
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 826 MTLLILSFAPVLavtgMIQTAAmagfanrdkQALKRAGKIATEAV-----ENIRTVVSLTRERAFEQMYEETLQTQHRNA 900
Cdd:PLN03130 1060 MPLLVLFYGAYL----YYQSTA---------REVKRLDSITRSPVyaqfgEALNGLSTIRAYKAYDRMAEINGRSMDNNI 1126
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 901 lkrahitgccyavshafvhfahaagfRFGAYLIQAGRMMP------EGMFIVFTAI------------AYGAMAIGETLV 962
Cdd:PLN03130 1127 --------------------------RFTLVNMSSNRWLAirletlGGLMIWLTASfavmqngraenqAAFASTMGLLLS 1180
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 963 WAPEYSKAKAGASHLFALLKNkpTINSCSQSG-------EKPDTCEGN-----------LEFREVSFVYpcRPEVP-VLQ 1023
Cdd:PLN03130 1181 YALNITSLLTAVLRLASLAEN--SLNAVERVGtyidlpsEAPLVIENNrpppgwpssgsIKFEDVVLRY--RPELPpVLH 1256
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1024 NMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVKELNVQWLRSQTAIVSQEPVLFNCSIAENIAyg 1103
Cdd:PLN03130 1257 GLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNLD-- 1334
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1104 dnsrmvPLEE-----IKEVADAANIHSFIEGLPRKYNTLVGLRGVQLSGGQKQRLAIARALLRKPKILLLDEATSALDNE 1178
Cdd:PLN03130 1335 ------PFNEhndadLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVR 1408
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|....*....
gi 568980685 1179 SEKVVQQALDKARRGKTCLVVAHRLSTIQNADMIVVLQNGSIKEQGTHQELLRNGDTYF 1237
Cdd:PLN03130 1409 TDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEGSAF 1467
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
1004-1235 |
2.59e-52 |
|
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: 183.30 E-value: 2.59e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1004 LEFREVSFVYPcrPEVPVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVKELNVQWLRSQTA 1083
Cdd:COG1122 1 IELENLSFSYP--GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1084 IVSQEPV--LFNCSIAENIAYGDNSRMVPLEEIKEVADAAnihsfiegLprkynTLVGLRGV------QLSGGQKQRLAI 1155
Cdd:COG1122 79 LVFQNPDdqLFAPTVEEDVAFGPENLGLPREEIRERVEEA--------L-----ELVGLEHLadrpphELSGGQKQRVAI 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1156 ARALLRKPKILLLDEATSALDNESEKVVQQALDK-ARRGKTCLVVAHRLSTI-QNADMIVVLQNGSIKEQGTHQELLRNG 1233
Cdd:COG1122 146 AGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRlNKEGKTVIIVTHDLDLVaELADRVIVLDDGRIVADGTPREVFSDY 225
|
..
gi 568980685 1234 DT 1235
Cdd:COG1122 226 EL 227
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1020-1242 |
9.39e-52 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 192.75 E-value: 9.39e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1020 PVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYdPMKGQVLLDGVDVKELNVQWLRSQTAIVSQEPVLFNCSIAEN 1099
Cdd:PRK11174 364 TLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDN 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1100 IAYGDNSrmVPLEEIKEVADAANIHSFIEGLPRKYNTLVGLRGVQLSGGQKQRLAIARALLRKPKILLLDEATSALDNES 1179
Cdd:PRK11174 443 VLLGNPD--ASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHS 520
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568980685 1180 EKVVQQALDKARRGKTCLVVAHRLSTIQNADMIVVLQNGSIKEQGTHQELLRNGDTYFKLVAA 1242
Cdd:PRK11174 521 EQLVMQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATLLAH 583
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
376-587 |
1.59e-51 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 180.36 E-value: 1.59e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 376 EFKNVSFSYPSRPSaKVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDIRAQNVRHYREQIGV 455
Cdd:cd03225 1 ELKNLSFSYPDGAR-PALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 456 VRQEP--VLFGTTIGNNIKFGRE--GVGEKEMEQAAREANAydfimafpkkfntLVGEKG------AQMSGGQKQRIAIA 525
Cdd:cd03225 80 VFQNPddQFFGPTVEEEVAFGLEnlGLPEEEIEERVEEALE-------------LVGLEGlrdrspFTLSGGQKQRVAIA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568980685 526 RALVRNPKILILDEATSALDTESESLVQTALEK-ASKGRTTIVVAHRLSTIRG-ADLIVTMKDG 587
Cdd:cd03225 147 GVLAMDPDILLLDEPTAGLDPAGRRELLELLKKlKAEGKTIIIVTHDLDLLLElADRVIVLEDG 210
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
681-951 |
1.43e-49 |
|
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: 177.06 E-value: 1.43e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 681 VVLGTLASALNGSVHPVFSIIFGKLV-TMFEDKNKATLKQDaeLYSMMLVVLGIVALVTYLMQGLFYGRAEENLAMRLRH 759
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILdVLLPDGDPETQALN--VYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 760 SAFKAMLYQDMAWYDDkeNNTGALTTTLAVDVAQIQGAATSRLGIVTQDVSNMSLSILISFIYGWEMTLLILSFAPVLAV 839
Cdd:pfam00664 79 KLFKKILRQPMSFFDT--NSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYIL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 840 TGMIQTAAMAGFANRDKQALKRAGKIATEAVENIRTVVSLTRERAFEQMYEETLQTQHRNALKRAHITGCCYAVSHAFVH 919
Cdd:pfam00664 157 VSAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGY 236
|
250 260 270
....*....|....*....|....*....|..
gi 568980685 920 FAHAAGFRFGAYLIQAGRMMPeGMFIVFTAIA 951
Cdd:pfam00664 237 LSYALALWFGAYLVISGELSV-GDLVAFLSLF 267
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
375-589 |
1.14e-48 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 170.86 E-value: 1.14e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 375 IEFKNVSFSYPSRpSAKVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDIRAQNVRHYREQIG 454
Cdd:cd03246 1 LEVENVSFRYPGA-EPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 455 VVRQEPVLFGTTIGNNIkfgregvgekemeqaareanaydfimafpkkfntlvgekgaqMSGGQKQRIAIARALVRNPKI 534
Cdd:cd03246 80 YLPQDDELFSGSIAENI------------------------------------------LSGGQRQRLGLARALYGNPRI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 568980685 535 LILDEATSALDTESESLVQTALEKASK-GRTTIVVAHRLSTIRGADLIVTMKDGMV 589
Cdd:cd03246 118 LVLDEPNSHLDVEGERALNQAIAALKAaGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
372-601 |
3.00e-48 |
|
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: 181.39 E-value: 3.00e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 372 EGNIEFKNVSFSYPSrPSAKVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDIRAQNVRHYRE 451
Cdd:TIGR01842 314 EGHLSVENVTIVPPG-GKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGK 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 452 QIGVVRQEPVLFGTTIGNNI-KFGREGVGEKEMEqAAREANAYDFIMAFPKKFNTLVGEKGAQMSGGQKQRIAIARALVR 530
Cdd:TIGR01842 393 HIGYLPQDVELFPGTVAENIaRFGENADPEKIIE-AAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALARALYG 471
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568980685 531 NPKILILDEATSALDTESESLVQTALEKASK-GRTTIVVAHRLSTIRGADLIVTMKDGMVVEKGTHAELMAK 601
Cdd:TIGR01842 472 DPKLVVLDEPNSNLDEEGEQALANAIKALKArGITVVVITHRPSLLGCVDKILVLQDGRIARFGERDEVLAK 543
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1004-1232 |
3.53e-48 |
|
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: 180.48 E-value: 3.53e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1004 LEFREVSFVYPCRP--EVPVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVKELN---VQWL 1078
Cdd:COG1123 261 LEVRNLSKRYPVRGkgGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSrrsLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1079 RSQTAIVSQEPVL-FNC--SIAENIAYG-DNSRMVPLEEIKEVADAAnihsfIE--GLPRKYntlVGLRGVQLSGGQKQR 1152
Cdd:COG1123 341 RRRVQMVFQDPYSsLNPrmTVGDIIAEPlRLHGLLSRAERRERVAEL-----LErvGLPPDL---ADRYPHELSGGQRQR 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1153 LAIARALLRKPKILLLDEATSALDnesekVVQQA--LD-----KARRGKTCLVVAHRLSTIQN-ADMIVVLQNGSIKEQG 1224
Cdd:COG1123 413 VAIARALALEPKLLILDEPTSALD-----VSVQAqiLNllrdlQRELGLTYLFISHDLAVVRYiADRVAVMYDGRIVEDG 487
|
....*...
gi 568980685 1225 THQELLRN 1232
Cdd:COG1123 488 PTEEVFAN 495
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
1002-1240 |
8.49e-48 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 183.40 E-value: 8.49e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1002 GNLEFREVSFVYP-CRPevpVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVKELNVQWLRS 1080
Cdd:TIGR01193 472 GDIVINDVSYSYGyGSN---ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQ 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1081 QTAIVSQEPVLFNCSIAENIAYGdNSRMVPLEEIKEVADAANIHSFIEGLPRKYNTLVGLRGVQLSGGQKQRLAIARALL 1160
Cdd:TIGR01193 549 FINYLPQEPYIFSGSILENLLLG-AKENVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALL 627
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1161 RKPKILLLDEATSALDNESEKVVQQALDKARRgKTCLVVAHRLSTIQNADMIVVLQNGSIKEQGTHQELLRNGDTYFKLV 1240
Cdd:TIGR01193 628 TDSKVLILDESTSNLDTITEKKIVNNLLNLQD-KTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYASLI 706
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
1004-1220 |
1.29e-47 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 167.78 E-value: 1.29e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1004 LEFREVSFVYPCRPEvPVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVKELNVQWLRSQTA 1083
Cdd:cd03246 1 LEVENVSFRYPGAEP-PVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1084 IVSQEPVLFNCSIAENIaygdnsrmvpleeikevadaanihsfieglprkyntlvglrgvqLSGGQKQRLAIARALLRKP 1163
Cdd:cd03246 80 YLPQDDELFSGSIAENI--------------------------------------------LSGGQRQRLGLARALYGNP 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 568980685 1164 KILLLDEATSALDNESEKVVQQALDKAR-RGKTCLVVAHRLSTIQNADMIVVLQNGSI 1220
Cdd:cd03246 116 RILVLDEPNSHLDVEGERALNQAIAALKaAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
375-587 |
6.93e-47 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 166.92 E-value: 6.93e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 375 IEFKNVSFSYPSRPsakVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDIRAQNVRHYREQIG 454
Cdd:COG4619 1 LELEGLSFRVGGKP---ILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 455 VVRQEPVLFGTTIGNNIKFGREGVGEKEMEQAAREANAYdfiMAFPKKF-NTLVGEkgaqMSGGQKQRIAIARALVRNPK 533
Cdd:COG4619 78 YVPQEPALWGGTVRDNLPFPFQLRERKFDRERALELLER---LGLPPDIlDKPVER----LSGGERQRLALIRALLLQPD 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 568980685 534 ILILDEATSALDTESESLVQTALEK--ASKGRTTIVVAHRLSTI-RGADLIVTMKDG 587
Cdd:COG4619 151 VLLLDEPTSALDPENTRRVEELLREylAEEGRAVLWVSHDPEQIeRVADRVLTLEAG 207
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
375-600 |
8.92e-47 |
|
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: 176.25 E-value: 8.92e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 375 IEFKNVSFSYPSRPSA--KVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDIRA---QNVRHY 449
Cdd:COG1123 261 LEVRNLSKRYPVRGKGgvRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKlsrRSLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 450 REQIGVVRQEPV--LF-GTTIGNNIKFG---REGVGEKEMEQAAREANA-----YDFIMAFPkkfntlvgekgAQMSGGQ 518
Cdd:COG1123 341 RRRVQMVFQDPYssLNpRMTVGDIIAEPlrlHGLLSRAERRERVAELLErvglpPDLADRYP-----------HELSGGQ 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 519 KQRIAIARALVRNPKILILDEATSALDTesesLVQTA-LE-----KASKGRTTIVVAHRLSTIRG-ADLIVTMKDGMVVE 591
Cdd:COG1123 410 RQRVAIARALALEPKLLILDEPTSALDV----SVQAQiLNllrdlQRELGLTYLFISHDLAVVRYiADRVAVMYDGRIVE 485
|
....*....
gi 568980685 592 KGTHAELMA 600
Cdd:COG1123 486 DGPTEEVFA 494
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
375-602 |
9.47e-47 |
|
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: 168.76 E-value: 9.47e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 375 IEFKNVSFSYPSRpSAKVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDIR-AQNVRHYREQI 453
Cdd:TIGR04520 1 IEVENVSFSYPES-EKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLdEENLWEIRKKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 454 GVVRQEP--VLFGTTIGNNIKFGRE--GVGEKEM----EQAAREANAYDFIMAFPkkfntlvgekgAQMSGGQKQRIAIA 525
Cdd:TIGR04520 80 GMVFQNPdnQFVGATVEDDVAFGLEnlGVPREEMrkrvDEALKLVGMEDFRDREP-----------HLLSGGQKQRVAIA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568980685 526 RALVRNPKILILDEATSALDTES-ESLVQTALE-KASKGRTTIVVAHRLSTIRGADLIVTMKDGMVVEKGTHAELMAKQ 602
Cdd:TIGR04520 149 GVLAMRPDIIILDEATSMLDPKGrKEVLETIRKlNKEEGITVISITHDMEEAVLADRVIVMNKGKIVAEGTPREIFSQV 227
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
1004-1218 |
1.26e-46 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 166.14 E-value: 1.26e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1004 LEFREVSFVYPCRPevpVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVKELNVQWLRSQTA 1083
Cdd:COG4619 1 LELEGLSFRVGGKP---ILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1084 IVSQEPVLFNCSIAENIAYGDNSRmvpleeiKEVADAANIHSFIE--GLPRKY-NTLVGlrgvQLSGGQKQRLAIARALL 1160
Cdd:COG4619 78 YVPQEPALWGGTVRDNLPFPFQLR-------ERKFDRERALELLErlGLPPDIlDKPVE----RLSGGERQRLALIRALL 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568980685 1161 RKPKILLLDEATSALDNESEKVVQQALDK--ARRGKTCLVVAHRLSTIQN-ADMIVVLQNG 1218
Cdd:COG4619 147 LQPDVLLLDEPTSALDPENTRRVEELLREylAEEGRAVLWVSHDPEQIERvADRVLTLEAG 207
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
1005-1218 |
1.35e-46 |
|
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: 166.49 E-value: 1.35e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1005 EFREVSFVYPcRPEVPVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVKELNVQWLRSQTAI 1084
Cdd:cd03225 1 ELKNLSFSYP-DGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1085 VSQEP--VLFNCSIAENIAYGDNSRMVPLEEIKEVADAANIHSFIEGLpRKYNTLvglrgvQLSGGQKQRLAIARALLRK 1162
Cdd:cd03225 80 VFQNPddQFFGPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGL-RDRSPF------TLSGGQKQRVAIAGVLAMD 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 568980685 1163 PKILLLDEATSALDNESEKVVQQALDK-ARRGKTCLVVAHRLSTIQN-ADMIVVLQNG 1218
Cdd:cd03225 153 PDILLLDEPTAGLDPAGRRELLELLKKlKAEGKTIIIVTHDLDLLLElADRVIVLEDG 210
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
1004-1223 |
1.60e-46 |
|
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: 166.49 E-value: 1.60e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1004 LEFREVSFVYP-CRPEVPVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVKELNvqwlrSQT 1082
Cdd:cd03293 1 LEVRNVSKTYGgGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPG-----PDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1083 AIVSQEPVLFN-CSIAENIAYGDNSRMVPLEEIKEVADAAnihsfIEglprkyntLVGLRGV------QLSGGQKQRLAI 1155
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNVALGLELQGVPKAEARERAEEL-----LE--------LVGLSGFenayphQLSGGMRQRVAL 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568980685 1156 ARALLRKPKILLLDEATSALDNESEKVVQQALDK--ARRGKTCLVVAHRLS-TIQNADMIVVLQN--GSIKEQ 1223
Cdd:cd03293 143 ARALAVDPDVLLLDEPFSALDALTREQLQEELLDiwRETGKTVLLVTHDIDeAVFLADRVVVLSArpGRIVAE 215
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
1004-1227 |
2.44e-46 |
|
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: 166.20 E-value: 2.44e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1004 LEFREVSFVYPcrpEVPVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYD-----PMKGQVLLDGVDVKEL--NVQ 1076
Cdd:cd03260 1 IELRDLNVYYG---DKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDLdvDVL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1077 WLRSQTAIVSQEPVLFNCSIAENIAYGDNSR-MVPLEEIKE-VADAANIhsfiEGLPRKYNTlvGLRGVQLSGGQKQRLA 1154
Cdd:cd03260 78 ELRRRVGMVFQKPNPFPGSIYDNVAYGLRLHgIKLKEELDErVEEALRK----AALWDEVKD--RLHALGLSGGQQQRLC 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568980685 1155 IARALLRKPKILLLDEATSALDNESEKVVQQALDKARRGKTCLVVAHRLSTIQN-ADMIVVLQNGSIKEQG-THQ 1227
Cdd:cd03260 152 LARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARvADRTAFLLNGRLVEFGpTEQ 226
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
1004-1224 |
4.88e-46 |
|
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: 163.64 E-value: 4.88e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1004 LEFREVSFVYPcRPEVPVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVKELNVQwLRSQTA 1083
Cdd:cd03247 1 LSINNVSFSYP-EQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKA-LSSLIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1084 IVSQEPVLFNCSIAENIaygdnsrmvpleeikevadaanihsfieglprkyntlvglrGVQLSGGQKQRLAIARALLRKP 1163
Cdd:cd03247 79 VLNQRPYLFDTTLRNNL-----------------------------------------GRRFSGGERQRLALARILLQDA 117
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568980685 1164 KILLLDEATSALDNESEKVVQQALDKARRGKTCLVVAHRLSTIQNADMIVVLQNGSIKEQG 1224
Cdd:cd03247 118 PIVLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
375-593 |
8.84e-46 |
|
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: 164.60 E-value: 8.84e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 375 IEFKNVSFSYPSRPSA-KVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDI---RAQNVRHYR 450
Cdd:cd03257 2 LEVKNLSVSFPTGGGSvKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLlklSRRLRKIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 451 EQIGVVRQEPvlFGT-----TIGNNIKFGREGVGeKEMEQAAREANAYDFIMAFPKKfNTLVGEKGAQMSGGQKQRIAIA 525
Cdd:cd03257 82 KEIQMVFQDP--MSSlnprmTIGEQIAEPLRIHG-KLSKKEARKEAVLLLLVGVGLP-EEVLNRYPHELSGGQRQRVAIA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568980685 526 RALVRNPKILILDEATSALDTESESLVQTALEKASK--GRTTIVVAHRLSTIRG-ADLIVTMKDGMVVEKG 593
Cdd:cd03257 158 RALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEelGLTLLFITHDLGVVAKiADRVAVMYAGKIVEEG 228
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
393-542 |
3.01e-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: 160.12 E-value: 3.01e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 393 LKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDIRAQNVRHYREQIGVVRQEPVLF-GTTIGNNI 471
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFpRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568980685 472 KFGREGVGEKEMEQAAReanAYDFI--MAFPKKFNTLVGEKGAQMSGGQKQRIAIARALVRNPKILILDEATS 542
Cdd:pfam00005 81 RLGLLLKGLSKREKDAR---AEEALekLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
375-593 |
4.56e-45 |
|
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: 160.56 E-value: 4.56e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 375 IEFKNVSFSYPSRPSaKVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDIRA-QNVRhyREQI 453
Cdd:cd03247 1 LSINNVSFSYPEQEQ-QVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDlEKAL--SSLI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 454 GVVRQEPVLFGTTIGNNIkfgregvgekemeqaareanaydfimafpkkfntlvgekGAQMSGGQKQRIAIARALVRNPK 533
Cdd:cd03247 78 SVLNQRPYLFDTTLRNNL---------------------------------------GRRFSGGERQRLALARILLQDAP 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 534 ILILDEATSALDTESESLVQTALEKASKGRTTIVVAHRLSTIRGADLIVTMKDGMVVEKG 593
Cdd:cd03247 119 IVLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
375-591 |
5.32e-45 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 162.13 E-value: 5.32e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 375 IEFKNVSFSYPSRPSA-KVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDIRAQN------VR 447
Cdd:COG1136 5 LELRNLTKSYGTGEGEvTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSerelarLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 448 hyREQIGVVRQEPVLFGT-TIGNNIKFGRE--GVGEKEMEQAAREANAY----DFIMAFPkkfntlvgekgAQMSGGQKQ 520
Cdd:COG1136 85 --RRHIGFVFQFFNLLPElTALENVALPLLlaGVSRKERRERARELLERvglgDRLDHRP-----------SQLSGGQQQ 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568980685 521 RIAIARALVRNPKILILDEATSALDTESESLVQTALEKASK--GRTTIVVAHRLSTIRGADLIVTMKDGMVVE 591
Cdd:COG1136 152 RVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRelGTTIVMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1004-1232 |
8.02e-45 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 166.04 E-value: 8.02e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1004 LEFREVSFVYPcrpEVPVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVKELNVQwlRSQTA 1083
Cdd:COG3842 6 LELENVSKRYG---DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPE--KRNVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1084 IVSQEPVLF-NCSIAENIAYGDNSRMVPLEEIKE-VADAANihsfieglprkyntLVGLRGV------QLSGGQKQRLAI 1155
Cdd:COG3842 81 MVFQDYALFpHLTVAENVAFGLRMRGVPKAEIRArVAELLE--------------LVGLEGLadryphQLSGGQQQRVAL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1156 ARALLRKPKILLLDEATSALDNESEKVVQQALDK--ARRGKTCLVVAHRLS---TIqnADMIVVLQNGSIKEQGTHQELL 1230
Cdd:COG3842 147 ARALAPEPRVLLLDEPLSALDAKLREEMREELRRlqRELGITFIYVTHDQEealAL--ADRIAVMNDGRIEQVGTPEEIY 224
|
..
gi 568980685 1231 RN 1232
Cdd:COG3842 225 ER 226
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
827-1203 |
1.34e-44 |
|
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: 170.23 E-value: 1.34e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 827 TLLILSFAPVLAVTGMIQTAAMAGFANR----DKQALKRA-GKIATEAVENIRTVVSLT---RERAFEQMYEETLQTQHR 898
Cdd:TIGR02868 149 AVLSVPAALILAAGLLLAGFVAPLVSLRaaraAEQALARLrGELAAQLTDALDGAAELVasgALPAALAQVEEADRELTR 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 899 NALKRAHITGCCYAVSHAFVHFAHAAGFRFGAYLIQAGRMMPegmfIVFTAIAYGAMAIGETLVWAP----EYSKAKAGA 974
Cdd:TIGR02868 229 AERRAAAATALGAALTLLAAGLAVLGALWAGGPAVADGRLAP----VTLAVLVLLPLAAFEAFAALPaaaqQLTRVRAAA 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 975 SHLFALLKNKPTINSCSQSGEKPDTCEG-NLEFREVSFVYPCRPevPVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQ 1053
Cdd:TIGR02868 305 ERIVEVLDAAGPVAEGSAPAAGAVGLGKpTLELRDLSAGYPGAP--PVLDGVSLDLPPGERVAILGPSGSGKSTLLATLA 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1054 RFYDPMKGQVLLDGVDVKELNVQWLRSQTAIVSQEPVLFNCSIAEN--IAYGDnsrmVPLEEIKEVADAANIHSFIEGLP 1131
Cdd:TIGR02868 383 GLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENlrLARPD----ATDEELWAALERVGLADWLRALP 458
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568980685 1132 RKYNTLVGLRGVQLSGGQKQRLAIARALLRKPKILLLDEATSALDNESEKVVQQALDKARRGKTCLVVAHRL 1203
Cdd:TIGR02868 459 DGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
373-594 |
1.39e-44 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 160.27 E-value: 1.39e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 373 GNIEFKNVSFSY-PSRPsaKVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDIRAQNVRHYRE 451
Cdd:cd03369 5 GEIEVENLSVRYaPDLP--PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 452 QIGVVRQEPVLFGTTIGNNI-KFGREGvgEKEMEQAAReanaydfimafpkkfntlVGEKGAQMSGGQKQRIAIARALVR 530
Cdd:cd03369 83 SLTIIPQDPTLFSGTIRSNLdPFDEYS--DEEIYGALR------------------VSEGGLNLSQGQRQLLCLARALLK 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568980685 531 NPKILILDEATSALDTESESLVQTALEKASKGRTTIVVAHRLSTIRGADLIVTMKDGMVVEKGT 594
Cdd:cd03369 143 RPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
95-332 |
1.47e-44 |
|
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: 163.11 E-value: 1.47e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 95 LTLYYIGIGAAALIFGYVQISFWVITAARQTTRIRKQFFHSILAQDISWFDGSDICELNTRMTGDINKLCDGIGDKIPLM 174
Cdd:cd18557 38 LALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFSSLLRQEIAFFDKHKTGELTSRLSSDTSVLQSAVTDNLSQL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 175 FQNISGFSIGLVISLIKSWKLSLVVLSTSPLIMASSALCSRMIISLTSKELDAYSKAGAVAEEALSSIQTVTAFGAQEKE 254
Cdd:cd18557 118 LRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASKIYGRYIRKLSKEVQDALAKAGQVAEESLSNIRTVRSFSAEEKE 197
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568980685 255 IQRYTQHLKDAKDAGIKRATASKLSLGAVYFFMNGAYGLAFWYGTSLIFGGEpgYTIGTILAVffsVIHSSYCIGSVA 332
Cdd:cd18557 198 IRRYSEALDRSYRLARKKALANALFQGITSLLIYLSLLLVLWYGGYLVLSGQ--LTVGELTSF---ILYTIMVASSVG 270
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
375-598 |
1.90e-44 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 161.32 E-value: 1.90e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 375 IEFKNVSFSYPSRPsakVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDI--RAQNVRHYREQ 452
Cdd:COG1126 2 IEIENLHKSFGDLE---VLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLtdSKKDINKLRRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 453 IGVVRQEPVLFG-TTIGNNIKFG----ReGVGEKEMEQAARE----------ANAYdfimafPkkfntlvgekgAQMSGG 517
Cdd:COG1126 79 VGMVFQQFNLFPhLTVLENVTLApikvK-KMSKAEAEERAMEllervgladkADAY------P-----------AQLSGG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 518 QKQRIAIARALVRNPKILILDEATSALDTEsesLVQTAL----EKASKGRTTIVVAHRLSTIRG-ADLIVTMKDGMVVEK 592
Cdd:COG1126 141 QQQRVAIARALAMEPKVMLFDEPTSALDPE---LVGEVLdvmrDLAKEGMTMVVVTHEMGFAREvADRVVFMDGGRIVEE 217
|
....*.
gi 568980685 593 GTHAEL 598
Cdd:COG1126 218 GPPEEF 223
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
375-601 |
2.00e-44 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 161.00 E-value: 2.00e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 375 IEFKNVSFSYPSRpsaKVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDIRAQNvRHYREQIG 454
Cdd:COG1131 1 IEVRGLTKRYGDK---TALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDP-AEVRRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 455 VVRQEPVLFGT-TIGNNIKFGRE--GVGEKEMEQAAREANAydfIMAFPKKFNTLVGekgaQMSGGQKQRIAIARALVRN 531
Cdd:COG1131 77 YVPQEPALYPDlTVRENLRFFARlyGLPRKEARERIDELLE---LFGLTDAADRKVG----TLSGGMKQRLGLALALLHD 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568980685 532 PKILILDEATSALDTESESLVQTALEK-ASKGRTTIVVAHRLSTI-RGADLIVTMKDGMVVEKGTHAELMAK 601
Cdd:COG1131 150 PELLILDEPTSGLDPEARRELWELLRElAAEGKTVLLSTHYLEEAeRLCDRVAIIDKGRIVADGTPDELKAR 221
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
375-600 |
2.62e-44 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 168.93 E-value: 2.62e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 375 IEFKNVSFSYPSRPsAKVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPE---DGCITVDENDIRAQNVRHYRE 451
Cdd:COG1123 5 LEVRDLSVRYPGGD-VPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 452 QIGVVRQEP--VLFGTTIGNNIKFGRE--GVGEKEMEQAAREANAYDFIMAFPKKFNtlvgekgAQMSGGQKQRIAIARA 527
Cdd:COG1123 84 RIGMVFQDPmtQLNPVTVGDQIAEALEnlGLSRAEARARVLELLEAVGLERRLDRYP-------HQLSGGQRQRVAIAMA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568980685 528 LVRNPKILILDEATSALDTESESLVQTALEKASK--GRTTIVVAHRLSTI-RGADLIVTMKDGMVVEKGTHAELMA 600
Cdd:COG1123 157 LALDPDLLIADEPTTALDVTTQAEILDLLRELQRerGTTVLLITHDLGVVaEIADRVVVMDDGRIVEDGPPEEILA 232
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
375-593 |
1.74e-43 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 158.11 E-value: 1.74e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 375 IEFKNVSFSYPSRpsaKVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYD-----PEDGCITVDENDIRAQNVR-- 447
Cdd:cd03260 1 IELRDLNVYYGDK---HALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDLDVDvl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 448 HYREQIGVVRQEPVLFGTTIGNNIKFGREGVGEKEMEQ-AAREANAYDfIMAFPKKFNTLVgeKGAQMSGGQKQRIAIAR 526
Cdd:cd03260 78 ELRRRVGMVFQKPNPFPGSIYDNVAYGLRLHGIKLKEElDERVEEALR-KAALWDEVKDRL--HALGLSGGQQQRLCLAR 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568980685 527 ALVRNPKILILDEATSALDTESESLVQTALEKASKGRTTIVVAHRLS-TIRGADLIVTMKDGMVVEKG 593
Cdd:cd03260 155 ALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQqAARVADRTAFLLNGRLVEFG 222
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1004-1222 |
1.92e-43 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 159.10 E-value: 1.92e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1004 LEFREVSFVYPCRP-EVPVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVKELnvqwlRSQT 1082
Cdd:COG1116 8 LELRGVSKRFPTGGgGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGP-----GPDR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1083 AIVSQEPVLFN-CSIAENIAYGDNSRMVPLEEIKEVADAAnihsfIEglprkyntLVGLRGV------QLSGGQKQRLAI 1155
Cdd:COG1116 83 GVVFQEPALLPwLTVLDNVALGLELRGVPKAERRERAREL-----LE--------LVGLAGFedayphQLSGGMRQRVAI 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568980685 1156 ARALLRKPKILLLDEATSALDNESEKVVQQALDK--ARRGKTCLVVAH------RLstiqnADMIVVLQN--GSIKE 1222
Cdd:COG1116 150 ARALANDPEVLLMDEPFGALDALTRERLQDELLRlwQETGKTVLFVTHdvdeavFL-----ADRVVVLSArpGRIVE 221
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
1002-1225 |
2.94e-43 |
|
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: 156.80 E-value: 2.94e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1002 GNLEFREVSFVYpcRPEVP-VLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVKELNVQWLRS 1080
Cdd:cd03369 5 GEIEVENLSVRY--APDLPpVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1081 QTAIVSQEPVLFNCSIAENIaygDNSRMVPLEEIKEVADAAnihsfiEGlprkyntlvglrGVQLSGGQKQRLAIARALL 1160
Cdd:cd03369 83 SLTIIPQDPTLFSGTIRSNL---DPFDEYSDEEIYGALRVS------EG------------GLNLSQGQRQLLCLARALL 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568980685 1161 RKPKILLLDEATSALDNESEKVVQQALDKARRGKTCLVVAHRLSTIQNADMIVVLQNGSIKEQGT 1225
Cdd:cd03369 142 KRPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
375-587 |
2.95e-43 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 156.88 E-value: 2.95e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 375 IEFKNVSFSYPS-RPSAKVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDIRAQNVR---HYR 450
Cdd:cd03255 1 IELKNLSKTYGGgGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKelaAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 451 -EQIGVVRQEPVLFGT-TIGNNIKFGRE--GVGEKEMEQAAREANAYdfiMAFPKKFNTLVgekgAQMSGGQKQRIAIAR 526
Cdd:cd03255 81 rRHIGFVFQSFNLLPDlTALENVELPLLlaGVPKKERRERAEELLER---VGLGDRLNHYP----SELSGGQQQRVAIAR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568980685 527 ALVRNPKILILDEATSALDTESESLVQTALEK--ASKGRTTIVVAHRLSTIRGADLIVTMKDG 587
Cdd:cd03255 154 ALANDPKIILADEPTGNLDSETGKEVMELLRElnKEAGTTIVVVTHDPELAEYADRIIELRDG 216
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
375-597 |
6.67e-43 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 155.98 E-value: 6.67e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 375 IEFKNVSFSYPsrPSAKVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDE---NDIRAQNVRHYRE 451
Cdd:COG2884 2 IRFENVSKRYP--GGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGqdlSRLKRREIPYLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 452 QIGVVRQE-PVLFGTTIGNNIKFGRE--GVGEKEMEQAAREA----NAYDFIMAFPkkfntlvgekgAQMSGGQKQRIAI 524
Cdd:COG2884 80 RIGVVFQDfRLLPDRTVYENVALPLRvtGKSRKEIRRRVREVldlvGLSDKAKALP-----------HELSGGEQQRVAI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568980685 525 ARALVRNPKILILDEATSALDTE-SESLVQtALEKASKGRTTIVVA-HRLSTIRGADL-IVTMKDGMVVEKGTHAE 597
Cdd:COG2884 149 ARALVNRPELLLADEPTGNLDPEtSWEIME-LLEEINRRGTTVLIAtHDLELVDRMPKrVLELEDGRLVRDEARGV 223
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
1004-1224 |
1.25e-42 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 154.98 E-value: 1.25e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1004 LEFREVSFVYPcrpEVPVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVKELNVQwlRSQTA 1083
Cdd:cd03259 1 LELKGLSKTYG---SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE--RRNIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1084 IVSQEPVLF-NCSIAENIAYGDNSRMVPLEEIKEVADAAnihsfIEglprkyntLVGLRGV------QLSGGQKQRLAIA 1156
Cdd:cd03259 76 MVFQDYALFpHLTVAENIAFGLKLRGVPKAEIRARVREL-----LE--------LVGLEGLlnryphELSGGQQQRVALA 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568980685 1157 RALLRKPKILLLDEATSALDNESEKVVQQALDK--ARRGKTCLVVAHRLS-TIQNADMIVVLQNGSIKEQG 1224
Cdd:cd03259 143 RALAREPSLLLLDEPLSALDAKLREELREELKElqRELGITTIYVTHDQEeALALADRIAVMNEGRIVQVG 213
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
376-587 |
1.43e-42 |
|
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: 152.78 E-value: 1.43e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 376 EFKNVSFSYPSRPsakVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDIRAQNVRHYREQIGV 455
Cdd:cd00267 1 EIENLSFRYGGRT---ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 456 VrqepvlfgttignnikfgregvgekemeqaareanaydfimafpkkfntlvgekgAQMSGGQKQRIAIARALVRNPKIL 535
Cdd:cd00267 78 V-------------------------------------------------------PQLSGGQRQRVALARALLLNPDLL 102
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 568980685 536 ILDEATSALDTESESLVQTALEK-ASKGRTTIVVAHRLSTI-RGADLIVTMKDG 587
Cdd:cd00267 103 LLDEPTSGLDPASRERLLELLRElAEEGRTVIIVTHDPELAeLAADRVIVLKDG 156
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1004-1232 |
2.01e-42 |
|
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: 155.05 E-value: 2.01e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1004 LEFREVSFVYPCRP-EVPVLQNMSLSIEKGKTVAFVGSSGCGKST---CVQLLQRfydPMKGQVLLDGVDVKELN---VQ 1076
Cdd:cd03258 2 IELKNVSKVFGDTGgKVTALKDVSLSVPKGEIFGIIGRSGAGKSTlirCINGLER---PTSGSVLVDGTDLTLLSgkeLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1077 WLRSQTAIVSQEPVLFNC-SIAENIAYgdnsrmvPLEeikevadaanihsfIEGLPRKYN--------TLVGLRG----- 1142
Cdd:cd03258 79 KARRRIGMIFQHFNLLSSrTVFENVAL-------PLE--------------IAGVPKAEIeervlellELVGLEDkaday 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1143 -VQLSGGQKQRLAIARALLRKPKILLLDEATSALDNESEKVVQQALDK--ARRGKTCLVVAHRLSTIQN-ADMIVVLQNG 1218
Cdd:cd03258 138 pAQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDinRELGLTIVLITHEMEVVKRiCDRVAVMEKG 217
|
250
....*....|....
gi 568980685 1219 SIKEQGTHQELLRN 1232
Cdd:cd03258 218 EVVEEGTVEEVFAN 231
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
375-601 |
2.90e-42 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 154.66 E-value: 2.90e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 375 IEFKNVSFSYPSRP-SAKVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDIRAQN---VRHYR 450
Cdd:cd03258 2 IELKNVSKVFGDTGgKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSgkeLRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 451 EQIGVVRQEPVLFGT-TIGNNIKFGRE--GVGEKEMEQAARE----ANAYDFIMAFPkkfntlvgekgAQMSGGQKQRIA 523
Cdd:cd03258 82 RRIGMIFQHFNLLSSrTVFENVALPLEiaGVPKAEIEERVLEllelVGLEDKADAYP-----------AQLSGGQKQRVG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 524 IARALVRNPKILILDEATSALDTESESLVQTALEKASK--GRTTIVVAHRLSTIRG-ADLIVTMKDGMVVEKGTHAELMA 600
Cdd:cd03258 151 IARALANNPKVLLCDEATSALDPETTQSILALLRDINRelGLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEEVFA 230
|
.
gi 568980685 601 K 601
Cdd:cd03258 231 N 231
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
375-602 |
3.67e-42 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 154.77 E-value: 3.67e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 375 IEFKNVSFSYPSRPsaKVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDIRAQNVRHYREQIG 454
Cdd:cd03295 1 IEFENVTKRYGGGK--KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 455 VVRQEPVLF-GTTIGNNIKF--GREGVGEKEMEQAAREANAydfIMAFPKKfnTLVGEKGAQMSGGQKQRIAIARALVRN 531
Cdd:cd03295 79 YVIQQIGLFpHMTVEENIALvpKLLKWPKEKIRERADELLA---LVGLDPA--EFADRYPHELSGGQQQRVGVARALAAD 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568980685 532 PKILILDEATSALDTESESLVQTALEKASK--GRTTIVVAHRL-STIRGADLIVTMKDGMVVEKGTHAELMAKQ 602
Cdd:cd03295 154 PPLLLMDEPFGALDPITRDQLQEEFKRLQQelGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEILRSP 227
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1004-1224 |
4.85e-42 |
|
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: 153.82 E-value: 4.85e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1004 LEFREVSFVYPCRP-EVPVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVKELNVQWL---R 1079
Cdd:cd03257 2 LEVKNLSVSFPTGGgSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRkirR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1080 SQTAIVSQEPVL-FN--CSIAENIA--YGDNSRMVPLEEIKEVADAANIHSfieGLPRKYntlVGLRGVQLSGGQKQRLA 1154
Cdd:cd03257 82 KEIQMVFQDPMSsLNprMTIGEQIAepLRIHGKLSKKEARKEAVLLLLVGV---GLPEEV---LNRYPHELSGGQRQRVA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568980685 1155 IARALLRKPKILLLDEATSALDneseKVVQ-QALD-----KARRGKTCLVVAHRLSTIQN-ADMIVVLQNGSIKEQG 1224
Cdd:cd03257 156 IARALALNPKLLIADEPTSALD----VSVQaQILDllkklQEELGLTLLFITHDLGVVAKiADRVAVMYAGKIVEEG 228
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1004-1232 |
7.19e-42 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 161.61 E-value: 7.19e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1004 LEFREVSFVYPCRpEVPVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDP---MKGQVLLDGVDVKELNVQWLRS 1080
Cdd:COG1123 5 LEVRDLSVRYPGG-DVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHggrISGEVLLDGRDLLELSEALRGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1081 QTAIVSQEP--VLFNCSIAENIAYGDNSRMVPLEEIKEVADAANIHSFIEGLPRKYNTlvglrgvQLSGGQKQRLAIARA 1158
Cdd:COG1123 84 RIGMVFQDPmtQLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPH-------QLSGGQRQRVAIAMA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568980685 1159 LLRKPKILLLDEATSALDNESEKVVQQALDKARR--GKTCLVVAHRLSTI-QNADMIVVLQNGSIKEQGTHQELLRN 1232
Cdd:COG1123 157 LALDPDLLIADEPTTALDVTTQAEILDLLRELQRerGTTVLLITHDLGVVaEIADRVVVMDDGRIVEDGPPEEILAA 233
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
375-584 |
9.26e-42 |
|
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: 152.63 E-value: 9.26e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 375 IEFKNVSFSYPSRPSA-KVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDIRAQNVRhyreqI 453
Cdd:cd03293 1 LEVRNVSKTYGGGGGAvTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD-----R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 454 GVVRQEPVLFG-TTIGNNIKFGREGVGEKEMEQAAReANAY-------DFIMAFPKkfntlvgekgaQMSGGQKQRIAIA 525
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNVALGLELQGVPKAEARER-AEELlelvglsGFENAYPH-----------QLSGGMRQRVALA 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568980685 526 RALVRNPKILILDEATSALDTESESLVQTALEK--ASKGRTTIVVAHRLS-TIRGADLIVTM 584
Cdd:cd03293 144 RALAVDPDVLLLDEPFSALDALTREQLQEELLDiwRETGKTVLLVTHDIDeAVFLADRVVVL 205
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
1004-1234 |
1.04e-41 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 154.51 E-value: 1.04e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1004 LEFREVSFVYPcRPEVPVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVK-ELNVQWLRSQT 1082
Cdd:TIGR04520 1 IEVENVSFSYP-ESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLdEENLWEIRKKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1083 AIVSQEP----VlfnCSIAEN-IAYGDNSRMVPLEEIKE-VADAANihsfieglprkyntLVGLRG------VQLSGGQK 1150
Cdd:TIGR04520 80 GMVFQNPdnqfV---GATVEDdVAFGLENLGVPREEMRKrVDEALK--------------LVGMEDfrdrepHLLSGGQK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1151 QRLAIARALLRKPKILLLDEATSALDNESEKVVQQALDKARR--GKTCLVVAHRLSTIQNADMIVVLQNGSIKEQGTHQE 1228
Cdd:TIGR04520 143 QRVAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKeeGITVISITHDMEEAVLADRVIVMNKGKIVAEGTPRE 222
|
....*.
gi 568980685 1229 LLRNGD 1234
Cdd:TIGR04520 223 IFSQVE 228
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
1022-1173 |
1.39e-41 |
|
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: 149.72 E-value: 1.39e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1022 LQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVKELNVQWLRSQTAIVSQEPVLFN-CSIAENI 1100
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPrLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568980685 1101 AYGDNSRMVPLEEIKEVADAAnIHSFieGLPRKYNTLVGLRGVQLSGGQKQRLAIARALLRKPKILLLDEATS 1173
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEA-LEKL--GLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
1004-1240 |
1.66e-41 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 152.53 E-value: 1.66e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1004 LEFREVSFVYPcrpEVPVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVKELNVQWlRSQTA 1083
Cdd:COG1131 1 IEVRGLTKRYG---DKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEV-RRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1084 IVSQEPVLF-NCSIAENIAYGDNSRMVPLEEIKEVADAAnIHSFieGLPRKYNTLVGlrgvQLSGGQKQRLAIARALLRK 1162
Cdd:COG1131 77 YVPQEPALYpDLTVRENLRFFARLYGLPRKEARERIDEL-LELF--GLTDAADRKVG----TLSGGMKQRLGLALALLHD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1163 PKILLLDEATSALDNESEKVVQQALDK-ARRGKTCLVVAHRLSTIQN-ADMIVVLQNGSIKEQGTHQELLRNG--DTYFK 1238
Cdd:COG1131 150 PELLILDEPTSGLDPEARRELWELLRElAAEGKTVLLSTHYLEEAERlCDRVAIIDKGRIVADGTPDELKARLleDVFLE 229
|
..
gi 568980685 1239 LV 1240
Cdd:COG1131 230 LT 231
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
375-589 |
2.15e-41 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 151.53 E-value: 2.15e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 375 IEFKNVSFSYPSRpsaKVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDI--RAQNVRHYREQ 452
Cdd:cd03262 1 IEIKNLHKSFGDF---HVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtdDKKNINELRQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 453 IGVVRQEPVLFG-TTIGNNIKFG---REGVGEKEMEQAAREANA----YDFIMAFPkkfntlvgekgAQMSGGQKQRIAI 524
Cdd:cd03262 78 VGMVFQQFNLFPhLTVLENITLApikVKGMSKAEAEERALELLEkvglADKADAYP-----------AQLSGGQQQRVAI 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 525 ARALVRNPKILILDEATSALDTEsesLVQTALEK----ASKGRTTIVVAHRLSTIRG-ADLIVTMKDGMV 589
Cdd:cd03262 147 ARALAMNPKVMLFDEPTSALDPE---LVGEVLDVmkdlAEEGMTMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1004-1231 |
3.61e-41 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 152.26 E-value: 3.61e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1004 LEFREVSFVYPCRPE-VPVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVKELNVQWLRSQT 1082
Cdd:COG1124 2 LEVRNLSVSYGQGGRrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1083 AIVSQEPvlfncsiaeniaYGD-NSRMvPLEEIkeVADAANIHSFIEGLPRKYNTL--VGL-------RGVQLSGGQKQR 1152
Cdd:COG1124 82 QMVFQDP------------YASlHPRH-TVDRI--LAEPLRIHGLPDREERIAELLeqVGLppsfldrYPHQLSGGQRQR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1153 LAIARALLRKPKILLLDEATSALDnesekVVQQA--LD-----KARRGKTCLVVAHRLSTIQN-ADMIVVLQNGSIKEQG 1224
Cdd:COG1124 147 VAIARALILEPELLLLDEPTSALD-----VSVQAeiLNllkdlREERGLTYLFVSHDLAVVAHlCDRVAVMQNGRIVEEL 221
|
....*..
gi 568980685 1225 THQELLR 1231
Cdd:COG1124 222 TVADLLA 228
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
375-602 |
3.68e-41 |
|
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: 151.50 E-value: 3.68e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 375 IEFKNVSFSYPSRPsakVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDIRAQNV---RHYRE 451
Cdd:cd03261 1 IELRGLTKSFGGRT---VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEaelYRLRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 452 QIGVVRQEPVLFGT-TIGNNIKFG-RE--GVGEKEMEQAAREanaydfimafpkKFNtLVGEKG------AQMSGGQKQR 521
Cdd:cd03261 78 RMGMLFQSGALFDSlTVFENVAFPlREhtRLSEEEIREIVLE------------KLE-AVGLRGaedlypAELSGGMKKR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 522 IAIARALVRNPKILILDEATSALD----TESESLVQTAleKASKGRTTIVVAHRLSTIRG-ADLIVTMKDGMVVEKGTHA 596
Cdd:cd03261 145 VALARALALDPELLLYDEPTAGLDpiasGVIDDLIRSL--KKELGLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPE 222
|
....*.
gi 568980685 597 ELMAKQ 602
Cdd:cd03261 223 ELRASD 228
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1018-1232 |
4.88e-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: 151.30 E-value: 4.88e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1018 EVPVLQNMSLSIEKGKTVAFVGSSGCGKST---CVQLLQRfydPMKGQVLLDGVDV--KELNVQWLRSQTAIVSQEPVLF 1092
Cdd:COG1126 13 DLEVLKGISLDVEKGEVVVIIGPSGSGKSTllrCINLLEE---PDSGTITVDGEDLtdSKKDINKLRRKVGMVFQQFNLF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1093 -NCSIAENIAYGD-NSRMVPLEEIKEVAdaanihsfieglpRKYNTLVGLRG------VQLSGGQKQRLAIARALLRKPK 1164
Cdd:COG1126 90 pHLTVLENVTLAPiKVKKMSKAEAEERA-------------MELLERVGLADkadaypAQLSGGQQQRVAIARALAMEPK 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568980685 1165 ILLLDEATSALD----NESEKVVQQAldkARRGKTCLVVAHRLSTIQN-ADMIVVLQNGSIKEQGTHQELLRN 1232
Cdd:COG1126 157 VMLFDEPTSALDpelvGEVLDVMRDL---AKEGMTMVVVTHEMGFAREvADRVVFMDGGRIVEEGPPEEFFEN 226
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
375-600 |
5.38e-41 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 151.29 E-value: 5.38e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 375 IEFKNVSFSYPSRPsakVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDIRAQNVRHY---RE 451
Cdd:COG1127 6 IEVRNLTKSFGDRV---VLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELyelRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 452 QIGVVRQEPVLFGT-TIGNNIKFG-RE--GVGEKEMEQAARE-------ANAYDFimaFPkkfntlvgekgAQMSGGQKQ 520
Cdd:COG1127 83 RIGMLFQGGALFDSlTVFENVAFPlREhtDLSEAEIRELVLEklelvglPGAADK---MP-----------SELSGGMRK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 521 RIAIARALVRNPKILILDEATSALD--TeSESLVQTALE-KASKGRTTIVVAHRLSTIRG-ADLIVTMKDGMVVEKGTHA 596
Cdd:COG1127 149 RVALARALALDPEILLYDEPTAGLDpiT-SAVIDELIRElRDELGLTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPE 227
|
....
gi 568980685 597 ELMA 600
Cdd:COG1127 228 ELLA 231
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
100-613 |
5.45e-41 |
|
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: 165.50 E-value: 5.45e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 100 IGIGAAALIFGY-VQISFWVITAARqttRIRKQFFHSILAQDISWFDGSDICELNTRMTGDINKLcDGIGDKIPLMFQNi 178
Cdd:TIGR00957 1014 LGILQGFAVFGYsMAVSIGGIQASR---VLHQDLLHNKLRSPMSFFERTPSGNLVNRFSKELDTV-DSMIPPVIKMFMG- 1088
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 179 SGFS-IGLVISLIKSWKLSLVVLSTSPLIMAssaLCSRMIISLTS--KELDAYSKAGAVAE--EALSSIQTVTAFGAQEK 253
Cdd:TIGR00957 1089 SLFNvIGALIVILLATPIAAVIIPPLGLLYF---FVQRFYVASSRqlKRLESVSRSPVYSHfnETLLGVSVIRAFEEQER 1165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 254 EIqrytqHLKDAK-DAGIKRATASKLSlgavyffmngayglAFWYGTSLIFGGepgyTIGTILAVFFSVIHSSycigSVA 332
Cdd:TIGR00957 1166 FI-----HQSDLKvDENQKAYYPSIVA--------------NRWLAVRLECVG----NCIVLFAALFAVISRH----SLS 1218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 333 PHLETFTVARG----AAFN--IFQVIDKKPNI------DNFS-TAGFVPECIE-----------GNIEFKNVSFSYpsRP 388
Cdd:TIGR00957 1219 AGLVGLSVSYSlqvtFYLNwlVRMSSEMETNIvaverlKEYSeTEKEAPWQIQetappsgwpprGRVEFRNYCLRY--RE 1296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 389 SAK-VLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDIRAQNVRHYREQIGVVRQEPVLFGTTI 467
Cdd:TIGR00957 1297 DLDlVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSL 1376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 468 GNNIK-FGRegVGEKEMEQAAREANAYDFIMAFPKKFNTLVGEKGAQMSGGQKQRIAIARALVRNPKILILDEATSALDT 546
Cdd:TIGR00957 1377 RMNLDpFSQ--YSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDL 1454
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568980685 547 ESESLVQTALEKASKGRTTIVVAHRLSTIRGADLIVTMKDGMVVEKGTHAELMAKQGLYYSlaMAQD 613
Cdd:TIGR00957 1455 ETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRGIFYS--MAKD 1519
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
375-570 |
8.67e-41 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 151.40 E-value: 8.67e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 375 IEFKNVSFSYPSRPSAK-VLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDIRAQNVRhyreqI 453
Cdd:COG1116 8 LELRGVSKRFPTGGGGVtALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPD-----R 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 454 GVVRQEPVLFG-TTIGNNIKFGREGVGEKEMEQAAReANAY-------DFIMAFPKkfntlvgekgaQMSGGQKQRIAIA 525
Cdd:COG1116 83 GVVFQEPALLPwLTVLDNVALGLELRGVPKAERRER-ARELlelvglaGFEDAYPH-----------QLSGGMRQRVAIA 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 568980685 526 RALVRNPKILILDEATSALDteseslVQTALE--------KASKGRTTIVVAH 570
Cdd:COG1116 151 RALANDPEVLLMDEPFGALD------ALTRERlqdellrlWQETGKTVLFVTH 197
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
375-599 |
8.92e-41 |
|
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: 150.96 E-value: 8.92e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 375 IEFKNVSFSYPSRPsakVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDIRAQNVRHYREQIG 454
Cdd:COG1120 2 LEAENLSVGYGGRP---VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 455 VVRQEPVL-FGTTIGNNIKFGR------EGVGEKEMEQAAREA----NAYDFIMafpKKFNTLvgekgaqmSGGQKQRIA 523
Cdd:COG1120 79 YVPQEPPApFGLTVRELVALGRyphlglFGRPSAEDREAVEEAlertGLEHLAD---RPVDEL--------SGGERQRVL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 524 IARALVRNPKILILDEATSALD----TESESLVQTalEKASKGRTTIVVAHRLS-TIRGADLIVTMKDGMVVEKGTHAEL 598
Cdd:COG1120 148 IARALAQEPPLLLLDEPTSHLDlahqLEVLELLRR--LARERGRTVVMVLHDLNlAARYADRLVLLKDGRIVAQGPPEEV 225
|
.
gi 568980685 599 M 599
Cdd:COG1120 226 L 226
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
375-600 |
1.10e-40 |
|
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: 150.72 E-value: 1.10e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 375 IEFKNVSFSYPSRPSAK-VLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDIRAQNVRHYREQI 453
Cdd:COG1124 2 LEVRNLSVSYGQGGRRVpVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 454 GVVRQEP---------VlfGTTIGNNIKFGREGVGEKEMEQAAREAN-AYDFIMAFPkkfntlvgekgAQMSGGQKQRIA 523
Cdd:COG1124 82 QMVFQDPyaslhprhtV--DRILAEPLRIHGLPDREERIAELLEQVGlPPSFLDRYP-----------HQLSGGQRQRVA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 524 IARALVRNPKILILDEATSALDTesesLVQTAL------EKASKGRTTIVVAHRLSTI-RGADLIVTMKDGMVVEKGTHA 596
Cdd:COG1124 149 IARALILEPELLLLDEPTSALDV----SVQAEIlnllkdLREERGLTYLFVSHDLAVVaHLCDRVAVMQNGRIVEELTVA 224
|
....
gi 568980685 597 ELMA 600
Cdd:COG1124 225 DLLA 228
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
1004-1218 |
1.37e-40 |
|
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: 147.72 E-value: 1.37e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1004 LEFREVSFVYPcrpEVPVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDV--KELNVQWLRSQ 1081
Cdd:cd03229 1 LELKNVSKRYG---QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLtdLEDELPPLRRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1082 TAIVSQEPVLF-NCSIAENIAYGdnsrmvpleeikevadaanihsfieglprkyntlvglrgvqLSGGQKQRLAIARALL 1160
Cdd:cd03229 78 IGMVFQDFALFpHLTVLENIALG-----------------------------------------LSGGQQQRVALARALA 116
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568980685 1161 RKPKILLLDEATSALDNESEKVVQQALD--KARRGKTCLVVAHRLSTIQN-ADMIVVLQNG 1218
Cdd:cd03229 117 MDPDVLLLDEPTSALDPITRREVRALLKslQAQLGITVVLVTHDLDEAARlADRVVVLRDG 177
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
1004-1232 |
1.38e-40 |
|
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: 150.14 E-value: 1.38e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1004 LEFREVSFVYPCRPevPVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVKELNVQWLRSQTA 1083
Cdd:cd03295 1 IEFENVTKRYGGGK--KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1084 IVSQEPVLF-NCSIAENIAygdnsrMVP-LEEIKEVADAANIHSFIE--GLPRKynTLVGLRGVQLSGGQKQRLAIARAL 1159
Cdd:cd03295 79 YVIQQIGLFpHMTVEENIA------LVPkLLKWPKEKIRERADELLAlvGLDPA--EFADRYPHELSGGQQQRVGVARAL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568980685 1160 LRKPKILLLDEATSALDNESEKVVQQALDKARR--GKTCLVVAHRL-STIQNADMIVVLQNGSIKEQGTHQELLRN 1232
Cdd:cd03295 151 AADPPLLLMDEPFGALDPITRDQLQEEFKRLQQelGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEILRS 226
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
375-587 |
1.46e-40 |
|
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: 148.77 E-value: 1.46e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 375 IEFKNVSFSYPSRP--SAKVLKGLNLKIKAGETVALVGPSGSGKSTtvqLLQRL---YDPEDGCITVdendiraqnvrhy 449
Cdd:cd03250 1 ISVEDASFTWDSGEqeTSFTLKDINLEVPKGELVAIVGPVGSGKSS---LLSALlgeLEKLSGSVSV------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 450 REQIGVVRQEPVLFGTTIGNNIKFGREGvgEKEMEQAAREANA--YDFIMaFPKKFNTLVGEKGAQMSGGQKQRIAIARA 527
Cdd:cd03250 65 PGSIAYVSQEPWIQNGTIRENILFGKPF--DEERYEKVIKACAlePDLEI-LPDGDLTEIGEKGINLSGGQKQRISLARA 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568980685 528 LVRNPKILILDEATSALDTES-----ESLVQTALekaSKGRTTIVVAHRLSTIRGADLIVTMKDG 587
Cdd:cd03250 142 VYSDADIYLLDDPLSAVDAHVgrhifENCILGLL---LNNKTRILVTHQLQLLPHADQIVVLDNG 203
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
375-587 |
1.94e-40 |
|
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: 147.33 E-value: 1.94e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 375 IEFKNVSFSYPSRpsaKVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDIRA--QNVRHYREQ 452
Cdd:cd03229 1 LELKNVSKRYGQK---TVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDleDELPPLRRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 453 IGVVRQEPVLF-GTTIGNNIKFGregvgekemeqaareanaydfimafpkkfntlvgekgaqMSGGQKQRIAIARALVRN 531
Cdd:cd03229 78 IGMVFQDFALFpHLTVLENIALG---------------------------------------LSGGQQQRVALARALAMD 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 568980685 532 PKILILDEATSALDTESESLVQTALE--KASKGRTTIVVAHRLS-TIRGADLIVTMKDG 587
Cdd:cd03229 119 PDVLLLDEPTSALDPITRREVRALLKslQAQLGITVVLVTHDLDeAARLADRVVVLRDG 177
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1004-1232 |
2.49e-40 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 152.54 E-value: 2.49e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1004 LEFREVSFVYPCRP-EVPVLQNMSLSIEKGKTVAFVGSSGCGKST---CVQLLQRfydPMKGQVLLDGVDVKELNVQWL- 1078
Cdd:COG1135 2 IELENLSKTFPTKGgPVTALDDVSLTIEKGEIFGIIGYSGAGKSTlirCINLLER---PTSGSVLVDGVDLTALSERELr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1079 --RSQTAIVSQEPVLFN-CSIAENIAYgdnsrmvPLEeikevadaanihsfIEGLPRKYNT--------LVGLRG----- 1142
Cdd:COG1135 79 aaRRKIGMIFQHFNLLSsRTVAENVAL-------PLE--------------IAGVPKAEIRkrvaelleLVGLSDkaday 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1143 -VQLSGGQKQRLAIARALLRKPKILLLDEATSALDNESEKVVQQALDKARR--GKTCLVVAHRLSTIQN-ADMIVVLQNG 1218
Cdd:COG1135 138 pSQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRelGLTIVLITHEMDVVRRiCDRVAVLENG 217
|
250
....*....|....
gi 568980685 1219 SIKEQGTHQELLRN 1232
Cdd:COG1135 218 RIVEQGPVLDVFAN 231
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
375-600 |
3.31e-40 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 150.55 E-value: 3.31e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 375 IEFKNVSFSYP--SRPSakvLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDIRAQNVRHYREQ 452
Cdd:PRK13635 6 IRVEHISFRYPdaATYA---LKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 453 IGVVRQEP--VLFGTTIGNNIKFGRE--GVGEKEM----EQAAREANAYDFIMAFPkkfntlvgekgAQMSGGQKQRIAI 524
Cdd:PRK13635 83 VGMVFQNPdnQFVGATVQDDVAFGLEniGVPREEMvervDQALRQVGMEDFLNREP-----------HRLSGGQKQRVAI 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568980685 525 ARALVRNPKILILDEATSALDTES-ESLVQTALE-KASKGRTTIVVAHRLSTIRGADLIVTMKDGMVVEKGTHAELMA 600
Cdd:PRK13635 152 AGVLALQPDIIILDEATSMLDPRGrREVLETVRQlKEQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFK 229
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
375-603 |
3.54e-40 |
|
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: 149.24 E-value: 3.54e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 375 IEFKNVSFSYPSRPsakVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDIRAQNvRHYREQIG 454
Cdd:COG4555 2 IEVENLSKKYGKVP---ALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEP-REARRQIG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 455 VVRQEPVLF-GTTIGNNIKFgregVGE-KEMEQAAREANAYDFI--MAFPKKFNTLVGEkgaqMSGGQKQRIAIARALVR 530
Cdd:COG4555 78 VLPDERGLYdRLTVRENIRY----FAElYGLFDEELKKRIEELIelLGLEEFLDRRVGE----LSTGMKKKVALARALVH 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568980685 531 NPKILILDEATSALDTESESLVQTALEK-ASKGRTTIVVAHRLSTI-RGADLIVTMKDGMVVEKGTHAELMAKQG 603
Cdd:COG4555 150 DPKVLLLDEPTNGLDVMARRLLREILRAlKKEGKTVLFSSHIMQEVeALCDRVVILHKGKVVAQGSLDELREEIG 224
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
1004-1219 |
5.49e-40 |
|
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: 147.23 E-value: 5.49e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1004 LEFREVSFVYPCRPEV--PVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVlldgvdvkelnvqWLRSQ 1081
Cdd:cd03250 1 ISVEDASFTWDSGEQEtsFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSV-------------SVPGS 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1082 TAIVSQEPVLFNCSIAENIAYGdnsrmVPLEE--IKEVADAANIHSFIEGLPRKYNTLVGLRGVQLSGGQKQRLAIARAL 1159
Cdd:cd03250 68 IAYVSQEPWIQNGTIRENILFG-----KPFDEerYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAV 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568980685 1160 LRKPKILLLDEATSALDNES-----EKVVQQALdkaRRGKTCLVVAHRLSTIQNADMIVVLQNGS 1219
Cdd:cd03250 143 YSDADIYLLDDPLSAVDAHVgrhifENCILGLL---LNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
375-598 |
1.60e-39 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 150.63 E-value: 1.60e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 375 IEFKNVSFSYPSRPsakVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDIraQNVRHYREQIG 454
Cdd:COG3842 6 LELENVSKRYGDVT---ALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDV--TGLPPEKRNVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 455 VVRQEPVLFG-TTIGNNIKFG--REGVGEKEMEQAAREAnaydfiMAfpkkfntLVGEKG------AQMSGGQKQRIAIA 525
Cdd:COG3842 81 MVFQDYALFPhLTVAENVAFGlrMRGVPKAEIRARVAEL------LE-------LVGLEGladrypHQLSGGQQQRVALA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 526 RALVRNPKILILDEATSALDTES-ESL------VQTALekaskGRTTIVVAHRLS---TIrgADLIVTMKDGMVVEKGTH 595
Cdd:COG3842 148 RALAPEPRVLLLDEPLSALDAKLrEEMreelrrLQREL-----GITFIYVTHDQEealAL--ADRIAVMNDGRIEQVGTP 220
|
...
gi 568980685 596 AEL 598
Cdd:COG3842 221 EEI 223
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
375-601 |
1.87e-39 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 148.34 E-value: 1.87e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 375 IEFKNVSFSYPSRPSAKVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDIRAQNVRHYREQIG 454
Cdd:PRK13650 5 IEVKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 455 VVRQEP--VLFGTTIGNNIKFGRE--GVGEKEMEQAAREANAYDFIMAFPKKfntlvgeKGAQMSGGQKQRIAIARALVR 530
Cdd:PRK13650 85 MVFQNPdnQFVGATVEDDVAFGLEnkGIPHEEMKERVNEALELVGMQDFKER-------EPARLSGGQKQRVAIAGAVAM 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568980685 531 NPKILILDEATSALDTESE-SLVQTALE-KASKGRTTIVVAHRLSTIRGADLIVTMKDGMVVEKGTHAELMAK 601
Cdd:PRK13650 158 RPKIIILDEATSMLDPEGRlELIKTIKGiRDDYQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFSR 230
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
375-598 |
2.52e-39 |
|
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: 146.56 E-value: 2.52e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 375 IEFKNVSFSYPSrpSAKVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDIRAQ---NVRHYRE 451
Cdd:cd03256 1 IEVENLSKTYPN--GKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLkgkALRQLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 452 QIGVVRQEPVLFG-TTIGNNIKFGREG-----------VGEKEMEQAAREANAYDFImafpKKFNTLVGekgaQMSGGQK 519
Cdd:cd03256 79 QIGMIFQQFNLIErLSVLENVLSGRLGrrstwrslfglFPKEEKQRALAALERVGLL----DKAYQRAD----QLSGGQQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 520 QRIAIARALVRNPKILILDEATSALDTE-SESLVQTALEKA-SKGRTTIVVAHRLSTIRG-ADLIVTMKDGMVVEKGTHA 596
Cdd:cd03256 151 QRVAIARALMQQPKLILADEPVASLDPAsSRQVMDLLKRINrEEGITVIVSLHQVDLAREyADRIVGLKDGRIVFDGPPA 230
|
..
gi 568980685 597 EL 598
Cdd:cd03256 231 EL 232
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1005-1232 |
3.76e-39 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 147.06 E-value: 3.76e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1005 EFREVSFVYPcRPEVPVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVKELNVQWLRSQTAI 1084
Cdd:PRK13632 9 KVENVSFSYP-NSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1085 VSQEP--VLFNCSIAENIAYGDNSRMVPLEEIK----EVADAANIHSFIEGLPRKyntlvglrgvqLSGGQKQRLAIARA 1158
Cdd:PRK13632 88 IFQNPdnQFIGATVEDDIAFGLENKKVPPKKMKdiidDLAKKVGMEDYLDKEPQN-----------LSGGQKQRVAIASV 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568980685 1159 LLRKPKILLLDEATSALDNESEKVVQQALDKAR--RGKTCLVVAHRLSTIQNADMIVVLQNGSIKEQGTHQELLRN 1232
Cdd:PRK13632 157 LALNPEIIIFDESTSMLDPKGKREIKKIMVDLRktRKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEILNN 232
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1004-1230 |
4.05e-39 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 146.34 E-value: 4.05e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1004 LEFREVSFVYPCRPevpVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVKELNVQWLRSQTA 1083
Cdd:COG1120 2 LEAENLSVGYGGRP---VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1084 IVSQEPVL-FNCSIAENIAYGDNSRMVPL--------EEIKEVADAANIHSFIEglpRKYNTlvglrgvqLSGGQKQRLA 1154
Cdd:COG1120 79 YVPQEPPApFGLTVRELVALGRYPHLGLFgrpsaedrEAVEEALERTGLEHLAD---RPVDE--------LSGGERQRVL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1155 IARALLRKPKILLLDEATSALD--NESEkvVQQALDK--ARRGKTCLVVAHRLS-TIQNADMIVVLQNGSIKEQGTHQEL 1229
Cdd:COG1120 148 IARALAQEPPLLLLDEPTSHLDlaHQLE--VLELLRRlaRERGRTVVMVLHDLNlAARYADRLVLLKDGRIVAQGPPEEV 225
|
.
gi 568980685 1230 L 1230
Cdd:COG1120 226 L 226
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1004-1223 |
6.25e-39 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 144.80 E-value: 6.25e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1004 LEFREVSFVYPC-RPEVPVLQNMSLSIEKGKTVAFVGSSGCGKST---CVQLLQRfydPMKGQVLLDGVDVKELN----V 1075
Cdd:COG1136 5 LELRNLTKSYGTgEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTllnILGGLDR---PTSGEVLIDGQDISSLSerelA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1076 QWLRSQTAIVSQE----PVLfncSIAENIA----YGDNSRMVPLEEIKEVADAANIHSFIEGLPRkyntlvglrgvQLSG 1147
Cdd:COG1136 82 RLRRRHIGFVFQFfnllPEL---TALENVAlpllLAGVSRKERRERARELLERVGLGDRLDHRPS-----------QLSG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568980685 1148 GQKQRLAIARALLRKPKILLLDEATSALDNESEKVVQQALDKARR--GKTCLVVAHRLSTIQNADMIVVLQNGSIKEQ 1223
Cdd:COG1136 148 GQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRelGTTIVMVTHDPELAARADRVIRLRDGRIVSD 225
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
375-590 |
6.59e-39 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 145.58 E-value: 6.59e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 375 IEFKNVSFSYPSRpsAKVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDI---RAQNVRHYRE 451
Cdd:COG3638 3 LELRNLSKRYPGG--TPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVtalRGRALRRLRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 452 QIGVVRQEPVLFG-TTIGNNIKFGRegVGE------------KEMEQAAREAnaydfimafpkkfntL--VG------EK 510
Cdd:COG3638 81 RIGMIFQQFNLVPrLSVLTNVLAGR--LGRtstwrsllglfpPEDRERALEA---------------LerVGladkayQR 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 511 GAQMSGGQKQRIAIARALVRNPKILILDEATSALDTESESLVQTALEKASK--GRTTIVVAHRLSTIRG-ADLIVTMKDG 587
Cdd:COG3638 144 ADQLSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIARedGITVVVNLHQVDLARRyADRIIGLRDG 223
|
...
gi 568980685 588 MVV 590
Cdd:COG3638 224 RVV 226
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
375-593 |
1.40e-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: 1.40e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 375 IEFKNVSFSYPSRPsakVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDIraQNVRHYREQIG 454
Cdd:cd03259 1 LELKGLSKTYGSVR---ALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDV--TGVPPERRNIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 455 VVRQEPVLFGT-TIGNNIKFG--REGVGEKEMEQAAREANAydfimafpkkfntLVGEKG------AQMSGGQKQRIAIA 525
Cdd:cd03259 76 MVFQDYALFPHlTVAENIAFGlkLRGVPKAEIRARVRELLE-------------LVGLEGllnrypHELSGGQQQRVALA 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568980685 526 RALVRNPKILILDEATSALDTESESLVQTALEKASK--GRTTIVVAHRLS-TIRGADLIVTMKDGMVVEKG 593
Cdd:cd03259 143 RALAREPSLLLLDEPLSALDAKLREELREELKELQRelGITTIYVTHDQEeALALADRIAVMNEGRIVQVG 213
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
1004-1220 |
3.65e-38 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 142.24 E-value: 3.65e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1004 LEFREVSFVYPCRPE-VPVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVKELNVQWL---- 1078
Cdd:cd03255 1 IELKNLSKTYGGGGEkVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1079 RSQTAIVSQE----PVLfncSIAENIAYGDNSRMVPLEEIKEVAdaaniHSFIE--GLPRKYNTLVGlrgvQLSGGQKQR 1152
Cdd:cd03255 81 RRHIGFVFQSfnllPDL---TALENVELPLLLAGVPKKERRERA-----EELLErvGLGDRLNHYPS----ELSGGQQQR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1153 LAIARALLRKPKILLLDEATSALDNESEKVVQQALDK--ARRGKTCLVVAHRLSTIQNADMIVVLQNGSI 1220
Cdd:cd03255 149 VAIARALANDPKIILADEPTGNLDSETGKEVMELLRElnKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
375-598 |
6.46e-38 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 145.61 E-value: 6.46e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 375 IEFKNVSFSYPSRPSA-KVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDIRAQN---VRHYR 450
Cdd:COG1135 2 IELENLSKTFPTKGGPvTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSereLRAAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 451 EQIGVVRQEPVLFGT-TIGNNIKFGRE--GVGEKEMEQAARE----------ANAYdfimafPkkfntlvgekgAQMSGG 517
Cdd:COG1135 82 RKIGMIFQHFNLLSSrTVAENVALPLEiaGVPKAEIRKRVAEllelvglsdkADAY------P-----------SQLSGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 518 QKQRIAIARALVRNPKILILDEATSALDTESeslvqTA-----LEKASK--GRTTIVVAHRLSTIRG-ADLIVTMKDGMV 589
Cdd:COG1135 145 QKQRVGIARALANNPKVLLCDEATSALDPET-----TRsildlLKDINRelGLTIVLITHEMDVVRRiCDRVAVLENGRI 219
|
....*....
gi 568980685 590 VEKGTHAEL 598
Cdd:COG1135 220 VEQGPVLDV 228
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
375-589 |
1.17e-37 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 139.07 E-value: 1.17e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 375 IEFKNVSFSYPSRPsakVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDIRaQNVRHYREQIG 454
Cdd:cd03230 1 IEVRNLSKRYGKKT---ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIK-KEPEEVKRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 455 VVRQEPVLFGttignnikfgregvgekemeqaarEANAYDFImafpkkfntlvgekgaQMSGGQKQRIAIARALVRNPKI 534
Cdd:cd03230 77 YLPEEPSLYE------------------------NLTVRENL----------------KLSGGMKQRLALAQALLHDPEL 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 568980685 535 LILDEATSALDTES-ESLVQTALEKASKGRTTIVVAHRLSTI-RGADLIVTMKDGMV 589
Cdd:cd03230 117 LILDEPTSGLDPESrREFWELLRELKKEGKTILLSSHILEEAeRLCDRVAILNNGRI 173
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1004-1230 |
1.67e-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: 1.67e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1004 LEFREVSFVYPcrpEVPVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVKELNvQWLRSQTA 1083
Cdd:COG4555 2 IEVENLSKKYG---KVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEP-REARRQIG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1084 IVSQEPVLF-NCSIAENIAYGDNSRMVPLEEIKEVADAAnIHSFieGLPRKYNTLVGlrgvQLSGGQKQRLAIARALLRK 1162
Cdd:COG4555 78 VLPDERGLYdRLTVRENIRYFAELYGLFDEELKKRIEEL-IELL--GLEEFLDRRVG----ELSTGMKKKVALARALVHD 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1163 PKILLLDEATSALDNESEKVVQQALDKAR-RGKTCLVVAHRLSTIQN-ADMIVVLQNGSIKEQGTHQELL 1230
Cdd:COG4555 151 PKVLLLDEPTNGLDVMARRLLREILRALKkEGKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDELR 220
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
97-345 |
2.09e-37 |
|
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: 142.68 E-value: 2.09e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 97 LYYIGIGAAALIFGYVQ-ISFWVITAaRQTTRIRKQFFHSILAQDISWFDGSDICELNTRMTGDINKLCDGIGDKIPLMF 175
Cdd:cd18572 40 LLLLLLSVLSGLFSGLRgGCFSYAGT-RLVRRLRRDLFRSLLRQDIAFFDATKTGELTSRLTSDCQKVSDPLSTNLNVFL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 176 QN-ISGFSiGLVISLIKSWKLSLVVLSTSPLIMASSALCSRMIISLTSKELDAYSKAGAVAEEALSSIQTVTAFGAQEKE 254
Cdd:cd18572 119 RNlVQLVG-GLAFMFSLSWRLTLLAFITVPVIALITKVYGRYYRKLSKEIQDALAEANQVAEEALSNIRTVRSFATEERE 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 255 IQRYTQHLKDAKDAGIKRATASKLSLGAVYFFMNGAYGLAFWYGTSLIFGGEpgYTIGTILAVFF---SVIHSSYCIGSV 331
Cdd:cd18572 198 ARRYERALDKALKLSVRQALAYAGYVAVNTLLQNGTQVLVLFYGGHLVLSGR--MSAGQLVTFMLyqqQLGEAFQSLGDV 275
|
250
....*....|....
gi 568980685 332 aphLETFTVARGAA 345
Cdd:cd18572 276 ---FSSLMQAVGAA 286
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1005-1218 |
2.21e-37 |
|
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: 137.76 E-value: 2.21e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1005 EFREVSFVYPcrpEVPVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVKELNVQWLRSQTAI 1084
Cdd:cd00267 1 EIENLSFRYG---GRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1085 VSQepvlfncsiaeniaygdnsrmvpleeikevadaanihsfieglprkyntlvglrgvqLSGGQKQRLAIARALLRKPK 1164
Cdd:cd00267 78 VPQ---------------------------------------------------------LSGGQRQRVALARALLLNPD 100
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 568980685 1165 ILLLDEATSALDNESEKVVQQALDK-ARRGKTCLVVAHRLSTIQNA-DMIVVLQNG 1218
Cdd:cd00267 101 LLLLDEPTSGLDPASRERLLELLRElAEEGRTVIIVTHDPELAELAaDRVIVLKDG 156
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
37-319 |
2.47e-37 |
|
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: 142.30 E-value: 2.47e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 37 MTLGILASMINGATVPLMSLVLGEISDHLIngclvqtnrtkyqncsqtQEKLNEDIIVLTLYYIGIGAAALIFGYVQISF 116
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLLIDDVI------------------PAGDLSLLLWIALLLLLLALLRALLSYLRRYL 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 117 WVITAARQTTRIRKQFFHSILAQDISWFDGSDICELNTRMTGDINKLCDGIGDKIPLMFQNISGFSIGLVISLIKSWKLS 196
Cdd:cd07346 63 AARLGQRVVFDLRRDLFRHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLT 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 197 LVVLSTSPLIMASSALCSRMIISLTSKELDAYSKAGAVAEEALSSIQTVTAFGAQEKEIQRYTQHLKDAKDAGIKRATAS 276
Cdd:cd07346 143 LVALLLLPLYVLILRYFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLS 222
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 568980685 277 KLSLGAVYFFMNGAYGLAFWYGTSLIFGGEPgyTIGTILAVFF 319
Cdd:cd07346 223 ALFSPLIGLLTALGTALVLLYGGYLVLQGSL--TIGELVAFLA 263
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
373-612 |
2.56e-37 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 153.74 E-value: 2.56e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 373 GNIEFKNVSFSY-PSRPSakVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDIRAQNVRHYRE 451
Cdd:PLN03130 1236 GSIKFEDVVLRYrPELPP--VLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRK 1313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 452 QIGVVRQEPVLFGTTIGNNIK-FGREGvgEKEMEQAAREANAYDFIMAFPKKFNTLVGEKGAQMSGGQKQRIAIARALVR 530
Cdd:PLN03130 1314 VLGIIPQAPVLFSGTVRFNLDpFNEHN--DADLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLR 1391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 531 NPKILILDEATSALDTESESLVQTALEKASKGRTTIVVAHRLSTIRGADLIVTMKDGMVVEKGTHAELMAKQGLYYSlAM 610
Cdd:PLN03130 1392 RSKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEGSAFS-KM 1470
|
..
gi 568980685 611 AQ 612
Cdd:PLN03130 1471 VQ 1472
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1004-1234 |
2.58e-37 |
|
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: 140.89 E-value: 2.58e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1004 LEFREVSFVYPcrpEVPVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVKELNV---QWLRS 1080
Cdd:COG1127 6 IEVRNLTKSFG---DRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEkelYELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1081 QTAIVSQEPVLF-NCSIAENIAYG--DNSRMvPLEEIKEVADAAnihsfIEglprkyntLVGLRGV------QLSGGQKQ 1151
Cdd:COG1127 83 RIGMLFQGGALFdSLTVFENVAFPlrEHTDL-SEAEIRELVLEK-----LE--------LVGLPGAadkmpsELSGGMRK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1152 RLAIARALLRKPKILLLDEATSALDNESEKVVQQALDKARR--GKTCLVVAHRLSTIQN-ADMIVVLQNGSIKEQGTHQE 1228
Cdd:COG1127 149 RVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDelGLTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPEE 228
|
....*.
gi 568980685 1229 LLRNGD 1234
Cdd:COG1127 229 LLASDD 234
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
375-618 |
2.98e-37 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 141.67 E-value: 2.98e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 375 IEFKNVSFSYPSRpSAKVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDIRAQNVRHYREQIG 454
Cdd:PRK13632 8 IKVENVSFSYPNS-ENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 455 VVRQEP--VLFGTTIGNNIKFGREG--VGEKEM----EQAAREANAYDFIMAFPKKfntlvgekgaqMSGGQKQRIAIAR 526
Cdd:PRK13632 87 IIFQNPdnQFIGATVEDDIAFGLENkkVPPKKMkdiiDDLAKKVGMEDYLDKEPQN-----------LSGGQKQRVAIAS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 527 ALVRNPKILILDEATSALDTES-ESLVQTALEKASKG-RTTIVVAHRLSTIRGADLIVTMKDGMVVEKGTHAELM----- 599
Cdd:PRK13632 156 VLALNPEIIIFDESTSMLDPKGkREIKKIMVDLRKTRkKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEILnnkei 235
|
250 260
....*....|....*....|..
gi 568980685 600 ---AKQGLYYSLAMAQDIKKVD 618
Cdd:PRK13632 236 lekAKIDSPFIYKLSKKLKGID 257
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
1021-1237 |
4.19e-37 |
|
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: 139.78 E-value: 4.19e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1021 VLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVKELNVQwlRSQTAIVSQEPVLF-NCSIAEN 1099
Cdd:cd03299 14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE--KRDISYVPQNYALFpHMTVYKN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1100 IAYGDNSRMVPLEEI-KEVADAANIHSFIEGLPRKYNTLvglrgvqlSGGQKQRLAIARALLRKPKILLLDEATSALDNE 1178
Cdd:cd03299 92 IAYGLKKRKVDKKEIeRKVLEIAEMLGIDHLLNRKPETL--------SGGEQQRVAIARALVVNPKILLLDEPFSALDVR 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568980685 1179 SEKVVQQALDKARR--GKTCLVVAHRLSTIQN-ADMIVVLQNGSIKEQGTHQELLRNGDTYF 1237
Cdd:cd03299 164 TKEKLREELKKIRKefGVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEVFKKPKNEF 225
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
391-1237 |
4.78e-37 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 152.63 E-value: 4.78e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 391 KVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDpedgcitVDENDIRAQnvrhyrEQIGVVRQEPVLFGTTIGNN 470
Cdd:PTZ00243 674 VLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFE-------ISEGRVWAE------RSIAYVPQQAWIMNATVRGN 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 471 IKFGREgvgekemEQAAREANAYDF------IMAFPKKFNTLVGEKGAQMSGGQKQRIAIARALVRNPKILILDEATSAL 544
Cdd:PTZ00243 741 ILFFDE-------EDAARLADAVRVsqleadLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSAL 813
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 545 DTE-SESLVQTALEKASKGRTTIVVAHRLSTIRGADLIVTMKDGMVVEKGTHAELMAKQgLYYSLA-------------- 609
Cdd:PTZ00243 814 DAHvGERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFMRTS-LYATLAaelkenkdskegda 892
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 610 ----MAQDIKKVDEQMESRTCST-AGNASYGSLCDVNSAKAPCTDQLEEAVhhqkTSLPEVSLLKIFKL-SKSEWPFVVL 683
Cdd:PTZ00243 893 daevAEVDAAPGGAVDHEPPVAKqEGNAEGGDGAALDAAAGRLMTREEKAS----GSVPWSTYVAYLRFcGGLHAAGFVL 968
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 684 GTLAsalngsVHPVFSIIFGKLVTMFEDKNkatLKQDAELYsmMLVVLGIVALVTYLMQGLFYGRAEenlAMR-----LR 758
Cdd:PTZ00243 969 ATFA------VTELVTVSSGVWLSMWSTRS---FKLSAATY--LYVYLGIVLLGTFSVPLRFFLSYE---AMRrgsrnMH 1034
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 759 HSAFKAMLYQDMAWYDdkenntgalTTTLavdvaqiqGAATSRLgivTQDVS------NMSLSILISFIYGWEMTLLILS 832
Cdd:PTZ00243 1035 RDLLRSVSRGTMSFFD---------TTPL--------GRILNRF---SRDIDildntlPMSYLYLLQCLFSICSSILVTS 1094
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 833 FAP-----VLAVTGMIQTAAMaGFANRDKQALKRAGKIA--------TEAVENIRTVVSLTRERAFEQMYEETLQTQH-- 897
Cdd:PTZ00243 1095 ASQpfvlvALVPCGYLYYRLM-QFYNSANREIRRIKSVAkspvftllEEALQGSATITAYGKAHLVMQEALRRLDVVYsc 1173
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 898 ---RNALKR-------------------AHITGCCYAVSH---AFVHFAHAAGFRFGA---YLIQAGRMMPEGMFIVFTA 949
Cdd:PTZ00243 1174 sylENVANRwlgvrveflsnivvtvialIGVIGTMLRATSqeiGLVSLSLTMAMQTTAtlnWLVRQVATVEADMNSVERL 1253
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 950 IAY------GAMAIGETLVWAPEYSKAKAgashlfALLKNKPTINSCSQSGEKPDTCE-GNLEFREVSFVYpcRPEVP-V 1021
Cdd:PTZ00243 1254 LYYtdevphEDMPELDEEVDALERRTGMA------ADVTGTVVIEPASPTSAAPHPVQaGSLVFEGVQMRY--REGLPlV 1325
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1022 LQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVKELNVQWLRSQTAIVSQEPVLFNCSIAENIA 1101
Cdd:PTZ00243 1326 LRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQNVD 1405
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1102 ygdnsrmvPLEEikevADAANIHSFIEglprkyntLVGLR-----------------GVQLSGGQKQRLAIARALLRK-P 1163
Cdd:PTZ00243 1406 --------PFLE----ASSAEVWAALE--------LVGLRervasesegidsrvlegGSNYSVGQRQLMCMARALLKKgS 1465
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568980685 1164 KILLLDEATSALDNESEKVVQQALDKARRGKTCLVVAHRLSTIQNADMIVVLQNGSIKEQGTHQELLRNGDTYF 1237
Cdd:PTZ00243 1466 GFILMDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELVMNRQSIF 1539
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1004-1232 |
8.28e-37 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 142.90 E-value: 8.28e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1004 LEFREVSFVYPcrpEVPVLQNMSLSIEKGKTVAFVGSSGCGKSTcvqLLqR----FYDPMKGQVLLDGVDVKELNVQwlR 1079
Cdd:COG3839 4 LELENVSKSYG---GVEALKDIDLDIEDGEFLVLLGPSGCGKST---LL-RmiagLEDPTSGEILIGGRDVTDLPPK--D 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1080 SQTAIVSQEPVLF-NCSIAENIAYGDNSRMVPLEEIKE-VADAA---NIHSFIEGLPRkyntlvglrgvQLSGGQKQRLA 1154
Cdd:COG3839 75 RNIAMVFQSYALYpHMTVYENIAFPLKLRKVPKAEIDRrVREAAellGLEDLLDRKPK-----------QLSGGQRQRVA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1155 IARALLRKPKILLLDEATSALDNE------SE-KVVQQaldkaRRGKTCLVVAHRLS---TIqnADMIVVLQNGSIKEQG 1224
Cdd:COG3839 144 LGRALVREPKVFLLDEPLSNLDAKlrvemrAEiKRLHR-----RLGTTTIYVTHDQVeamTL--ADRIAVMNDGRIQQVG 216
|
....*...
gi 568980685 1225 THQELLRN 1232
Cdd:COG3839 217 TPEELYDR 224
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
375-604 |
8.88e-37 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 139.45 E-value: 8.88e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 375 IEFKNVSFSYPSRPsakVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDendirAQNVRHYREQIG 454
Cdd:COG1121 7 IELENLTVSYGGRP---VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLF-----GKPPRRARRRIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 455 VVRQ-------------EPVLFGTTIGNNIkFGREGvgeKEMEQAAREA----NAYDFImafpkkfNTLVGEkgaqMSGG 517
Cdd:COG1121 79 YVPQraevdwdfpitvrDVVLMGRYGRRGL-FRRPS---RADREAVDEAlervGLEDLA-------DRPIGE----LSGG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 518 QKQRIAIARALVRNPKILILDEATSALDTESESLVQTALEK-ASKGRTTIVVAHRLSTIRG-ADLIVTMKDGMVVEkGTH 595
Cdd:COG1121 144 QQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRElRREGKTILVVTHDLGAVREyFDRVLLLNRGLVAH-GPP 222
|
....*....
gi 568980685 596 AELMAKQGL 604
Cdd:COG1121 223 EEVLTPENL 231
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
1004-1231 |
1.03e-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: 138.79 E-value: 1.03e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1004 LEFREVSFVYPCRPevpVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVKELNV---QWLRS 1080
Cdd:cd03261 1 IELRGLTKSFGGRT---VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEaelYRLRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1081 QTAIVSQEPVLFNC-SIAENIAYG--DNSRMvPLEEIKEVAdaanihsfIEGLprkynTLVGLRGV------QLSGGQKQ 1151
Cdd:cd03261 78 RMGMLFQSGALFDSlTVFENVAFPlrEHTRL-SEEEIREIV--------LEKL-----EAVGLRGAedlypaELSGGMKK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1152 RLAIARALLRKPKILLLDEATSALDNESEKVVQQALDKARR--GKTCLVVAHRLSTI-QNADMIVVLQNGSIKEQGTHQE 1228
Cdd:cd03261 144 RVALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKelGLTSIMVTHDLDTAfAIADRIAVLYDGKIVAEGTPEE 223
|
...
gi 568980685 1229 LLR 1231
Cdd:cd03261 224 LRA 226
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
375-569 |
1.44e-36 |
|
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: 137.54 E-value: 1.44e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 375 IEFKNVSFSYPsrPSAKVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITV---DENDIRAQNVRHYRE 451
Cdd:cd03292 1 IEFINVTKTYP--NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVngqDVSDLRGRAIPYLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 452 QIGVVRQEPVLFGT-TIGNNIKFGREGVGEKEMEQAAREANAYDfimafpkkfntLVGEKG------AQMSGGQKQRIAI 524
Cdd:cd03292 79 KIGVVFQDFRLLPDrNVYENVAFALEVTGVPPREIRKRVPAALE-----------LVGLSHkhralpAELSGGEQQRVAI 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 568980685 525 ARALVRNPKILILDEATSALDTESESLVQTALEKASKGRTTIVVA 569
Cdd:cd03292 148 ARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVA 192
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
98-603 |
1.61e-36 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 150.90 E-value: 1.61e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 98 YYIGIgAAALIFGYVQI----SFWVITAARQTT-RIRKQFFHSILAQDISWFDGSDICELNTRMTGDINKLCDGIGDK-- 170
Cdd:PLN03232 951 FYIVV-YALLGFGQVAVtftnSFWLISSSLHAAkRLHDAMLNSILRAPMLFFHTNPTGRVINRFSKDIGDIDRNVANLmn 1029
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 171 --IPLMFQNISGFSIGLVISLIKSWK-LSLVVLSTSPLIMASSAlcSRMIisltsKELDAYSKAGAVAE--EALSSIQTV 245
Cdd:PLN03232 1030 mfMNQLWQLLSTFALIGTVSTISLWAiMPLLILFYAAYLYYQST--SREV-----RRLDSVTRSPIYAQfgEALNGLSSI 1102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 246 TAFGAQEkeiqRYTQHLKDAKDAGIKRATASKLSLGAVYFFMNGAYGLAFWYGTSLifgGEPGYTIGTILAVFFSVIHS- 324
Cdd:PLN03232 1103 RAYKAYD----RMAKINGKSMDNNIRFTLANTSSNRWLTIRLETLGGVMIWLTATF---AVLRNGNAENQAGFASTMGLl 1175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 325 -SYCIgSVAPHLETFTVARGAAFNIFQVIDKKPN-IDNFSTAGFV-----PEC---IEGNIEFKNVSFSY-PSRPSakVL 393
Cdd:PLN03232 1176 lSYTL-NITTLLSGVLRQASKAENSLNSVERVGNyIDLPSEATAIiennrPVSgwpSRGSIKFEDVHLRYrPGLPP--VL 1252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 394 KGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDIRAQNVRHYREQIGVVRQEPVLFGTTIGNNIKF 473
Cdd:PLN03232 1253 HGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNIDP 1332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 474 GREGvGEKEMEQAAREANAYDFIMAFPKKFNTLVGEKGAQMSGGQKQRIAIARALVRNPKILILDEATSALDTESESLVQ 553
Cdd:PLN03232 1333 FSEH-NDADLWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQ 1411
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 568980685 554 TALEKASKGRTTIVVAHRLSTIRGADLIVTMKDGMVVEKGTHAELMAKQG 603
Cdd:PLN03232 1412 RTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDT 1461
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
375-599 |
3.57e-36 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 137.53 E-value: 3.57e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 375 IEFKNVSFSYPSrpsAKVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDIR--AQNVRHYREQ 452
Cdd:PRK09493 2 IEFKNVSKHFGP---TQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpKVDERLIRQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 453 IGVVRQEPVLF-GTTIGNNIKFGR---EGVGEKEMEQAAREanaydfimafpkkfntLVGEKG---------AQMSGGQK 519
Cdd:PRK09493 79 AGMVFQQFYLFpHLTALENVMFGPlrvRGASKEEAEKQARE----------------LLAKVGlaerahhypSELSGGQQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 520 QRIAIARALVRNPKILILDEATSALDTESESLVQTALEK-ASKGRTTIVVAHRLSTIR--GADLIVtMKDGMVVEKGTHA 596
Cdd:PRK09493 143 QRVAIARALAVKPKLMLFDEPTSALDPELRHEVLKVMQDlAEEGMTMVIVTHEIGFAEkvASRLIF-IDKGRIAEDGDPQ 221
|
...
gi 568980685 597 ELM 599
Cdd:PRK09493 222 VLI 224
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
375-604 |
3.79e-36 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 138.78 E-value: 3.79e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 375 IEFKNVSFSYPSRPSAkVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPED---GCITVDENDIRAQNVRHYRE 451
Cdd:PRK13640 6 VEFKHVSFTYPDSKKP-ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDnpnSKITVDGITLTAKTVWDIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 452 QIGVVRQEP--VLFGTTIGNNIKFGRE--GVGEKEMEQAAREANA----YDFIMAFPkkfntlvgekgAQMSGGQKQRIA 523
Cdd:PRK13640 85 KVGIVFQNPdnQFVGATVGDDVAFGLEnrAVPRPEMIKIVRDVLAdvgmLDYIDSEP-----------ANLSGGQKQRVA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 524 IARALVRNPKILILDEATSALDTESE----SLVQTALEKasKGRTTIVVAHRLSTIRGADLIVTMKDGMVVEKGTHAELM 599
Cdd:PRK13640 154 IAGILAVEPKIIILDESTSMLDPAGKeqilKLIRKLKKK--NNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIF 231
|
....*
gi 568980685 600 AKQGL 604
Cdd:PRK13640 232 SKVEM 236
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1004-1237 |
3.93e-36 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 140.67 E-value: 3.93e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1004 LEFREVSFVYPcrpEVPVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVK-ELNVQwlRSQT 1082
Cdd:COG1118 3 IEVRNISKRFG---SFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFtNLPPR--ERRV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1083 AIVSQEPVLF-NCSIAENIAYGDNSRMVPLEEIKEVAdaaniHSFIEglprkyntLVGLRGV------QLSGGQKQRLAI 1155
Cdd:COG1118 78 GFVFQHYALFpHMTVAENIAFGLRVRPPSKAEIRARV-----EELLE--------LVQLEGLadrypsQLSGGQRQRVAL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1156 ARALLRKPKILLLDEATSALD----NESEKVVQQALDkaRRGKTCLVVAH------RLstiqnADMIVVLQNGSIKEQGT 1225
Cdd:COG1118 145 ARALAVEPEVLLLDEPFGALDakvrKELRRWLRRLHD--ELGGTTVFVTHdqeealEL-----ADRVVVMNQGRIEQVGT 217
|
250
....*....|..
gi 568980685 1226 HQELLRNGDTYF 1237
Cdd:COG1118 218 PDEVYDRPATPF 229
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1004-1222 |
4.34e-36 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 136.72 E-value: 4.34e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1004 LEFREVSFVYPcrPEVPVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVKELN---VQWLRS 1080
Cdd:COG2884 2 IRFENVSKRYP--GGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKrreIPYLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1081 QTAIVSQE-PVLFNCSIAENIAYgdnsrmvPLE-------EIKEVADAAnihsfiegLprkynTLVGLRG------VQLS 1146
Cdd:COG2884 80 RIGVVFQDfRLLPDRTVYENVAL-------PLRvtgksrkEIRRRVREV--------L-----DLVGLSDkakalpHELS 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568980685 1147 GGQKQRLAIARALLRKPKILLLDEATSALDNE-SEKVVqQALDKA-RRGKTCLVVAHRLSTIQNADM-IVVLQNGSIKE 1222
Cdd:COG2884 140 GGEQQRVAIARALVNRPELLLADEPTGNLDPEtSWEIM-ELLEEInRRGTTVLIATHDLELVDRMPKrVLELEDGRLVR 217
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
375-598 |
4.53e-36 |
|
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: 136.98 E-value: 4.53e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 375 IEFKNVSFSYPSRPsakVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDIraQNVRHYREQIG 454
Cdd:cd03300 1 IELENVSKFYGGFV---ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI--TNLPPHKRPVN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 455 VVRQEPVLF-GTTIGNNIKFGREGVGEKEMEQAAREANAYDFImafpkKFNTLVGEKGAQMSGGQKQRIAIARALVRNPK 533
Cdd:cd03300 76 TVFQNYALFpHLTVFENIAFGLRLKKLPKAEIKERVAEALDLV-----QLEGYANRKPSQLSGGQQQRVAIARALVNEPK 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568980685 534 ILILDEATSALDTESESLVQTALEKASK--GRTTIVVAHRLS-TIRGADLIVTMKDGMVVEKGTHAEL 598
Cdd:cd03300 151 VLLLDEPLGALDLKLRKDMQLELKRLQKelGITFVFVTHDQEeALTMSDRIAVMNKGKIQQIGTPEEI 218
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
1004-1220 |
3.01e-35 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 135.18 E-value: 3.01e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1004 LEFREVSFVYPcrPEVPVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVKELN---VQWLRS 1080
Cdd:COG3638 3 LELRNLSKRYP--GGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRgraLRRLRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1081 QTAIVSQEPVLF-NCSIAENI---AYGDNS------RMVPLEEIKEVADAanihsfiegLPRkyntlVGL------RGVQ 1144
Cdd:COG3638 81 RIGMIFQQFNLVpRLSVLTNVlagRLGRTStwrsllGLFPPEDRERALEA---------LER-----VGLadkayqRADQ 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568980685 1145 LSGGQKQRLAIARALLRKPKILLLDEATSALDNESEKVVQQALDKA--RRGKTCLVVAHRLSTIQN-ADMIVVLQNGSI 1220
Cdd:COG3638 147 LSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIarEDGITVVVNLHQVDLARRyADRIIGLRDGRV 225
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
1004-1237 |
3.01e-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: 134.29 E-value: 3.01e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1004 LEFREVSFVYPcrpEVPVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVkeLNVQWLRSQTA 1083
Cdd:cd03300 1 IELENVSKFYG---GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI--TNLPPHKRPVN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1084 IVSQEPVLF-NCSIAENIAYGDNSRMVPLEEIKE-VADAANIHSfIEGLPRKYNTlvglrgvQLSGGQKQRLAIARALLR 1161
Cdd:cd03300 76 TVFQNYALFpHLTVFENIAFGLRLKKLPKAEIKErVAEALDLVQ-LEGYANRKPS-------QLSGGQQQRVAIARALVN 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568980685 1162 KPKILLLDEATSALDNESEKVVQQALDKARR--GKTCLVVAHRLS-TIQNADMIVVLQNGSIKEQGTHQELLRNGDTYF 1237
Cdd:cd03300 148 EPKVLLLDEPLGALDLKLRKDMQLELKRLQKelGITFVFVTHDQEeALTMSDRIAVMNKGKIQQIGTPEEIYEEPANRF 226
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
1020-1243 |
3.65e-35 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 135.04 E-value: 3.65e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1020 PVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVKELNVQWLRSQTAIVSQEPVLFNCSIAEN 1099
Cdd:cd03288 35 PVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFN 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1100 IaygDNSRMVPLEEIKEVADAANIHSFIEGLPRKYNTLVGLRGVQLSGGQKQRLAIARALLRKPKILLLDEATSALDNES 1179
Cdd:cd03288 115 L---DPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMAT 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568980685 1180 EKVVQQALDKARRGKTCLVVAHRLSTIQNADMIVVLQNGSIKEQGTHQELLRNGDTYF-KLVAAH 1243
Cdd:cd03288 192 ENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEDGVFaSLVRTD 256
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
373-611 |
4.10e-35 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 135.04 E-value: 4.10e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 373 GNIEFKNVSFSYPS--RPsakVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDIRAQNVRHYR 450
Cdd:cd03288 18 GEIKIHDLCVRYENnlKP---VLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 451 EQIGVVRQEPVLFGTTIGNNIKFGREGVGEKEMEqAAREANAYDFIMAFPKKFNTLVGEKGAQMSGGQKQRIAIARALVR 530
Cdd:cd03288 95 SRLSIILQDPILFSGSIRFNLDPECKCTDDRLWE-ALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVR 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 531 NPKILILDEATSALDTESESLVQTALEKASKGRTTIVVAHRLSTIRGADLIVTMKDGMVVEKGTHAELMAKQ-GLYYSLA 609
Cdd:cd03288 174 KSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEdGVFASLV 253
|
..
gi 568980685 610 MA 611
Cdd:cd03288 254 RT 255
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
397-601 |
6.84e-35 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 134.69 E-value: 6.84e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 397 NLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDIRA------QNVRhyREQIGVVRQEPVLF-GTTIGN 469
Cdd:cd03294 44 SLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAmsrkelRELR--RKKISMVFQSFALLpHRTVLE 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 470 NIKFGRE--GVGEKEMEQAAREANAydfimafpkkfntLVGEKG------AQMSGGQKQRIAIARALVRNPKILILDEAT 541
Cdd:cd03294 122 NVAFGLEvqGVPRAEREERAAEALE-------------LVGLEGwehkypDELSGGMQQRVGLARALAVDPDILLMDEAF 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568980685 542 SALDTESESLVQTALEK--ASKGRTTIVVAHRLS-TIRGADLIVTMKDGMVVEKGTHAELMAK 601
Cdd:cd03294 189 SALDPLIRREMQDELLRlqAELQKTIVFITHDLDeALRLGDRIAIMKDGRLVQVGTPEEILTN 251
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
375-598 |
8.41e-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: 8.41e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 375 IEFKNVSFSYPSRP-SAKVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDP---EDGCITVDENDIRA---QNVR 447
Cdd:COG0444 2 LEVRNLKVYFPTRRgVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKlseKELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 448 HYR-EQIGVVRQE------PVLfgtTIGNNIKFG---REGVGEKEMEQAAREA-------NAYDFIMAFPKkfntlvgek 510
Cdd:COG0444 82 KIRgREIQMIFQDpmtslnPVM---TVGDQIAEPlriHGGLSKAEARERAIELlervglpDPERRLDRYPH--------- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 511 gaQMSGGQKQRIAIARALVRNPKILILDEATSALDTesesLVQtA--LE-----KASKGRTTIVVAHRLSTIRG-ADLIV 582
Cdd:COG0444 150 --ELSGGMRQRVMIARALALEPKLLIADEPTTALDV----TIQ-AqiLNllkdlQRELGLAILFITHDLGVVAEiADRVA 222
|
250
....*....|....*.
gi 568980685 583 TMKDGMVVEKGTHAEL 598
Cdd:COG0444 223 VMYAGRIVEEGPVEEL 238
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
40-316 |
9.37e-35 |
|
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: 135.07 E-value: 9.37e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 40 GILASMINGATVPLMSLVLGEISDHLINGCLVQTNRTKyqncsqtqEKLNEDIIVLTLYYIGIGAAALIFGyvqisfWVI 119
Cdd:cd18780 1 GTIALLVSSGTNLALPYFFGQVIDAVTNHSGSGGEEAL--------RALNQAVLILLGVVLIGSIATFLRS------WLF 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 120 TAA--RQTTRIRKQFFHSILAQDISWFDGSDICELNTRMTGDINKLCDGIGDKIPLMFQNISGFSIGLVISLIKSWKLSL 197
Cdd:cd18780 67 TLAgeRVVARLRKRLFSAIIAQEIAFFDVTRTGELLNRLSSDTQVLQNAVTVNLSMLLRYLVQIIGGLVFMFTTSWKLTL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 198 VVLSTSPLIMASSALCSRMIISLTSKELDAYSKAGAVAEEALSSIQTVTAFGAQEKEIQRYTQHLKDAKDAGIKRATASK 277
Cdd:cd18780 147 VMLSVVPPLSIGAVIYGKYVRKLSKKFQDALAAASTVAEESISNIRTVRSFAKETKEVSRYSEKINESYLLGKKLARASG 226
|
250 260 270
....*....|....*....|....*....|....*....
gi 568980685 278 LSLGAVYFFMNGAYGLAFWYGTSLIFGGEpgYTIGTILA 316
Cdd:cd18780 227 GFNGFMGAAAQLAIVLVLWYGGRLVIDGE--LTTGLLTS 263
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
375-612 |
1.02e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 134.11 E-value: 1.02e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 375 IEFKNVSFSYPSrPSAKVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDIRAQNVRHYREQIG 454
Cdd:PRK13648 8 IVFKNVSFQYQS-DASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 455 VVRQEP--VLFGTTIGNNIKFGREG--VGEKEME----QAAREANAYDFIMAFPKkfntlvgekgaQMSGGQKQRIAIAR 526
Cdd:PRK13648 87 IVFQNPdnQFVGSIVKYDVAFGLENhaVPYDEMHrrvsEALKQVDMLERADYEPN-----------ALSGGQKQRVAIAG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 527 ALVRNPKILILDEATSALDTESE----SLVQTAleKASKGRTTIVVAHRLSTIRGADLIVTMKDGMVVEKGTHAELMAKQ 602
Cdd:PRK13648 156 VLALNPSVIILDEATSMLDPDARqnllDLVRKV--KSEHNITIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFDHA 233
|
250
....*....|....*...
gi 568980685 603 --------GLYYSLAMAQ 612
Cdd:PRK13648 234 eeltriglDLPFPIKINQ 251
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
376-593 |
1.17e-34 |
|
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: 131.02 E-value: 1.17e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 376 EFKNVSFSYPSRPsakVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDIRAQNVRHYREQIGV 455
Cdd:cd03214 1 EVENLSVGYGGRT---VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 456 VrqepvlfgttignnikfgregvgekemEQAAREANAYDFIMafpKKFNTLvgekgaqmSGGQKQRIAIARALVRNPKIL 535
Cdd:cd03214 78 V---------------------------PQALELLGLAHLAD---RPFNEL--------SGGERQRVLLARALAQEPPIL 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568980685 536 ILDEATSALD--TESE--SLVQTalEKASKGRTTIVVAHRLS-TIRGADLIVTMKDGMVVEKG 593
Cdd:cd03214 120 LLDEPTSHLDiaHQIEllELLRR--LARERGKTVVMVLHDLNlAARYADRVILLKDGRIVAQG 180
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
375-597 |
1.91e-34 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 134.02 E-value: 1.91e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 375 IEFKNVSFSY-PSRPSAKV-LKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDIRAQNV--RHYR 450
Cdd:PRK13637 3 IKIENLTHIYmEGTPFEKKaLDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVklSDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 451 EQIGVVRQEP--VLFGTTIGNNIKFG--REGVGEKEMEQAAREAnaydfiMAFPK-KFNTLVGEKGAQMSGGQKQRIAIA 525
Cdd:PRK13637 83 KKVGLVFQYPeyQLFEETIEKDIAFGpiNLGLSEEEIENRVKRA------MNIVGlDYEDYKDKSPFELSGGQKRRVAIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568980685 526 RALVRNPKILILDEATSALD--TESESLVQTALEKASKGRTTIVVAHRLSTI-RGADLIVTMKDGMVVEKGTHAE 597
Cdd:PRK13637 157 GVVAMEPKILILDEPTAGLDpkGRDEILNKIKELHKEYNMTIILVSHSMEDVaKLADRIIVMNKGKCELQGTPRE 231
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
144-1243 |
2.27e-34 |
|
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: 143.90 E-value: 2.27e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 144 FDGSDICELNTRMTGDINKLCDGIGdkiPLMFQNISGFSIGLVISLIksWKL--SLVVLSTSPLIMAS--SALCSRMIIS 219
Cdd:TIGR01271 173 LDKISTGQLVSLLSNNLNKFDEGLA---LAHFVWIAPLQVILLMGLI--WELleVNGFCGLGFLILLAlfQACLGQKMMP 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 220 LTSKELDAYSKAGAVAEEALSSIQTVTAFGAQEkeiqrytqhlkdAKDAGIKRATASKLSL----GAVYFFMNGAYglaF 295
Cdd:TIGR01271 248 YRDKRAGKISERLAITSEIIENIQSVKAYCWEE------------AMEKIIKNIRQDELKLtrkiAYLRYFYSSAF---F 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 296 WYGTSLIFGGEPGYTI--GTILAVFFSVIhsSYCI-------GSVAPHLETFTVARGAAFNIFQVIDKKP---------- 356
Cdd:TIGR01271 313 FSGFFVVFLSVVPYALikGIILRRIFTTI--SYCIvlrmtvtRQFPGAIQTWYDSLGAITKIQDFLCKEEyktleynltt 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 357 ------NIDNFSTAGF--VPECIEGNIEFKNVS-------FSYPSRPSAKVLKGLNLKIKAGETVALVGPSGSGKSTTVQ 421
Cdd:TIGR01271 391 tevemvNVTASWDEGIgeLFEKIKQNNKARKQPngddglfFSNFSLYVTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLM 470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 422 LLQRLYDPEDGCItvdendiraqnvRHyREQIGVVRQEPVLFGTTIGNNIKFGREgVGEKEMEQAAREANAYDFIMAFPK 501
Cdd:TIGR01271 471 MIMGELEPSEGKI------------KH-SGRISFSPQTSWIMPGTIKDNIIFGLS-YDEYRYTSVIKACQLEEDIALFPE 536
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 502 KFNTLVGEKGAQMSGGQKQRIAIARALVRNPKILILDEATSALDTESE-SLVQTALEKASKGRTTIVVAHRLSTIRGADL 580
Cdd:TIGR01271 537 KDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEkEIFESCLCKLMSNKTRILVTSKLEHLKKADK 616
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 581 IVTMKDGMVVEKGTHAELMAKQGLYYSLAMAQD----IKKvdEQMES------RTCSTAGNASYGSLCDvnSAKAPCTDQ 650
Cdd:TIGR01271 617 ILLLHEGVCYFYGTFSELQAKRPDFSSLLLGLEafdnFSA--ERRNSiltetlRRVSIDGDSTVFSGPE--TIKQSFKQP 692
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 651 LEEAVHHQKTSLPEVSLLKIFKLSksewpFVVLGTLASALNGSVHPVFSIIFGKLVTMFEDKNKATLKQDAELYSMMLVV 730
Cdd:TIGR01271 693 PPEFAEKRKQSIILNPIASARKFS-----FVQMGPQKAQATTIEDAVREPSERKFSLVPEDEQGEESLPRGNQYHHGLQH 767
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 731 LG-----IVALVTYLMQGlfygraeENLaMRLRHSAFKAMLY--------------------------------QDM--A 771
Cdd:TIGR01271 768 QAqrrqsVLQLMTHSNRG-------ENR-REQLQTSFRKKSSitqqnelaseldiysrrlskdsvyeiseeineEDLkeC 839
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 772 WYDDKEN--NTGALTTTL--------------------AVDVAQ------IQGAATSRLGIVTQDVSN-----MSLSILI 818
Cdd:TIGR01271 840 FADERENvfETTTWNTYLryittnrnlvfvlifclvifLAEVAAsllglwLITDNPSAPNYVDQQHANasspdVQKPVII 919
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 819 S--------FIY-GWEMTLLILSF---------------------------AP--------------------------- 835
Cdd:TIGR01271 920 TptsayyifYIYvGTADSVLALGFfrglplvhtlltvskrlheqmlhsvlqAPmavlntmkagrilnrftkdmaiiddml 999
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 836 ----------VLAVTGMIQTAA-------------------MAGFANRDKQALKR-----AGKIATEAVENIR---TVVS 878
Cdd:TIGR01271 1000 pltlfdfiqlTLIVLGAIFVVSvlqpyifiaaipvavifimLRAYFLRTSQQLKQleseaRSPIFSHLITSLKglwTIRA 1079
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 879 LTRERAFEQMYEETLQTQHRN-ALKRAHITGCCYAVSHAFVHFAHAAGF-RFGAYLIQAGRMmpeGMFIVFtaiaygAMA 956
Cdd:TIGR01271 1080 FGRQSYFETLFHKALNLHTANwFLYLSTLRWFQMRIDIIFVFFFIAVTFiAIGTNQDGEGEV---GIILTL------AMN 1150
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 957 IGETLVWAPEYSKAKAG----ASHLFALLkNKPTINSCSQSGEKPDTCEGNL--EFREVSFVYPCRPEV----------- 1019
Cdd:TIGR01271 1151 ILSTLQWAVNSSIDVDGlmrsVSRVFKFI-DLPQEEPRPSGGGGKYQLSTVLviENPHAQKCWPSGGQMdvqgltakyte 1229
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1020 ---PVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDpMKGQVLLDGVDVKELNVQWLRSQTAIVSQEPVLFNCSI 1096
Cdd:TIGR01271 1230 agrAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTF 1308
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1097 AENIaygDNSRMVPLEEIKEVADAANIHSFIEGLPRKYNTLVGLRGVQLSGGQKQRLAIARALLRKPKILLLDEATSALD 1176
Cdd:TIGR01271 1309 RKNL---DPYEQWSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLD 1385
|
1290 1300 1310 1320 1330 1340
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568980685 1177 NESEKVVQQALDKARRGKTCLVVAHRLSTIQNADMIVVLQNGSIKEQGTHQELLrNGDTYFKLVAAH 1243
Cdd:TIGR01271 1386 PVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLL-NETSLFKQAMSA 1451
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
375-598 |
4.87e-34 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 137.84 E-value: 4.87e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 375 IEFKNVSFSYPSrpsAKVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDIRAQNVRHYREQ-I 453
Cdd:COG1129 5 LEMRGISKSFGG---VKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQAAgI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 454 GVVRQEPVLFGT-TIGNNIKFGRE-----GVGEKEMEQAAREanaydfIMA---FPKKFNTLVGEkgaqMSGGQKQRIAI 524
Cdd:COG1129 82 AIIHQELNLVPNlSVAENIFLGREprrggLIDWRAMRRRARE------LLArlgLDIDPDTPVGD----LSVAQQQLVEI 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568980685 525 ARALVRNPKILILDEATSAL-DTESESLVQTALEKASKGRTTIVVAHRLSTIRG-ADLIVTMKDGMVVEKGTHAEL 598
Cdd:COG1129 152 ARALSRDARVLILDEPTASLtEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEiADRVTVLRDGRLVGTGPVAEL 227
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1004-1176 |
5.06e-34 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 131.70 E-value: 5.06e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1004 LEFREVSFVYPcrpEVPVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYD--P---MKGQVLLDGVDV--KELNVQ 1076
Cdd:COG1117 12 IEVRNLNVYYG---DKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDliPgarVEGEILLDGEDIydPDVDVV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1077 WLRSQTAIVSQEPVLFNCSIAENIAYG-----DNSRMVpLEEI-----------KEVADaaNIHSfieglprkyntlvgl 1140
Cdd:COG1117 89 ELRRRVGMVFQKPNPFPKSIYDNVAYGlrlhgIKSKSE-LDEIveeslrkaalwDEVKD--RLKK--------------- 150
|
170 180 190
....*....|....*....|....*....|....*.
gi 568980685 1141 RGVQLSGGQKQRLAIARALLRKPKILLLDEATSALD 1176
Cdd:COG1117 151 SALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALD 186
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
1004-1224 |
1.06e-33 |
|
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: 129.30 E-value: 1.06e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1004 LEFREVSFVYPcrpEVPVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDV-----KELNVqwl 1078
Cdd:cd03301 1 VELENVTKRFG---NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVtdlppKDRDI--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1079 rsqtAIVSQEPVLF-NCSIAENIAYGDNSRMVPLEEIKE-VADAANIHSfIEGLPRKYNTlvglrgvQLSGGQKQRLAIA 1156
Cdd:cd03301 75 ----AMVFQNYALYpHMTVYDNIAFGLKLRKVPKDEIDErVREVAELLQ-IEHLLDRKPK-------QLSGGQRQRVALG 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568980685 1157 RALLRKPKILLLDEATSALDNESEKVVQQALDK--ARRGKTCLVVAH-RLSTIQNADMIVVLQNGSIKEQG 1224
Cdd:cd03301 143 RAIVREPKVFLMDEPLSNLDAKLRVQMRAELKRlqQRLGTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1020-1228 |
1.09e-33 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 134.30 E-value: 1.09e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1020 PVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVKELNVQwlRSQTAIVSQEPVLF-NCSIAE 1098
Cdd:PRK09452 28 EVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE--NRHVNTVFQSYALFpHMTVFE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1099 NIAYGDNSRMVPLEEIKE-VADA---ANIHSFIEGLPRkyntlvglrgvQLSGGQKQRLAIARALLRKPKILLLDEATSA 1174
Cdd:PRK09452 106 NVAFGLRMQKTPAAEITPrVMEAlrmVQLEEFAQRKPH-----------QLSGGQQQRVAIARAVVNKPKVLLLDESLSA 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 568980685 1175 LDNESEKVVQQALDKARR--GKTCLVVAH-RLSTIQNADMIVVLQNGSIKEQGTHQE 1228
Cdd:PRK09452 175 LDYKLRKQMQNELKALQRklGITFVFVTHdQEEALTMSDRIVVMRDGRIEQDGTPRE 231
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1004-1234 |
1.30e-33 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 131.29 E-value: 1.30e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1004 LEFREVSFVYPcRPEVPVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVKELNVQWLRSQTA 1083
Cdd:PRK13635 6 IRVEHISFRYP-DAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1084 IVSQEP--VLFNCSIAENIAYGDNSRMVPLEEIKEVADAA----NIHSFIEGLPRKyntlvglrgvqLSGGQKQRLAIAR 1157
Cdd:PRK13635 85 MVFQNPdnQFVGATVQDDVAFGLENIGVPREEMVERVDQAlrqvGMEDFLNREPHR-----------LSGGQKQRVAIAG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1158 ALLRKPKILLLDEATSALDNESEkvvQQALDKARRGK-----TCLVVAHRLSTIQNADMIVVLQNGSIKEQGTHQELLRN 1232
Cdd:PRK13635 154 VLALQPDIIILDEATSMLDPRGR---REVLETVRQLKeqkgiTVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFKS 230
|
..
gi 568980685 1233 GD 1234
Cdd:PRK13635 231 GH 232
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1021-1237 |
1.46e-33 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 133.31 E-value: 1.46e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1021 VLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVKELNVQwlRSQTAIVSQEPVLF-NCSIAEN 1099
Cdd:PRK11432 21 VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQ--QRDICMVFQSYALFpHMSLGEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1100 IAYGDNSRMVPLEEIKE-VADAAnihsfieglprkynTLVGLRGV------QLSGGQKQRLAIARALLRKPKILLLDEAT 1172
Cdd:PRK11432 99 VGYGLKMLGVPKEERKQrVKEAL--------------ELVDLAGFedryvdQISGGQQQRVALARALILKPKVLLFDEPL 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568980685 1173 SALD-----NESEKV--VQQALdkarrGKTCLVVAHRLS-TIQNADMIVVLQNGSIKEQGTHQELLRNGDTYF 1237
Cdd:PRK11432 165 SNLDanlrrSMREKIreLQQQF-----NITSLYVTHDQSeAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRF 232
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
375-598 |
1.65e-33 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 132.96 E-value: 1.65e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 375 IEFKNVSFSYPSRpsaKVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDIRAQnvRHYRE-QI 453
Cdd:COG1118 3 IEVRNISKRFGSF---TLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTN--LPPRErRV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 454 GVVRQEPVLFG-TTIGNNIKFG--REGVGEKEMEQAARE----------ANAYdfimafPkkfntlvgekgAQMSGGQKQ 520
Cdd:COG1118 78 GFVFQHYALFPhMTVAENIAFGlrVRPPSKAEIRARVEEllelvqleglADRY------P-----------SQLSGGQRQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 521 RIAIARALVRNPKILILDEATSALDTEseslVQTALEK------ASKGRTTIVVAH------RLstirgADLIVTMKDGM 588
Cdd:COG1118 141 RVALARALAVEPEVLLLDEPFGALDAK----VRKELRRwlrrlhDELGGTTVFVTHdqeealEL-----ADRVVVMNQGR 211
|
250
....*....|
gi 568980685 589 VVEKGTHAEL 598
Cdd:COG1118 212 IEQVGTPDEV 221
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
375-593 |
1.75e-33 |
|
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: 128.91 E-value: 1.75e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 375 IEFKNVSFSYPSRpsaKVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDIraQNVRHYREQIG 454
Cdd:cd03301 1 VELENVTKRFGNV---TALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDV--TDLPPKDRDIA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 455 VVRQEPVLF-GTTIGNNIKFG--REGVGEKEMEQAAREAnaydfimAFPKKFNTLVGEKGAQMSGGQKQRIAIARALVRN 531
Cdd:cd03301 76 MVFQNYALYpHMTVYDNIAFGlkLRKVPKDEIDERVREV-------AELLQIEHLLDRKPKQLSGGQRQRVALGRAIVRE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568980685 532 PKILILDEATSALDTESESLVQTALEKASK--GRTTIVVAH---RLSTIrgADLIVTMKDGMVVEKG 593
Cdd:cd03301 149 PKVFLMDEPLSNLDAKLRVQMRAELKRLQQrlGTTTIYVTHdqvEAMTM--ADRIAVMNDGQIQQIG 213
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
375-598 |
1.76e-33 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 132.89 E-value: 1.76e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 375 IEFKNVSFSYPSRPsakVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDE---NDIRAQNvRHyre 451
Cdd:COG3839 4 LELENVSKSYGGVE---ALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGrdvTDLPPKD-RN--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 452 qIGVVRQEPVLFGT-TIGNNIKFG--REGVGEKEMEQAAREAnaydfimAfpkkfnTLVG------EKGAQMSGGQKQRI 522
Cdd:COG3839 77 -IAMVFQSYALYPHmTVYENIAFPlkLRKVPKAEIDRRVREA-------A------ELLGledlldRKPKQLSGGQRQRV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 523 AIARALVRNPKILILDEATSALDTEsesL-VQTALE----KASKGRTTIVVAHRLS---TIrgADLIVTMKDGMVVEKGT 594
Cdd:COG3839 143 ALGRALVREPKVFLLDEPLSNLDAK---LrVEMRAEikrlHRRLGTTTIYVTHDQVeamTL--ADRIAVMNDGRIQQVGT 217
|
....
gi 568980685 595 HAEL 598
Cdd:COG3839 218 PEEL 221
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
1005-1224 |
1.99e-33 |
|
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: 127.55 E-value: 1.99e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1005 EFREVSFVYPCRPevpVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVKELNVQWLRSQTAI 1084
Cdd:cd03214 1 EVENLSVGYGGRT---VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1085 VSQepvlfncsiaeniaygdnsrmvpleeikeVADAANIHSFIEglpRKYNTLvglrgvqlSGGQKQRLAIARALLRKPK 1164
Cdd:cd03214 78 VPQ-----------------------------ALELLGLAHLAD---RPFNEL--------SGGERQRVLLARALAQEPP 117
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568980685 1165 ILLLDEATSALD--NESE--KVVQQAldKARRGKTCLVVAHRLS-TIQNADMIVVLQNGSIKEQG 1224
Cdd:cd03214 118 ILLLDEPTSHLDiaHQIEllELLRRL--ARERGKTVVMVLHDLNlAARYADRVILLKDGRIVAQG 180
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1005-1225 |
2.19e-33 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 132.62 E-value: 2.19e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1005 EFREVSFVYPC-RPEVPVLQNMSLSIEKGKTVAFVGSSGCGKST---CVQLLQRfydPMKGQVLLDGVDVKELNVQWLRS 1080
Cdd:PRK11153 3 ELKNISKVFPQgGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTlirCINLLER---PTSGRVLVDGQDLTALSEKELRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1081 ---QTAIVSQEpvlFNC----SIAENIAYgdnsrmvPLEeikeVA--DAANIHSFIEGLPrkynTLVGL---RGV---QL 1145
Cdd:PRK11153 80 arrQIGMIFQH---FNLlssrTVFDNVAL-------PLE----LAgtPKAEIKARVTELL----ELVGLsdkADRypaQL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1146 SGGQKQRLAIARALLRKPKILLLDEATSALDNESEKVVQQALDKARR--GKTCLVVAHRLSTI-QNADMIVVLQNGSIKE 1222
Cdd:PRK11153 142 SGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRelGLTIVLITHEMDVVkRICDRVAVIDAGRLVE 221
|
...
gi 568980685 1223 QGT 1225
Cdd:PRK11153 222 QGT 224
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
1019-1232 |
5.64e-33 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 129.30 E-value: 5.64e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1019 VPVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVKELN---VQWLRSQT-AIVSQEPVLF-N 1093
Cdd:cd03294 37 TVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSrkeLRELRRKKiSMVFQSFALLpH 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1094 CSIAENIAYGDNSRMVPLEEIKEVA----DAANIHSFIEGLPRkyntlvglrgvQLSGGQKQRLAIARALLRKPKILLLD 1169
Cdd:cd03294 117 RTVLENVAFGLEVQGVPRAEREERAaealELVGLEGWEHKYPD-----------ELSGGMQQRVGLARALAVDPDILLMD 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568980685 1170 EATSALDNESEKVVQQALDK--ARRGKTCLVVAHRLS-TIQNADMIVVLQNGSIKEQGTHQELLRN 1232
Cdd:cd03294 186 EAFSALDPLIRREMQDELLRlqAELQKTIVFITHDLDeALRLGDRIAIMKDGRLVQVGTPEEILTN 251
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
1021-1220 |
8.47e-33 |
|
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: 126.88 E-value: 8.47e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1021 VLQNMSLSIEKGKTVAFVGSSGCGKST---CVQLLQRfydPMKGQVLLDGVDV--KELNVQWLRSQTAIVSQEPVLF-NC 1094
Cdd:cd03262 15 VLKGIDLTVKKGEVVVIIGPSGSGKSTllrCINLLEE---PDSGTIIIDGLKLtdDKKNINELRQKVGMVFQQFNLFpHL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1095 SIAENIAYGdnsrmvPLEEIKEVADAAnihsfiEGLPRKYNTLVGLRGV------QLSGGQKQRLAIARALLRKPKILLL 1168
Cdd:cd03262 92 TVLENITLA------PIKVKGMSKAEA------EERALELLEKVGLADKadaypaQLSGGQQQRVAIARALAMNPKVMLF 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 568980685 1169 DEATSALD----NESEKVVQQAldkARRGKTCLVVAHRLSTIQN-ADMIVVLQNGSI 1220
Cdd:cd03262 160 DEPTSALDpelvGEVLDVMKDL---AEEGMTMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
376-575 |
1.12e-32 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 126.49 E-value: 1.12e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 376 EFKNVSFSYPSRPsakVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDendirAQNVRHYREQIGV 455
Cdd:cd03235 1 EVEDLTVSYGGHP---VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVF-----GKPLEKERKRIGY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 456 VRQEPVL---FGTTI------GNNIKFGREGVGEKEMEQAAREA----NAYDFImafpkkfNTLVGEkgaqMSGGQKQRI 522
Cdd:cd03235 73 VPQRRSIdrdFPISVrdvvlmGLYGHKGLFRRLSKADKAKVDEAlervGLSELA-------DRQIGE----LSGGQQQRV 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 568980685 523 AIARALVRNPKILILDEATSALDTESESLVQTALEK-ASKGRTTIVVAHRLSTI 575
Cdd:cd03235 142 LLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRElRREGMTILVVTHDLGLV 195
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1004-1232 |
1.15e-32 |
|
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: 129.79 E-value: 1.15e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1004 LEFREVSFVYPCRP-EVPVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDP---MKGQVLLDGVDVKELN---VQ 1076
Cdd:COG0444 2 LEVRNLKVYFPTRRgVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSekeLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1077 WLR-SQTAIVSQEPvlFNC---------SIAENIAYgdnSRMVPLEEIKEVAdaanihsfIEGLprkynTLVGLRGV--- 1143
Cdd:COG0444 82 KIRgREIQMIFQDP--MTSlnpvmtvgdQIAEPLRI---HGGLSKAEARERA--------IELL-----ERVGLPDPerr 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1144 ------QLSGGQKQRLAIARALLRKPKILLLDEATSALDnesekV-VQ-QALD-----KARRGKTCLVVAHRLSTI-QNA 1209
Cdd:COG0444 144 ldryphELSGGMRQRVMIARALALEPKLLIADEPTTALD-----VtIQaQILNllkdlQRELGLAILFITHDLGVVaEIA 218
|
250 260
....*....|....*....|...
gi 568980685 1210 DMIVVLQNGSIKEQGTHQELLRN 1232
Cdd:COG0444 219 DRVAVMYAGRIVEEGPVEELFEN 241
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
1004-1220 |
1.58e-32 |
|
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: 124.43 E-value: 1.58e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1004 LEFREVSFVYPcrpEVPVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVKELNVQwLRSQTA 1083
Cdd:cd03230 1 IEVRNLSKRYG---KKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEE-VKRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1084 IVSQEPVLF-NCSIAENIaygdnsrmvpleeikevadaanihsfieglprkyntlvglrgvQLSGGQKQRLAIARALLRK 1162
Cdd:cd03230 77 YLPEEPSLYeNLTVRENL-------------------------------------------KLSGGMKQRLALAQALLHD 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1163 PKILLLDEATSALDNESEKVVQQALDK-ARRGKTCLVVAHRLSTIQN-ADMIVVLQNGSI 1220
Cdd:cd03230 114 PELLILDEPTSGLDPESRREFWELLRElKKEGKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
392-601 |
2.08e-32 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 126.30 E-value: 2.08e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 392 VLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDIraQNVRHYREQIGVVRQEPVLF-GTTIGNN 470
Cdd:cd03299 14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDI--TNLPPEKRDISYVPQNYALFpHMTVYKN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 471 IKFG--REGVGEKEMEQAAREanaydfiMAFPKKFNTLVGEKGAQMSGGQKQRIAIARALVRNPKILILDEATSALDTES 548
Cdd:cd03299 92 IAYGlkKRKVDKKEIERKVLE-------IAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRT 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 568980685 549 ESLVQTALEKASK--GRTTIVVAHRLSTIRG-ADLIVTMKDGMVVEKGTHAELMAK 601
Cdd:cd03299 165 KEKLREELKKIRKefGVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEVFKK 220
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
1004-1229 |
3.49e-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: 125.76 E-value: 3.49e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1004 LEFREVSFVYPcrPEVPVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVKELNVQWL---RS 1080
Cdd:cd03256 1 IEVENLSKTYP--NGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALrqlRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1081 QTAIVSQEPVLFN-CSIAENIAYGDNSRM---------VPLEEIKEVADAanihsfiegLPRkyntlVGL------RGVQ 1144
Cdd:cd03256 79 QIGMIFQQFNLIErLSVLENVLSGRLGRRstwrslfglFPKEEKQRALAA---------LER-----VGLldkayqRADQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1145 LSGGQKQRLAIARALLRKPKILLLDEATSALDNESEKVVQQALDKARR--GKTCLVVAHRLSTI-QNADMIVVLQNGSIK 1221
Cdd:cd03256 145 LSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINReeGITVIVSLHQVDLArEYADRIVGLKDGRIV 224
|
....*...
gi 568980685 1222 EQGTHQEL 1229
Cdd:cd03256 225 FDGPPAEL 232
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
375-601 |
4.58e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 127.20 E-value: 4.58e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 375 IEFKNVSFSY----PSRPSAkvLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDIRAQN----V 446
Cdd:PRK13646 3 IRFDNVSYTYqkgtPYEHQA--IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTkdkyI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 447 RHYREQIGVVRQ--EPVLFGTTIGNNIKFGREGVGekeMEQAAREANAYDFIM--AFPKKfntLVGEKGAQMSGGQKQRI 522
Cdd:PRK13646 81 RPVRKRIGMVFQfpESQLFEDTVEREIIFGPKNFK---MNLDEVKNYAHRLLMdlGFSRD---VMSQSPFQMSGGQMRKI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 523 AIARALVRNPKILILDEATSALDTESESLVQTALEK--ASKGRTTIVVAHRLSTI-RGADLIVTMKDGMVVEKGTHAELM 599
Cdd:PRK13646 155 AIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSlqTDENKTIILVSHDMNEVaRYADEVIVMKEGSIVSQTSPKELF 234
|
..
gi 568980685 600 AK 601
Cdd:PRK13646 235 KD 236
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
375-600 |
1.01e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 125.98 E-value: 1.01e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 375 IEFKNVSFSYPSRPSAKVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDIRAQNVRHYREQIG 454
Cdd:PRK13642 5 LEVENLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 455 VVRQEP--VLFGTTIGNNIKFGRE--GVGEKEMEQAAREA----NAYDFIMAFPkkfntlvgekgAQMSGGQKQRIAIAR 526
Cdd:PRK13642 85 MVFQNPdnQFVGATVEDDVAFGMEnqGIPREEMIKRVDEAllavNMLDFKTREP-----------ARLSGGQKQRVAVAG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568980685 527 ALVRNPKILILDEATSALDTESESLVQTALE--KASKGRTTIVVAHRLSTIRGADLIVTMKDGMVVEKGTHAELMA 600
Cdd:PRK13642 154 IIALRPEIIILDESTSMLDPTGRQEIMRVIHeiKEKYQLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFA 229
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
374-596 |
1.09e-31 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 124.74 E-value: 1.09e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 374 NIEFKNVSFSYPSRPsakVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDEN------DIRAQNVR 447
Cdd:COG4161 2 SIQLKNINCFYGSHQ---ALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHqfdfsqKPSEKAIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 448 HYREQIGVVRQE----PVLfgTTIGNNI-------KFGREGVGEKEMEQAAREANAyDFIMAFPkkfntlvgekgAQMSG 516
Cdd:COG4161 79 LLRQKVGMVFQQynlwPHL--TVMENLIeapckvlGLSKEQAREKAMKLLARLRLT-DKADRFP-----------LHLSG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 517 GQKQRIAIARALVRNPKILILDEATSALDTE-SESLVQTALEKASKGRTTIVVAHRLSTIRG-ADLIVTMKDGMVVEKGT 594
Cdd:COG4161 145 GQQQRVAIARALMMEPQVLLFDEPTAALDPEiTAQVVEIIRELSQTGITQVIVTHEVEFARKvASQVVYMEKGRIIEQGD 224
|
..
gi 568980685 595 HA 596
Cdd:COG4161 225 AS 226
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
1009-1221 |
1.25e-31 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 123.14 E-value: 1.25e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1009 VSFVYPCRPEVpvLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVKelnvQWLRSQTA-IVSQ 1087
Cdd:cd03226 5 ISFSYKKGTEI--LDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIK----AKERRKSIgYVMQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1088 EP--VLFNCSIAENIAYGDNSRMVPLEEIKEVADAANIHSFIEGLPRkyntlvglrgvQLSGGQKQRLAIARALLRKPKI 1165
Cdd:cd03226 79 DVdyQLFTDSVREELLLGLKELDAGNEQAETVLKDLDLYALKERHPL-----------SLSGGQKQRLAIAAALLSGKDL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 568980685 1166 LLLDEATSALDNESEKVVQQALDK-ARRGKTCLVVAHRLSTIQN-ADMIVVLQNGSIK 1221
Cdd:cd03226 148 LIFDEPTSGLDYKNMERVGELIRElAAQGKAVIVITHDYEFLAKvCDRVLLLANGAIV 205
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
378-590 |
1.29e-31 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 123.14 E-value: 1.29e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 378 KNVSFSYpsRPSAKVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDIRAqnvRHYREQIGVVR 457
Cdd:cd03226 3 ENISFSY--KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKA---KERRKSIGYVM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 458 QEP--VLFGTTIGNNIKFGREGVGEK--EMEQAAREANAYDFIMAFPkkfntlvgekgAQMSGGQKQRIAIARALVRNPK 533
Cdd:cd03226 78 QDVdyQLFTDSVREELLLGLKELDAGneQAETVLKDLDLYALKERHP-----------LSLSGGQKQRLAIAAALLSGKD 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 568980685 534 ILILDEATSALDTES-ESLVQTALEKASKGRTTIVVAHRLSTI-RGADLIVTMKDGMVV 590
Cdd:cd03226 147 LLIFDEPTSGLDYKNmERVGELIRELAAQGKAVIVITHDYEFLaKVCDRVLLLANGAIV 205
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
392-600 |
1.76e-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: 1.76e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 392 VLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDIRAQN--------VRHYREQIGVVRQEPVLF 463
Cdd:PRK11264 18 VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARslsqqkglIRQLRQHVGFVFQNFNLF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 464 -GTTIGNNIKFGR---EGVGEKEMEQAAREANAYDFIM----AFPKKfntlvgekgaqMSGGQKQRIAIARALVRNPKIL 535
Cdd:PRK11264 98 pHRTVLENIIEGPvivKGEPKEEATARARELLAKVGLAgketSYPRR-----------LSGGQQQRVAIARALAMRPEVI 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568980685 536 ILDEATSALDTESESLVQTALEK-ASKGRTTIVVAHRLSTIRG-ADLIVTMKDGMVVEKGTHAELMA 600
Cdd:PRK11264 167 LFDEPTSALDPELVGEVLNTIRQlAQEKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKALFA 233
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
375-590 |
2.24e-31 |
|
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: 121.00 E-value: 2.24e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 375 IEFKNVSFSYPSrpsAKVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDIRAQNVRHYReqig 454
Cdd:cd03216 1 LELRGITKRFGG---VKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDAR---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 455 vvrqepvlfgttignnikfgREGVGekemeqaareanaydfiMAFpkkfntlvgekgaQMSGGQKQRIAIARALVRNPKI 534
Cdd:cd03216 74 --------------------RAGIA-----------------MVY-------------QLSVGERQMVEIARALARNARL 103
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 568980685 535 LILDEATSAL-DTESESLVQTALEKASKGRTTIVVAHRLSTIRG-ADLIVTMKDGMVV 590
Cdd:cd03216 104 LILDEPTAALtPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEiADRVTVLRDGRVV 161
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
84-345 |
2.79e-31 |
|
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: 124.90 E-value: 2.79e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 84 TQEKLNEDIIVLTLYYIGIGAAALIFGYVQISFWVITAARQTTRIRKQFFHSILAQDISWFDGSDICELNTRMTGDINKL 163
Cdd:cd18576 27 LGGGDTASLNQIALLLLGLFLLQAVFSFFRIYLFARVGERVVADLRKDLYRHLQRLPLSFFHERRVGELTSRLSNDVTQI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 164 CDGIGDKIPLMFQNISGFSIGLVISLIKSWKLSLVVLSTSPLIMASSALCSRMIISLTSKELDAYSKAGAVAEEALSSIQ 243
Cdd:cd18576 107 QDTLTTTLAEFLRQILTLIGGVVLLFFISWKLTLLMLATVPVVVLVAVLFGRRIRKLSKKVQDELAEANTIVEETLQGIR 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 244 TVTAFGAQEKEIQRYTQHLKDAKDAGIKRATASKLSLGAVYFFMNGAYGLAFWYGTSLIFGGEpgYTIGTILA-VFFSV- 321
Cdd:cd18576 187 VVKAFTREDYEIERYRKALERVVKLALKRARIRALFSSFIIFLLFGAIVAVLWYGGRLVLAGE--LTAGDLVAfLLYTLf 264
|
250 260
....*....|....*....|....
gi 568980685 322 IHSSycIGSVAPHLETFTVARGAA 345
Cdd:cd18576 265 IAGS--IGSLADLYGQLQKALGAS 286
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1026-1232 |
2.83e-31 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 126.00 E-value: 2.83e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1026 SLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVKELN---VQWLRSQTAIVSQEPvlfncsiaeniaY 1102
Cdd:COG4608 38 SFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSgreLRPLRRRMQMVFQDP------------Y 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1103 GD-NSRMV-------PLeEIKEVADAANIHSFIEGLPRKyntlVGLRGV-------QLSGGQKQRLAIARALLRKPKILL 1167
Cdd:COG4608 106 ASlNPRMTvgdiiaePL-RIHGLASKAERRERVAELLEL----VGLRPEhadryphEFSGGQRQRIGIARALALNPKLIV 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568980685 1168 LDEATSALDnesekVVQQA------LD-KARRGKTCLVVAHRLSTIQN-ADMIVVLQNGSIKEQGTHQELLRN 1232
Cdd:COG4608 181 CDEPVSALD-----VSIQAqvlnllEDlQDELGLTYLFISHDLSVVRHiSDRVAVMYLGKIVEIAPRDELYAR 248
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
391-600 |
4.32e-31 |
|
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: 129.80 E-value: 4.32e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 391 KVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLyDPEDGCITVDENDI---RAQNVRHYREQIGVVRQEPvlFGT-- 465
Cdd:COG4172 300 KAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRL-IPSEGEIRFDGQDLdglSRRALRPLRRRMQVVFQDP--FGSls 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 466 ---TIGNNIKFG----REGVGEKEMEQAAREANAY-----DFIMAFPKKFntlvgekgaqmSGGQKQRIAIARALVRNPK 533
Cdd:COG4172 377 prmTVGQIIAEGlrvhGPGLSAAERRARVAEALEEvgldpAARHRYPHEF-----------SGGQRQRIAIARALILEPK 445
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568980685 534 ILILDEATSALDteseSLVQT---ALEK---ASKGRTTIVVAHRLSTIRG-ADLIVTMKDGMVVEKGTHAELMA 600
Cdd:COG4172 446 LLVLDEPTSALD----VSVQAqilDLLRdlqREHGLAYLFISHDLAVVRAlAHRVMVMKDGKVVEQGPTEQVFD 515
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1020-1237 |
5.13e-31 |
|
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: 122.45 E-value: 5.13e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1020 PVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVKELNVQwlRSQTAIVSQEPVLF-NCSIAE 1098
Cdd:cd03296 16 VALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQ--ERNVGFVFQHYALFrHMTVFD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1099 NIAYGdnSRMVPleeIKEVADAANIHSFIEGLPRkyntLVGLRGV------QLSGGQKQRLAIARALLRKPKILLLDEAT 1172
Cdd:cd03296 94 NVAFG--LRVKP---RSERPPEAEIRAKVHELLK----LVQLDWLadrypaQLSGGQRQRVALARALAVEPKVLLLDEPF 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568980685 1173 SALDNESEKVVQQALDKA--RRGKTCLVVAHRLS-TIQNADMIVVLQNGSIKEQGTHQELLRNGDTYF 1237
Cdd:cd03296 165 GALDAKVRKELRRWLRRLhdELHVTTVFVTHDQEeALEVADRVVVMNKGRIEQVGTPDEVYDHPASPF 232
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
375-591 |
6.23e-31 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 122.84 E-value: 6.23e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 375 IEFKNVSFSYPSRpsaKVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGC-----ITVDENDIRAQNVR-- 447
Cdd:COG1117 12 IEVRNLNVYYGDK---QALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDLIPGArvegeILLDGEDIYDPDVDvv 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 448 HYREQIGVVRQEPVLFGTTIGNNIKFG-RE-GVGEK-EM----EQAAREANAYDfimafpkkfntlvgE-------KGAQ 513
Cdd:COG1117 89 ELRRRVGMVFQKPNPFPKSIYDNVAYGlRLhGIKSKsELdeivEESLRKAALWD--------------EvkdrlkkSALG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 514 MSGGQKQRIAIARALVRNPKILILDEATSALDTES----ESLVQTaLekasKGRTTIV-VAHRLS-TIRGADLIVTMKDG 587
Cdd:COG1117 155 LSGGQQQRLCIARALAVEPEVLLMDEPTSALDPIStakiEELILE-L----KKDYTIViVTHNMQqAARVSDYTAFFYLG 229
|
....
gi 568980685 588 MVVE 591
Cdd:COG1117 230 ELVE 233
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1004-1231 |
7.60e-31 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 122.12 E-value: 7.60e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1004 LEFREVSFVYPcrpEVPVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVKElnvQWLR---- 1079
Cdd:COG1121 7 IELENLTVSYG---GRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRR---ARRRigyv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1080 SQTAIVSQE-PVlfncSIAENIAYGDNSRMVPL----EEIKEVADAAnihsfIEglprkyntLVGLRGV------QLSGG 1148
Cdd:COG1121 81 PQRAEVDWDfPI----TVRDVVLMGRYGRRGLFrrpsRADREAVDEA-----LE--------RVGLEDLadrpigELSGG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1149 QKQRLAIARALLRKPKILLLDEATSALDNESEKVVQQALDK-ARRGKTCLVVAHRLSTI-QNADMIVVLqNGSIKEQGTH 1226
Cdd:COG1121 144 QQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRElRREGKTILVVTHDLGAVrEYFDRVLLL-NRGLVAHGPP 222
|
....*
gi 568980685 1227 QELLR 1231
Cdd:COG1121 223 EEVLT 227
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
1020-1230 |
7.86e-31 |
|
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: 122.99 E-value: 7.86e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1020 PVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVKELN---VQWLRSQTAIVSQE-PVLFN-- 1093
Cdd:TIGR02769 25 PVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDrkqRRAFRRDVQLVFQDsPSAVNpr 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1094 CSIAENIAygdnSRMVPLEEIKEVADAANIHSFIEglprkyntLVGLRG-------VQLSGGQKQRLAIARALLRKPKIL 1166
Cdd:TIGR02769 105 MTVRQIIG----EPLRHLTSLDESEQKARIAELLD--------MVGLRSedadklpRQLSGGQLQRINIARALAVKPKLI 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568980685 1167 LLDEATSALDNESEKVVQQALDK--ARRGKTCLVVAHRLSTIQN-ADMIVVLQNGSIKEQGTHQELL 1230
Cdd:TIGR02769 173 VLDEAVSNLDMVLQAVILELLRKlqQAFGTAYLFITHDLRLVQSfCQRVAVMDKGQIVEECDVAQLL 239
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
386-601 |
1.03e-30 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 124.46 E-value: 1.03e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 386 SRPSAKV--LKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDI---RAQNVRHYREQIGVVRQEP 460
Cdd:COG4608 25 GRTVGVVkaVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDItglSGRELRPLRRRMQMVFQDP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 461 vlFGT-----TIGNNIKFGRE--GVG-EKEMEQAAREA------NAyDFIMAFPKKFntlvgekgaqmSGGQKQRIAIAR 526
Cdd:COG4608 105 --YASlnprmTVGDIIAEPLRihGLAsKAERRERVAELlelvglRP-EHADRYPHEF-----------SGGQRQRIGIAR 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568980685 527 ALVRNPKILILDEATSALDTESESLVQTALE--KASKGRTTIVVAHRLSTIRG-ADLIVTMKDGMVVEKGTHAELMAK 601
Cdd:COG4608 171 ALALNPKLIVCDEPVSALDVSIQAQVLNLLEdlQDELGLTYLFISHDLSVVRHiSDRVAVMYLGKIVEIAPRDELYAR 248
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
375-601 |
1.50e-30 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 124.14 E-value: 1.50e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 375 IEFKNVSFSYPSRPSAKV-LKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDI---RAQNVRHYR 450
Cdd:PRK11153 2 IELKNISKVFPQGGRTIHaLNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLtalSEKELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 451 EQIGVVRQE-PVLFGTTIGNNIKFGREGVGEKEMEQAAREANAYDfimafpkkfntLVG--EKG----AQMSGGQKQRIA 523
Cdd:PRK11153 82 RQIGMIFQHfNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLE-----------LVGlsDKAdrypAQLSGGQKQRVA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 524 IARALVRNPKILILDEATSALDTESESLVQTALEKASK--GRTTIVVAHRLSTIRG-ADLIVTMKDGMVVEKGTHAELMA 600
Cdd:PRK11153 151 IARALASNPKVLLCDEATSALDPATTRSILELLKDINRelGLTIVLITHEMDVVKRiCDRVAVIDAGRLVEQGTVSEVFS 230
|
.
gi 568980685 601 K 601
Cdd:PRK11153 231 H 231
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1003-1231 |
1.53e-30 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 121.02 E-value: 1.53e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1003 NLEFREVSFVYPCRPevpvlQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVKELNVqwlrSQ- 1081
Cdd:COG3840 1 MLRLDDLTYRYGDFP-----LRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPP----AEr 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1082 -TAIVSQEPVLFN-CSIAENIAYGDNSRMVP-LEEIKEVADAA---NIHSFIEGLPRkyntlvglrgvQLSGGQKQRLAI 1155
Cdd:COG3840 72 pVSMLFQENNLFPhLTVAQNIGLGLRPGLKLtAEQRAQVEQALervGLAGLLDRLPG-----------QLSGGQRQRVAL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1156 ARALLRKPKILLLDEATSALD----NESEKVVQQALDkaRRGKTCLVVAHRLSTIQN-ADMIVVLQNGSIKEQGTHQELL 1230
Cdd:COG3840 141 ARCLVRKRPILLLDEPFSALDpalrQEMLDLVDELCR--ERGLTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAALL 218
|
.
gi 568980685 1231 R 1231
Cdd:COG3840 219 D 219
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
391-593 |
2.41e-30 |
|
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: 119.71 E-value: 2.41e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 391 KVLKGLNLKIK---AGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDE---NDIRAQ-NVRHYREQIGVVRQEPVLF 463
Cdd:cd03297 8 KRLPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvlFDSRKKiNLPPQQRKIGLVFQQYALF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 464 -GTTIGNNIKFGREGVGEKEMEQAAREANAYdfiMAFPKkfntLVGEKGAQMSGGQKQRIAIARALVRNPKILILDEATS 542
Cdd:cd03297 88 pHLNVRENLAFGLKRKRNREDRISVDELLDL---LGLDH----LLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFS 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 568980685 543 ALDTESESLVQTALEKASK--GRTTIVVAHRLSTI-RGADLIVTMKDGMVVEKG 593
Cdd:cd03297 161 ALDRALRLQLLPELKQIKKnlNIPVIFVTHDLSEAeYLADRIVVMEDGRLQYIG 214
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
375-594 |
2.50e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 121.78 E-value: 2.50e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 375 IEFKNVSFSYPS-RP-SAKVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDIRAQ----NVRH 448
Cdd:PRK13649 3 INLQNVSYTYQAgTPfEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTsknkDIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 449 YREQIGVVRQ--EPVLFGTTIGNNIKFGRE--GVGEKEMEQAAREANAYDFIMafpkkfNTLVGEKGAQMSGGQKQRIAI 524
Cdd:PRK13649 83 IRKKVGLVFQfpESQLFEETVLKDVAFGPQnfGVSQEEAEALAREKLALVGIS------ESLFEKNPFELSGGQMRRVAI 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568980685 525 ARALVRNPKILILDEATSALDTESESLVQTALEKASKGRTTIV-VAHRLSTIRG-ADLIVTMKDGMVVEKGT 594
Cdd:PRK13649 157 AGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVlVTHLMDDVANyADFVYVLEKGKLVLSGK 228
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
375-604 |
2.74e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 122.05 E-value: 2.74e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 375 IEFKNVSFSY-PSRPSAK-VLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDIRAQ----NVRH 448
Cdd:PRK13634 3 ITFQKVEHRYqYKTPFERrALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGkknkKLKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 449 YREQIGVVRQ--EPVLFGTTIGNNIKFGRE--GVGEKEMEQAAREANAydfimafpkkfntLVG------EKGA-QMSGG 517
Cdd:PRK13634 83 LRKKVGIVFQfpEHQLFEETVEKDICFGPMnfGVSEEDAKQKAREMIE-------------LVGlpeellARSPfELSGG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 518 QKQRIAIARALVRNPKILILDEATSALDTESESLVQTALEK--ASKGRTTIVVAHRLSTI-RGADLIVTMKDGMVVEKGT 594
Cdd:PRK13634 150 QMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKlhKEKGLTTVLVTHSMEDAaRYADQIVVMHKGTVFLQGT 229
|
250
....*....|....*.
gi 568980685 595 ------HAELMAKQGL 604
Cdd:PRK13634 230 preifaDPDELEAIGL 245
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
375-598 |
2.81e-30 |
|
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: 120.52 E-value: 2.81e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 375 IEFKNVSFSYPSRPSakvLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDIRAQNVRhyREQIG 454
Cdd:cd03296 3 IEVRNVSKRFGDFVA---LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQ--ERNVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 455 VVRQEPVLFG-TTIGNNIKFGREgvgEKEMEQAAREANAYDFIMAFPKkfntLVGEKG------AQMSGGQKQRIAIARA 527
Cdd:cd03296 78 FVFQHYALFRhMTVFDNVAFGLR---VKPRSERPPEAEIRAKVHELLK----LVQLDWladrypAQLSGGQRQRVALARA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568980685 528 LVRNPKILILDEATSALDTESESLVQTALEKASK--GRTTIVVAHRLS-TIRGADLIVTMKDGMVVEKGTHAEL 598
Cdd:cd03296 151 LAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDelHVTTVFVTHDQEeALEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1004-1232 |
3.04e-30 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 120.20 E-value: 3.04e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1004 LEFREVSFVYPcrpEVPVLQNMSLSIEKGKTVAFVGSSGCGKST---CVQLLQRFYDpmkGQVLLDGVDVK--ELNVQWL 1078
Cdd:PRK09493 2 IEFKNVSKHFG---PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTllrCINKLEEITS---GDLIVDGLKVNdpKVDERLI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1079 RSQTAIVSQEPVLFNCSIA-ENIAYGD-NSRMVPLEEIKEVADAanihsfiegLPRKyntlVGLRG------VQLSGGQK 1150
Cdd:PRK09493 76 RQEAGMVFQQFYLFPHLTAlENVMFGPlRVRGASKEEAEKQARE---------LLAK----VGLAErahhypSELSGGQQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1151 QRLAIARALLRKPKILLLDEATSALDNE-SEKVVQQALDKARRGKTCLVVAHRLSTIQN-ADMIVVLQNGSIKEQGTHQE 1228
Cdd:PRK09493 143 QRVAIARALAVKPKLMLFDEPTSALDPElRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKvASRLIFIDKGRIAEDGDPQV 222
|
....
gi 568980685 1229 LLRN 1232
Cdd:PRK09493 223 LIKN 226
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
1005-1215 |
4.58e-30 |
|
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: 118.79 E-value: 4.58e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1005 EFREVSFVYPcrpEVPVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVKELnvqwlRSQTAI 1084
Cdd:cd03235 1 EVEDLTVSYG---GHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE-----RKRIGY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1085 VSQEPVL---FNCSIAENIAYGDNSRMVPLEEIKEvADAANIHSFIEglprkyntLVGLRGV------QLSGGQKQRLAI 1155
Cdd:cd03235 73 VPQRRSIdrdFPISVRDVVLMGLYGHKGLFRRLSK-ADKAKVDEALE--------RVGLSELadrqigELSGGQQQRVLL 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568980685 1156 ARALLRKPKILLLDEATSALDNESEKVVQQALDK-ARRGKTCLVVAHRLSTIQN-ADMIVVL 1215
Cdd:cd03235 144 ARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRElRREGMTILVVTHDLGLVLEyFDRVLLL 205
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1004-1232 |
4.87e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 121.06 E-value: 4.87e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1004 LEFREVSFVYPcRPEVPVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDP---MKGQVLLDGVDVKELNVQWLRS 1080
Cdd:PRK13640 6 VEFKHVSFTYP-DSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDGITLTAKTVWDIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1081 QTAIVSQEP--VLFNCSIAENIAYGDNSRMVPLEE-IKEVADAAN---IHSFIEGLPRkyntlvglrgvQLSGGQKQRLA 1154
Cdd:PRK13640 85 KVGIVFQNPdnQFVGATVGDDVAFGLENRAVPRPEmIKIVRDVLAdvgMLDYIDSEPA-----------NLSGGQKQRVA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1155 IARALLRKPKILLLDEATSALDNESEKVVQQALDKARRGK--TCLVVAHRLSTIQNADMIVVLQNGSIKEQGTHQELLRN 1232
Cdd:PRK13640 154 IAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNnlTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFSK 233
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
375-600 |
7.38e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 120.18 E-value: 7.38e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 375 IEFKNVSFSYPSRPSAkvLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDIRAQN--VRHYREQ 452
Cdd:PRK13639 2 LETRDLKYSYPDGTEA--LKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKksLLEVRKT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 453 IGVVRQEP--VLFGTTIGNNIKFG--REGVGEKEMEQAAREANAYDFIMAFPKKfntlvgeKGAQMSGGQKQRIAIARAL 528
Cdd:PRK13639 80 VGIVFQNPddQLFAPTVEEDVAFGplNLGLSKEEVEKRVKEALKAVGMEGFENK-------PPHHLSGGQKKRVAIAGIL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568980685 529 VRNPKILILDEATSALDTESESLVQTALEKASK-GRTTIVVAHRLSTI-RGADLIVTMKDGMVVEKGTHAELMA 600
Cdd:PRK13639 153 AMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKeGITIIISTHDVDLVpVYADKVYVMSDGKIIKEGTPKEVFS 226
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
375-624 |
9.49e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 119.84 E-value: 9.49e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 375 IEFKNVSFSYPSrpSAKVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDIRAQNVRHYREQIG 454
Cdd:PRK13647 5 IEVEDLHFRYKD--GTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 455 VVRQEP--VLFGTTIGNNIKFG--REGVGEKEMEQAAREA----NAYDFIMAFPKkfntlvgekgaQMSGGQKQRIAIAR 526
Cdd:PRK13647 83 LVFQDPddQVFSSTVWDDVAFGpvNMGLDKDEVERRVEEAlkavRMWDFRDKPPY-----------HLSYGQKKRVAIAG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 527 ALVRNPKILILDEATSALDTESESLVQTALEKASKGRTTIVVA-HRLS-TIRGADLIVTMKDGMVVEKG-----THAELM 599
Cdd:PRK13647 152 VLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVAtHDVDlAAEWADQVIVLKEGRVLAEGdksllTDEDIV 231
|
250 260
....*....|....*....|....*
gi 568980685 600 AKQGLYYSLAmAQDIKKVDEQMESR 624
Cdd:PRK13647 232 EQAGLRLPLV-AQIFEDLPELGQSK 255
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1009-1235 |
1.16e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 120.15 E-value: 1.16e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1009 VSFVY-PCRP-EVPVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDV--KELNVQWLRSQTAI 1084
Cdd:PRK13637 8 LTHIYmEGTPfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdKKVKLSDIRKKVGL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1085 VSQEP--VLFNCSIAENIAYGDNSRMVPLEEIKE-VADAANIhsfiEGLPrkYNTLVGLRGVQLSGGQKQRLAIARALLR 1161
Cdd:PRK13637 88 VFQYPeyQLFEETIEKDIAFGPINLGLSEEEIENrVKRAMNI----VGLD--YEDYKDKSPFELSGGQKRRVAIAGVVAM 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568980685 1162 KPKILLLDEATSALDNES-EKVVQQALDKARRGK-TCLVVAHRLSTIQN-ADMIVVLQNGSIKEQGTHQELLRNGDT 1235
Cdd:PRK13637 162 EPKILILDEPTAGLDPKGrDEILNKIKELHKEYNmTIILVSHSMEDVAKlADRIIVMNKGKCELQGTPREVFKEVET 238
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
375-581 |
1.17e-29 |
|
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: 117.58 E-value: 1.17e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 375 IEFKNVSFSYPSRPsakVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDIRAQnVRHYREQIG 454
Cdd:COG4133 3 LEAENLSCRRGERL---LFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDA-REDYRRRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 455 VVRQEPVLFGT-TIGNNIKFGREGVGEKEMEQAAREANAYdfiMAFPKKFNTLVGekgaQMSGGQKQRIAIARALVRNPK 533
Cdd:COG4133 79 YLGHADGLKPElTVRENLRFWAALYGLRADREAIDEALEA---VGLAGLADLPVR----QLSAGQKRRVALARLLLSPAP 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 568980685 534 ILILDEATSALDTESESLVQTAL-EKASKGRTTIVVAHRLSTIRGADLI 581
Cdd:COG4133 152 LWLLDEPFTALDAAGVALLAELIaAHLARGGAVLLTTHQPLELAAARVL 200
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1004-1201 |
1.18e-29 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 119.20 E-value: 1.18e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1004 LEFREVSFVYP-CRPEVPVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVkelnvQWLRSQT 1082
Cdd:COG4525 4 LTVRHVSVRYPgGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPV-----TGPGADR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1083 AIVSQEPVLFN-CSIAENIAYGDNSRMVPLEEIKEVAdaanihsfieglpRKYNTLVGLRGV------QLSGGQKQRLAI 1155
Cdd:COG4525 79 GVVFQKDALLPwLNVLDNVAFGLRLRGVPKAERRARA-------------EELLALVGLADFarrriwQLSGGMRQRVGI 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 568980685 1156 ARALLRKPKILLLDEATSALDNESEKVVQQALDK--ARRGKTCLVVAH 1201
Cdd:COG4525 146 ARALAADPRFLLMDEPFGALDALTREQMQELLLDvwQRTGKGVFLITH 193
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
375-595 |
1.26e-29 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 118.58 E-value: 1.26e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 375 IEFKNVSFSYPSrpsAKVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDEN------DIRAQNVRH 448
Cdd:PRK11124 3 IQLNGINCFYGA---HQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNhfdfskTPSDKAIRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 449 YREQIGVVRQE----PVLfgTTIGNNIkfgrE------GVGEKEMEQAAREANAY----DFIMAFPkkfntlvgekgAQM 514
Cdd:PRK11124 80 LRRNVGMVFQQynlwPHL--TVQQNLI----EapcrvlGLSKDQALARAEKLLERlrlkPYADRFP-----------LHL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 515 SGGQKQRIAIARALVRNPKILILDEATSALDTE-SESLVQTALEKASKGRTTIVVAHRLSTIRG-ADLIVTMKDGMVVEK 592
Cdd:PRK11124 143 SGGQQQRVAIARALMMEPQVLLFDEPTAALDPEiTAQIVSIIRELAETGITQVIVTHEVEVARKtASRVVYMENGHIVEQ 222
|
...
gi 568980685 593 GTH 595
Cdd:PRK11124 223 GDA 225
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
680-975 |
1.49e-29 |
|
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: 119.97 E-value: 1.49e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 680 FVVLGTLASALngsvHPVFsiiFGKLV-TMFEDKNKATLKQDAelySMMLVVLGIVALVTYlMQGLFYGRAEENLAMRLR 758
Cdd:cd18557 4 FLLISSAAQLL----LPYL---IGRLIdTIIKGGDLDVLNELA---LILLAIYLLQSVFTF-VRYYLFNIAGERIVARLR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 759 HSAFKAMLYQDMAWYDdkENNTGALTTTLAVDVAQIQGAATSRLGIVTQDVSNMSLSILISFIYGWEMTLLILSFAPVLA 838
Cdd:cd18557 73 RDLFSSLLRQEIAFFD--KHKTGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 839 VTGMIQTAAMAGFANRDKQALKRAGKIATEAVENIRTVVSLTRERAFEQMYEETLQTQHRNALKRAHITGCCYAVSHAFV 918
Cdd:cd18557 151 IASKIYGRYIRKLSKEVQDALAKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQGITSLLI 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 919 HFAHAAGFRFGAYLIQAGRMMPEGM--FIVFTA-IAYGAMAIGETLvwaPEYSKAkAGAS 975
Cdd:cd18557 231 YLSLLLVLWYGGYLVLSGQLTVGELtsFILYTImVASSVGGLSSLL---ADIMKA-LGAS 286
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
1004-1201 |
1.75e-29 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 117.12 E-value: 1.75e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1004 LEFREVSFVYPcrPEVPVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVKELN---VQWLRS 1080
Cdd:cd03292 1 IEFINVTKTYP--NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRgraIPYLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1081 QTAIVSQE-PVLFNCSIAENIAYGDNSRMVPLEEI-KEVADAANIhsfiEGLPRKYNTLvglrGVQLSGGQKQRLAIARA 1158
Cdd:cd03292 79 KIGVVFQDfRLLPDRNVYENVAFALEVTGVPPREIrKRVPAALEL----VGLSHKHRAL----PAELSGGEQQRVAIARA 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 568980685 1159 LLRKPKILLLDEATSALDNESEKVVQQALDKA-RRGKTCLVVAH 1201
Cdd:cd03292 151 IVNSPTILIADEPTGNLDPDTTWEIMNLLKKInKAGTTVVVATH 194
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
375-599 |
2.00e-29 |
|
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: 118.26 E-value: 2.00e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 375 IEFKNVSFSYPSRPsakVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGC-ITVDENDIRAQNVRHYREQI 453
Cdd:COG1119 4 LELRNVTVRRGGKT---ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdVRLFGERRGGEDVWELRKRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 454 GVV---------RQEPVL-------FGTTignnikfGREGVGEKEMEQAAREanaydfIMAF-------PKKFNTLvgek 510
Cdd:COG1119 81 GLVspalqlrfpRDETVLdvvlsgfFDSI-------GLYREPTDEQRERARE------LLELlglahlaDRPFGTL---- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 511 gaqmSGGQKQRIAIARALVRNPKILILDEATSALDTESESLVQTALEK-ASKGRTTIV-VAHRLSTI-RGADLIVTMKDG 587
Cdd:COG1119 144 ----SQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKlAAEGAPTLVlVTHHVEEIpPGITHVLLLKDG 219
|
250
....*....|..
gi 568980685 588 MVVEKGTHAELM 599
Cdd:COG1119 220 RVVAAGPKEEVL 231
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
1021-1232 |
2.74e-29 |
|
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: 117.54 E-value: 2.74e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1021 VLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVKELNVQwLRSQTAIVS--QEPVLF-NCSIA 1097
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPH-EIARLGIGRtfQIPRLFpELTVL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1098 ENIA--------YGDNSRMVPLEEIKEVADAANIHSFIeGLPRKYNTLVGlrgvQLSGGQKQRLAIARALLRKPKILLLD 1169
Cdd:cd03219 94 ENVMvaaqartgSGLLLARARREEREARERAEELLERV-GLADLADRPAG----ELSYGQQRRLEIARALATDPKLLLLD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568980685 1170 EATSAL-DNESEKVVQQALDKARRGKTCLVVAHRLSTIQN-ADMIVVLQNGSIKEQGTHQELLRN 1232
Cdd:cd03219 169 EPAAGLnPEETEELAELIRELRERGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGTPDEVRNN 233
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1004-1232 |
4.11e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 118.17 E-value: 4.11e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1004 LEFREVSFVYPcrPEVPVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVKELN-VQWLRSQT 1082
Cdd:PRK13644 2 IRLENVSYSYP--DGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSkLQGIRKLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1083 AIVSQEP--VLFNCSIAENIAYGDNSRMVPLEEIKEVADAANIHSFIEglprKYNTlvglRGVQ-LSGGQKQRLAIARAL 1159
Cdd:PRK13644 80 GIVFQNPetQFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLE----KYRH----RSPKtLSGGQGQCVALAGIL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568980685 1160 LRKPKILLLDEATSALDNESEKVVQQALDKA-RRGKTCLVVAHRLSTIQNADMIVVLQNGSIKEQGTHQELLRN 1232
Cdd:PRK13644 152 TMEPECLIFDEVTSMLDPDSGIAVLERIKKLhEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLSD 225
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1004-1234 |
5.57e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 117.91 E-value: 5.57e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1004 LEFREVSFVYPCRPEVPVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVKELNVQWLRSQTA 1083
Cdd:PRK13650 5 IEVKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1084 IVSQEP--VLFNCSIAENIAYGDNSRMVPLEEIKEVADAANihsfieglprkynTLVGLRG------VQLSGGQKQRLAI 1155
Cdd:PRK13650 85 MVFQNPdnQFVGATVEDDVAFGLENKGIPHEEMKERVNEAL-------------ELVGMQDfkerepARLSGGQKQRVAI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1156 ARALLRKPKILLLDEATSALDNESEKVVQQALDKARR--GKTCLVVAHRLSTIQNADMIVVLQNGSIKEQGTHQELLRNG 1233
Cdd:PRK13650 152 AGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDdyQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFSRG 231
|
.
gi 568980685 1234 D 1234
Cdd:PRK13650 232 N 232
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
375-598 |
6.00e-29 |
|
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: 116.07 E-value: 6.00e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 375 IEFKNVSFSYPSRPSaKVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDIRAQNVRHYREqIG 454
Cdd:cd03263 1 LQIRNLTKTYKKGTK-PAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQS-LG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 455 VVRQEPVLFGT-TIGNNIKF-GR-EGVGEKEMEQaarEANAYDFIMAFPKKFNTLVGekgaQMSGGQKQRIAIARALVRN 531
Cdd:cd03263 79 YCPQFDALFDElTVREHLRFyARlKGLPKSEIKE---EVELLLRVLGLTDKANKRAR----TLSGGMKRKLSLAIALIGG 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568980685 532 PKILILDEATSALDTESESLVQTALEKASKGRTTIVVAHRLSTIRG-ADLIVTMKDGMVVEKGTHAEL 598
Cdd:cd03263 152 PSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEAlCDRIAIMSDGKLRCIGSPQEL 219
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
1023-1224 |
6.37e-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: 6.37e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1023 QNM--SLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVKELNVQwlRSQTAIVSQEPVLF-NCSIAEN 1099
Cdd:cd03298 13 QPMhfDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA--DRPVSMLFQENNLFaHLTVEQN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1100 IAYGDNSRMVPLEEIKEVADAANIHSFIEGLPRKyntlvglRGVQLSGGQKQRLAIARALLRKPKILLLDEATSALDNES 1179
Cdd:cd03298 91 VGLGLSPGLKLTAEDRQAIEVALARVGLAGLEKR-------LPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPAL 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 568980685 1180 EKVVQQALDK--ARRGKTCLVVAHRLSTIQN-ADMIVVLQNGSIKEQG 1224
Cdd:cd03298 164 RAEMLDLVLDlhAETKMTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
374-600 |
6.41e-29 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 116.01 E-value: 6.41e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 374 NIEFKNVSFSYPSRPsakvlKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDIRAQNVrhYREQI 453
Cdd:COG3840 1 MLRLDDLTYRYGDFP-----LRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPP--AERPV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 454 GVVRQEPVLFG-TTIGNNIKFG-----REGVGEKE-MEQAAREANAYDFIMAFPkkfntlvgekgAQMSGGQKQRIAIAR 526
Cdd:COG3840 74 SMLFQENNLFPhLTVAQNIGLGlrpglKLTAEQRAqVEQALERVGLAGLLDRLP-----------GQLSGGQRQRVALAR 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 527 ALVRNPKILILDEATSALD----TESESLV-QTALEkasKGRTTIVVAHRLSTIRG-ADLIVTMKDGMVVEKGTHAELMA 600
Cdd:COG3840 143 CLVRKRPILLLDEPFSALDpalrQEMLDLVdELCRE---RGLTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAALLD 219
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
991-1233 |
6.64e-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: 126.21 E-value: 6.64e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 991 SQSGEKPDTCE--------GN-LEFREVSFVYpCRPEVPVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKG 1061
Cdd:TIGR00957 615 SHEELEPDSIErrtikpgeGNsITVHNATFTW-ARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEG 693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1062 QVLLDGvdvkelnvqwlrsQTAIVSQEPVLFNCSIAENIAYGDnsrmvPLEE--IKEVADAANIHSFIEGLPRKYNTLVG 1139
Cdd:TIGR00957 694 HVHMKG-------------SVAYVPQQAWIQNDSLRENILFGK-----ALNEkyYQQVLEACALLPDLEILPSGDRTEIG 755
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1140 LRGVQLSGGQKQRLAIARALLRKPKILLLDEATSALDNESEKVVQQAL---DKARRGKTCLVVAHRLSTIQNADMIVVLQ 1216
Cdd:TIGR00957 756 EKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVigpEGVLKNKTRILVTHGISYLPQVDVIIVMS 835
|
250
....*....|....*...
gi 568980685 1217 NGSIKEQGTHQELL-RNG 1233
Cdd:TIGR00957 836 GGKISEMGSYQELLqRDG 853
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
1018-1232 |
6.78e-29 |
|
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: 115.61 E-value: 6.78e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1018 EVPVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVKELNV-QWLRSQTAIVSQEPVLF-NCS 1095
Cdd:cd03224 12 KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPhERARAGIGYVPEGRRIFpELT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1096 IAENIAYGDNSRmvpleeiKEVADAANIHSFIEGLPR---KYNTLVGlrgvQLSGGQKQRLAIARALLRKPKILLLDEAT 1172
Cdd:cd03224 92 VEENLLLGAYAR-------RRAKRKARLERVYELFPRlkeRRKQLAG----TLSGGEQQMLAIARALMSRPKLLLLDEPS 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568980685 1173 SALdneSEKVVQQ---ALDK-ARRGKTCLVVAHRLSTIQN-ADMIVVLQNGSIKEQGTHQELLRN 1232
Cdd:cd03224 161 EGL---APKIVEEifeAIRElRDEGVTILLVEQNARFALEiADRAYVLERGRVVLEGTAAELLAD 222
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
375-591 |
1.68e-28 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 114.84 E-value: 1.68e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 375 IEFKNVSFSYPSRPSA-KVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDI-------RAQnV 446
Cdd:COG4181 9 IELRGLTKTVGTGAGElTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLfaldedaRAR-L 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 447 RhyREQIGVVRQEPVLFGT-TIGNNIKFGREGVGEKEMEQAARE----------ANAYdfimafPkkfntlvgekgAQMS 515
Cdd:COG4181 88 R--ARHVGFVFQSFQLLPTlTALENVMLPLELAGRRDARARARAllervglghrLDHY------P-----------AQLS 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568980685 516 GGQKQRIAIARALVRNPKILILDEATSALDTESESLVQTALE--KASKGRTTIVVAHRLSTIRGADLIVTMKDGMVVE 591
Cdd:COG4181 149 GGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFelNRERGTTLVLVTHDPALAARCDRVLRLRAGRLVE 226
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
392-600 |
2.25e-28 |
|
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: 114.45 E-value: 2.25e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 392 VLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDIRAQNVrHYREQIGV--VRQEPVLFGT-TIG 468
Cdd:cd03224 15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPP-HERARAGIgyVPEGRRIFPElTVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 469 NNIKFGREGVGEKEmeQAAREANAYDFimaFPKkFNTLVGEKGAQMSGGQKQRIAIARALVRNPKILILDEATSALdteS 548
Cdd:cd03224 94 ENLLLGAYARRRAK--RKARLERVYEL---FPR-LKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGL---A 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 568980685 549 ESLVQ---TALEK-ASKGRTTIVVAHRLSTIRG-ADLIVTMKDGMVVEKGTHAELMA 600
Cdd:cd03224 165 PKIVEeifEAIRElRDEGVTILLVEQNARFALEiADRAYVLERGRVVLEGTAAELLA 221
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1004-1237 |
2.72e-28 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 118.40 E-value: 2.72e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1004 LEFREVSFVYPCRPEVpvlQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVKelNVQWLRSQTA 1083
Cdd:PRK11607 20 LEIRNLTKSFDGQHAV---DDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLS--HVPPYQRPIN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1084 IVSQEPVLF-NCSIAENIAYGDNSRMVPLEEIKE-VADAANIHSFIEGLPRKYNtlvglrgvQLSGGQKQRLAIARALLR 1161
Cdd:PRK11607 95 MMFQSYALFpHMTVEQNIAFGLKQDKLPKAEIASrVNEMLGLVHMQEFAKRKPH--------QLSGGQRQRVALARSLAK 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568980685 1162 KPKILLLDEATSALDNESEKVVQ-QALDKARR-GKTCLVVAH-RLSTIQNADMIVVLQNGSIKEQGTHQELLRNGDTYF 1237
Cdd:PRK11607 167 RPKLLLLDEPMGALDKKLRDRMQlEVVDILERvGVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRY 245
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
375-594 |
3.46e-28 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 118.13 E-value: 3.46e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 375 IEFKNVSFSYPSRPsakVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDIraQNVRHYREQIG 454
Cdd:PRK09452 15 VELRGISKSFDGKE---VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDI--THVPAENRHVN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 455 VVRQEPVLF-GTTIGNNIKFG--REGVGEKEMEQAAREANAydfiMAfpkKFNTLVGEKGAQMSGGQKQRIAIARALVRN 531
Cdd:PRK09452 90 TVFQSYALFpHMTVFENVAFGlrMQKTPAAEITPRVMEALR----MV---QLEEFAQRKPHQLSGGQQQRVAIARAVVNK 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568980685 532 PKILILDEATSALDTESESLVQTALEKASK--GRTTIVVAH----RLSTirgADLIVTMKDGMVVEKGT 594
Cdd:PRK09452 163 PKVLLLDESLSALDYKLRKQMQNELKALQRklGITFVFVTHdqeeALTM---SDRIVVMRDGRIEQDGT 228
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
102-306 |
4.48e-28 |
|
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: 115.69 E-value: 4.48e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 102 IGAAALifgYVQISFWVITAARQTTRIRKQFFHSILAQDISWFDGSDICELNTRMTGDINKLCDGIGDKIPLMFQNISGF 181
Cdd:cd18573 53 VGAAAN---FGRVYLLRIAGERIVARLRKRLFKSILRQDAAFFDKNKTGELVSRLSSDTSVVGKSLTQNLSDGLRSLVSG 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 182 SIGLVISLIKSWKLSLVVLSTSPLIMASSALCSRMIISLTSKELDAYSKAGAVAEEALSSIQTVTAFGAQEKEIQRYTQH 261
Cdd:cd18573 130 VGGIGMMLYISPKLTLVMLLVVPPIAVGAVFYGRYVRKLSKQVQDALADATKVAEERLSNIRTVRAFAAERKEVERYAKK 209
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 568980685 262 LKDAKDAGIKRATASKLSLGAVYFFMNGAYGLAFWYGTSLIFGGE 306
Cdd:cd18573 210 VDEVFDLAKKEALASGLFFGSTGFSGNLSLLSVLYYGGSLVASGE 254
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1004-1214 |
5.08e-28 |
|
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: 112.57 E-value: 5.08e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1004 LEFREVSFVypcRPEVPVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVKELNVQWlRSQTA 1083
Cdd:COG4133 3 LEAENLSCR---RGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDY-RRRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1084 IVSQEPVLF-NCSIAENIA-----YGDNsrmVPLEEIKEVADAANIHSFIEGLPRkyntlvglrgvQLSGGQKQRLAIAR 1157
Cdd:COG4133 79 YLGHADGLKpELTVRENLRfwaalYGLR---ADREAIDEALEAVGLAGLADLPVR-----------QLSAGQKRRVALAR 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 568980685 1158 ALLRKPKILLLDEATSALDNESEKVVQQAL-DKARRGKTCLVVAHRLSTIQNADMIVV 1214
Cdd:COG4133 145 LLLSPAPLWLLDEPFTALDAAGVALLAELIaAHLARGGAVLLTTHQPLELAAARVLDL 202
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
1031-1224 |
1.01e-27 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 112.00 E-value: 1.01e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1031 KGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGV----DVKELNVQWLRSQTAIVSQEPVLF-NCSIAENIAYG-- 1103
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlfdSRKKINLPPQQRKIGLVFQQYALFpHLNVRENLAFGlk 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1104 DNSRMVPLEEIKEVADAANIHSfieglprkyntLVGLRGVQLSGGQKQRLAIARALLRKPKILLLDEATSALDNESEKVV 1183
Cdd:cd03297 102 RKRNREDRISVDELLDLLGLDH-----------LLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 568980685 1184 QQALDK--ARRGKTCLVVAHRLSTIQN-ADMIVVLQNGSIKEQG 1224
Cdd:cd03297 171 LPELKQikKNLNIPVIFVTHDLSEAEYlADRIVVMEDGRLQYIG 214
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
375-593 |
1.06e-27 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 111.90 E-value: 1.06e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 375 IEFKNVSFSYPSRpsaKVLKGLNLKIKAGETvALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDIRAQnVRHYREQIG 454
Cdd:cd03264 1 LQLENLTKRYGKK---RALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQ-PQKLRRRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 455 VVRQEPVLFgttigNNIKfGRE---------GVGEKEMEQAAREA----NAYDFimafpkkfntlVGEKGAQMSGGQKQR 521
Cdd:cd03264 76 YLPQEFGVY-----PNFT-VREfldyiawlkGIPSKEVKARVDEVlelvNLGDR-----------AKKKIGSLSGGMRRR 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568980685 522 IAIARALVRNPKILILDEATSALDTESESLVQTALEKASKGRTTIVVAHRLSTIRG-ADLIVTMKDGMVVEKG 593
Cdd:cd03264 139 VGIAQALVGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1018-1232 |
1.42e-27 |
|
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: 119.02 E-value: 1.42e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1018 EVPVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFyDPMKGQVLLDGVDVKELN---VQWLRSQTAIVSQEPvlfnc 1094
Cdd:COG4172 298 HVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRL-IPSEGEIRFDGQDLDGLSrraLRPLRRRMQVVFQDP----- 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1095 siaeniaYGD-NSRMvPLEEIkeVADAANIHsFIEGLPRKYNTLVG--LRGVQL------------SGGQKQRLAIARAL 1159
Cdd:COG4172 372 -------FGSlSPRM-TVGQI--IAEGLRVH-GPGLSAAERRARVAeaLEEVGLdpaarhryphefSGGQRQRIAIARAL 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1160 LRKPKILLLDEATSALDneseKVVQ-QALD-----KARRGKTCLVVAHRLSTIQN-ADMIVVLQNGSIKEQGTHQELLRN 1232
Cdd:COG4172 441 ILEPKLLVLDEPTSALD----VSVQaQILDllrdlQREHGLAYLFISHDLAVVRAlAHRVMVMKDGKVVEQGPTEQVFDA 516
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
375-604 |
1.49e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 113.64 E-value: 1.49e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 375 IEFKNVSFSYPSRPSAK---VLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDIR-AQNVRHYR 450
Cdd:PRK13633 5 IKCKNVSYKYESNEESTeklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSdEENLWDIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 451 EQIGVVRQEP--VLFGTTIGNNIKFGREGVG------EKEMEQAAREANAYDFimafpKKFNTLVgekgaqMSGGQKQRI 522
Cdd:PRK13633 85 NKAGMVFQNPdnQIVATIVEEDVAFGPENLGippeeiRERVDESLKKVGMYEY-----RRHAPHL------LSGGQKQRV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 523 AIARALVRNPKILILDEATSALDTESESLVQTALEKASK--GRTTIVVAHRLSTIRGADLIVTMKDGMVVEKGT------ 594
Cdd:PRK13633 154 AIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKkyGITIILITHYMEEAVEADRIIVMDSGKVVMEGTpkeifk 233
|
250
....*....|
gi 568980685 595 HAELMAKQGL 604
Cdd:PRK13633 234 EVEMMKKIGL 243
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1004-1218 |
1.64e-27 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 109.83 E-value: 1.64e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1004 LEFREVSFVYPcrpEVPVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGvdvkelnvqwlrsqta 1083
Cdd:cd03216 1 LELRGITKRFG---GVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDG---------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1084 ivsqEPVLFNcSIAENIAYGdnSRMVPleeikevadaanihsfieglprkyntlvglrgvQLSGGQKQRLAIARALLRKP 1163
Cdd:cd03216 62 ----KEVSFA-SPRDARRAG--IAMVY---------------------------------QLSVGERQMVEIARALARNA 101
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 568980685 1164 KILLLDEATSAL-DNESEKVVQQALDKARRGKTCLVVAHRLSTIQN-ADMIVVLQNG 1218
Cdd:cd03216 102 RLLILDEPTAALtPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEiADRVTVLRDG 158
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
1004-1229 |
2.20e-27 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 111.44 E-value: 2.20e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1004 LEFREVSFVYPCRPeVPVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVKElNVQWLRSQTA 1083
Cdd:cd03263 1 LQIRNLTKTYKKGT-KPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1084 IVSQEPVLF-NCSIAENIAYgdNSRM--VPLEEIKEVADAAnIHSFieGLPRKYNTLVGlrgvQLSGGQKQRLAIARALL 1160
Cdd:cd03263 79 YCPQFDALFdELTVREHLRF--YARLkgLPKSEIKEEVELL-LRVL--GLTDKANKRAR----TLSGGMKRKLSLAIALI 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1161 RKPKILLLDEATSALDNESEKVVQQALDKARRGKTCLVVAHRLSTIQN-ADMIVVLQNGSIKEQGTHQEL 1229
Cdd:cd03263 150 GGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEAlCDRIAIMSDGKLRCIGSPQEL 219
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
373-604 |
2.22e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 113.56 E-value: 2.22e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 373 GNIEFKNVSFSYPSRP--SAKVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDIRA-----QN 445
Cdd:PRK13645 5 KDIILDNVSYTYAKKTpfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPAnlkkiKE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 446 VRHYREQIGVVRQEP--VLFGTTIGNNIKFGREGVGEKEMEQAAREANAYDFImAFPKKFntlVGEKGAQMSGGQKQRIA 523
Cdd:PRK13645 85 VKRLRKEIGLVFQFPeyQLFQETIEKDIAFGPVNLGENKQEAYKKVPELLKLV-QLPEDY---VKRSPFELSGGQKRRVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 524 IARALVRNPKILILDEATSALDTESESLVQTALEKASK--GRTTIVVAHRLSTI-RGADLIVTMKDGMVVEKGTHAELMA 600
Cdd:PRK13645 161 LAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKeyKKRIIMVTHNMDQVlRIADEVIVMHEGKVISIGSPFEIFS 240
|
....
gi 568980685 601 KQGL 604
Cdd:PRK13645 241 NQEL 244
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
1022-1232 |
2.60e-27 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 115.90 E-value: 2.60e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1022 LQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVKELNVQWLRS----QTAIVSQEPVLF-NCSI 1096
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREvrrkKIAMVFQSFALMpHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1097 AENIAYGDNSRMVPLEEIKEVA-DA---ANIHSFIEGLPRkyntlvglrgvQLSGGQKQRLAIARALLRKPKILLLDEAT 1172
Cdd:PRK10070 124 LDNTAFGMELAGINAEERREKAlDAlrqVGLENYAHSYPD-----------ELSGGMRQRVGLARALAINPDILLMDEAF 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568980685 1173 SALDNESEKVVQQALDK--ARRGKTCLVVAHRL-STIQNADMIVVLQNGSIKEQGTHQELLRN 1232
Cdd:PRK10070 193 SALDPLIRTEMQDELVKlqAKHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEILNN 255
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
1017-1219 |
2.79e-27 |
|
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: 111.27 E-value: 2.79e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1017 PEVPVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVKELNVQWLRSQT----AIVSQEPVLF 1092
Cdd:cd03290 12 SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNrysvAYAAQKPWLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1093 NCSIAENIAYGDnsrmvPL--EEIKEVADAANIHSFIEGLPRKYNTLVGLRGVQLSGGQKQRLAIARALLRKPKILLLDE 1170
Cdd:cd03290 92 NATVEENITFGS-----PFnkQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDD 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 568980685 1171 ATSALD-NESEKVVQQALDKARRG--KTCLVVAHRLSTIQNADMIVVLQNGS 1219
Cdd:cd03290 167 PFSALDiHLSDHLMQEGILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDGS 218
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
49-302 |
2.91e-27 |
|
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: 113.17 E-value: 2.91e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 49 ATVPLMSLVLGEI-----SDHLINGCLVQTNrtkyqncsqtQEKLNEDIIVLTLYYIGIGAAALIFGyvqiSFWVITAAR 123
Cdd:cd18784 1 AFFFLLAAAVGEIfipyyTGQVIDGIVIEKS----------QDKFSRAIIIMGLLAIASSVAAGIRG----GLFTLAMAR 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 124 QTTRIRKQFFHSILAQDISWFDGSDICELNTRMTGDINKLCDgigdkipLMFQNISGF------SIGLVISLIK-SWKLS 196
Cdd:cd18784 67 LNIRIRNLLFRSIVSQEIGFFDTVKTGDITSRLTSDTTTMSD-------TVSLNLNIFlrslvkAIGVIVFMFKlSWQLS 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 197 LVVLSTSPLIMASSALCSRMIISLTSKELDAYSKAGAVAEEALSSIQTVTAFGAQEKEIQRYTQHLKDAKDAGIKRATAS 276
Cdd:cd18784 140 LVTLIGLPLIAIVSKVYGDYYKKLSKAVQDSLAKANEVAEETISSIRTVRSFANEDGEANRYSEKLKDTYKLKIKEALAY 219
|
250 260
....*....|....*....|....*.
gi 568980685 277 KLSLGAVYFFMNGAYGLAFWYGTSLI 302
Cdd:cd18784 220 GGYVWSNELTELALTVSTLYYGGHLV 245
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1020-1219 |
3.84e-27 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 117.99 E-value: 3.84e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1020 PVLQNMSLSIEKGKTVAFVGSSGCGKSTcvqLLQ------RFYDpmkGQVLL-DGVDVkelnvqwlrsqtAIVSQEPVLF 1092
Cdd:COG4178 377 PLLEDLSLSLKPGERLLITGPSGSGKST---LLRaiaglwPYGS---GRIARpAGARV------------LFLPQRPYLP 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1093 NCSIAENIAYGDNSRMVPLEEIKEVADAANIHSFIEGLPRKYNtlvglRGVQLSGGQKQRLAIARALLRKPKILLLDEAT 1172
Cdd:COG4178 439 LGTLREALLYPATAEAFSDAELREALEAVGLGHLAERLDEEAD-----WDQVLSLGEQQRLAFARLLLHKPDWLFLDEAT 513
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 568980685 1173 SALDNESEKVVQQALDKARRGKTCLVVAHRLSTIQNADMIVVLQNGS 1219
Cdd:COG4178 514 SALDEENEAALYQLLREELPGTTVISVGHRSTLAAFHDRVLELTGDG 560
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1020-1216 |
3.94e-27 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 110.96 E-value: 3.94e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1020 PVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVKELNVQWLRSQTAIVSQEPVLFNCSIAEN 1099
Cdd:PRK10247 21 KILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTLFGDTVYDN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1100 IAYGDNSRMVPLEEIKEVADAANIhsfieGLPrkyNTLVGLRGVQLSGGQKQRLAIARALLRKPKILLLDEATSALDNES 1179
Cdd:PRK10247 101 LIFPWQIRNQQPDPAIFLDDLERF-----ALP---DTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESN 172
|
170 180 190
....*....|....*....|....*....|....*....
gi 568980685 1180 EKVVQQALDKARRGKTCLV--VAHRLSTIQNADMIVVLQ 1216
Cdd:PRK10247 173 KHNVNEIIHRYVREQNIAVlwVTHDKDEINHADKVITLQ 211
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1004-1234 |
3.99e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 112.14 E-value: 3.99e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1004 LEFREVSFVYpcRPEVPVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVKELNVQWLRSQTA 1083
Cdd:PRK13647 5 IEVEDLHFRY--KDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1084 IVSQEP--VLFNCSIAENIAYGDNSRMVPLEEIKEVADAA----NIHSFIEGLPRkyntlvglrgvQLSGGQKQRLAIAR 1157
Cdd:PRK13647 83 LVFQDPddQVFSSTVWDDVAFGPVNMGLDKDEVERRVEEAlkavRMWDFRDKPPY-----------HLSYGQKKRVAIAG 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568980685 1158 ALLRKPKILLLDEATSALDNESEKVVQQALDK-ARRGKTCLVVAHRLS-TIQNADMIVVLQNGSIKEQGThQELLRNGD 1234
Cdd:PRK13647 152 VLAMDPDVIVLDEPMAYLDPRGQETLMEILDRlHNQGKTVIVATHDVDlAAEWADQVIVLKEGRVLAEGD-KSLLTDED 229
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
1018-1224 |
4.37e-27 |
|
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: 110.00 E-value: 4.37e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1018 EVPVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVKELNVQWLRSQTAIvsQEPVLF-NCSI 1096
Cdd:cd03268 12 KKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRRIGALI--EAPGFYpNLTA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1097 AENIAYGDNSRMVPLEEIKEVADaanihsfieglprkyntLVGLRGV------QLSGGQKQRLAIARALLRKPKILLLDE 1170
Cdd:cd03268 90 RENLRLLARLLGIRKKRIDEVLD-----------------VVGLKDSakkkvkGFSLGMKQRLGIALALLGNPDLLILDE 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 568980685 1171 ATSALDNESEKVVQQAL-DKARRGKTCLVVAHRLSTIQN-ADMIVVLQNGSIKEQG 1224
Cdd:cd03268 153 PTNGLDPDGIKELRELIlSLRDQGITVLISSHLLSEIQKvADRIGIINKGKLIEEG 208
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
375-593 |
4.94e-27 |
|
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: 109.56 E-value: 4.94e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 375 IEFKNVSFSYPSRPSA---KVLKGLNLKIKAGETVALVGPSGSGKSTTVQLL--QRLYDPEDGCITVDENDIRAQNvrhY 449
Cdd:cd03213 4 LSFRNLTVTVKSSPSKsgkQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGRPLDKRS---F 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 450 REQIGVVRQEPVLFGTtignnikfgregvgekemeQAAREAnaydfiMAFPKKFNTLvgekgaqmSGGQKQRIAIARALV 529
Cdd:cd03213 81 RKIIGYVPQDDILHPT-------------------LTVRET------LMFAAKLRGL--------SGGERKRVSIALELV 127
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568980685 530 RNPKILILDEATSALDTESESLVQTALEK-ASKGRTTIVVAHRLST--IRGADLIVTMKDGMVVEKG 593
Cdd:cd03213 128 SNPSLLFLDEPTSGLDSSSALQVMSLLRRlADTGRTIICSIHQPSSeiFELFDKLLLLSQGRVIYFG 194
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
1004-1234 |
5.66e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 112.42 E-value: 5.66e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1004 LEFREVSFVYpcRPEVP----VLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLdGVDV-----KELN 1074
Cdd:PRK13634 3 ITFQKVEHRY--QYKTPferrALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI-GERVitagkKNKK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1075 VQWLRSQTAIVSQ--EPVLFNCSIAENIAYGDNSRMVPLEEIKEVAdaanihsfieglpRKYNTLVGL-------RGVQL 1145
Cdd:PRK13634 80 LKPLRKKVGIVFQfpEHQLFEETVEKDICFGPMNFGVSEEDAKQKA-------------REMIELVGLpeellarSPFEL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1146 SGGQKQRLAIARALLRKPKILLLDEATSALDNESEKVVQQALDKARR--GKTCLVVAHRLSTIQN-ADMIVVLQNGSIKE 1222
Cdd:PRK13634 147 SGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKekGLTTVLVTHSMEDAARyADQIVVMHKGTVFL 226
|
250
....*....|..
gi 568980685 1223 QGTHQELLRNGD 1234
Cdd:PRK13634 227 QGTPREIFADPD 238
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
681-958 |
6.31e-27 |
|
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: 112.26 E-value: 6.31e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 681 VVLGTLASALNGSVHPVFSIIFGKLVtmfedkNKATLKQDAELYSMMLVVLGIVALVTYLMQGL---FYGRAEENLAMRL 757
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLLI------DDVIPAGDLSLLLWIALLLLLLALLRALLSYLrryLAARLGQRVVFDL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 758 RHSAFKAMLYQDMAWYDdkENNTGALTTTLAVDVAQIQGAATSRLGIVTQDVSNMSLSILISFIYGWEMTLLILSFAPVL 837
Cdd:cd07346 75 RRDLFRHLQRLSLSFFD--RNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLY 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 838 AVTGMIQTAAMAGFANRDKQALKRAGKIATEAVENIRTVVSLTRERAFEQMYEETLQTQHRNALKRAHITGCCYAVSHAF 917
Cdd:cd07346 153 VLILRYFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLL 232
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 568980685 918 VHFAHAAGFRFGAYLIQAGRMMPeGMFIVFtaIAYGAMAIG 958
Cdd:cd07346 233 TALGTALVLLYGGYLVLQGSLTI-GELVAF--LAYLGMLFG 270
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
1026-1234 |
1.05e-26 |
|
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: 113.28 E-value: 1.05e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1026 SLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDV----KELNVQWLRSQTAIVSQEPVLF-NCSIAENI 1100
Cdd:TIGR02142 17 DFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLfdsrKGIFLPPEKRRIGYVFQEARLFpHLSVRGNL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1101 AYGDNSRMVPLEEIK--EVADAANIHSFIEGLPRKyntlvglrgvqLSGGQKQRLAIARALLRKPKILLLDEATSALDNE 1178
Cdd:TIGR02142 97 RYGMKRARPSERRISfeRVIELLGIGHLLGRLPGR-----------LSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDP 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 568980685 1179 SEKVVQQALDKARR--GKTCLVVAHRLSTIQN-ADMIVVLQNGSIKEQGTHQELLRNGD 1234
Cdd:TIGR02142 166 RKYEILPYLERLHAefGIPILYVSHSLQEVLRlADRVVVLEDGRVAAAGPIAEVWASPD 224
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1004-1234 |
1.16e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 111.00 E-value: 1.16e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1004 LEFREVSFVYPcRPEVPVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVKELNVQWLRSQTA 1083
Cdd:PRK13648 8 IVFKNVSFQYQ-SDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1084 IVSQEPV-LFNCSIAE-NIAYGDNSRMVPLEE----IKEVADAANIHSFIEGLPRkyntlvglrgvQLSGGQKQRLAIAR 1157
Cdd:PRK13648 87 IVFQNPDnQFVGSIVKyDVAFGLENHAVPYDEmhrrVSEALKQVDMLERADYEPN-----------ALSGGQKQRVAIAG 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568980685 1158 ALLRKPKILLLDEATSALDNESEKVVQQALDKARRGK--TCLVVAHRLSTIQNADMIVVLQNGSIKEQGTHQELLRNGD 1234
Cdd:PRK13648 156 VLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFDHAE 234
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
375-584 |
1.81e-26 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 109.03 E-value: 1.81e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 375 IEFKNVSFSYPSRpsaKVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDIRAQNVRHYREQIG 454
Cdd:PRK10247 8 LQLQNVGYLAGDA---KILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 455 VVRQEPVLFGTTIGNNIKFGREGVGEKEMEQAAReanayDFIMAFPKKFNTLvgEKG-AQMSGGQKQRIAIARALVRNPK 533
Cdd:PRK10247 85 YCAQTPTLFGDTVYDNLIFPWQIRNQQPDPAIFL-----DDLERFALPDTIL--TKNiAELSGGEKQRISLIRNLQFMPK 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 568980685 534 ILILDEATSALDTESESLVQTALEK--ASKGRTTIVVAHRLSTIRGADLIVTM 584
Cdd:PRK10247 158 VLLLDEITSALDESNKHNVNEIIHRyvREQNIAVLWVTHDKDEINHADKVITL 210
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
375-598 |
2.76e-26 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 111.74 E-value: 2.76e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 375 IEFKNVSFSYPSrpsAKVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDIRAQNVRhyREQIG 454
Cdd:PRK11432 7 VVLKNITKRFGS---NTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQ--QRDIC 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 455 VVRQEPVLF-GTTIGNNIKFG--REGVGEKEMEQAAREANAYDFIMAFPKKFNTlvgekgaQMSGGQKQRIAIARALVRN 531
Cdd:PRK11432 82 MVFQSYALFpHMSLGENVGYGlkMLGVPKEERKQRVKEALELVDLAGFEDRYVD-------QISGGQQQRVALARALILK 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568980685 532 PKILILDEATSALDTeseSLVQTALEKASK-----GRTTIVVAHRLS-TIRGADLIVTMKDGMVVEKGTHAEL 598
Cdd:PRK11432 155 PKVLLFDEPLSNLDA---NLRRSMREKIRElqqqfNITSLYVTHDQSeAFAVSDTVIVMNKGKIMQIGSPQEL 224
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
1021-1243 |
3.51e-26 |
|
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: 109.56 E-value: 3.51e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1021 VLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDpMKGQVLLDGVDVKELNVQWLRSQTAIVSQEPVLFNCSIAENI 1100
Cdd:cd03289 19 VLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKAFGVIPQKVFIFSGTFRKNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1101 -AYGDNSRmvplEEIKEVADAANIHSFIEGLPRKYNTLVGLRGVQLSGGQKQRLAIARALLRKPKILLLDEATSALDNES 1179
Cdd:cd03289 98 dPYGKWSD----EEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPIT 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568980685 1180 EKVVQQALDKARRGKTCLVVAHRLSTIQNADMIVVLQNGSIKEQGTHQELLrNGDTYFKLVAAH 1243
Cdd:cd03289 174 YQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLL-NEKSHFKQAISP 236
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
375-599 |
4.44e-26 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 108.56 E-value: 4.44e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 375 IEFKNVSFSYPSRpsaKVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDIRAQNVRHYREQI- 453
Cdd:PRK11231 3 LRTENLTVGYGTK---RILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLa 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 454 ----------GVVRQEPVLFGTTIGNNIkFGREGVGEKEMEQAAREANAYDfimafpkkfnTLVGEKGAQMSGGQKQRIA 523
Cdd:PRK11231 80 llpqhhltpeGITVRELVAYGRSPWLSL-WGRLSAEDNARVNQAMEQTRIN----------HLADRRLTDLSGGQRQRAF 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 524 IARALVRNPKILILDEATSALD----TESESLVQtalEKASKGRTTIVVAHRLS-TIRGADLIVTMKDGMVVEKGTHAEL 598
Cdd:PRK11231 149 LAMVLAQDTPVVLLDEPTTYLDinhqVELMRLMR---ELNTQGKTVVTVLHDLNqASRYCDHLVVLANGHVMAQGTPEEV 225
|
.
gi 568980685 599 M 599
Cdd:PRK11231 226 M 226
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1004-1218 |
4.91e-26 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 113.57 E-value: 4.91e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1004 LEFREVSFVYPcrpEVPVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVKELNVQwlRSQT- 1082
Cdd:COG1129 5 LEMRGISKSFG---GVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPR--DAQAa 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1083 --AIVSQEPVLF-NCSIAENIAYGD---NSRMVPLEEIKEVADAAnIHSFieGLPRKYNTLVGlrgvQLSGGQKQRLAIA 1156
Cdd:COG1129 80 giAIIHQELNLVpNLSVAENIFLGReprRGGLIDWRAMRRRAREL-LARL--GLDIDPDTPVG----DLSVAQQQLVEIA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568980685 1157 RALLRKPKILLLDEATSAL-DNESEKVVQQALDKARRGKTCLVVAHRLSTIQN-ADMIVVLQNG 1218
Cdd:COG1129 153 RALSRDARVLILDEPTASLtEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEiADRVTVLRDG 216
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
375-602 |
7.76e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 108.76 E-value: 7.76e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 375 IEFKNVSFSY-PSRP-SAKVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDIRAQ----NVRH 448
Cdd:PRK13641 3 IKFENVDYIYsPGTPmEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPEtgnkNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 449 YREQIGVVRQ--EPVLFGTTIGNNIKFGRE--GVGEKEMEQAAREanaydfimaFPKKF---NTLVGEKGAQMSGGQKQR 521
Cdd:PRK13641 83 LRKKVSLVFQfpEAQLFENTVLKDVEFGPKnfGFSEDEAKEKALK---------WLKKVglsEDLISKSPFELSGGQMRR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 522 IAIARALVRNPKILILDEATSALDTES-ESLVQTALEKASKGRTTIVVAHRLSTI-RGADLIVTMKDGMVVEKGTHAELM 599
Cdd:PRK13641 154 VAIAGVMAYEPEILCLDEPAAGLDPEGrKEMMQLFKDYQKAGHTVILVTHNMDDVaEYADDVLVLEHGKLIKHASPKEIF 233
|
...
gi 568980685 600 AKQ 602
Cdd:PRK13641 234 SDK 236
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
375-593 |
7.82e-26 |
|
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: 106.53 E-value: 7.82e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 375 IEFKNVSFSYPSRPsakVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDIraQNVRHYREQIG 454
Cdd:cd03268 1 LKTNDLTKTYGKKR---VLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSY--QKNIEALRRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 455 VVRQEPVLFG--TTIGNNIKFGRE-GVGEKEMEQAAREANaydfIMAFPKKfntlvgeKGAQMSGGQKQRIAIARALVRN 531
Cdd:cd03268 76 ALIEAPGFYPnlTARENLRLLARLlGIRKKRIDEVLDVVG----LKDSAKK-------KVKGFSLGMKQRLGIALALLGN 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568980685 532 PKILILDEATSALDTES-ESLVQTALEKASKGRTTIVVAHRLSTIRG-ADLIVTMKDGMVVEKG 593
Cdd:cd03268 145 PDLLILDEPTNGLDPDGiKELRELILSLRDQGITVLISSHLLSEIQKvADRIGIINKGKLIEEG 208
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
375-593 |
8.09e-26 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 107.94 E-value: 8.09e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 375 IEFKNVSFSYPSRpsaKVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYD--PE---DGCITVDENDI---RAQNV 446
Cdd:PRK14239 6 LQVSDLSVYYNKK---KALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnPEvtiTGSIVYNGHNIyspRTDTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 447 RhYREQIGVVRQEPVLFGTTIGNNIKFGR--EGVGEKE-----MEQAAREANAYDfimafpkKFNTLVGEKGAQMSGGQK 519
Cdd:PRK14239 83 D-LRKEIGMVFQQPNPFPMSIYENVVYGLrlKGIKDKQvldeaVEKSLKGASIWD-------EVKDRLHDSALGLSGGQQ 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568980685 520 QRIAIARALVRNPKILILDEATSALDTESESLVQTALEKASKGRTTIVVAHRLSTI-RGADLIVTMKDGMVVEKG 593
Cdd:PRK14239 155 QRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQAsRISDRTGFFLDGDLIEYN 229
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1004-1230 |
8.86e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 108.64 E-value: 8.86e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1004 LEFREVSFVYPCRPEVPVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVKELNVQWLRSQTA 1083
Cdd:PRK13642 5 LEVENLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1084 IVSQEP--VLFNCSIAENIAYGDNSRMVPLEEIKEVAD----AANIHSFIEGLPrkyntlvglrgVQLSGGQKQRLAIAR 1157
Cdd:PRK13642 85 MVFQNPdnQFVGATVEDDVAFGMENQGIPREEMIKRVDeallAVNMLDFKTREP-----------ARLSGGQKQRVAVAG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568980685 1158 ALLRKPKILLLDEATSALD----NESEKVVQQALDKARRgkTCLVVAHRLSTIQNADMIVVLQNGSIKEQGTHQELL 1230
Cdd:PRK13642 154 IIALRPEIIILDESTSMLDptgrQEIMRVIHEIKEKYQL--TVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELF 228
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1016-1231 |
1.05e-25 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 107.85 E-value: 1.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1016 RPEVPVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVKELN-VQW--LRSQTAIVSQEPV-L 1091
Cdd:PRK10419 22 HQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNrAQRkaFRRDIQMVFQDSIsA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1092 FNC--SIAENIAYgdnsrmvPLEEIKEVADAANIHSFIEGLprkynTLVGL-------RGVQLSGGQKQRLAIARALLRK 1162
Cdd:PRK10419 102 VNPrkTVREIIRE-------PLRHLLSLDKAERLARASEML-----RAVDLddsvldkRPPQLSGGQLQRVCLARALAVE 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568980685 1163 PKILLLDEATSALDneseKVVQ-QALD-----KARRGKTCLVVAHRLSTIQN-ADMIVVLQNGSIKEQGTHQELLR 1231
Cdd:PRK10419 170 PKLLILDEAVSNLD----LVLQaGVIRllkklQQQFGTACLFITHDLRLVERfCQRVMVMDNGQIVETQPVGDKLT 241
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1018-1232 |
1.16e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 108.25 E-value: 1.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1018 EVPVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVKELNVQW-LRSQTAIVSQEP--VLFNC 1094
Cdd:PRK13633 22 EKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLWdIRNKAGMVFQNPdnQIVAT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1095 SIAENIAYGDNSRMVPLEEIKEVADAA----NIHSFieglpRKYNTLVglrgvqLSGGQKQRLAIARALLRKPKILLLDE 1170
Cdd:PRK13633 102 IVEEDVAFGPENLGIPPEEIRERVDESlkkvGMYEY-----RRHAPHL------LSGGQKQRVAIAGILAMRPECIIFDE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568980685 1171 ATSALDNESEKVVQQALDKARR--GKTCLVVAHRLSTIQNADMIVVLQNGSIKEQGTHQELLRN 1232
Cdd:PRK13633 171 PTAMLDPSGRREVVNTIKELNKkyGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEIFKE 234
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
375-593 |
1.22e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 108.63 E-value: 1.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 375 IEFKNVSFSYPSR-PSA-KVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCI------------------ 434
Cdd:PRK13651 3 IKVKNIVKIFNKKlPTElKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknkkktkekek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 435 TVDENDI------RAQNVRHYREQIGVVRQ--EPVLFGTTIGNNIKFG--REGVGEKEMEQAAREanaYDFIMAFPKKFn 504
Cdd:PRK13651 83 VLEKLVIqktrfkKIKKIKEIRRRVGVVFQfaEYQLFEQTIEKDIIFGpvSMGVSKEEAKKRAAK---YIELVGLDESY- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 505 tlVGEKGAQMSGGQKQRIAIARALVRNPKILILDEATSALDTESESLVQTALEKASK-GRTTIVVAHRL-STIRGADLIV 582
Cdd:PRK13651 159 --LQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKqGKTIILVTHDLdNVLEWTKRTI 236
|
250
....*....|.
gi 568980685 583 TMKDGMVVEKG 593
Cdd:PRK13651 237 FFKDGKIIKDG 247
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
375-606 |
1.44e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 107.77 E-value: 1.44e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 375 IEFKNVSFSYPSRPSAkvLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITV---DENDIraQNVRHYRE 451
Cdd:PRK13644 2 IRLENVSYSYPDGTPA--LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVsgiDTGDF--SKLQGIRK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 452 QIGVVRQEP--VLFGTTIGNNIKFGREGVG------EKEMEQAAREANAYDFIMAFPKkfntlvgekgaQMSGGQKQRIA 523
Cdd:PRK13644 78 LVGIVFQNPetQFVGRTVEEDLAFGPENLClppieiRKRVDRALAEIGLEKYRHRSPK-----------TLSGGQGQCVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 524 IARALVRNPKILILDEATSALDTESESLVQTALEKA-SKGRTTIVVAHRLSTIRGADLIVTMKDGMVVEKGTHAELMAKQ 602
Cdd:PRK13644 147 LAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLhEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLSDV 226
|
....
gi 568980685 603 GLYY 606
Cdd:PRK13644 227 SLQT 230
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
375-600 |
1.61e-25 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 107.23 E-value: 1.61e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 375 IEFKNVSFSY------PSRPSAKVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDI------- 441
Cdd:COG4167 5 LEVRNLSKTFkyrtglFRRQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLeygdyky 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 442 RAQNVR----------HYREQIGVVRQEPVLFGTtignnikfgregvgekEMEQAAREAnaydfimafpKKFNTL--VG- 508
Cdd:COG4167 85 RCKHIRmifqdpntslNPRLNIGQILEEPLRLNT----------------DLTAEEREE----------RIFATLrlVGl 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 509 -----EKGAQM-SGGQKQRIAIARALVRNPKILILDEATSALDTESES-LVQTALE-KASKGRTTIVVAHRLSTIRG-AD 579
Cdd:COG4167 139 lpehaNFYPHMlSSGQKQRVALARALILQPKIIIADEALAALDMSVRSqIINLMLElQEKLGISYIYVSQHLGIVKHiSD 218
|
250 260
....*....|....*....|.
gi 568980685 580 LIVTMKDGMVVEKGTHAELMA 600
Cdd:COG4167 219 KVLVMHQGEVVEYGKTAEVFA 239
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1004-1235 |
1.89e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 107.47 E-value: 1.89e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1004 LEFREVSFVYPCRPEVpvLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVKELNVQWL--RSQ 1081
Cdd:PRK13639 2 LETRDLKYSYPDGTEA--LKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLevRKT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1082 TAIVSQEP--VLFNCSIAENIAYGDNSRMVPLEEI-KEVADAanihsfiegLPRkyntlVGLRGVQ------LSGGQKQR 1152
Cdd:PRK13639 80 VGIVFQNPddQLFAPTVEEDVAFGPLNLGLSKEEVeKRVKEA---------LKA-----VGMEGFEnkpphhLSGGQKKR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1153 LAIARALLRKPKILLLDEATSALD-NESEKVVQQALDKARRGKTCLVVAHRLSTIQ-NADMIVVLQNGSIKEQGTHQELL 1230
Cdd:PRK13639 146 VAIAGILAMKPEIIVLDEPTSGLDpMGASQIMKLLYDLNKEGITIIISTHDVDLVPvYADKVYVMSDGKIIKEGTPKEVF 225
|
....*
gi 568980685 1231 RNGDT 1235
Cdd:PRK13639 226 SDIET 230
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1004-1234 |
2.38e-25 |
|
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: 105.83 E-value: 2.38e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1004 LEFREVSFVYPcrpEVPVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVkelnvQWLRSQT- 1082
Cdd:COG0410 4 LEVENLHAGYG---GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDI-----TGLPPHRi 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1083 -----AIVSQEPVLF-NCSIAENI---AYGDNSRMVPLEEIKEVADAanihsFieglPR---KYNTLVGlrgvQLSGGQK 1150
Cdd:COG0410 76 arlgiGYVPEGRRIFpSLTVEENLllgAYARRDRAEVRADLERVYEL-----F----PRlkeRRRQRAG----TLSGGEQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1151 QRLAIARALLRKPKILLLDEATSALdneSEKVVQQALDK----ARRGKTCLVV---AHRLSTIqnADMIVVLQNGSIKEQ 1223
Cdd:COG0410 143 QMLAIGRALMSRPKLLLLDEPSLGL---APLIVEEIFEIirrlNREGVTILLVeqnARFALEI--ADRAYVLERGRIVLE 217
|
250
....*....|.
gi 568980685 1224 GTHQELLRNGD 1234
Cdd:COG0410 218 GTAAELLADPE 228
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1026-1230 |
2.83e-25 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 105.82 E-value: 2.83e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1026 SLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDvkelnvqwlrsQTAIV-SQEPV--------LFN-CS 1095
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQD-----------HTTTPpSRRPVsmlfqennLFShLT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1096 IAENIAYG-------DNSRMVPLEEIkevADAANIHSFIEGLPRkyntlvglrgvQLSGGQKQRLAIARALLRKPKILLL 1168
Cdd:PRK10771 88 VAQNIGLGlnpglklNAAQREKLHAI---ARQMGIEDLLARLPG-----------QLSGGQRQRVALARCLVREQPILLL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568980685 1169 DEATSALD----NESEKVVQQALDkaRRGKTCLVVAHRLS-TIQNADMIVVLQNGSIKEQGTHQELL 1230
Cdd:PRK10771 154 DEPFSALDpalrQEMLTLVSQVCQ--ERQLTLLMVSHSLEdAARIAPRSLVVADGRIAWDGPTDELL 218
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
375-545 |
3.16e-25 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 106.48 E-value: 3.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 375 IEFKNVSFSYPSRPSAK-VLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDIRAQNVRHyreqi 453
Cdd:COG4525 4 LTVRHVSVRYPGGGQPQpALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGADR----- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 454 GVVRQEPVLFG-TTIGNNIKFGRE--GVGEKEMEQAAREANAydfimafpkkfntLVGEKGA------QMSGGQKQRIAI 524
Cdd:COG4525 79 GVVFQKDALLPwLNVLDNVAFGLRlrGVPKAERRARAEELLA-------------LVGLADFarrriwQLSGGMRQRVGI 145
|
170 180
....*....|....*....|.
gi 568980685 525 ARALVRNPKILILDEATSALD 545
Cdd:COG4525 146 ARALAADPRFLLMDEPFGALD 166
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
1010-1239 |
3.20e-25 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 114.06 E-value: 3.20e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1010 SFVYPCRPEVPVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLdgvdvkelnvqwLRSQTAIVSQEP 1089
Cdd:PLN03130 621 YFSWDSKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDASVV------------IRGTVAYVPQVS 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1090 VLFNCSIAENIAYGdnsrmVPLEEIK--EVADAANIHSFIEGLPRKYNTLVGLRGVQLSGGQKQRLAIARALLRKPKILL 1167
Cdd:PLN03130 689 WIFNATVRDNILFG-----SPFDPERyeRAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYI 763
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568980685 1168 LDEATSALDnesEKVVQQALDK----ARRGKTCLVVAHRLSTIQNADMIVVLQNGSIKEQGTHQELLRNGDTYFKL 1239
Cdd:PLN03130 764 FDDPLSALD---AHVGRQVFDKcikdELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSNNGPLFQKL 836
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1004-1217 |
4.31e-25 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 104.49 E-value: 4.31e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1004 LEFREVSFvypCRPEVPVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDP---MKGQVLLDGVDVKELNVQwlRS 1080
Cdd:COG4136 2 LSLENLTI---TLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALPAE--QR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1081 QTAIVSQEPVLF-NCSIAENIAYGDNSRmVPLEEIKEVADAAnihsfiegLPRkyntlVGLRGV------QLSGGQKQRL 1153
Cdd:COG4136 77 RIGILFQDDLLFpHLSVGENLAFALPPT-IGRAQRRARVEQA--------LEE-----AGLAGFadrdpaTLSGGQRARV 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568980685 1154 AIARALLRKPKILLLDEATSALDNE-SEKVVQQALDKAR-RGKTCLVVAHRLSTIQNADMIVVLQN 1217
Cdd:COG4136 143 ALLRALLAEPRALLLDEPFSKLDAAlRAQFREFVFEQIRqRGIPALLVTHDEEDAPAAGRVLDLGN 208
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
375-598 |
4.88e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 106.74 E-value: 4.88e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 375 IEFKNVSFSY-PSRP-SAKVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDE----NDIRAQNVRH 448
Cdd:PRK13643 2 IKFEKVNYTYqPNSPfASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDivvsSTSKQKEIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 449 YREQIGVVRQEP--VLFGTTIGNNIKFGRE--GVGEKEMEQAAREANAydfIMAFPKKFntlvGEKGA-QMSGGQKQRIA 523
Cdd:PRK13643 82 VRKKVGVVFQFPesQLFEETVLKDVAFGPQnfGIPKEKAEKIAAEKLE---MVGLADEF----WEKSPfELSGGQMRRVA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568980685 524 IARALVRNPKILILDEATSALDTESESLVQTALEKASK-GRTTIVVAHRLSTIRG-ADLIVTMKDGMVVEKGTHAEL 598
Cdd:PRK13643 155 IAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQsGQTVVLVTHLMDDVADyADYVYLLEKGHIISCGTPSDV 231
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
1004-1233 |
6.15e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 106.40 E-value: 6.15e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1004 LEFREVSFVY-PCRP-EVPVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDV----KELNVQW 1077
Cdd:PRK13646 3 IRFDNVSYTYqKGTPyEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIthktKDKYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1078 LRSQTAIVSQ--EPVLFNCSIAENIAYGDNSRMVPLEEIKEVAdaanIHSFIE-GLPRKyntLVGLRGVQLSGGQKQRLA 1154
Cdd:PRK13646 83 VRKRIGMVFQfpESQLFEDTVEREIIFGPKNFKMNLDEVKNYA----HRLLMDlGFSRD---VMSQSPFQMSGGQMRKIA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1155 IARALLRKPKILLLDEATSALDNESEKVVQQALDKAR--RGKTCLVVAHRLSTI-QNADMIVVLQNGSIKEQGTHQELLR 1231
Cdd:PRK13646 156 IVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtdENKTIILVSHDMNEVaRYADEVIVMKEGSIVSQTSPKELFK 235
|
..
gi 568980685 1232 NG 1233
Cdd:PRK13646 236 DK 237
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
34-320 |
7.68e-25 |
|
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: 105.98 E-value: 7.68e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 34 IVLMTLGILASMINgatvPLmslVLGEISDHLINGclvqtnrtkyqncsqtqeKLNEDIIVLTLYYIGIGAAALIFGYVQ 113
Cdd:cd18542 5 ILALLLATALNLLI----PL---LIRRIIDSVIGG------------------GLRELLWLLALLILGVALLRGVFRYLQ 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 114 ISFWVITAARQTTRIRKQFFHSILAQDISWFDGSDICELNTRMTGDINKLCDGIGDKIPLMFQNISGFSIGLVISLIKSW 193
Cdd:cd18542 60 GYLAEKASQKVAYDLRNDLYDHLQRLSFSFHDKARTGDLMSRCTSDVDTIRRFLAFGLVELVRAVLLFIGALIIMFSINW 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 194 KLSLVVLSTSPLIMASSALCSRMIISLTSKELDAYSKAGAVAEEALSSIQTVTAFGAQEKEIQRYTQHLKDAKDAGIKRA 273
Cdd:cd18542 140 KLTLISLAIIPFIALFSYVFFKKVRPAFEEIREQEGELNTVLQENLTGVRVVKAFAREDYEIEKFDKENEEYRDLNIKLA 219
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 568980685 274 TASKLSLGAVYFFMNGAYGLAFWYGTSLIFGGEpgYTIGTiLAVFFS 320
Cdd:cd18542 220 KLLAKYWPLMDFLSGLQIVLVLWVGGYLVINGE--ITLGE-LVAFIS 263
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
375-599 |
7.74e-25 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 105.17 E-value: 7.74e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 375 IEFKNVSFSYPSRPsakVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDIRAQNVRHYREQIG 454
Cdd:COG4604 2 IEIKNVSKRYGGKV---VLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 455 VVRQEPVLfgttignNIK--------FGR----EGVGEKEMEQAAREANAYDFIMAFPKKF-NTLvgekgaqmSGGQKQR 521
Cdd:COG4604 79 ILRQENHI-------NSRltvrelvaFGRfpysKGRLTAEDREIIDEAIAYLDLEDLADRYlDEL--------SGGQRQR 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 522 IAIARALVRNPKILILDEATSALDTE-SESLVQTaLEKAS--KGRTTIVVAHRLS-TIRGADLIVTMKDGMVVEKGTHAE 597
Cdd:COG4604 144 AFIAMVLAQDTDYVLLDEPLNNLDMKhSVQMMKL-LRRLAdeLGKTVVIVLHDINfASCYADHIVAMKDGRVVAQGTPEE 222
|
..
gi 568980685 598 LM 599
Cdd:COG4604 223 II 224
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
375-602 |
8.44e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 105.70 E-value: 8.44e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 375 IEFKNVSFSYPSRPSAkvLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDEN--DIRAQNVRHYREQ 452
Cdd:PRK13636 6 LKVEELNYNYSDGTHA--LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpiDYSRKGLMKLRES 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 453 IGVVRQEP--VLFGTTIGNNIKFGREGVG--EKEMEQAAREANAYDFIMAFPKKfntlvgeKGAQMSGGQKQRIAIARAL 528
Cdd:PRK13636 84 VGMVFQDPdnQLFSASVYQDVSFGAVNLKlpEDEVRKRVDNALKRTGIEHLKDK-------PTHCLSFGQKKRVAIAGVL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568980685 529 VRNPKILILDEATSALDTESESLVQTALEKASK--GRTTIVVAHRLSTIR-GADLIVTMKDGMVVEKGTHAELMAKQ 602
Cdd:PRK13636 157 VMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKelGLTIIIATHDIDIVPlYCDNVFVMKEGRVILQGNPKEVFAEK 233
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
375-594 |
1.13e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 104.73 E-value: 1.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 375 IEFKNVSFSYPSRpsaKVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPE-----DGCITVDENDI--RAQNVR 447
Cdd:PRK14258 8 IKVNNLSFYYDTQ---KILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELEsevrvEGRVEFFNQNIyeRRVNLN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 448 HYREQIGVVRQEPVLFGTTIGNNIKFGREGVG-------EKEMEQAAREANAYDFImafpkkfNTLVGEKGAQMSGGQKQ 520
Cdd:PRK14258 85 RLRRQVSMVHPKPNLFPMSVYDNVAYGVKIVGwrpkleiDDIVESALKDADLWDEI-------KHKIHKSALDLSGGQQQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 521 RIAIARALVRNPKILILDEATSALDTES----ESLVQTALEKASkgRTTIVVAHRLSTI-RGADLIVTMKD-----GMVV 590
Cdd:PRK14258 158 RLCIARALAVKPKVLLMDEPCFGLDPIAsmkvESLIQSLRLRSE--LTMVIVSHNLHQVsRLSDFTAFFKGnenriGQLV 235
|
....
gi 568980685 591 EKGT 594
Cdd:PRK14258 236 EFGL 239
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
393-598 |
1.29e-24 |
|
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: 103.60 E-value: 1.29e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 393 LKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDIRaQNVRHYREQIGVVRQEPVLFGTTIG--NN 470
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVV-REPREVRRRIGIVFQDLSVDDELTGweNL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 471 IKFGR-EGVGEKEMEQAAREANAYdfiMAFPKKFNTLVGekgaQMSGGQKQRIAIARALVRNPKILILDEATSALDTESE 549
Cdd:cd03265 95 YIHARlYGVPGAERRERIDELLDF---VGLLEAADRLVK----TYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTR 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 568980685 550 SLVQTALEK--ASKGRTTIVVAHRLSTIRG-ADLIVTMKDGMVVEKGTHAEL 598
Cdd:cd03265 168 AHVWEYIEKlkEEFGMTILLTTHYMEEAEQlCDRVAIIDHGRIIAEGTPEEL 219
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
391-600 |
1.56e-24 |
|
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: 103.67 E-value: 1.56e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 391 KVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDIRAQNVrHYREQIGVVR--QEPVLFGT-TI 467
Cdd:cd03219 14 VALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPP-HEIARLGIGRtfQIPRLFPElTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 468 ------------GNNIKFGREGVGEKEMEQAAREanaydfIMAF---PKKFNTLVGEkgaqMSGGQKQRIAIARALVRNP 532
Cdd:cd03219 93 lenvmvaaqartGSGLLLARARREEREARERAEE------LLERvglADLADRPAGE----LSYGQQRRLEIARALATDP 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 533 KILILDEATSAL-DTESESLVQTALEKASKGRTTIVVAHRLSTIRG-ADLIVTMKDGMVVEKGTHAELMA 600
Cdd:cd03219 163 KLLLLDEPAAGLnPEETEELAELIRELRERGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGTPDEVRN 232
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
377-570 |
1.80e-24 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 109.00 E-value: 1.80e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 377 FKNVSFSYPSRPsakVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITvdendiRAQNVRhyreqIGVV 456
Cdd:COG0488 1 LENLSKSFGGRP---LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVS------IPKGLR-----IGYL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 457 RQEPVLF-GTTIGNNIKFGREGV----------------GEKEMEQAAR------EANAYDF------IMA---FPKK-F 503
Cdd:COG0488 67 PQEPPLDdDLTVLDTVLDGDAELraleaeleeleaklaePDEDLERLAElqeefeALGGWEAearaeeILSglgFPEEdL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568980685 504 NTLVGEkgaqMSGGQKQRIAIARALVRNPKILILDEATSALDTES----ESLVqtaleKASKGrTTIVVAH 570
Cdd:COG0488 147 DRPVSE----LSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESiewlEEFL-----KNYPG-TVLVVSH 207
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
375-593 |
2.35e-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: 102.57 E-value: 2.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 375 IEFKNVSFSYPSRPSAkvlkgLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDIRAQNVRhyREQIG 454
Cdd:cd03298 1 VRLDKIRFSYGEQPMH-----FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA--DRPVS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 455 VVRQEPVLFG-TTIGNNIKFGR------EGVGEKEMEQAAREANAYDFIMAFPKkfntlvgekgaQMSGGQKQRIAIARA 527
Cdd:cd03298 74 MLFQENNLFAhLTVEQNVGLGLspglklTAEDRQAIEVALARVGLAGLEKRLPG-----------ELSGGERQRVALARV 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568980685 528 LVRNPKILILDEATSALDTESESLVQTALEK--ASKGRTTIVVAHRLSTIRG-ADLIVTMKDGMVVEKG 593
Cdd:cd03298 143 LVRDKPVLLLDEPFAALDPALRAEMLDLVLDlhAETKMTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
392-600 |
2.40e-24 |
|
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: 109.00 E-value: 2.40e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 392 VLKGLNLKIKAGETVALVGPSGSGKSTT----VQLLQRLYDPEDGCITVDENDIRAQNVRHYRE----QIGVVRQEPV-- 461
Cdd:COG4172 25 AVKGVSFDIAAGETLALVGESGSGKSVTalsiLRLLPDPAAHPSGSILFDGQDLLGLSERELRRirgnRIAMIFQEPMts 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 462 ---LFgtTIGNNIkfgRE------GVGEKEMEQAAREA-------NAYDFIMAFPKkfntlvgekgaQMSGGQKQRIAIA 525
Cdd:COG4172 105 lnpLH--TIGKQI---AEvlrlhrGLSGAAARARALELlervgipDPERRLDAYPH-----------QLSGGQRQRVMIA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 526 RALVRNPKILILDEATSALD-TeseslVQTA-LE-----KASKGRTTIVVAHRLSTIRG-ADLIVTMKDGMVVEKGTHAE 597
Cdd:COG4172 169 MALANEPDLLIADEPTTALDvT-----VQAQiLDllkdlQRELGMALLLITHDLGVVRRfADRVAVMRQGEIVEQGPTAE 243
|
...
gi 568980685 598 LMA 600
Cdd:COG4172 244 LFA 246
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
375-598 |
2.54e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 103.45 E-value: 2.54e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 375 IEFKNVSFSYPSrpsAKVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYD--PE---DGCITVDENDIRAQNVRHY 449
Cdd:PRK14247 4 IEIRDLKVSFGQ---VEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElyPEarvSGEVYLDGQDIFKMDVIEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 450 REQIGVVRQEPVLFGT-TIGNNIKFG----REGVGEKEMEQAAREAnaYDFIMAFPKKFNTLvGEKGAQMSGGQKQRIAI 524
Cdd:PRK14247 81 RRRVQMVFQIPNPIPNlSIFENVALGlklnRLVKSKKELQERVRWA--LEKAQLWDEVKDRL-DAPAGKLSGGQQQRLCI 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568980685 525 ARALVRNPKILILDEATSALDTESESLVQTALEKASKGRTTIVVAH-RLSTIRGADLIVTMKDGMVVEKGTHAEL 598
Cdd:PRK14247 158 ARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHfPQQAARISDYVAFLYKGQIVEWGPTREV 232
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
375-599 |
2.72e-24 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 103.73 E-value: 2.72e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 375 IEFKNVSFSYPS------RPSAKVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDIRAQNvrh 448
Cdd:TIGR02769 3 LEVRDVTHTYRTgglfgaKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLD--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 449 yREQIGVVRQE-PVLFGTTIG--NNIKFGREGVGE--------KEMEQAAREANAYDFIMAFPKKFNTLvgekGAQMSGG 517
Cdd:TIGR02769 80 -RKQRRAFRRDvQLVFQDSPSavNPRMTVRQIIGEplrhltslDESEQKARIAELLDMVGLRSEDADKL----PRQLSGG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 518 QKQRIAIARALVRNPKILILDEATSALDTESESLVQTALEK--ASKGRTTIVVAHRLSTI-RGADLIVTMKDGMVVEKGT 594
Cdd:TIGR02769 155 QLQRINIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKlqQAFGTAYLFITHDLRLVqSFCQRVAVMDKGQIVEECD 234
|
....*
gi 568980685 595 HAELM 599
Cdd:TIGR02769 235 VAQLL 239
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
381-593 |
2.80e-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: 2.80e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 381 SFSYPSRPsAKVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDIrAQNVRHYREQIGVVRQEP 460
Cdd:cd03266 10 RFRDVKKT-VQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDV-VKEPAEARRRLGFVSDST 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 461 VLFG--TTIGNNIKFGR-EGVGEKEMEQAAREanaydfiMAFPKKFNTLVGEKGAQMSGGQKQRIAIARALVRNPKILIL 537
Cdd:cd03266 88 GLYDrlTARENLEYFAGlYGLKGDELTARLEE-------LADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 568980685 538 DEATSALD-TESESLVQTALEKASKGRTTIVVAHRLSTI-RGADLIVTMKDGMVVEKG 593
Cdd:cd03266 161 DEPTTGLDvMATRALREFIRQLRALGKCILFSTHIMQEVeRLCDRVVVLHRGRVVYEG 218
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
378-600 |
2.92e-24 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 103.61 E-value: 2.92e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 378 KNVSFSYPS------RPSAKVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDIRAQNvrhyRE 451
Cdd:PRK10419 7 SGLSHHYAHgglsgkHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLN----RA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 452 QIGVVRQE-PVLFGTTIG--NNIKFGREGVGEK-----EMEQAAREANAYDFIMAFPKKfNTLVGEKGAQMSGGQKQRIA 523
Cdd:PRK10419 83 QRKAFRRDiQMVFQDSISavNPRKTVREIIREPlrhllSLDKAERLARASEMLRAVDLD-DSVLDKRPPQLSGGQLQRVC 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 524 IARALVRNPKILILDEATSALDTESESLVQTALEKASKGRTT--IVVAHRLSTI-RGADLIVTMKDGMVVEKGTHAELMA 600
Cdd:PRK10419 162 LARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTacLFITHDLRLVeRFCQRVMVMDNGQIVETQPVGDKLT 241
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1018-1232 |
3.05e-24 |
|
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: 108.62 E-value: 3.05e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1018 EVPVLQNMSLSIEKGKTVAFVGSSGCGKS----TCVQLLQRFYDPMKGQVLLDGVDVKELNVQWLR----SQTAIVSQEP 1089
Cdd:COG4172 22 TVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERELRrirgNRIAMIFQEP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1090 vlfncsiaeniaygdnsrMV---PLEEI-KEVADAANIHsfiEGLPRK--------YNTLVGLRGV---------QLSGG 1148
Cdd:COG4172 102 ------------------MTslnPLHTIgKQIAEVLRLH---RGLSGAaararaleLLERVGIPDPerrldayphQLSGG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1149 QKQRLAIARALLRKPKILLLDEATSALDnesekVVQQA--LD-----KARRGKTCLVVAHRLSTIQN-ADMIVVLQNGSI 1220
Cdd:COG4172 161 QRQRVMIAMALANEPDLLIADEPTTALD-----VTVQAqiLDllkdlQRELGMALLLITHDLGVVRRfADRVAVMRQGEI 235
|
250
....*....|..
gi 568980685 1221 KEQGTHQELLRN 1232
Cdd:COG4172 236 VEQGPTAELFAA 247
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1021-1230 |
3.31e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 103.20 E-value: 3.31e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1021 VLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRF---YDP---MKGQVLLDGVDVKELNVQWLRSQTAIVSQEPVLF-N 1093
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLieiYDSkikVDGKVLYFGKDIFQIDAIKLRKEVGMVFQQPNPFpH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1094 CSIAENIAYgdnsrmvPLEEiKEVADAANIHSFIE------GLPRKYNTLVGLRGVQLSGGQKQRLAIARALLRKPKILL 1167
Cdd:PRK14246 105 LSIYDNIAY-------PLKS-HGIKEKREIKKIVEeclrkvGLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568980685 1168 LDEATSALDNESEKVVQQALDKARRGKTCLVVAHRLSTIQN-ADMIVVLQNGSIKEQGTHQELL 1230
Cdd:PRK14246 177 MDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARvADYVAFLYNGELVEWGSSNEIF 240
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
1004-1225 |
4.47e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 103.67 E-value: 4.47e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1004 LEFREVSFVYPC-RP-EVPVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDV----KELNVQW 1077
Cdd:PRK13649 3 INLQNVSYTYQAgTPfEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLItstsKNKDIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1078 LRSQTAIVSQ--EPVLFNCSIAENIAYGDNSRMVPLEEikevadaanihsfIEGLPRKYNTLVGL-------RGVQLSGG 1148
Cdd:PRK13649 83 IRKKVGLVFQfpESQLFEETVLKDVAFGPQNFGVSQEE-------------AEALAREKLALVGIseslfekNPFELSGG 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568980685 1149 QKQRLAIARALLRKPKILLLDEATSALDNESEKVVQQALDKARR-GKTCLVVAHRLSTIQN-ADMIVVLQNGSIKEQGT 1225
Cdd:PRK13649 150 QMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQsGMTIVLVTHLMDDVANyADFVYVLEKGKLVLSGK 228
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
53-322 |
7.34e-24 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350019 [Multi-domain] Cd Length: 289 Bit Score: 103.33 E-value: 7.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 53 LMSLVLGEISDHLINGCLVQTNRtkyqncsqtqEKLNEDIIVLtlyyIGIGAAALIFGYVQISFWVITAARQTTRIRKQF 132
Cdd:cd18575 10 AATLALGQGLRLLIDQGFAAGNT----------ALLNRAFLLL----LAVALVLALASALRFYLVSWLGERVVADLRKAV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 133 FHSILAQDISWFDGSDICELNTRMTGDINKLCDGIGDKIPLMFQNISGFSIGLVISLIKSWKLSLVVLSTSPLIMASSAL 212
Cdd:cd18575 76 FAHLLRLSPSFFETTRTGEVLSRLTTDTTLIQTVVGSSLSIALRNLLLLIGGLVMLFITSPKLTLLVLLVIPLVVLPIIL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 213 CSRMIISLTSKELDAYSKAGAVAEEALSSIQTVTAFGAQEKEIQRYTQHLKDAKDAGIKRATASKLSLGAVYFFMNGAYG 292
Cdd:cd18575 156 FGRRVRRLSRASQDRLADLSAFAEETLSAIKTVQAFTREDAERQRFATAVEAAFAAALRRIRARALLTALVIFLVFGAIV 235
|
250 260 270
....*....|....*....|....*....|.
gi 568980685 293 LAFWYGTSLIFGGEpgYTIGTILA-VFFSVI 322
Cdd:cd18575 236 FVLWLGAHDVLAGR--MSAGELSQfVFYAVL 264
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
379-598 |
8.10e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 102.43 E-value: 8.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 379 NVSFSYPSRPSAKVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDEN------DIRAQNVRHYREQ 452
Cdd:PRK14246 12 NISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkDIFQIDAIKLRKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 453 IGVVRQEPVLF-GTTIGNNIKFGREGVGEKE-------MEQAAREANAYdfimafpKKFNTLVGEKGAQMSGGQKQRIAI 524
Cdd:PRK14246 92 VGMVFQQPNPFpHLSIYDNIAYPLKSHGIKEkreikkiVEECLRKVGLW-------KEVYDRLNSPASQLSGGQQQRLTI 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568980685 525 ARALVRNPKILILDEATSALDTESESLVQTALEKASKGRTTIVVAHRLSTI-RGADLIVTMKDGMVVEKGTHAEL 598
Cdd:PRK14246 165 ARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVaRVADYVAFLYNGELVEWGSSNEI 239
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1020-1231 |
9.29e-24 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 102.16 E-value: 9.29e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1020 PVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVKELNVQWLRSQTAIVSQEPVL-FNCSIAE 1098
Cdd:PRK13548 16 TLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQHSSLsFPFTVEE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1099 NIAYGdnsRMvPLEEIKEVADAanihsfiegLPRKYNTLVGLRGV------QLSGGQKQRLAIARALLR------KPKIL 1166
Cdd:PRK13548 96 VVAMG---RA-PHGLSRAEDDA---------LVAAALAQVDLAHLagrdypQLSGGEQQRVQLARVLAQlwepdgPPRWL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568980685 1167 LLDEATSALD-NESEKVVQQALDKAR-RGKTCLVVAHRLS-TIQNADMIVVLQNGSIKEQGTHQELLR 1231
Cdd:PRK13548 163 LLDEPTSALDlAHQHHVLRLARQLAHeRGLAVIVVLHDLNlAARYADRIVLLHQGRLVADGTPAEVLT 230
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
374-594 |
1.12e-23 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 104.01 E-value: 1.12e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 374 NIEFKNVSFSYPSRpsaKVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDIRAQnvrHYRE-Q 452
Cdd:PRK10851 2 SIEIANIKKSFGRT---QVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRL---HARDrK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 453 IGVVRQEPVLF-GTTIGNNIKFG-----------REGVGEK-----EMEQAAREANAYdfimafPkkfntlvgekgAQMS 515
Cdd:PRK10851 76 VGFVFQHYALFrHMTVFDNIAFGltvlprrerpnAAAIKAKvtqllEMVQLAHLADRY------P-----------AQLS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 516 GGQKQRIAIARALVRNPKILILDEATSALDTESESLVQTALEKASK--GRTTIVVAH-RLSTIRGADLIVTMKDGMVVEK 592
Cdd:PRK10851 139 GGQKQRVALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEelKFTSVFVTHdQEEAMEVADRVVVMSQGNIEQA 218
|
..
gi 568980685 593 GT 594
Cdd:PRK10851 219 GT 220
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
373-611 |
1.14e-23 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 109.10 E-value: 1.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 373 GNIEFKNVSFSYpsRPSAK-VLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDIRAQNVRHYRE 451
Cdd:PTZ00243 1307 GSLVFEGVQMRY--REGLPlVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRR 1384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 452 QIGVVRQEPVLFGTTIGNNIK-F----------GREGVGEKemEQAAREANAYDfimafpkkfnTLVGEKGAQMSGGQKQ 520
Cdd:PTZ00243 1385 QFSMIPQDPVLFDGTVRQNVDpFleassaevwaALELVGLR--ERVASESEGID----------SRVLEGGSNYSVGQRQ 1452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 521 RIAIARALVRNPKILIL-DEATSALDTESESLVQTALEKASKGRTTIVVAHRLSTIRGADLIVTMKDGMVVEKGTHAEL- 598
Cdd:PTZ00243 1453 LMCMARALLKKGSGFILmDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELv 1532
|
250
....*....|...
gi 568980685 599 MAKQGLYYSLAMA 611
Cdd:PTZ00243 1533 MNRQSIFHSMVEA 1545
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1004-1206 |
1.16e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 102.04 E-value: 1.16e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1004 LEFREVSFVYPCRPevpVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDpMKGQVLLDG--------VDVKELNV 1075
Cdd:PRK14258 8 IKVNNLSFYYDTQK---ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNE-LESEVRVEGrveffnqnIYERRVNL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1076 QWLRSQTAIVSQEPVLFNCSIAENIAYGDN----SRMVPLEEIKEVA-DAANIHSFIEGLPRKyntlvglRGVQLSGGQK 1150
Cdd:PRK14258 84 NRLRRQVSMVHPKPNLFPMSVYDNVAYGVKivgwRPKLEIDDIVESAlKDADLWDEIKHKIHK-------SALDLSGGQQ 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 568980685 1151 QRLAIARALLRKPKILLLDEATSALDNESEKVVQQALD--KARRGKTCLVVAHRLSTI 1206
Cdd:PRK14258 157 QRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQslRLRSELTMVIVSHNLHQV 214
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1004-1218 |
1.29e-23 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 99.55 E-value: 1.29e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1004 LEFREVSF---VYPCRPEVPVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLL--QRFYDPMKGQVLLDGVDVKElnvQWL 1078
Cdd:cd03213 4 LSFRNLTVtvkSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGRPLDK---RSF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1079 RSQTAIVSQEPVLFNC-SIAENIAYgdnsrmvpleeikevadAANihsfieglprkyntlvgLRGvqLSGGQKQRLAIAR 1157
Cdd:cd03213 81 RKIIGYVPQDDILHPTlTVRETLMF-----------------AAK-----------------LRG--LSGGERKRVSIAL 124
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568980685 1158 ALLRKPKILLLDEATSALDNESEKVVQQALDK-ARRGKTCLVVAHRLST--IQNADMIVVLQNG 1218
Cdd:cd03213 125 ELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRlADTGRTIICSIHQPSSeiFELFDKLLLLSQG 188
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
678-1229 |
1.57e-23 |
|
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: 108.46 E-value: 1.57e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 678 WPFVVLGTLA--SALNGSVHPvfsIIFGKLVTMFEDKNKATLKQDAELySMMLVVLGIVAlvTYLMQGLFYGRaeENLAM 755
Cdd:TIGR01271 80 WRFVFYGILLyfGEATKAVQP---LLLGRIIASYDPFNAPEREIAYYL-ALGLCLLFIVR--TLLLHPAIFGL--HHLGM 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 756 RLRHSAFkAMLYQDMAWYDDK---ENNTGALTTTLAVDVAQI-QGAATSRLGIVTQdvsnMSLSILISFIygWEM----T 827
Cdd:TIGR01271 152 QMRIALF-SLIYKKTLKLSSRvldKISTGQLVSLLSNNLNKFdEGLALAHFVWIAP----LQVILLMGLI--WELlevnG 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 828 LLILSFAPVLAVTGMIQTAAMAGFanRDKqalkRAGKIA------TEAVENIRTVVSLTRERAFEQMYEETLQTQHRNAL 901
Cdd:TIGR01271 225 FCGLGFLILLALFQACLGQKMMPY--RDK----RAGKISerlaitSEIIENIQSVKAYCWEEAMEKIIKNIRQDELKLTR 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 902 KRAhitgccyavshaFVHFAHAAGFRFGAYLIQAGRMMP----EGMFI--VFTAIAYGA---MAIGETLVWA-------- 964
Cdd:TIGR01271 299 KIA------------YLRYFYSSAFFFSGFFVVFLSVVPyaliKGIILrrIFTTISYCIvlrMTVTRQFPGAiqtwydsl 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 965 ------------PEYSKAK------------------AGASHLFALLKNkptinscSQSGEKPDTCEGNLEFREVSFVYp 1014
Cdd:TIGR01271 367 gaitkiqdflckEEYKTLEynltttevemvnvtaswdEGIGELFEKIKQ-------NNKARKQPNGDDGLFFSNFSLYV- 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1015 crpeVPVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGvdvkelnvqwlrsQTAIVSQEPVLFNC 1094
Cdd:TIGR01271 439 ----TPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG-------------RISFSPQTSWIMPG 501
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1095 SIAENIAYGdnsrmVPLEEIK--EVADAANIHSFIEGLPRKYNTLVGLRGVQLSGGQKQRLAIARALLRKPKILLLDEAT 1172
Cdd:TIGR01271 502 TIKDNIIFG-----LSYDEYRytSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPF 576
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 568980685 1173 SALDNESEK-VVQQALDKARRGKTCLVVAHRLSTIQNADMIVVLQNGSIKEQGTHQEL 1229
Cdd:TIGR01271 577 THLDVVTEKeIFESCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSEL 634
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1019-1232 |
1.59e-23 |
|
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: 101.27 E-value: 1.59e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1019 VPVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVKELNVQwlrsqtAIVS-------QEPVL 1091
Cdd:COG0411 17 LVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPH------RIARlgiartfQNPRL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1092 F-NCSIAENIA--------YGDNSRMVPL-------EEIKEVADAAnihsfIE--GLPRKYNTLVGlrgvQLSGGQKQRL 1153
Cdd:COG0411 91 FpELTVLENVLvaaharlgRGLLAALLRLprarreeREARERAEEL-----LErvGLADRADEPAG----NLSYGQQRRL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1154 AIARALLRKPKILLLDEATSAL-DNESEKVVQ--QALdKARRGKTCLVVAHRLSTIQN-ADMIVVLQNGSIKEQGTHQEL 1229
Cdd:COG0411 162 EIARALATEPKLLLLDEPAAGLnPEETEELAEliRRL-RDERGITILLIEHDMDLVMGlADRIVVLDFGRVIAEGTPAEV 240
|
...
gi 568980685 1230 LRN 1232
Cdd:COG0411 241 RAD 243
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
1022-1218 |
1.62e-23 |
|
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: 100.62 E-value: 1.62e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1022 LQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVKELNvqwlrSQTAIVSQEPVLFN-CSIAENI 1100
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPG-----PDRMVVFQNYSLLPwLTVRENI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1101 AYGDNS--RMVPLEEIKEVADaanihsfieglprKYNTLVGLRGV------QLSGGQKQRLAIARALLRKPKILLLDEAT 1172
Cdd:TIGR01184 76 ALAVDRvlPDLSKSERRAIVE-------------EHIALVGLTEAadkrpgQLSGGMKQRVAIARALSIRPKVLLLDEPF 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 568980685 1173 SALDNESEKVVQQALDK--ARRGKTCLVVAHRL-STIQNADMIVVLQNG 1218
Cdd:TIGR01184 143 GALDALTRGNLQEELMQiwEEHRVTVLMVTHDVdEALLLSDRVVMLTNG 191
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
1004-1224 |
1.70e-23 |
|
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: 99.96 E-value: 1.70e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1004 LEFREVSFVYP-CRpevpVLQNMSLSIEKGKTvAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVKElNVQWLRSQT 1082
Cdd:cd03264 1 LQLENLTKRYGkKR----ALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLRRRI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1083 AIVSQEPVLF-NCSIAENIAY-----GDNSRMVPlEEIKEVADAANIHSFieglprkYNTLVGlrgvQLSGGQKQRLAIA 1156
Cdd:cd03264 75 GYLPQEFGVYpNFTVREFLDYiawlkGIPSKEVK-ARVDEVLELVNLGDR-------AKKKIG----SLSGGMRRRVGIA 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568980685 1157 RALLRKPKILLLDEATSALDNESEKVVQQALDKARRGKTCLVVAHRLSTIQN-ADMIVVLQNGSIKEQG 1224
Cdd:cd03264 143 QALVGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
391-599 |
1.99e-23 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 100.53 E-value: 1.99e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 391 KVLKGLNLKIKAGETVALVGPSGSGKSTTVQLL--QRLYDPEDGCITVDENDI-------RAqnvrhyREQIGVVRQEPV 461
Cdd:COG0396 14 EILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLmgHPKYEVTSGSILLDGEDIlelspdeRA------RAGIFLAFQYPV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 462 LFgttignnikfgrEGVGEKEMEQAAREANAYDFIMAFpkKFNTLVGEKGAQM---------------SGGQKQRIAIAR 526
Cdd:COG0396 88 EI------------PGVSVSNFLRTALNARRGEELSAR--EFLKLLKEKMKELgldedfldryvnegfSGGEKKRNEILQ 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568980685 527 ALVRNPKILILDEATSALDTESESLVQTALEK-ASKGRTTIVVAH--RLSTIRGADLIVTMKDGMVVEKGThAELM 599
Cdd:COG0396 154 MLLLEPKLAILDETDSGLDIDALRIVAEGVNKlRSPDRGILIITHyqRILDYIKPDFVHVLVDGRIVKSGG-KELA 228
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1018-1232 |
2.19e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 100.76 E-value: 2.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1018 EVPVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYD-----PMKGQVLLDGVDVKELNVQWLRSQTAIVSQEP-VL 1091
Cdd:PRK14247 15 QVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDIFKMDVIELRRRVQMVFQIPnPI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1092 FNCSIAENIAYG------DNSRMVPLEEIKEVADAANIHsfiEGLPRKYNTLVGlrgvQLSGGQKQRLAIARALLRKPKI 1165
Cdd:PRK14247 95 PNLSIFENVALGlklnrlVKSKKELQERVRWALEKAQLW---DEVKDRLDAPAG----KLSGGQQQRLCIARALAFQPEV 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568980685 1166 LLLDEATSALDNESEKVVQQALDKARRGKTCLVVAH------RLStiqnaDMIVVLQNGSIKEQGTHQELLRN 1232
Cdd:PRK14247 168 LLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHfpqqaaRIS-----DYVAFLYKGQIVEWGPTREVFTN 235
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
375-590 |
2.21e-23 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 106.73 E-value: 2.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 375 IEFKNVSFSYPS-RPSAKVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDIRAQN----VRHY 449
Cdd:PRK10535 5 LELKDIRRSYPSgEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDadalAQLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 450 REQIGVVRQE-PVLFGTTIGNNIKFGREGVGekeMEQAAREANAYDFIMAFpkKFNTLVGEKGAQMSGGQKQRIAIARAL 528
Cdd:PRK10535 85 REHFGFIFQRyHLLSHLTAAQNVEVPAVYAG---LERKQRLLRAQELLQRL--GLEDRVEYQPSQLSGGQQQRVSIARAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568980685 529 VRNPKILILDEATSALDTESESLVQTALEK-ASKGRTTIVVAHRLSTIRGADLIVTMKDGMVV 590
Cdd:PRK10535 160 MNGGQVILADEPTGALDSHSGEEVMAILHQlRDRGHTVIIVTHDPQVAAQAERVIEIRDGEIV 222
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
1022-1203 |
2.59e-23 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 101.01 E-value: 2.59e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1022 LQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPM-----KGQVLLDGVDV--KELNVQWLRSQTAIVSQEPVLFNC 1094
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLIpgfrvEGKVTFHGKNLyaPDVDPVEVRRRIGMVFQKPNPFPK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1095 SIAENIAYGD--NSRMVPLEEIKEVA--DAAnihsFIEGLPRKYNTlvglRGVQLSGGQKQRLAIARALLRKPKILLLDE 1170
Cdd:PRK14243 106 SIYDNIAYGAriNGYKGDMDELVERSlrQAA----LWDEVKDKLKQ----SGLSLSGGQQQRLCIARAIAVQPEVILMDE 177
|
170 180 190
....*....|....*....|....*....|...
gi 568980685 1171 ATSALDNESEKVVQQALDKARRGKTCLVVAHRL 1203
Cdd:PRK14243 178 PCSALDPISTLRIEELMHELKEQYTIIIVTHNM 210
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1021-1239 |
2.67e-23 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 102.85 E-value: 2.67e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1021 VLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVKELNVQwlRSQTAIVSQEPVLF-NCSIAEN 1099
Cdd:PRK10851 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHAR--DRKVGFVFQHYALFrHMTVFDN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1100 IAYGdnSRMVPLeeiKEVADAANIHSFI---------EGLPRKYNTlvglrgvQLSGGQKQRLAIARALLRKPKILLLDE 1170
Cdd:PRK10851 95 IAFG--LTVLPR---RERPNAAAIKAKVtqllemvqlAHLADRYPA-------QLSGGQKQRVALARALAVEPQILLLDE 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568980685 1171 ATSALDNESEKVVQQALDKARR--GKTCLVVAH-RLSTIQNADMIVVLQNGSIKEQGTHQELLRNGDTYFKL 1239
Cdd:PRK10851 163 PFGALDAQVRKELRRWLRQLHEelKFTSVFVTHdQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATRFVL 234
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1004-1230 |
3.20e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 101.08 E-value: 3.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1004 LEFREVSFVYPCRPEVpvLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDG--VDVKELNVQWLRSQ 1081
Cdd:PRK13636 6 LKVEELNYNYSDGTHA--LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkpIDYSRKGLMKLRES 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1082 TAIVSQEP--VLFNCSIAENIAYGDNSRMVPLEEIKEVADAANIHSFIEGLPRKYNTLvglrgvqLSGGQKQRLAIARAL 1159
Cdd:PRK13636 84 VGMVFQDPdnQLFSASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHC-------LSFGQKKRVAIAGVL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568980685 1160 LRKPKILLLDEATSALD----NESEKVVQQALDKArrGKTCLVVAHRLSTIQ-NADMIVVLQNGSIKEQGTHQELL 1230
Cdd:PRK13636 157 VMEPKVLVLDEPTAGLDpmgvSEIMKLLVEMQKEL--GLTIIIATHDIDIVPlYCDNVFVMKEGRVILQGNPKEVF 230
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
1013-1231 |
3.21e-23 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 107.56 E-value: 3.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1013 YPCRPEVpVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVlldgvdvkelnvqWLRSQTAIVSQEPVLF 1092
Cdd:PTZ00243 668 FELEPKV-LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV-------------WAERSIAYVPQQAWIM 733
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1093 NCSIAENIAYGDNSRMVPLEEIKEV----ADAANIHSFIEglprkynTLVGLRGVQLSGGQKQRLAIARALLRKPKILLL 1168
Cdd:PTZ00243 734 NATVRGNILFFDEEDAARLADAVRVsqleADLAQLGGGLE-------TEIGEKGVNLSGGQKARVSLARAVYANRDVYLL 806
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568980685 1169 DEATSALDNE-SEKVVQQALDKARRGKTCLVVAHRLSTIQNADMIVVLQNGSIKEQGTHQELLR 1231
Cdd:PTZ00243 807 DDPLSALDAHvGERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFMR 870
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
375-570 |
4.78e-23 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 99.77 E-value: 4.78e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 375 IEFKNVSFSYPSRPsakVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDIRAQNVRHyreqiG 454
Cdd:PRK11248 2 LQISHLYADYGGKP---ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER-----G 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 455 VVRQ-EPVLFGTTIGNNIKFGRE--GVGEKEMEQAAREANAydfimafpkkfntLVGEKGA------QMSGGQKQRIAIA 525
Cdd:PRK11248 74 VVFQnEGLLPWRNVQDNVAFGLQlaGVEKMQRLEIAHQMLK-------------KVGLEGAekryiwQLSGGQRQRVGIA 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 568980685 526 RALVRNPKILILDEATSALDTESESLVQTALEK--ASKGRTTIVVAH 570
Cdd:PRK11248 141 RALAANPQLLLLDEPFGALDAFTREQMQTLLLKlwQETGKQVLLITH 187
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1018-1220 |
5.00e-23 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 100.16 E-value: 5.00e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1018 EVPVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVKELNVqWLRSQT-AIVSQEPVL---FN 1093
Cdd:COG1101 18 EKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPE-YKRAKYiGRVFQDPMMgtaPS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1094 CSIAEN--IAYGDNSRM-----VpleeikevaDAANIHSFIE-------GLPRKYNTLVGLrgvqLSGGQKQRLAIARAL 1159
Cdd:COG1101 97 MTIEENlaLAYRRGKRRglrrgL---------TKKRRELFREllatlglGLENRLDTKVGL----LSGGQRQALSLLMAT 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568980685 1160 LRKPKILLLDEATSALDNESEKVVQQALDK--ARRGKTCLVVAHRLS-TIQNADMIVVLQNGSI 1220
Cdd:COG1101 164 LTKPKLLLLDEHTAALDPKTAALVLELTEKivEENNLTTLMVTHNMEqALDYGNRLIMMHEGRI 227
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
375-593 |
5.04e-23 |
|
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: 98.51 E-value: 5.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 375 IEFKNVSFSYPSrpsAKVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDIRAQNvrhyREQIG 454
Cdd:cd03269 1 LEVENVTKRFGR---VTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA----RNRIG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 455 VVRQEPVLF-GTTIGNNIK-FGR-EGVGEKEmeqAAREANAYdfimafPKKFNtlVGEKGA----QMSGGQKQRIAIARA 527
Cdd:cd03269 74 YLPEERGLYpKMKVIDQLVyLAQlKGLKKEE---ARRRIDEW------LERLE--LSEYANkrveELSKGNQQKVQFIAA 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568980685 528 LVRNPKILILDEATSALDTESESLVQTAL-EKASKGRTTIVVAHRLSTI-RGADLIVTMKDGMVVEKG 593
Cdd:cd03269 143 VIHDPELLILDEPFSGLDPVNVELLKDVIrELARAGKTVILSTHQMELVeELCDRVLLLNKGRAVLYG 210
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
393-599 |
5.28e-23 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 103.19 E-value: 5.28e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 393 LKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDI------RAQNVRhyREQIGVVRQEPVLF-GT 465
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIakisdaELREVR--RKKIAMVFQSFALMpHM 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 466 TIGNNIKFGRE--GVGEKEMEQAA----REANAYDFIMAFPKkfntlvgekgaQMSGGQKQRIAIARALVRNPKILILDE 539
Cdd:PRK10070 122 TVLDNTAFGMElaGINAEERREKAldalRQVGLENYAHSYPD-----------ELSGGMRQRVGLARALAINPDILLMDE 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568980685 540 ATSALDTESESLVQTALEK--ASKGRTTIVVAHRL-STIRGADLIVTMKDGMVVEKGTHAELM 599
Cdd:PRK10070 191 AFSALDPLIRTEMQDELVKlqAKHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
376-600 |
5.64e-23 |
|
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: 98.90 E-value: 5.64e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 376 EFKNVSFSYPSrpsAKVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDIRAQNVrHYREQ--I 453
Cdd:COG0410 5 EVENLHAGYGG---IHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPP-HRIARlgI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 454 GVVRQEPVLFGT-TIGNNIKFGREGVGEKEMEQAAREAnAYDFimaFPKkfntlVGE----KGAQMSGGQKQRIAIARAL 528
Cdd:COG0410 81 GYVPEGRRIFPSlTVEENLLLGAYARRDRAEVRADLER-VYEL---FPR-----LKErrrqRAGTLSGGEQQMLAIGRAL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568980685 529 VRNPKILILDEATSALdteSESLVQT---ALEKASKGRTTIVV----AHRLSTIrgADLIVTMKDGMVVEKGTHAELMA 600
Cdd:COG0410 152 MSRPKLLLLDEPSLGL---APLIVEEifeIIRRLNREGVTILLveqnARFALEI--ADRAYVLERGRIVLEGTAAELLA 225
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
375-599 |
6.05e-23 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 104.34 E-value: 6.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 375 IEFKNVSFSYPSrpsAKVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDIRAQNVRHYREQ-I 453
Cdd:COG3845 6 LELRGITKRFGG---VVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDAIALgI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 454 GVVRQEPVLFGT-TIGNNIKFGREGVGEK--EMEQAAREanaydfIMAFPKKF------NTLVGekgaQMSGGQKQRIAI 524
Cdd:COG3845 83 GMVHQHFMLVPNlTVAENIVLGLEPTKGGrlDRKAARAR------IRELSERYgldvdpDAKVE----DLSVGEQQRVEI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 525 ARALVRNPKILILDEATSAL-DTESESLVQTALEKASKGRTTIVVAHRLSTIRG-ADLIVTMKDGMVVekGTH------- 595
Cdd:COG3845 153 LKALYRGARILILDEPTAVLtPQEADELFEILRRLAAEGKSIIFITHKLREVMAiADRVTVLRRGKVV--GTVdtaetse 230
|
....*..
gi 568980685 596 ---AELM 599
Cdd:COG3845 231 eelAELM 237
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1022-1212 |
6.58e-23 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 99.46 E-value: 6.58e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1022 LQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYD-----PMKGQVLLDGVDV---KELNVQwLRSQTAIVSQEPVLFN 1093
Cdd:PRK14239 21 LNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnpevTITGSIVYNGHNIyspRTDTVD-LRKEIGMVFQQPNPFP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1094 CSIAENIAYGdnSRMVPLEEiKEVADAANIHSFI------EGLPRKYNTLVGLrgvqlSGGQKQRLAIARALLRKPKILL 1167
Cdd:PRK14239 100 MSIYENVVYG--LRLKGIKD-KQVLDEAVEKSLKgasiwdEVKDRLHDSALGL-----SGGQQQRVCIARVLATSPKIIL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 568980685 1168 LDEATSALDNESEKVVQQALDKARRGKTCLVVAHrlsTIQNADMI 1212
Cdd:PRK14239 172 LDEPTSALDPISAGKIEETLLGLKDDYTMLLVTR---SMQQASRI 213
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
379-627 |
8.18e-23 |
|
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: 99.93 E-value: 8.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 379 NVSFSYPSRPSAKVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCItvdendiraqnvRHyREQIGVVRQ 458
Cdd:cd03291 39 NLFFSNLCLVGAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKI------------KH-SGRISFSSQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 459 EPVLFGTTIGNNIKFGREgVGEKEMEQAAREANAYDFIMAFPKKFNTLVGEKGAQMSGGQKQRIAIARALVRNPKILILD 538
Cdd:cd03291 106 FSWIMPGTIKENIIFGVS-YDEYRYKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLD 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 539 EATSALD--TESEsLVQTALEKASKGRTTIVVAHRLSTIRGADLIVTMKDGMVVEKGTHAELMAKQGLYYSLAMAQDikK 616
Cdd:cd03291 185 SPFGYLDvfTEKE-IFESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSLRPDFSSKLMGYD--T 261
|
250
....*....|.
gi 568980685 617 VDEQMESRTCS 627
Cdd:cd03291 262 FDQFSAERRNS 272
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
375-599 |
8.94e-23 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 99.08 E-value: 8.94e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 375 IEFKNVSFSYPSRPsakVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDIRAQNVRHYREQIG 454
Cdd:PRK13548 3 LEARNLSVRLGGRT---LLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 455 VVRQEPVL-FGTTIGNNIKFGRE--GVGEKEMEQAAREAnaydfiMAfpkkfntLVGEKG------AQMSGGQKQRIAIA 525
Cdd:PRK13548 80 VLPQHSSLsFPFTVEEVVAMGRAphGLSRAEDDALVAAA------LA-------QVDLAHlagrdyPQLSGGEQQRVQLA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 526 RALVR------NPKILILDEATSALD-TESESLVQTALEKASK-GRTTIVVAHRLS-TIRGADLIVTMKDGMVVEKGTHA 596
Cdd:PRK13548 147 RVLAQlwepdgPPRWLLLDEPTSALDlAHQHHVLRLARQLAHErGLAVIVVLHDLNlAARYADRIVLLHQGRLVADGTPA 226
|
...
gi 568980685 597 ELM 599
Cdd:PRK13548 227 EVL 229
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1019-1225 |
9.34e-23 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 100.81 E-value: 9.34e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1019 VPVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVKELN---VQWLRSQTAIVSQEPvlfncs 1095
Cdd:PRK11308 28 VKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADpeaQKLLRQKIQIVFQNP------ 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1096 iaeniaYGD-NSRM---VPLEE---IKEVADAANIHSFIEGLPRKyntlVGLRGVQ-------LSGGQKQRLAIARALLR 1161
Cdd:PRK11308 102 ------YGSlNPRKkvgQILEEpllINTSLSAAERREKALAMMAK----VGLRPEHydryphmFSGGQRQRIAIARALML 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568980685 1162 KPKILLLDEATSALDnesekVVQQA------LDKARRGKTCLV-VAHRLSTIQN-ADMIVVLQNGSIKEQGT 1225
Cdd:PRK11308 172 DPDVVVADEPVSALD-----VSVQAqvlnlmMDLQQELGLSYVfISHDLSVVEHiADEVMVMYLGRCVEKGT 238
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
391-611 |
1.03e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 100.70 E-value: 1.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 391 KVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDE----------------NDIRAQNVRHYREQIG 454
Cdd:PRK13631 40 VALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDiyigdkknnhelitnpYSKKIKNFKELRRRVS 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 455 VVRQEP--VLFGTTIGNNIKFGREGVGEKEMEqAAREANAYDFIMAFPKKFntlVGEKGAQMSGGQKQRIAIARALVRNP 532
Cdd:PRK13631 120 MVFQFPeyQLFKDTIEKDIMFGPVALGVKKSE-AKKLAKFYLNKMGLDDSY---LERSPFGLSGGQKRRVAIAGILAIQP 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 533 KILILDEATSALDTESES-LVQTALEKASKGRTTIVVAHRLSTI-RGADLIVTMKDGMVVEKGTHAELMAKQGLYYSLAM 610
Cdd:PRK13631 196 EILIFDEPTAGLDPKGEHeMMQLILDAKANNKTVFVITHTMEHVlEVADEVIVMDKGKILKTGTPYEIFTDQHIINSTSI 275
|
.
gi 568980685 611 A 611
Cdd:PRK13631 276 Q 276
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
372-587 |
1.84e-22 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 103.35 E-value: 1.84e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 372 EGNIEFKNVSFSypsRPSAKVL-KGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENdiraqnvrhyr 450
Cdd:COG4178 360 DGALALEDLTLR---TPDGRPLlEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPAG----------- 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 451 EQIGVVRQEPVLFGTTIGNNIKF--GREGVGEKEMEQAAREANAYDFImafpKKFNTlVGEKGAQMSGGQKQRIAIARAL 528
Cdd:COG4178 426 ARVLFLPQRPYLPLGTLREALLYpaTAEAFSDAELREALEAVGLGHLA----ERLDE-EADWDQVLSLGEQQRLAFARLL 500
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 568980685 529 VRNPKILILDEATSALDTESESLVQTALEKASKGRTTIVVAHRLSTIRGADLIVTMKDG 587
Cdd:COG4178 501 LHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHRSTLAAFHDRVLELTGD 559
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1021-1232 |
1.86e-22 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 97.90 E-value: 1.86e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1021 VLQNMSLSIEKGKTVAFVGSSGCGKST---CVQLLQRfydPMKGQVLLDGVDV---KELNVQW-----LRSQTAIVSQEP 1089
Cdd:PRK11264 18 VLHGIDLEVKPGEVVAIIGPSGSGKTTllrCINLLEQ---PEAGTIRVGDITIdtaRSLSQQKglirqLRQHVGFVFQNF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1090 VLF-NCSIAENIAYGdnsrmvPLEEIKEVADAAnihsfiEGLPRKYNTLVGLRGVQ------LSGGQKQRLAIARALLRK 1162
Cdd:PRK11264 95 NLFpHRTVLENIIEG------PVIVKGEPKEEA------TARARELLAKVGLAGKEtsyprrLSGGQQQRVAIARALAMR 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568980685 1163 PKILLLDEATSALDNEsekVVQQALDK----ARRGKTCLVVAHRLSTIQN-ADMIVVLQNGSIKEQGTHQELLRN 1232
Cdd:PRK11264 163 PEVILFDEPTSALDPE---LVGEVLNTirqlAQEKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKALFAD 234
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
392-587 |
1.90e-22 |
|
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: 97.50 E-value: 1.90e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 392 VLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDEN----DI-RAQ-----NVRhyREQIGVVRQ--- 458
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDggwvDLaQASpreilALR--RRTIGYVSQflr 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 459 ------------EPVLfgttignnikfgREGVGEKEMEQAAREANAYdfimafpkkFNtlVGEK-----GAQMSGGQKQR 521
Cdd:COG4778 104 viprvsaldvvaEPLL------------ERGVDREEARARARELLAR---------LN--LPERlwdlpPATFSGGEQQR 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568980685 522 IAIARALVRNPKILILDEATSALDTESESLVQTALEKASKGRTTIV-VAHRLSTIRG-ADLIVTMKDG 587
Cdd:COG4778 161 VNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIgIFHDEEVREAvADRVVDVTPF 228
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
375-570 |
2.04e-22 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 100.29 E-value: 2.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 375 IEFKNVSFSYPSRPsakVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDIRAQnVRHYREQIG 454
Cdd:PRK13536 42 IDLAGVSKSYGDKA---VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPAR-ARLARARIG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 455 VVRQEPVL---FgTTIGNNIKFGRE-GVGEKEMEQAAreANAYDFiMAFPKKFNTLVgekgAQMSGGQKQRIAIARALVR 530
Cdd:PRK13536 118 VVPQFDNLdleF-TVRENLLVFGRYfGMSTREIEAVI--PSLLEF-ARLESKADARV----SDLSGGMKRRLTLARALIN 189
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 568980685 531 NPKILILDEATSALDTESESLVQTALEK-ASKGRTTIVVAH 570
Cdd:PRK13536 190 DPQLLILDEPTTGLDPHARHLIWERLRSlLARGKTILLTTH 230
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1004-1234 |
2.44e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 98.75 E-value: 2.44e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1004 LEFREVSFVYPcrPEVPV----LQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVK----ELNV 1075
Cdd:PRK13641 3 IKFENVDYIYS--PGTPMekkgLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgNKNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1076 QWLRSQTAIVSQ--EPVLFNCSIAENIAYG--------DNSRMVPLEEIKEVadaanihsfieGLPrkyNTLVGLRGVQL 1145
Cdd:PRK13641 81 KKLRKKVSLVFQfpEAQLFENTVLKDVEFGpknfgfseDEAKEKALKWLKKV-----------GLS---EDLISKSPFEL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1146 SGGQKQRLAIARALLRKPKILLLDEATSALDNESEK-VVQQALDKARRGKTCLVVAHRLSTI-QNADMIVVLQNGSIKEQ 1223
Cdd:PRK13641 147 SGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKeMMQLFKDYQKAGHTVILVTHNMDDVaEYADDVLVLEHGKLIKH 226
|
250
....*....|.
gi 568980685 1224 GTHQELLRNGD 1234
Cdd:PRK13641 227 ASPKEIFSDKE 237
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
397-614 |
2.48e-22 |
|
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: 100.18 E-value: 2.48e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 397 NLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDE----NDIRAQNVRHYREQIGVVRQEPVLFGT-TIGNNI 471
Cdd:COG4148 19 DFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGevlqDSARGIFLPPHRRRIGYVFQEARLFPHlSVRGNL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 472 KFGregvgekeMEQAAREANAYDF--------ImafpkkfNTLVGEKGAQMSGGQKQRIAIARALVRNPKILILDEATSA 543
Cdd:COG4148 99 LYG--------RKRAPRAERRISFdevvellgI-------GHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAA 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568980685 544 LDTESESLVQTALEK-ASKGRTTIV-VAHRLSTI-RGADLIVTMKDGMVVEKGTHAELMAKQGLyYSLAMAQDI 614
Cdd:COG4148 164 LDLARKAEILPYLERlRDELDIPILyVSHSLDEVaRLADHVVLLEQGRVVASGPLAEVLSRPDL-LPLAGGEEA 236
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
1009-1229 |
2.54e-22 |
|
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: 98.39 E-value: 2.54e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1009 VSFVYPCRPEVPVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVKELNVQWLRSQTaivsqe 1088
Cdd:cd03291 40 LFFSNLCLVGAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRISFSSQFSWIMPGT------ 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1089 pvlfncsIAENIAYG---DNSRMvpleeiKEVADAANIHSFIEGLPRKYNTLVGLRGVQLSGGQKQRLAIARALLRKPKI 1165
Cdd:cd03291 114 -------IKENIIFGvsyDEYRY------KSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADL 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568980685 1166 LLLDEATSALDNESEK-VVQQALDKARRGKTCLVVAHRLSTIQNADMIVVLQNGSIKEQGTHQEL 1229
Cdd:cd03291 181 YLLDSPFGYLDVFTEKeIFESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSEL 245
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
376-547 |
2.65e-22 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 96.40 E-value: 2.65e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 376 EFKNVSFSYPSRPsakVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPE---DGCITVDENDIRAQNVrhYREQ 452
Cdd:COG4136 3 SLENLTITLGGRP---LLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTALPA--EQRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 453 IGVVRQEPVLFG-TTIGNNIKFG-REGVGEKE----MEQAAREANAYDFIMAFPkkfntlvgekgAQMSGGQKQRIAIAR 526
Cdd:COG4136 78 IGILFQDDLLFPhLSVGENLAFAlPPTIGRAQrrarVEQALEEAGLAGFADRDP-----------ATLSGGQRARVALLR 146
|
170 180
....*....|....*....|.
gi 568980685 527 ALVRNPKILILDEATSALDTE 547
Cdd:COG4136 147 ALLAEPRALLLDEPFSKLDAA 167
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
391-600 |
2.83e-22 |
|
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: 97.80 E-value: 2.83e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 391 KVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDIRAQNVrHYREQIGVVR--QEPVLFG---- 464
Cdd:COG0411 18 VAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPP-HRIARLGIARtfQNPRLFPeltv 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 465 --------------TTIGNNIKFGREGVGEKEMEQAAREanaydfIMAFPK---KFNTLVGEkgaqMSGGQKQRIAIARA 527
Cdd:COG0411 97 lenvlvaaharlgrGLLAALLRLPRARREEREARERAEE------LLERVGladRADEPAGN----LSYGQQRRLEIARA 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568980685 528 LVRNPKILILDEATSAL-DTESESLVQTALE-KASKGRTTIVVAHRLSTIRG-ADLIVTMKDGMVVEKGTHAELMA 600
Cdd:COG0411 167 LATEPKLLLLDEPAAGLnPEETEELAELIRRlRDERGITILLIEHDMDLVMGlADRIVVLDFGRVIAEGTPAEVRA 242
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1021-1232 |
3.66e-22 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 97.35 E-value: 3.66e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1021 VLQNMSLSIEKGKTVAFVGSSGCGKST---CVQLLQRfydPMKGQVLLDGVDVK-------ELNV------QWLRSQTAI 1084
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTflrCINFLEK---PSEGSIVVNGQTINlvrdkdgQLKVadknqlRLLRTRLTM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1085 VSQEpvlFNCSiaeniaygdnSRMVPLEEIKEVADAANIHSFIEGLPR--KYNTLVGLRG-------VQLSGGQKQRLAI 1155
Cdd:PRK10619 97 VFQH---FNLW----------SHMTVLENVMEAPIQVLGLSKQEARERavKYLAKVGIDEraqgkypVHLSGGQQQRVSI 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568980685 1156 ARALLRKPKILLLDEATSALDNESEKVVQQALDK-ARRGKTCLVVAHRLSTIQN-ADMIVVLQNGSIKEQGTHQELLRN 1232
Cdd:PRK10619 164 ARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQlAEEGKTMVVVTHEMGFARHvSSHVIFLHQGKIEEEGAPEQLFGN 242
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
383-598 |
4.28e-22 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 99.01 E-value: 4.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 383 SYPSRPSA--KVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDIRAQN---VRHYREQIGVVR 457
Cdd:PRK15079 25 QWFWQPPKtlKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKddeWRAVRSDIQMIF 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 458 QEPVLF---GTTIGNNI---------KFGREGVGEKEMEQAAREANAYDFIMAFPKKFntlvgekgaqmSGGQKQRIAIA 525
Cdd:PRK15079 105 QDPLASlnpRMTIGEIIaeplrtyhpKLSRQEVKDRVKAMMLKVGLLPNLINRYPHEF-----------SGGQCQRIGIA 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568980685 526 RALVRNPKILILDEATSALDTESESLVQTALEKASK--GRTTIVVAHRLSTIRG-ADLIVTMKDGMVVEKGTHAEL 598
Cdd:PRK15079 174 RALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQRemGLSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEV 249
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
388-588 |
4.31e-22 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 96.25 E-value: 4.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 388 PSAKVLKGLNLKIKAGETVALVGPSGSGKST----TVQLLQRLYDPEDGCITVDENDIRAQNVRHYREQIGVVRQEPVLF 463
Cdd:cd03290 12 SGLATLSNINIRIPTGQLTMIVGQVGCGKSSlllaILGEMQTLEGKVHWSNKNESEPSFEATRSRNRYSVAYAAQKPWLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 464 GTTIGNNIKFGREGvgEKEMEQAAREANAYD-FIMAFPKKFNTLVGEKGAQMSGGQKQRIAIARALVRNPKILILDEATS 542
Cdd:cd03290 92 NATVEENITFGSPF--NKQRYKAVTDACSLQpDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFS 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 568980685 543 ALDTE-SESLVQTALEK--ASKGRTTIVVAHRLSTIRGADLIVTMKDGM 588
Cdd:cd03290 170 ALDIHlSDHLMQEGILKflQDDKRTLVLVTHKLQYLPHADWIIAMKDGS 218
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
1021-1229 |
4.95e-22 |
|
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: 96.05 E-value: 4.95e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1021 VLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVKELNVQWL-RSQTAIVSQEPVLF-NCSIAE 1098
Cdd:TIGR03410 15 ILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERaRAGIAYVPQGREIFpRLTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1099 NI-----AYGDNSRMVPlEEIKEVADAanIHSFiegLPRkyntlvglRGVQLSGGQKQRLAIARALLRKPKILLLDEATS 1173
Cdd:TIGR03410 95 NLltglaALPRRSRKIP-DEIYELFPV--LKEM---LGR--------RGGDLSGGQQQQLAIARALVTRPKLLLLDEPTE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 568980685 1174 ALDNESEKVVQQALDK--ARRGKTCLVVAHRLS-TIQNADMIVVLQNGSIKEQGTHQEL 1229
Cdd:TIGR03410 161 GIQPSIIKDIGRVIRRlrAEGGMAILLVEQYLDfARELADRYYVMERGRVVASGAGDEL 219
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1008-1201 |
5.20e-22 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 96.69 E-value: 5.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1008 EVSFVYPCRPEVPVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVKELNvqwlrSQTAIVSQ 1087
Cdd:PRK11248 3 QISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPG-----AERGVVFQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1088 -EPVLFNCSIAENIAYGDNSRMVPLEEIKEVAdaanihsfieglpRKYNTLVGLRGV------QLSGGQKQRLAIARALL 1160
Cdd:PRK11248 78 nEGLLPWRNVQDNVAFGLQLAGVEKMQRLEIA-------------HQMLKKVGLEGAekryiwQLSGGQRQRVGIARALA 144
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 568980685 1161 RKPKILLLDEATSALDNESEKVVQQALDK--ARRGKTCLVVAH 1201
Cdd:PRK11248 145 ANPQLLLLDEPFGALDAFTREQMQTLLLKlwQETGKQVLLITH 187
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
375-604 |
5.70e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 97.18 E-value: 5.70e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 375 IEFKNVSFSYpsRPSAKVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDIRAQNVRHYREQIG 454
Cdd:PRK13652 4 IETRDLCYSY--SGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 455 VVRQEP--VLFGTTIGNNIKFGREGVGEKEMEQAAREANAYDFImafpkKFNTLVGEKGAQMSGGQKQRIAIARALVRNP 532
Cdd:PRK13652 82 LVFQNPddQIFSPTVEQDIAFGPINLGLDEETVAHRVSSALHML-----GLEELRDRVPHHLSGGEKKRVAIAGVIAMEP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568980685 533 KILILDEATSALDTESESLVQTALEKASK--GRTTIVVAHRLSTI-RGADLIVTMKDGMVVEKGTHAELMAKQGL 604
Cdd:PRK13652 157 QVLVLDEPTAGLDPQGVKELIDFLNDLPEtyGMTVIFSTHQLDLVpEMADYIYVMDKGRIVAYGTVEEIFLQPDL 231
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
1016-1224 |
6.70e-22 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 95.80 E-value: 6.70e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1016 RPEVPVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLL---QRFYDPMKGQVLLDGvdvKELNVQWLRSQTAIVSQEPVLF 1092
Cdd:cd03234 17 NKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAIsgrVEGGGTTSGQILFNG---QPRKPDQFQKCVAYVRQDDILL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1093 NC-SIAENIAYGDNSRM------------VPLEEIKEVADAANIHSFIEGLprkyntlvglrgvqlSGGQKQRLAIARAL 1159
Cdd:cd03234 94 PGlTVRETLTYTAILRLprkssdairkkrVEDVLLRDLALTRIGGNLVKGI---------------SGGERRRVSIAVQL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568980685 1160 LRKPKILLLDEATSALDNESE-KVVQQALDKARRGKTCLVVAH--RLSTIQNADMIVVLQNGSIKEQG 1224
Cdd:cd03234 159 LWDPKVLILDEPTSGLDSFTAlNLVSTLSQLARRNRIVILTIHqpRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
391-600 |
6.72e-22 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 96.58 E-value: 6.72e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 391 KVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDIR-------------AQNVRHYREQIGVVR 457
Cdd:PRK10619 19 EVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlkvadKNQLRLLRTRLTMVF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 458 QEPVL--FGTTIGNNIKFGREGVGEKEMEqaARE-ANAYDFIMAFPKKFNtlvGEKGAQMSGGQKQRIAIARALVRNPKI 534
Cdd:PRK10619 99 QHFNLwsHMTVLENVMEAPIQVLGLSKQE--ARErAVKYLAKVGIDERAQ---GKYPVHLSGGQQQRVSIARALAMEPEV 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568980685 535 LILDEATSALDTESESLVQTALEK-ASKGRTTIVVAHRLSTIRG-ADLIVTMKDGMVVEKGTHAELMA 600
Cdd:PRK10619 174 LLFDEPTSALDPELVGEVLRIMQQlAEEGKTMVVVTHEMGFARHvSSHVIFLHQGKIEEEGAPEQLFG 241
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1018-1222 |
6.83e-22 |
|
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: 95.96 E-value: 6.83e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1018 EVPVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVKELN----VQWLRSQTAIVSQ-EPVLF 1092
Cdd:COG4181 24 ELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDedarARLRARHVGFVFQsFQLLP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1093 NCSIAENIaygdnsrMVPLEeIKEVADAANIHSfiEGLPRkyntlVGL------RGVQLSGGQKQRLAIARALLRKPKIL 1166
Cdd:COG4181 104 TLTALENV-------MLPLE-LAGRRDARARAR--ALLER-----VGLghrldhYPAQLSGGEQQRVALARAFATEPAIL 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 568980685 1167 LLDEATSALDNESEKVVQQALD--KARRGKTCLVVAHRLSTIQNADMIVVLQNGSIKE 1222
Cdd:COG4181 169 FADEPTGNLDAATGEQIIDLLFelNRERGTTLVLVTHDPALAARCDRVLRLRAGRLVE 226
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
701-938 |
6.96e-22 |
|
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: 97.58 E-value: 6.96e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 701 IFGKLVTMF---EDKNKATLKQDAELYSMMLVVLGIVALVTYLMQGLFyGRAEENLAMRLRHSAFKAMLYQDMAWYDDke 777
Cdd:cd18573 18 AIGKLIDVAskeSGDIEIFGLSLKTFALALLGVFVVGAAANFGRVYLL-RIAGERIVARLRKRLFKSILRQDAAFFDK-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 778 NNTGALTTTLAVDVAQIQGAATSRLGIVTQDVSNMSLSILISFIYGWEMTLLILSFAPVLAVTGMIQTAAMAGFANRDKQ 857
Cdd:cd18573 95 NKTGELVSRLSSDTSVVGKSLTQNLSDGLRSLVSGVGGIGMMLYISPKLTLVMLLVVPPIAVGAVFYGRYVRKLSKQVQD 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 858 ALKRAGKIATEAVENIRTVVSLTRERAFEQMYEETLQTQHRNALKRAHITGCCYAVSHAFVHFAHAAGFRFGAYLIQAGR 937
Cdd:cd18573 175 ALADATKVAEERLSNIRTVRAFAAERKEVERYAKKVDEVFDLAKKEALASGLFFGSTGFSGNLSLLSVLYYGGSLVASGE 254
|
.
gi 568980685 938 M 938
Cdd:cd18573 255 L 255
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1020-1230 |
1.16e-21 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 95.85 E-value: 1.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1020 PVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVKELNVQWLRSQTAIVSQEPVL-FNCSIAE 1098
Cdd:PRK11231 16 RILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHHLTpEGITVRE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1099 NIAYGdNSRMVPLEEIKEVADAANIHSFIEGLprKYNTLVGLRGVQLSGGQKQRLAIARALLRKPKILLLDEATSALD-- 1176
Cdd:PRK11231 96 LVAYG-RSPWLSLWGRLSAEDNARVNQAMEQT--RINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDin 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 568980685 1177 --NESEKVVQQALDKarrGKTCLVVAHRLS-TIQNADMIVVLQNGSIKEQGTHQELL 1230
Cdd:PRK11231 173 hqVELMRLMRELNTQ---GKTVVTVLHDLNqASRYCDHLVVLANGHVMAQGTPEEVM 226
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
396-606 |
1.29e-21 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 97.88 E-value: 1.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 396 LNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDE---NDIRAQ-NVRHYREQIGVVRQEPVLFG-TTIGNN 470
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGrtlFDSRKGiFLPPEKRRIGYVFQEARLFPhLSVRGN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 471 IKFGREGVGEKEmeQAAREANAYDFIMAFPkkfntLVGEKGAQMSGGQKQRIAIARALVRNPKILILDEATSALDTESES 550
Cdd:TIGR02142 96 LRYGMKRARPSE--RRISFERVIELLGIGH-----LLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKY 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 568980685 551 LVQTALEK--ASKGRTTIVVAHRLSTI-RGADLIVTMKDGMVVEKGTHAELMAKQGLYY 606
Cdd:TIGR02142 169 EILPYLERlhAEFGIPILYVSHSLQEVlRLADRVVVLEDGRVAAAGPIAEVWASPDLPW 227
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
392-593 |
1.72e-21 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 100.16 E-value: 1.72e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 392 VLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEdGCITVDENDIRAQNVRH---YREQIGVVRQEPVLFGTTIG 468
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINSQ-GEIWFDGQPLHNLNRRQllpVRHRIQVVFQDPNSSLNPRL 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 469 NNIKFGREG--VGEKEMEQAAREANAYDFIMA----------FPKKFntlvgekgaqmSGGQKQRIAIARALVRNPKILI 536
Cdd:PRK15134 380 NVLQIIEEGlrVHQPTLSAAQREQQVIAVMEEvgldpetrhrYPAEF-----------SGGQRQRIAIARALILKPSLII 448
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 537 LDEATSALDTESESLVQTALEKASKGR--TTIVVAHRLSTIRG-ADLIVTMKDGMVVEKG 593
Cdd:PRK15134 449 LDEPTSSLDKTVQAQILALLKSLQQKHqlAYLFISHDLHVVRAlCHQVIVLRQGEVVEQG 508
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
37-322 |
1.76e-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: 96.34 E-value: 1.76e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 37 MTLGILASMINGATVPLMSLVLGEISDHLINgclvqtnrtkyqncsqtqEKLNEDIIVLTLYYIGIGAAALIFGYVQISF 116
Cdd:cd18552 1 LALAILGMILVAATTAALAWLLKPLLDDIFV------------------EKDLEALLLVPLAIIGLFLLRGLASYLQTYL 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 117 WVITAARQTTRIRKQFFHSILAQDISWFDGSDICELNTRMTGDINKLCDGIGDKIPLMFQNisGFS-IGLVISLI-KSWK 194
Cdd:cd18552 63 MAYVGQRVVRDLRNDLFDKLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVRD--PLTvIGLLGVLFyLDWK 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 195 LSLVVLSTSPLIMASSALCSRMIISLTSKELDAYSKAGAVAEEALSSIQTVTAFGAQEKEIQRYTQHLKDAKDAGIKRAT 274
Cdd:cd18552 141 LTLIALVVLPLAALPIRRIGKRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIAR 220
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 568980685 275 ASKLSLGAVYFFMNGAYGLAFWYGTSLIFGGEpgYTIGTilavFFSVI 322
Cdd:cd18552 221 ARALSSPLMELLGAIAIALVLWYGGYQVISGE--LTPGE----FISFI 262
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
1004-1236 |
3.37e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 95.92 E-value: 3.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1004 LEFREVSFVY-PCRP-EVPVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVKEL-------- 1073
Cdd:PRK13651 3 IKVKNIVKIFnKKLPtELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKkktkekek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1074 ----------------NVQWLRSQTAIVSQ--EPVLFNCSIAENIAYGDNSRMVPLEEIKEVAdaanihsfieglpRKYN 1135
Cdd:PRK13651 83 vleklviqktrfkkikKIKEIRRRVGVVFQfaEYQLFEQTIEKDIIFGPVSMGVSKEEAKKRA-------------AKYI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1136 TLVGL-------RGVQLSGGQKQRLAIARALLRKPKILLLDEATSALDNESEKVVQQALDKA-RRGKTCLVVAHRL-STI 1206
Cdd:PRK13651 150 ELVGLdesylqrSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLnKQGKTIILVTHDLdNVL 229
|
250 260 270
....*....|....*....|....*....|
gi 568980685 1207 QNADMIVVLQNGSIkeqgthqelLRNGDTY 1236
Cdd:PRK13651 230 EWTKRTIFFKDGKI---------IKDGDTY 250
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
375-598 |
3.40e-21 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 97.21 E-value: 3.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 375 IEFKNVSFSYPSRPSakvLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDIraQNVRHYREQIG 454
Cdd:PRK11607 20 LEIRNLTKSFDGQHA---VDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDL--SHVPPYQRPIN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 455 VVRQEPVLF-GTTIGNNIKFG--REGVGEKEMEQAAREANAYDFIMAFPKKfntlvgeKGAQMSGGQKQRIAIARALVRN 531
Cdd:PRK11607 95 MMFQSYALFpHMTVEQNIAFGlkQDKLPKAEIASRVNEMLGLVHMQEFAKR-------KPHQLSGGQRQRVALARSLAKR 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568980685 532 PKILILDEATSALDTESESLVQTA----LEKAskGRTTIVVAH-RLSTIRGADLIVTMKDGMVVEKGTHAEL 598
Cdd:PRK11607 168 PKLLLLDEPMGALDKKLRDRMQLEvvdiLERV--GVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
397-600 |
3.44e-21 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 93.88 E-value: 3.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 397 NLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDIRAQNVRhyREQIGVVRQEPVLFG-TTIGNNIKFG- 474
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS--RRPVSMLFQENNLFShLTVAQNIGLGl 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 475 ----REGVGEKE-MEQAAREANAYDFIMAFPkkfntlvgekgAQMSGGQKQRIAIARALVRNPKILILDEATSALD---- 545
Cdd:PRK10771 97 npglKLNAAQREkLHAIARQMGIEDLLARLP-----------GQLSGGQRQRVALARCLVREQPILLLDEPFSALDpalr 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 568980685 546 TESESLVQTALEKasKGRTTIVVAHRLS-TIRGADLIVTMKDGMVVEKGTHAELMA 600
Cdd:PRK10771 166 QEMLTLVSQVCQE--RQLTLLMVSHSLEdAARIAPRSLVVADGRIAWDGPTDELLS 219
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
393-572 |
3.67e-21 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 94.46 E-value: 3.67e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 393 LKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYD-----PEDGCITVDENDIRAQNVR--HYREQIGVVRQEPVLFGT 465
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDlipgfRVEGKVTFHGKNLYAPDVDpvEVRRRIGMVFQKPNPFPK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 466 TIGNNIKFGREGVGEKE-----MEQAAREANAYDFImafPKKFNtlvgEKGAQMSGGQKQRIAIARALVRNPKILILDEA 540
Cdd:PRK14243 106 SIYDNIAYGARINGYKGdmdelVERSLRQAALWDEV---KDKLK----QSGLSLSGGQQQRLCIARAIAVQPEVILMDEP 178
|
170 180 190
....*....|....*....|....*....|..
gi 568980685 541 TSALDTESESLVQTALEKASKGRTTIVVAHRL 572
Cdd:PRK14243 179 CSALDPISTLRIEELMHELKEQYTIIIVTHNM 210
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
379-600 |
4.68e-21 |
|
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: 93.38 E-value: 4.68e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 379 NVSFSYPSRpsaKVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDIRAQNVrHYREQIGV--V 456
Cdd:cd03218 5 NLSKRYGKR---KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPM-HKRARLGIgyL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 457 RQEPVLF-GTTIGNNIKFGREGVGEKEMEQAAReanaydfIMAFPKKFN--TLVGEKGAQMSGGQKQRIAIARALVRNPK 533
Cdd:cd03218 81 PQEASIFrKLTVEENILAVLEIRGLSKKEREEK-------LEELLEEFHitHLRKSKASSLSGGERRRVEIARALATNPK 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568980685 534 ILILDEATSALDTESESLVQTALEK-ASKG----------RTTIVVAHRLSTIRgadlivtmkDGMVVEKGTHAELMA 600
Cdd:cd03218 154 FLLLDEPFAGVDPIAVQDIQKIIKIlKDRGigvlitdhnvRETLSITDRAYIIY---------EGKVLAEGTPEEIAA 222
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1008-1230 |
5.51e-21 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 96.83 E-value: 5.51e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1008 EVSFVYPCRPEVPVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVKELNVQWLRSQTAIVSQ 1087
Cdd:PRK09536 5 DVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1088 EPVL-FNCSIAENIAYGDN---SRMVPLEEikevADAANIHSFIEglpRKYNTLVGLRGV-QLSGGQKQRLAIARALLRK 1162
Cdd:PRK09536 85 DTSLsFEFDVRQVVEMGRTphrSRFDTWTE----TDRAAVERAME---RTGVAQFADRPVtSLSGGERQRVLLARALAQA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1163 PKILLLDEATSALD-NESEKVVQQALDKARRGKTCLVVAHRLS-TIQNADMIVVLQNGSIKEQGTHQELL 1230
Cdd:PRK09536 158 TPVLLLDEPTASLDiNHQVRTLELVRRLVDDGKTAVAAIHDLDlAARYCDELVLLADGRVRAAGPPADVL 227
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
391-593 |
5.68e-21 |
|
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: 92.20 E-value: 5.68e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 391 KVLKGLNLKIKAGETVALVGPSGSGKSTtvqLLQRL-----YDPEDGCITVDENDI-------RAqnvrhyREQIGVVRQ 458
Cdd:cd03217 14 EILKGVNLTIKKGEVHALMGPNGSGKST---LAKTImghpkYEVTEGEILFKGEDItdlppeeRA------RLGIFLAFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 459 EPVLF-GTTIGNNIKFGREGvgekemeqaareanaydfimafpkkfntlvgekgaqMSGGQKQRIAIARALVRNPKILIL 537
Cdd:cd03217 85 YPPEIpGVKNADFLRYVNEG------------------------------------FSGGEKKRNEILQLLLLEPDLAIL 128
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 538 DEATSALDTESESLVQTALEK-ASKGRTTIVVAHR---LSTIRgADLIVTMKDGMVVEKG 593
Cdd:cd03217 129 DEPDSGLDIDALRLVAEVINKlREEGKSVLIITHYqrlLDYIK-PDRVHVLYDGRIVKSG 187
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
1004-1217 |
6.51e-21 |
|
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: 91.06 E-value: 6.51e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1004 LEFREVSFVYPcrPEVPVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGvdvkelnvqwlRSQTA 1083
Cdd:cd03223 1 IELENLSLATP--DGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPE-----------GEDLL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1084 IVSQEPVLFNCSIAENIAYgdnsrmvPLEEIkevadaanihsfieglprkyntlvglrgvqLSGGQKQRLAIARALLRKP 1163
Cdd:cd03223 68 FLPQRPYLPLGTLREQLIY-------PWDDV------------------------------LSGGEQQRLAFARLLLHKP 110
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 568980685 1164 KILLLDEATSALDNESEKVVQQALDKarRGKTCLVVAHRLSTIQNADMIVVLQN 1217
Cdd:cd03223 111 KFVFLDEATSALDEESEDRLYQLLKE--LGITVISVGHRPSLWKFHDRVLDLDG 162
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
375-602 |
7.71e-21 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 94.87 E-value: 7.71e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 375 IEFKNVSFSYPSRpsaKVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDIrAQNVRHYREQIG 454
Cdd:PRK13537 8 IDFRNVEKRYGDK---LVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPV-PSRARHARQRVG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 455 VVRQ----EPVLfgTTIGNNIKFGREgVGEKEMEQAAREANAYDFiMAFPKKFNTLVGEkgaqMSGGQKQRIAIARALVR 530
Cdd:PRK13537 84 VVPQfdnlDPDF--TVRENLLVFGRY-FGLSAAAARALVPPLLEF-AKLENKADAKVGE----LSGGMKRRLTLARALVN 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568980685 531 NPKILILDEATSALDTESESLVQTALEK-ASKGRTTIVVAHRLSTI-RGADLIVTMKDGMVVEKGTHAELMAKQ 602
Cdd:PRK13537 156 DPDVLVLDEPTTGLDPQARHLMWERLRSlLARGKTILLTTHFMEEAeRLCDRLCVIEEGRKIAEGAPHALIESE 229
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
383-584 |
7.79e-21 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 91.53 E-value: 7.79e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 383 SYPSRPsakVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDIRAQNVRHYReqigVVRQEPVl 462
Cdd:NF040873 1 GYGGRP---VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQRSE----VPDSLPL- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 463 fgtTIGNNIKFGREG-VGEKEMEQAAREANAYDFIMAFpkKFNTLVGEKGAQMSGGQKQRIAIARALVRNPKILILDEAT 541
Cdd:NF040873 73 ---TVRDLVAMGRWArRGLWRRLTRDDRAAVDDALERV--GLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPT 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 568980685 542 SALDTESESLVQTAL-EKASKGRTTIVVAHRLSTIRGADLIVTM 584
Cdd:NF040873 148 TGLDAESRERIIALLaEEHARGATVVVVTHDLELVRRADPCVLL 191
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1016-1224 |
8.23e-21 |
|
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: 92.43 E-value: 8.23e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1016 RPEVPVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVKElNVQWLRSQTAIVSQEPVLFN-C 1094
Cdd:cd03266 15 KKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-EPAEARRRLGFVSDSTGLYDrL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1095 SIAENIAY--------GDNSrmvpLEEIKEVADAANIHSFIEglprkyntlvgLRGVQLSGGQKQRLAIARALLRKPKIL 1166
Cdd:cd03266 94 TARENLEYfaglyglkGDEL----TARLEELADRLGMEELLD-----------RRVGGFSTGMRQKVAIARALVHDPPVL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1167 LLDEATSALDNESEKVVQQALDKARR-GKTCLVVAHRLSTIQN-ADMIVVLQNGSIKEQG 1224
Cdd:cd03266 159 LLDEPTTGLDVMATRALREFIRQLRAlGKCILFSTHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1018-1236 |
9.05e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 94.92 E-value: 9.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1018 EVPVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDV----------------KELNVQWLRSQ 1081
Cdd:PRK13631 38 ELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIgdkknnhelitnpyskKIKNFKELRRR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1082 TAIVSQEP--VLFNCSIAENIAYGDNSRMVPLEEIKEVADaanihSFIEGLPRKYNTLvGLRGVQLSGGQKQRLAIARAL 1159
Cdd:PRK13631 118 VSMVFQFPeyQLFKDTIEKDIMFGPVALGVKKSEAKKLAK-----FYLNKMGLDDSYL-ERSPFGLSGGQKRRVAIAGIL 191
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568980685 1160 LRKPKILLLDEATSALDNESEK-VVQQALDKARRGKTCLVVAHRLSTI-QNADMIVVLQNGSIKEQGTHQELLRNGDTY 1236
Cdd:PRK13631 192 AIQPEILIFDEPTAGLDPKGEHeMMQLILDAKANNKTVFVITHTMEHVlEVADEVIVMDKGKILKTGTPYEIFTDQHII 270
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1018-1229 |
9.26e-21 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 95.87 E-value: 9.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1018 EVPVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVKElnVQWLRSQTAIVSQEPVLF-NCSI 1096
Cdd:PRK11000 15 DVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMND--VPPAERGVGMVFQSYALYpHLSV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1097 AENIAYGDNSRMVPLEEI-KEVADAANIHSFIEGLPRKYNTLvglrgvqlSGGQKQRLAIARALLRKPKILLLDEATSAL 1175
Cdd:PRK11000 93 AENMSFGLKLAGAKKEEInQRVNQVAEVLQLAHLLDRKPKAL--------SGGQRQRVAIGRTLVAEPSVFLLDEPLSNL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 568980685 1176 DneSEKVVQQALDKA----RRGKTCLVVAH-RLSTIQNADMIVVLQNGSIKEQGTHQEL 1229
Cdd:PRK11000 165 D--AALRVQMRIEISrlhkRLGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
375-598 |
1.25e-20 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 94.02 E-value: 1.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 375 IEFKNVSFSYPSRpsaKVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDIRAQNVRHyreqIG 454
Cdd:COG4152 2 LELKGLTKRFGDK---TAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRRR----IG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 455 VVRQEPVLF-GTTIGNNIK-FGR-EGVGEKEmeqaAREAnaydfIMAFPKKFNtlVGEKGA----QMSGGQKQRIAIARA 527
Cdd:COG4152 75 YLPEERGLYpKMKVGEQLVyLARlKGLSKAE----AKRR-----ADEWLERLG--LGDRANkkveELSKGNQQKVQLIAA 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568980685 528 LVRNPKILILDEATSALDTES-ESLVQTALEKASKGRTTIVVAHRLSTI-RGADLIVTMKDGMVVEKGTHAEL 598
Cdd:COG4152 144 LLHDPELLILDEPFSGLDPVNvELLKDVIRELAAKGTTVIFSSHQMELVeELCDRIVIINKGRKVLSGSVDEI 216
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
375-571 |
1.27e-20 |
|
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: 90.29 E-value: 1.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 375 IEFKNVSFSYPSrpSAKVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCItvdendiraqnVRHYREQIG 454
Cdd:cd03223 1 IELENLSLATPD--GRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI-----------GMPEGEDLL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 455 VVRQEPVLfgtTIGNnikfgregvgekemeqaAREANAYDFimafpkkfntlvgekGAQMSGGQKQRIAIARALVRNPKI 534
Cdd:cd03223 68 FLPQRPYL---PLGT-----------------LREQLIYPW---------------DDVLSGGEQQRLAFARLLLHKPKF 112
|
170 180 190
....*....|....*....|....*....|....*...
gi 568980685 535 LILDEATSALDTESESLVQTALEKASkgrTTIV-VAHR 571
Cdd:cd03223 113 VFLDEATSALDEESEDRLYQLLKELG---ITVIsVGHR 147
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
105-306 |
1.42e-20 |
|
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: 93.76 E-value: 1.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 105 AALIFGYvqISFWVITAARQTTRIRKQFFHSILAQDISWFDGSDICELNTRMTGDIN------KLCDGIGDKIplMFQni 178
Cdd:cd18574 56 SLLTFAY--ISLLSVVGERVAARLRNDLFSSLLRQDIAFFDTHRTGELVNRLTADVQefkssfKQCVSQGLRS--VTQ-- 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 179 sgfSIGLVISLIK-SWKLSLVVLSTSPLIMASSALCSRMIISLTSKELDAYSKAGAVAEEALSSIQTVTAFGAQEKEIQR 257
Cdd:cd18574 130 ---TVGCVVSLYLiSPKLTLLLLVIVPVVVLVGTLYGSFLRKLSRRAQAQVAKATGVADEALGNIRTVRAFAMEDRELEL 206
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 568980685 258 YTQHLKDAkdagikRATASKLSLG-AVY-----FFMNGAYGLAFWYGTSLIFGGE 306
Cdd:cd18574 207 YEEEVEKA------AKLNEKLGLGiGIFqglsnLALNGIVLGVLYYGGSLVSRGE 255
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
374-598 |
1.47e-20 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 95.10 E-value: 1.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 374 NIEFKNVSFSYPSrpsAKVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDpedgcITVDE---NDIRAQNVRHYR 450
Cdd:PRK11000 3 SVTLRNVTKAYGD---VVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLED-----ITSGDlfiGEKRMNDVPPAE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 451 EQIGVVRQEPVLF-GTTIGNNIKFGREGVGEKEMEQAAREANAYDFImafpkKFNTLVGEKGAQMSGGQKQRIAIARALV 529
Cdd:PRK11000 75 RGVGMVFQSYALYpHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVL-----QLAHLLDRKPKALSGGQRQRVAIGRTLV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568980685 530 RNPKILILDEATSALDTeseSL-VQTALE--KASK--GRTTIVVAH-RLSTIRGADLIVTMKDGMVVEKGTHAEL 598
Cdd:PRK11000 150 AEPSVFLLDEPLSNLDA---ALrVQMRIEisRLHKrlGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
375-599 |
1.55e-20 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 95.68 E-value: 1.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 375 IEFKNVSFSYPSRPsakVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDIRAQNVRHYREQIG 454
Cdd:PRK09536 4 IDVSDLSVEFGDTT---VLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 455 VVRQEPVL-FGTTIGNNIKFGR----------EGVGEKEMEQAAREANAYDFImafPKKFNTLvgekgaqmSGGQKQRIA 523
Cdd:PRK09536 81 SVPQDTSLsFEFDVRQVVEMGRtphrsrfdtwTETDRAAVERAMERTGVAQFA---DRPVTSL--------SGGERQRVL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 524 IARALVRNPKILILDEATSALDTESEslVQT---ALEKASKGRTTIVVAHRLS-TIRGADLIVTMKDGMVVEKGTHAELM 599
Cdd:PRK09536 150 LARALAQATPVLLLDEPTASLDINHQ--VRTlelVRRLVDDGKTAVAAIHDLDlAARYCDELVLLADGRVRAAGPPADVL 227
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
1036-1234 |
1.89e-20 |
|
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: 94.40 E-value: 1.89e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1036 AFVGSSGCGKSTCVQL---LQRfydPMKGQVLLDGVDvkelnvqWLRSQTAI-----------VSQEPVLF-NCSIAENI 1100
Cdd:COG4148 29 ALFGPSGSGKTTLLRAiagLER---PDSGRIRLGGEV-------LQDSARGIflpphrrrigyVFQEARLFpHLSVRGNL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1101 AYG-----DNSRMVPLEEIkevadaanihsfIEglprkyntLVGL-----RGV-QLSGGQKQRLAIARALLRKPKILLLD 1169
Cdd:COG4148 99 LYGrkrapRAERRISFDEV------------VE--------LLGIghlldRRPaTLSGGERQRVAIGRALLSSPRLLLMD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568980685 1170 EATSALDNESEKVVQQALDKARR--GKTCLVVAHRLSTIQN-ADMIVVLQNGSIKEQGTHQELLRNGD 1234
Cdd:COG4148 159 EPLAALDLARKAEILPYLERLRDelDIPILYVSHSLDEVARlADHVVLLEQGRVVASGPLAEVLSRPD 226
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
375-587 |
1.93e-20 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 96.54 E-value: 1.93e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 375 IEFKNVSFSYPSrpsAKVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYdPE---DGCITVDENDIRAQNVRHyRE 451
Cdd:PRK13549 6 LEMKNITKTFGG---VKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHgtyEGEIIFEGEELQASNIRD-TE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 452 QIGVV--RQEPVLF-GTTIGNNIKFGREGVGEKEMEQAAREANAYDFIMAFpkKFNTLVGEKGAQMSGGQKQRIAIARAL 528
Cdd:PRK13549 81 RAGIAiiHQELALVkELSVLENIFLGNEITPGGIMDYDAMYLRAQKLLAQL--KLDINPATPVGNLGLGQQQLVEIAKAL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568980685 529 VRNPKILILDEATSALdTESESLVQTALEK--ASKGRTTIVVAHRLSTIRG-ADLIVTMKDG 587
Cdd:PRK13549 159 NKQARLLILDEPTASL-TESETAVLLDIIRdlKAHGIACIYISHKLNEVKAiSDTICVIRDG 219
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
378-589 |
3.83e-20 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 91.66 E-value: 3.83e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 378 KNVSFSYPSRpsaKVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGcitvdenDIRAQN--VRHYREQIGV 455
Cdd:PRK11247 16 NAVSKRYGER---TVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAG-------ELLAGTapLAEAREDTRL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 456 VRQEPVLFG-TTIGNNIKFGREGVGEKEMEQAAREANAYDFIMAFPkkfntlvgekgAQMSGGQKQRIAIARALVRNPKI 534
Cdd:PRK11247 86 MFQDARLLPwKKVIDNVGLGLKGQWRDAALQALAAVGLADRANEWP-----------AALSGGQKQRVALARALIHRPGL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 535 LILDEATSALDT----ESESLVQTALEKasKGRTTIVVAHRLS-TIRGADLIVTMKDGMV 589
Cdd:PRK11247 155 LLLDEPLGALDAltriEMQDLIESLWQQ--HGFTVLLVTHDVSeAVAMADRVLLIEEGKI 212
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1016-1225 |
4.03e-20 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 90.91 E-value: 4.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1016 RPEVPVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGvdvkelNVQWL--------RSQTAIvsq 1087
Cdd:COG1134 36 REEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG------RVSALlelgagfhPELTGR--- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1088 EPVLFNCSIaeniaYGdnsrmVPLEEIKEVADA----ANIHSFIEgLP-RKYntlvglrgvqlSGGQKQRLAIARALLRK 1162
Cdd:COG1134 107 ENIYLNGRL-----LG-----LSRKEIDEKFDEivefAELGDFID-QPvKTY-----------SSGMRARLAFAVATAVD 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568980685 1163 PKILLLDEATSALDNE-SEKVVQQALDKARRGKTCLVVAHRLSTIQN-ADMIVVLQNGSIKEQGT 1225
Cdd:COG1134 165 PDILLVDEVLAVGDAAfQKKCLARIRELRESGRTVIFVSHSMGAVRRlCDRAIWLEKGRLVMDGD 229
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1004-1230 |
4.52e-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: 90.91 E-value: 4.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1004 LEFREVSFVypcRPEVPVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVL------LDGVDVKELnvqw 1077
Cdd:COG1119 4 LELRNVTVR---RGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDVrlfgerRGGEDVWEL---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1078 lRSQTAIVSQEpvlfncsIAENIAYGDNSRMVpleeikeVADAAniHSFIeGLPRKYN-----------TLVGLRGV--- 1143
Cdd:COG1119 77 -RKRIGLVSPA-------LQLRFPRDETVLDV-------VLSGF--FDSI-GLYREPTdeqrerarellELLGLAHLadr 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1144 ---QLSGGQKQRLAIARALLRKPKILLLDEATSALDNESEKVVQQALDK-ARRGKTCLV-VAHRLSTIQNA-DMIVVLQN 1217
Cdd:COG1119 139 pfgTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKlAAEGAPTLVlVTHHVEEIPPGiTHVLLLKD 218
|
250
....*....|...
gi 568980685 1218 GSIKEQGTHQELL 1230
Cdd:COG1119 219 GRVVAAGPKEEVL 231
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1021-1227 |
4.57e-20 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 90.84 E-value: 4.57e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1021 VLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDG--------VDVKElnVQWLRSQTAIVSQEPVLF 1092
Cdd:PRK11124 17 ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhfdfsktPSDKA--IRELRRNVGMVFQQYNLW 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1093 -NCSIAENIAYGDN-----SRMVPLEEIKEVADAANIHSFIEGLPrkyntlvglrgVQLSGGQKQRLAIARALLRKPKIL 1166
Cdd:PRK11124 95 pHLTVQQNLIEAPCrvlglSKDQALARAEKLLERLRLKPYADRFP-----------LHLSGGQQQRVAIARALMMEPQVL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568980685 1167 LLDEATSALDNE-SEKVVQQALDKARRGKTCLVVAHRLSTIQN-ADMIVVLQNGSIKEQGTHQ 1227
Cdd:PRK11124 164 LFDEPTAALDPEiTAQIVSIIRELAETGITQVIVTHEVEVARKtASRVVYMENGHIVEQGDAS 226
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1004-1234 |
4.58e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 92.10 E-value: 4.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1004 LEFREVSFVYpcRPEVP----VLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDV----KELNV 1075
Cdd:PRK13643 2 IKFEKVNYTY--QPNSPfasrALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVsstsKQKEI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1076 QWLRSQTAIVSQEP--VLFNCSIAENIAYGDNSRMVPLEEIKEVAdAANIHsfIEGLPRKYNTLVGLrgvQLSGGQKQRL 1153
Cdd:PRK13643 80 KPVRKKVGVVFQFPesQLFEETVLKDVAFGPQNFGIPKEKAEKIA-AEKLE--MVGLADEFWEKSPF---ELSGGQMRRV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1154 AIARALLRKPKILLLDEATSALDNESEKVVQQALDKARR-GKTCLVVAHRLSTIQN-ADMIVVLQNGSIKEQGTHQELLR 1231
Cdd:PRK13643 154 AIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQsGQTVVLVTHLMDDVADyADYVYLLEKGHIISCGTPSDVFQ 233
|
...
gi 568980685 1232 NGD 1234
Cdd:PRK13643 234 EVD 236
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1021-1232 |
4.60e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 91.06 E-value: 4.60e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1021 VLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYD-----PMKGQVLLDGVDV--KELNVQWLRSQTAIVSQEPVLF- 1092
Cdd:PRK14267 19 VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGRNIysPDVDPIEVRREVGMVFQYPNPFp 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1093 NCSIAENIAYGD--NSRMVPLEEIKEVAD-AANIHSFIEGLPRKYNTLVGlrgvQLSGGQKQRLAIARALLRKPKILLLD 1169
Cdd:PRK14267 99 HLTIYDNVAIGVklNGLVKSKKELDERVEwALKKAALWDEVKDRLNDYPS----NLSGGQRQRLVIARALAMKPKILLMD 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568980685 1170 EATSALDNESEKVVQQALDKARRGKTCLVVAHrlSTIQNA---DMIVVLQNGSIKEQGTHQELLRN 1232
Cdd:PRK14267 175 EPTANIDPVGTAKIEELLFELKKEYTIVLVTH--SPAQAArvsDYVAFLYLGKLIEVGPTRKVFEN 238
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
1018-1224 |
4.77e-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: 90.03 E-value: 4.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1018 EVPVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVKELNvqwlRSQTAIVSQEPVLF-NCSI 1096
Cdd:cd03269 12 RVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA----RNRIGYLPEERGLYpKMKV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1097 AENIAYGDNSRMVPLEEIKevadaANIHSFIE--GLPRKYNTLVGlrgvQLSGGQKQRLAIARALLRKPKILLLDEATSA 1174
Cdd:cd03269 88 IDQLVYLAQLKGLKKEEAR-----RRIDEWLErlELSEYANKRVE----ELSKGNQQKVQFIAAVIHDPELLILDEPFSG 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 568980685 1175 LDNESEKVVQQAL-DKARRGKTCLVVAHRLSTIQN-ADMIVVLQNGSIKEQG 1224
Cdd:cd03269 159 LDPVNVELLKDVIrELARAGKTVILSTHQMELVEElCDRVLLLNKGRAVLYG 210
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
1003-1226 |
5.03e-20 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 90.84 E-value: 5.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1003 NLEFREVSFVYPcrpEVPVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDG------VDVKELNVQ 1076
Cdd:COG4161 2 SIQLKNINCFYG---SHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGhqfdfsQKPSEKAIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1077 WLRSQTAIVSQEPVLF-NCSIAENIAYG-----DNSRMVPLEEIKEVADAANIHSFIEGLPrkyntlvglrgVQLSGGQK 1150
Cdd:COG4161 79 LLRQKVGMVFQQYNLWpHLTVMENLIEApckvlGLSKEQAREKAMKLLARLRLTDKADRFP-----------LHLSGGQQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568980685 1151 QRLAIARALLRKPKILLLDEATSALDNE-SEKVVQQALDKARRGKTCLVVAHRLSTIQN-ADMIVVLQNGSIKEQGTH 1226
Cdd:COG4161 148 QRVAIARALMMEPQVLLFDEPTAALDPEiTAQVVEIIRELSQTGITQVIVTHEVEFARKvASQVVYMEKGRIIEQGDA 225
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1004-1234 |
5.75e-20 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 91.36 E-value: 5.75e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1004 LEFREVSFvypCRPEVPVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVKELNVQWL---RS 1080
Cdd:PRK11831 8 VDMRGVSF---TRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLytvRK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1081 QTAIVSQEPVLF-NCSIAENIAYgdnsrmvPLEEIKEVADAAnIHSFI----EGlprkyntlVGLRGV------QLSGGQ 1149
Cdd:PRK11831 85 RMSMLFQSGALFtDMNVFDNVAY-------PLREHTQLPAPL-LHSTVmmklEA--------VGLRGAaklmpsELSGGM 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1150 KQRLAIARALLRKPKILLLDEATSALDNESEKVVQQALDKARR--GKTCLVVAHRLSTIQN-ADMIVVLQNGSIKEQGTH 1226
Cdd:PRK11831 149 ARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSalGVTCVVVSHDVPEVLSiADHAYIVADKKIVAHGSA 228
|
....*...
gi 568980685 1227 QELLRNGD 1234
Cdd:PRK11831 229 QALQANPD 236
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
684-956 |
5.93e-20 |
|
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: 91.78 E-value: 5.93e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 684 GTLASALNGSVHPVFSIIFGKLV-TMFEDKNKATLKQDAELysmMLVVLGIVALVTYLMQGLFyGRAEENLAMRLRHSAF 762
Cdd:cd18576 1 GLILLLLSSAIGLVFPLLAGQLIdAALGGGDTASLNQIALL---LLGLFLLQAVFSFFRIYLF-ARVGERVVADLRKDLY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 763 KAMLYQDMAWYDdkENNTGALTTTLAVDVAQIQGAATSRLGIVTQDVSNMSLSILISFIYGWEMTLLILSFAPVLAVTGM 842
Cdd:cd18576 77 RHLQRLPLSFFH--ERRVGELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWKLTLLMLATVPVVVLVAV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 843 IQTAAMAGFANRDKQALKRAGKIATEAVENIRTVVSLTRERAFEQMYEETLQTQHRNALKRAHITGccyavshAFVHFAH 922
Cdd:cd18576 155 LFGRRIRKLSKKVQDELAEANTIVEETLQGIRVVKAFTREDYEIERYRKALERVVKLALKRARIRA-------LFSSFII 227
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 568980685 923 AAGFR-------FGAYLIQAGRMMPEG--MFIVFTAIAYGAMA 956
Cdd:cd18576 228 FLLFGaivavlwYGGRLVLAGELTAGDlvAFLLYTLFIAGSIG 270
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
392-598 |
6.07e-20 |
|
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: 90.28 E-value: 6.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 392 VLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDI-------RAqnvrhyREQIGVVRQEPVLFG 464
Cdd:TIGR03410 15 ILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDItklppheRA------RAGIAYVPQGREIFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 465 T-TIGNNIKFGREGVGEKEmeqAAREANAYDFimaFPKKFNTLvGEKGAQMSGGQKQRIAIARALVRNPKILILDEATSA 543
Cdd:TIGR03410 89 RlTVEENLLTGLAALPRRS---RKIPDEIYEL---FPVLKEML-GRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPTEG 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 568980685 544 LDTESESLVQTALEK--ASKGRTTIVVAHRLSTIRG-ADLIVTMKDGMVVEKGTHAEL 598
Cdd:TIGR03410 162 IQPSIIKDIGRVIRRlrAEGGMAILLVEQYLDFARElADRYYVMERGRVVASGAGDEL 219
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
375-570 |
6.23e-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: 6.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 375 IEFKNVSFSYPSRPsakVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVdendiraqnvrhyreqig 454
Cdd:cd03221 1 IELENLSKTYGGKL---LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTW------------------ 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 455 vvrqepvlfgttiGNNIKFGregvgekemeqaareanaYdfimaFPkkfntlvgekgaQMSGGQKQRIAIARALVRNPKI 534
Cdd:cd03221 60 -------------GSTVKIG------------------Y-----FE------------QLSGGEKMRLALAKLLLENPNL 91
|
170 180 190
....*....|....*....|....*....|....*....
gi 568980685 535 LILDEATSALDTESeslvQTALE---KASKGrTTIVVAH 570
Cdd:cd03221 92 LLLDEPTNHLDLES----IEALEealKEYPG-TVILVSH 125
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1004-1234 |
6.40e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 91.40 E-value: 6.40e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1004 LEFREVSFVYpcRPEVPVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVKELNVQWLRSQTA 1083
Cdd:PRK13652 4 IETRDLCYSY--SGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1084 IVSQEP--VLFNCSIAENIAYGDNSRMVPLEEIKEVADAA----NIHSFIEGLPRkyntlvglrgvQLSGGQKQRLAIAR 1157
Cdd:PRK13652 82 LVFQNPddQIFSPTVEQDIAFGPINLGLDEETVAHRVSSAlhmlGLEELRDRVPH-----------HLSGGEKKRVAIAG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1158 ALLRKPKILLLDEATSALDNESEKVVQQALDK--ARRGKTCLVVAHRLSTI-QNADMIVVLQNGSIKEQGTHQELLRNGD 1234
Cdd:PRK13652 151 VIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDlpETYGMTVIFSTHQLDLVpEMADYIYVMDKGRIVAYGTVEEIFLQPD 230
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1020-1235 |
6.83e-20 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 91.22 E-value: 6.83e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1020 PVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDG--VDVKELNVQWLRSQTAIVSQEP--VLFNCS 1095
Cdd:PRK13638 15 PVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGkpLDYSKRGLLALRQQVATVFQDPeqQIFYTD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1096 IAENIAYGDNSRMVPLEEIKEVADAANihsfieglprkynTLVGLRGVQ------LSGGQKQRLAIARALLRKPKILLLD 1169
Cdd:PRK13638 95 IDSDIAFSLRNLGVPEAEITRRVDEAL-------------TLVDAQHFRhqpiqcLSHGQKKRVAIAGALVLQARYLLLD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568980685 1170 EATSALDNESEKVVQQALDK-ARRGKTCLVVAHRLSTI-QNADMIVVLQNGSIKEQGTHQELLRNGDT 1235
Cdd:PRK13638 162 EPTAGLDPAGRTQMIAIIRRiVAQGNHVIISSHDIDLIyEISDAVYVLRQGQILTHGAPGEVFACTEA 229
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1003-1241 |
7.03e-20 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 92.98 E-value: 7.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1003 NLEFREVSFVYPCRpeVPVLQNMSLSIEKGKTVAFVGSSGCGKSTcvqLLQrfydpM--------KGQVLLDGVDVKEL- 1073
Cdd:PRK11650 3 GLKLQAVRKSYDGK--TQVIKGIDLDVADGEFIVLVGPSGCGKST---LLR-----MvagleritSGEIWIGGRVVNELe 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1074 ----NVqwlrsqtAIVSQEPVLF-NCSIAENIAYGDNSRMVPLEEIKE-VADAA---NIHSFIEGLPRkyntlvglrgvQ 1144
Cdd:PRK11650 73 padrDI-------AMVFQNYALYpHMSVRENMAYGLKIRGMPKAEIEErVAEAArilELEPLLDRKPR-----------E 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1145 LSGGQKQRLAIARALLRKPKILLLDEATSALDnesEKV-VQQALD----KARRGKTCLVVAH-RLSTIQNADMIVVLQNG 1218
Cdd:PRK11650 135 LSGGQRQRVAMGRAIVREPAVFLFDEPLSNLD---AKLrVQMRLEiqrlHRRLKTTSLYVTHdQVEAMTLADRVVVMNGG 211
|
250 260
....*....|....*....|...
gi 568980685 1219 SIKEQGTHQELLRNGDTYFklVA 1241
Cdd:PRK11650 212 VAEQIGTPVEVYEKPASTF--VA 232
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1004-1218 |
7.23e-20 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 94.71 E-value: 7.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1004 LEFREVSFVYPcrpEVPVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVKelnvqwLRS-QT 1082
Cdd:COG3845 6 LELRGITKRFG---GVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVR------IRSpRD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1083 AI------VSQEPVLF-NCSIAENIAYGDNSRMVPLEEIKEVADAanihsfIEGLPRKY------NTLVGlrgvQLSGGQ 1149
Cdd:COG3845 77 AIalgigmVHQHFMLVpNLTVAENIVLGLEPTKGGRLDRKAARAR------IRELSERYgldvdpDAKVE----DLSVGE 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568980685 1150 KQRLAIARALLRKPKILLLDEATSAL-DNESEKVVqQALDK-ARRGKTCLVVAHRLSTI-QNADMIVVLQNG 1218
Cdd:COG3845 147 QQRVEILKALYRGARILILDEPTAVLtPQEADELF-EILRRlAAEGKSIIFITHKLREVmAIADRVTVLRRG 217
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
391-601 |
7.38e-20 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 92.33 E-value: 7.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 391 KVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDIR---AQNVRHYREQIGVVRQEPvlfgtti 467
Cdd:PRK11308 29 KALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLkadPEAQKLLRQKIQIVFQNP------- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 468 gnnikFG----REGVGEkemeqaareanaydfIMAFPKKFNTLVG-----EKGAQM------------------SGGQKQ 520
Cdd:PRK11308 102 -----YGslnpRKKVGQ---------------ILEEPLLINTSLSaaerrEKALAMmakvglrpehydryphmfSGGQRQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 521 RIAIARALVRNPKILILDEATSALDTESESLV-------QTALekaskGRTTIVVAHRLSTIRG-ADLIVTMKDGMVVEK 592
Cdd:PRK11308 162 RIAIARALMLDPDVVVADEPVSALDVSVQAQVlnlmmdlQQEL-----GLSYVFISHDLSVVEHiADEVMVMYLGRCVEK 236
|
....*....
gi 568980685 593 GTHAELMAK 601
Cdd:PRK11308 237 GTKEQIFNN 245
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
1018-1242 |
8.47e-20 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 90.13 E-value: 8.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1018 EVPVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLL--QRFYDPMKGQVLLDGVDVKELNVQwLRSQTAI-VS-QEPV--- 1090
Cdd:COG0396 12 GKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLmgHPKYEVTSGSILLDGEDILELSPD-ERARAGIfLAfQYPVeip 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1091 -------LfncSIAENIAYGDNSRMVP-LEEIKEVADAANI-HSFIEglpRKYNtlVGLrgvqlSGGQKQRLAIARALLR 1161
Cdd:COG0396 91 gvsvsnfL---RTALNARRGEELSAREfLKLLKEKMKELGLdEDFLD---RYVN--EGF-----SGGEKKRNEILQMLLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1162 KPKILLLDEATSALDNESEKVVQQALDKARR-GKTCLVVAH--RLSTIQNADMIVVLQNGSIKEQGTH---QELLRNG-D 1234
Cdd:COG0396 158 EPKLAILDETDSGLDIDALRIVAEGVNKLRSpDRGILIITHyqRILDYIKPDFVHVLVDGRIVKSGGKelaLELEEEGyD 237
|
....*...
gi 568980685 1235 TYFKLVAA 1242
Cdd:COG0396 238 WLKEEAAA 245
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
373-589 |
1.23e-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: 90.30 E-value: 1.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 373 GNIEFKNVSFSYPSRPSAkVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEdGCITVDENDIRAQNVRHYREQ 452
Cdd:cd03289 1 GQMTVKDLTAKYTEGGNA-VLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSWNSVPLQKWRKA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 453 IGVVRQEPVLFGTTIGNNIK-FGREGvgEKEMEQAAREANAYDFIMAFPKKFNTLVGEKGAQMSGGQKQRIAIARALVRN 531
Cdd:cd03289 79 FGVIPQKVFIFSGTFRKNLDpYGKWS--DEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSK 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 568980685 532 PKILILDEATSALDTESESLVQTALEKASKGRTTIVVAHRLSTIRGADLIVTMKDGMV 589
Cdd:cd03289 157 AKILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKV 214
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
382-628 |
1.29e-19 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 90.45 E-value: 1.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 382 FSYPSRPsakVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDEN--DIRAQNVRHYREQIGVVRQE 459
Cdd:PRK13638 9 FRYQDEP---VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKplDYSKRGLLALRQQVATVFQD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 460 P--VLFGTTIGNNIKFGREGVGEKEMEQAAREANAYdfimafpkkfnTLVGEKGAQ------MSGGQKQRIAIARALVRN 531
Cdd:PRK13638 86 PeqQIFYTDIDSDIAFSLRNLGVPEAEITRRVDEAL-----------TLVDAQHFRhqpiqcLSHGQKKRVAIAGALVLQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 532 PKILILDEATSALDTESESLVQTALEK-ASKGRTTIVVAHRLSTI-RGADLIVTMKDGMVVEKGTHAELMAKQGLYYSLA 609
Cdd:PRK13638 155 ARYLLLDEPTAGLDPAGRTQMIAIIRRiVAQGNHVIISSHDIDLIyEISDAVYVLRQGQILTHGAPGEVFACTEAMEQAG 234
|
250 260
....*....|....*....|
gi 568980685 610 MAQD-IKKVDEQMESRTCST 628
Cdd:PRK13638 235 LTQPwLVKLHTQLGLPLCKT 254
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
378-599 |
1.31e-19 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 90.23 E-value: 1.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 378 KNVSFSYPSRpsaKVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDIRAQNVRHYREQIGVVR 457
Cdd:PRK10575 15 RNVSFRVPGR---TLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 458 QE-PVLFGTTIGNNIKFGRE---------GVGEKE-MEQAAreanaydfimafpkkfnTLVGEKG-AQ-----MSGGQKQ 520
Cdd:PRK10575 92 QQlPAAEGMTVRELVAIGRYpwhgalgrfGAADREkVEEAI-----------------SLVGLKPlAHrlvdsLSGGERQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 521 RIAIARALVRNPKILILDEATSALDTESESLVQTALEKAS--KGRTTIVVAHRLS-TIRGADLIVTMKDGMVVEKGTHAE 597
Cdd:PRK10575 155 RAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSqeRGLTVIAVLHDINmAARYCDYLVALRGGEMIAQGTPAE 234
|
..
gi 568980685 598 LM 599
Cdd:PRK10575 235 LM 236
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
375-590 |
1.47e-19 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 89.76 E-value: 1.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 375 IEFKNVS--FsYPSRPSAK-VLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDIRAQNVrHYR- 450
Cdd:COG1101 2 LELKNLSktF-NPGTVNEKrALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPE-YKRa 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 451 EQIGVVRQEPVLfGT----TIGNNI--------KFG-REGVGEKEMEQAaREANAyDFIMAFPKKFNTLVGekgaQMSGG 517
Cdd:COG1101 80 KYIGRVFQDPMM-GTapsmTIEENLalayrrgkRRGlRRGLTKKRRELF-RELLA-TLGLGLENRLDTKVG----LLSGG 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568980685 518 QKQRIAIARALVRNPKILILDEATSALDTESESLVQTALEK--ASKGRTTIVVAHRLS-TIRGADLIVTMKDGMVV 590
Cdd:COG1101 153 QRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKivEENNLTTLMVTHNMEqALDYGNRLIMMHEGRII 228
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
374-593 |
1.52e-19 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 88.87 E-value: 1.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 374 NIEFKNVSFSYPS-RPSAKVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPED---GCITVDENDIRAQNVRhy 449
Cdd:cd03234 3 VLPWWDVGLKAKNwNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFNGQPRKPDQFQ-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 450 rEQIGVVRQEPVLF-GTTIGNNIKFGREGVGEKEMEQAAREANAYDFIM---AFPKKFNTLVGekgaQMSGGQKQRIAIA 525
Cdd:cd03234 81 -KCVAYVRQDDILLpGLTVRETLTYTAILRLPRKSSDAIRKKRVEDVLLrdlALTRIGGNLVK----GISGGERRRVSIA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568980685 526 RALVRNPKILILDEATSALDTESE-SLVQTALEKASKGRTTIVVAH--RLSTIRGADLIVTMKDGMVVEKG 593
Cdd:cd03234 156 VQLLWDPKVLILDEPTSGLDSFTAlNLVSTLSQLARRNRIVILTIHqpRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
1021-1220 |
1.54e-19 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 89.74 E-value: 1.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1021 VLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVKELnvqwlRSQTAIVSQEPVLFNC-SIAEN 1099
Cdd:PRK11247 27 VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEA-----REDTRLMFQDARLLPWkKVIDN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1100 IAYG--DNSRMVPLEEIKEV--ADAANihsfieGLPrkyntlvglrgVQLSGGQKQRLAIARALLRKPKILLLDEATSAL 1175
Cdd:PRK11247 102 VGLGlkGQWRDAALQALAAVglADRAN------EWP-----------AALSGGQKQRVALARALIHRPGLLLLDEPLGAL 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 568980685 1176 DNESEKVVQQALDK--ARRGKTCLVVAHRLS-TIQNADMIVVLQNGSI 1220
Cdd:PRK11247 165 DALTRIEMQDLIESlwQQHGFTVLLVTHDVSeAVAMADRVLLIEEGKI 212
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
39-320 |
1.63e-19 |
|
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: 90.55 E-value: 1.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 39 LGILASMINGATVPLMSLVLGEISDHLINGCLVQtnrtkyqncsqtqeklnEDIIVLTLYYIGIGAAALIFGYVQiSFWV 118
Cdd:cd18541 3 LGILFLILVDLLQLLIPRIIGRAIDALTAGTLTA-----------------SQLLRYALLILLLALLIGIFRFLW-RYLI 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 119 ITAARQTTR-IRKQFFHSILAQDISWFDGSDICELNTRMTGDINKLCDGIGDKIPLMFQNISGFSIGLVISLIKSWKLSL 197
Cdd:cd18541 65 FGASRRIEYdLRNDLFAHLLTLSPSFYQKNRTGDLMARATNDLNAVRMALGPGILYLVDALFLGVLVLVMMFTISPKLTL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 198 VVLSTSPLIMASSALCSRMIISLTSKELDAYSKAGAVAEEALSSIQTVTAFGAQEKEIQRYTQHLKDAKDAGIKRATASK 277
Cdd:cd18541 145 IALLPLPLLALLVYRLGKKIHKRFRKVQEAFSDLSDRVQESFSGIRVIKAFVQEEAEIERFDKLNEEYVEKNLRLARVDA 224
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 568980685 278 LSLGAVYFFMNGAYGLAFWYGTSLIFGGEpgYTIGTILAvFFS 320
Cdd:cd18541 225 LFFPLIGLLIGLSFLIVLWYGGRLVIRGT--ITLGDLVA-FNS 264
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
375-591 |
1.66e-19 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 93.59 E-value: 1.66e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 375 IEFKNVSFSYPSRPsakVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITvdendiRAQNVRhyreqIG 454
Cdd:COG0488 316 LELEGLSKSYGDKT---LLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVK------LGETVK-----IG 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 455 VVRQEPVLF--GTTIGNNIKFGREGvgekemeqaAREANAYDFIMAF---PKKFNTLVGEkgaqMSGGQKQRIAIARALV 529
Cdd:COG0488 382 YFDQHQEELdpDKTVLDELRDGAPG---------GTEQEVRGYLGRFlfsGDDAFKPVGV----LSGGEKARLALAKLLL 448
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568980685 530 RNPKILILDEATSALDTES-ESLVQtALEkASKGrTTIVVAH-R--LSTIrgADLIVTMKDGMVVE 591
Cdd:COG0488 449 SPPNVLLLDEPTNHLDIETlEALEE-ALD-DFPG-TVLLVSHdRyfLDRV--ATRILEFEDGGVRE 509
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
100-316 |
1.99e-19 |
|
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: 90.19 E-value: 1.99e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 100 IGIGAAALIFGYVQISFWVITAARQTTRIRKQFFHSILAQDISWFDGSDICELNTRMTGDINKLCDGIGDKIPLMFQNIS 179
Cdd:cd18551 43 VALFLLQAVLSALSSYLLGRTGERVVLDLRRRLWRRLLRLPVSFFDRRRSGDLVSRVTNDTTLLRELITSGLPQLVTGVL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 180 GFSIGLVISLIKSWKLSLVVLSTSPLIMASSALCSRMIISLTSKELDAYSKAGAVAEEALSSIQTVTAFGAQEKEIQRYT 259
Cdd:cd18551 123 TVVGAVVLMFLLDWVLTLVTLAVVPLAFLIILPLGRRIRKASKRAQDALGELSAALERALSAIRTVKASNAEERETKRGG 202
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 568980685 260 QHLKDAKDAGIKRATASKLSLGAVYFFMNGAYGLAFWYGTSLIFGGEpgYTIGTILA 316
Cdd:cd18551 203 EAAERLYRAGLKAAKIEALIGPLMGLAVQLALLVVLGVGGARVASGA--LTVGTLVA 257
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
1017-1215 |
2.19e-19 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 87.29 E-value: 2.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1017 PEVPVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVKELNVQwlrsQTAIvsqePVLFNCSI 1096
Cdd:NF040873 3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQ----RSEV----PDSLPLTV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1097 AENIAYGDNSRMVPLEEIKEVADAANIHSfiegLPRkyntlVGLRGV------QLSGGQKQRLAIARALLRKPKILLLDE 1170
Cdd:NF040873 75 RDLVAMGRWARRGLWRRLTRDDRAAVDDA----LER-----VGLADLagrqlgELSGGQRQRALLAQGLAQEADLLLLDE 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 568980685 1171 ATSALDNESEKVVQQAL-DKARRGKTCLVVAHRLSTIQNADMIVVL 1215
Cdd:NF040873 146 PTTGLDAESRERIIALLaEEHARGATVVVVTHDLELVRRADPCVLL 191
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
1020-1232 |
2.54e-19 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 88.37 E-value: 2.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1020 PVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVKELNVqWLRSQTAI--VSQEPVLF-NCSI 1096
Cdd:cd03218 14 KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPM-HKRARLGIgyLPQEASIFrKLTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1097 AENIaygdnsrMVPLEEIKEvaDAANIHSFIEGLPRKYN--TLVGLRGVQLSGGQKQRLAIARALLRKPKILLLDEATSA 1174
Cdd:cd03218 93 EENI-------LAVLEIRGL--SKKEREEKLEELLEEFHitHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAG 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1175 LDNESEKVVQQALDKAR-RGKTCLVVAHRLS-TIQNADMIVVLQNGSIKEQGTHQELLRN 1232
Cdd:cd03218 164 VDPIAVQDIQKIIKILKdRGIGVLITDHNVReTLSITDRAYIIYEGKVLAEGTPEEIAAN 223
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1020-1230 |
2.87e-19 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 92.85 E-value: 2.87e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1020 PVLQNMSLSIEKGKTVAFVGSSGCGKS-TCVQLLQRFYDP----MKGQVLLDGVDVKELNVQWLR----SQTAIVSQEPv 1090
Cdd:PRK15134 23 TVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFHGESLLHASEQTLRgvrgNKIAMIFQEP- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1091 lfncsiaeniaygdnsrMV---PLEEI-KEVADAANIH----------SFIEGLPRkyntlVGLRGV---------QLSG 1147
Cdd:PRK15134 102 -----------------MVslnPLHTLeKQLYEVLSLHrgmrreaargEILNCLDR-----VGIRQAakrltdyphQLSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1148 GQKQRLAIARALLRKPKILLLDEATSALDNESEKVVQQALDKARR--GKTCLVVAHRLSTI-QNADMIVVLQNGSIKEQG 1224
Cdd:PRK15134 160 GERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQelNMGLLFITHNLSIVrKLADRVAVMQNGRCVEQN 239
|
....*.
gi 568980685 1225 THQELL 1230
Cdd:PRK15134 240 RAATLF 245
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
1016-1224 |
3.36e-19 |
|
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: 87.97 E-value: 3.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1016 RPEVPVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDG--VDVKELNVQWLRSQTAIvsqEPVLFN 1093
Cdd:cd03220 32 VGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGrvSSLLGLGGGFNPELTGR---ENIYLN 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1094 CSIaeniaYGdnsrmVPLEEIKEVADAanIHSFIEgLPRKYNTLVGlrgvQLSGGQKQRLAIARALLRKPKILLLDEATS 1173
Cdd:cd03220 109 GRL-----LG-----LSRKEIDEKIDE--IIEFSE-LGDFIDLPVK----TYSSGMKARLAFAIATALEPDILLIDEVLA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 568980685 1174 ALDNE-SEKVVQQALDKARRGKTCLVVAHRLSTI-QNADMIVVLQNGSIKEQG 1224
Cdd:cd03220 172 VGDAAfQEKCQRRLRELLKQGKTVILVSHDPSSIkRLCDRALVLEKGKIRFDG 224
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
386-587 |
3.40e-19 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 92.76 E-value: 3.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 386 SRPSAKVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDIRAQNVRHYREQ-IGVVRQEPVLFG 464
Cdd:PRK10762 13 AFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQEAgIGIIHQELNLIP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 465 T-TIGNNIKFGREGVGE------KEMEQAAreanayDFIMA---FPKKFNTLVGEkgaqMSGGQKQRIAIARALVRNPKI 534
Cdd:PRK10762 93 QlTIAENIFLGREFVNRfgridwKKMYAEA------DKLLArlnLRFSSDKLVGE----LSIGEQQMVEIAKVLSFESKV 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 568980685 535 LILDEATSAL-DTESESLVQTALEKASKGRTTIVVAHRLSTI-RGADLIVTMKDG 587
Cdd:PRK10762 163 IIMDEPTDALtDTETESLFRVIRELKSQGRGIVYISHRLKEIfEICDDVTVFRDG 217
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1004-1220 |
3.75e-19 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 93.25 E-value: 3.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1004 LEFREVSFVYPCRPE-VPVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVKELNVQWL---- 1078
Cdd:PRK10535 5 LELKDIRRSYPSGEEqVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALaqlr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1079 RSQTAIVSQE-PVLFNCSIAENI----AYGDNSRMVPLEEIKEVADAAnihsfieGLPRKyntlVGLRGVQLSGGQKQRL 1153
Cdd:PRK10535 85 REHFGFIFQRyHLLSHLTAAQNVevpaVYAGLERKQRLLRAQELLQRL-------GLEDR----VEYQPSQLSGGQQQRV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568980685 1154 AIARALLRKPKILLLDEATSALDNESEKVVQQALDKAR-RGKTCLVVAHRLSTIQNADMIVVLQNGSI 1220
Cdd:PRK10535 154 SIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRdRGHTVIIVTHDPQVAAQAERVIEIRDGEI 221
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
371-600 |
4.86e-19 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 88.69 E-value: 4.86e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 371 IEGNIEFKNVS--FSYPS----RPSAKVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDI--- 441
Cdd:PRK15112 1 VETLLEVRNLSktFRYRTgwfrRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLhfg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 442 ----RAQNVR----------HYREQIGVVRQEPVLFGTTIGNNIKfgregvgEKEMEQAARE-------ANAYDFIMAfp 500
Cdd:PRK15112 81 dysyRSQRIRmifqdpstslNPRQRISQILDFPLRLNTDLEPEQR-------EKQIIETLRQvgllpdhASYYPHMLA-- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 501 kkfntlvgekgaqmsGGQKQRIAIARALVRNPKILILDEATSALDTESES-LVQTALEKASK-GRTTIVVAHRLSTIRG- 577
Cdd:PRK15112 152 ---------------PGQKQRLGLARALILRPKVIIADEALASLDMSMRSqLINLMLELQEKqGISYIYVTQHLGMMKHi 216
|
250 260
....*....|....*....|...
gi 568980685 578 ADLIVTMKDGMVVEKGTHAELMA 600
Cdd:PRK15112 217 SDQVLVMHQGEVVERGSTADVLA 239
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
391-594 |
5.57e-19 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 88.15 E-value: 5.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 391 KVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLY--DPEDGC------ITVDENDIRAQNVRHYREQIGVVRQE--- 459
Cdd:PRK09984 18 QALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgDKSAGShiellgRTVQREGRLARDIRKSRANTGYIFQQfnl 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 460 ----PVLFGTTIG--NNIKFGREGVGEKEMEQAAREANAYDFI-MAFpkkfntLVGEKGAQMSGGQKQRIAIARALVRNP 532
Cdd:PRK09984 98 vnrlSVLENVLIGalGSTPFWRTCFSWFTREQKQRALQALTRVgMVH------FAHQRVSTLSGGQQQRVAIARALMQQA 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568980685 533 KILILDEATSALDTESESLVQTALEKASK--GRTTIVVAHRLS-TIRGADLIVTMKDGMVVEKGT 594
Cdd:PRK09984 172 KVILADEPIASLDPESARIVMDTLRDINQndGITVVVTLHQVDyALRYCERIVALRQGHVFYDGS 236
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
375-593 |
6.78e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 87.59 E-value: 6.78e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 375 IEFKNVSFSYPSRpsaKVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYD-PEDGCItvdENDIRAQNVRHY---- 449
Cdd:PRK14267 5 IETVNLRVYYGSN---HVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElNEEARV---EGEVRLFGRNIYspdv 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 450 -----REQIGVVRQEPVLF-GTTIGNNIKFGREGVG--------EKEMEQAAREANAYDfimafpkKFNTLVGEKGAQMS 515
Cdd:PRK14267 79 dpievRREVGMVFQYPNPFpHLTIYDNVAIGVKLNGlvkskkelDERVEWALKKAALWD-------EVKDRLNDYPSNLS 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568980685 516 GGQKQRIAIARALVRNPKILILDEATSALDTESESLVQTALEKASKGRTTIVVAHR-LSTIRGADLIVTMKDGMVVEKG 593
Cdd:PRK14267 152 GGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSpAQAARVSDYVAFLYLGKLIEVG 230
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
684-938 |
7.06e-19 |
|
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: 88.46 E-value: 7.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 684 GTLA---SALNGSVHPVFsiiFGKLV----TMFEDKNKATLKqdaELYSMMLVVLGIVAL--VTYLMQGLFYGRAEENLA 754
Cdd:cd18780 1 GTIAllvSSGTNLALPYF---FGQVIdavtNHSGSGGEEALR---ALNQAVLILLGVVLIgsIATFLRSWLFTLAGERVV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 755 MRLRHSAFKAMLYQDMAWYDdkENNTGALTTTLAVDVAQIQGAATSRLGIVTQDVSNMSLSILISFIYGWEMTLLILSFA 834
Cdd:cd18780 75 ARLRKRLFSAIIAQEIAFFD--VTRTGELLNRLSSDTQVLQNAVTVNLSMLLRYLVQIIGGLVFMFTTSWKLTLVMLSVV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 835 PVLAVTGMIQTAAMAGFANRDKQALKRAGKIATEAVENIRTVVSLTRERAFEQMYEETLQTQHRNALKRAHITGCCYAVS 914
Cdd:cd18780 153 PPLSIGAVIYGKYVRKLSKKFQDALAAASTVAEESISNIRTVRSFAKETKEVSRYSEKINESYLLGKKLARASGGFNGFM 232
|
250 260
....*....|....*....|....
gi 568980685 915 HAFVHFAHAAGFRFGAYLIQAGRM 938
Cdd:cd18780 233 GAAAQLAIVLVLWYGGRLVIDGEL 256
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
1002-1232 |
7.73e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 88.53 E-value: 7.73e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1002 GNLEFREVSFVYPCRP--EVPVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDV-----KELN 1074
Cdd:PRK13645 5 KDIILDNVSYTYAKKTpfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIpanlkKIKE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1075 VQWLRSQTAIVSQEP--VLFNCSIAENIAYGDNSRMVPLEEI-KEVADAANIHSfiegLPRKYntlVGLRGVQLSGGQKQ 1151
Cdd:PRK13645 85 VKRLRKEIGLVFQFPeyQLFQETIEKDIAFGPVNLGENKQEAyKKVPELLKLVQ----LPEDY---VKRSPFELSGGQKR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1152 RLAIARALLRKPKILLLDEATSALDNESEKVVQQALDKARR--GKTCLVVAHRLSTI-QNADMIVVLQNGSIKEQGTHQE 1228
Cdd:PRK13645 158 RVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKeyKKRIIMVTHNMDQVlRIADEVIVMHEGKVISIGSPFE 237
|
....
gi 568980685 1229 LLRN 1232
Cdd:PRK13645 238 IFSN 241
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
378-539 |
9.89e-19 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 87.01 E-value: 9.89e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 378 KNVSFSYPSRPsakVLKGLNLKIKAGETVALVGPSGSGKSTT----VQLLQrlydPEDGCITVDENDI-------RAqnv 446
Cdd:COG1137 7 ENLVKSYGKRT---VVKDVSLEVNQGEIVGLLGPNGAGKTTTfymiVGLVK----PDSGRIFLDGEDIthlpmhkRA--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 447 rhyREQIGVVRQEPVLF-GTTIGNNIKFGREGVGEKEMEQAAReanaydfimafpkkFNTLVGE---------KGAQMSG 516
Cdd:COG1137 77 ---RLGIGYLPQEASIFrKLTVEDNILAVLELRKLSKKEREER--------------LEELLEEfgithlrksKAYSLSG 139
|
170 180
....*....|....*....|...
gi 568980685 517 GQKQRIAIARALVRNPKILILDE 539
Cdd:COG1137 140 GERRRVEIARALATNPKFILLDE 162
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
393-587 |
1.20e-18 |
|
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: 86.37 E-value: 1.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 393 LKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDIRAQNvrhyREQIGVVRQEPVLFGTTIGNNIK 472
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPG----PDRMVVFQNYSLLPWLTVRENIA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 473 FGREGVgEKEMEQAAREANAYDFImafpkkfnTLVG------EKGAQMSGGQKQRIAIARALVRNPKILILDEATSALDT 546
Cdd:TIGR01184 77 LAVDRV-LPDLSKSERRAIVEEHI--------ALVGlteaadKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDA 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 568980685 547 ESESLVQTALEKASK--GRTTIVVAHRL-STIRGADLIVTMKDG 587
Cdd:TIGR01184 148 LTRGNLQEELMQIWEehRVTVLMVTHDVdEALLLSDRVVMLTNG 191
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1020-1231 |
1.24e-18 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 87.06 E-value: 1.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1020 PVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVKELNVQWLRSQTAIVSQEPVL-FNCSIAE 1098
Cdd:COG4604 15 VVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAILRQENHInSRLTVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1099 NIAYG--DNSRMVPLEEIKEVADAAnIHSF-IEGLPRKYNTlvglrgvQLSGGQKQRLAIARALLRKPKILLLDEATSAL 1175
Cdd:COG4604 95 LVAFGrfPYSKGRLTAEDREIIDEA-IAYLdLEDLADRYLD-------ELSGGQRQRAFIAMVLAQDTDYVLLDEPLNNL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568980685 1176 D-NESekvVQ--QALDKA--RRGKTCLVVAHRLstiqN-----ADMIVVLQNGSIKEQGTHQELLR 1231
Cdd:COG4604 167 DmKHS---VQmmKLLRRLadELGKTVVIVLHDI----NfascyADHIVAMKDGRVVAQGTPEEIIT 225
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
375-598 |
1.40e-18 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 90.88 E-value: 1.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 375 IEFKNVSFSYPSRPsakVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDI-RAQNVRHYREQI 453
Cdd:PRK15439 12 LCARSISKQYSGVE---VLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCaRLTPAKAHQLGI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 454 GVVRQEPVLFGT-TIGNNIKFG--REGVGEKEMEQAAREANAY-DFIMafpkkfntlvgeKGAQMSGGQKQRIAIARALV 529
Cdd:PRK15439 89 YLVPQEPLLFPNlSVKENILFGlpKRQASMQKMKQLLAALGCQlDLDS------------SAGSLEVADRQIVEILRGLM 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568980685 530 RNPKILILDEATSALD-TESESLVQTALEKASKGRTTIVVAHRLSTIRG-ADLIVTMKDGMVVEKGTHAEL 598
Cdd:PRK15439 157 RDSRILILDEPTASLTpAETERLFSRIRELLAQGVGIVFISHKLPEIRQlADRISVMRDGTIALSGKTADL 227
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
995-1235 |
1.61e-18 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 86.77 E-value: 1.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 995 EKPDTCEGNLEFREVSFVYPCRPevpVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVKELN 1074
Cdd:PRK10575 3 EYTNHSDTTFALRNVSFRVPGRT---LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1075 VQWLRSQTAIVSQE-PVLFNCSIAENIAYGDNSRMVPLEEIKeVADAANIHSFIeglprkynTLVGLRGV------QLSG 1147
Cdd:PRK10575 80 SKAFARKVAYLPQQlPAAEGMTVRELVAIGRYPWHGALGRFG-AADREKVEEAI--------SLVGLKPLahrlvdSLSG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1148 GQKQRLAIARALLRKPKILLLDEATSALDNESEKVVQ---QALDKaRRGKTCLVVAHRLS-TIQNADMIVVLQNGSIKEQ 1223
Cdd:PRK10575 151 GERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLalvHRLSQ-ERGLTVIAVLHDINmAARYCDYLVALRGGEMIAQ 229
|
250
....*....|..
gi 568980685 1224 GTHQELLRnGDT 1235
Cdd:PRK10575 230 GTPAELMR-GET 240
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
92-305 |
1.64e-18 |
|
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: 87.53 E-value: 1.64e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 92 IIVLTLyyIGIGAAALIFgyVQISFWVITAARQTTRIRKQFFHSILAQDISWFDGSDICELNTRMTGDINKLCDGIGDKI 171
Cdd:cd18589 39 ITVMSL--LTIASAVSEF--VCDLIYNITMSRIHSRLQGLVFAAVLRQEIAFFDSNQTGDIVSRVTTDTEDMSESLSENL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 172 PLMFQNISGFSIGLVISLIKSWKLSLVVLSTSPLIMASSALCSRMIISLTSKELDAYSKAGAVAEEALSSIQTVTAFGAQ 251
Cdd:cd18589 115 SLLMWYLARGLFLFIFMLWLSPKLALLTALGLPLLLLVPKFVGKFQQSLAVQVQKSLARANQVAVETFSAMKTVRSFANE 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 568980685 252 EKEIQRYTQHLKDAKDAGIKRATASKLSLgavyfFMNGAYGLA-----FWYGTSLIFGG 305
Cdd:cd18589 195 EGEAQRYRQRLQKTYRLNKKEAAAYAVSM-----WTSSFSGLAlkvgiLYYGGQLVTAG 248
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
120-345 |
1.71e-18 |
|
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: 87.39 E-value: 1.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 120 TAARQTTRIRKQFFHSILAQDISWFDGSDICELNTRMTGDINKLCDGIGDKIPLMFQNI--SGFSIGLVISLikSWKLSL 197
Cdd:cd18590 63 TLSRLNLRLRHQLFSSLVQQDIGFFEKTKTGDLTSRLSTDTTLMSRSVALNANVLLRSLvkTLGMLGFMLSL--SWQLTL 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 198 VVLSTSPLIMASSALCSRMIISLTSKELDAYSKAGAVAEEALSSIQTVTAFGAQEKEIQRYTQHLKDAKDAGIKRATASK 277
Cdd:cd18590 141 LTLIEMPLTAIAQKVYNTYHQKLSQAVQDSIAKAGELAREAVSSIRTVRSFKAEEEEACRYSEALERTYNLKDRRDTVRA 220
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568980685 278 LSLGAVYFFMNGAYGLAFWYGTSLIFGGEpgYTIGTILAVFFSVIHSSYCIGSVAPHLETFTVARGAA 345
Cdd:cd18590 221 VYLLVRRVLQLGVQVLMLYCGRQLIQSGH--LTTGSLVSFILYQKNLGSYVRTLVYIYGDMLSNVGAA 286
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1018-1219 |
2.01e-18 |
|
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: 85.56 E-value: 2.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1018 EVPVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLD----GVDVKELNVQ---WLRSQT-AIVSQ-- 1087
Cdd:COG4778 23 RLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRhdggWVDLAQASPReilALRRRTiGYVSQfl 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1088 -------------EPVLfncsiaeniaygdnSRMVPLEEIKEVAdAANIHSFieGLPRKyntLVGLRGVQLSGGQKQRLA 1154
Cdd:COG4778 103 rviprvsaldvvaEPLL--------------ERGVDREEARARA-RELLARL--NLPER---LWDLPPATFSGGEQQRVN 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568980685 1155 IARALLRKPKILLLDEATSALDNESEKVVQQALDKARRGKTCLV-VAHRLSTIQN-ADMIVVLQNGS 1219
Cdd:COG4778 163 IARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIgIFHDEEVREAvADRVVDVTPFS 229
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
92-316 |
2.08e-18 |
|
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: 87.06 E-value: 2.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 92 IIVLTLYYIGIGAAALIFGYVQISFWVITAARQTTRIRKQFFHSILAQDISWFDGSDICELNTRMTGDINKLCDGIGDKI 171
Cdd:cd18544 40 LLLLALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRDLFSHIQRLPLSFFDRTPVGRLVTRVTNDTEALNELFTSGL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 172 PLMFQNIsgFSIG--LVISLIKSWKLSLVVLSTSPLIMASSALCSRMIISLTSKELDAYSKAGAVAEEALSSIQTVTAFG 249
Cdd:cd18544 120 VTLIGDL--LLLIgiLIAMFLLNWRLALISLLVLPLLLLATYLFRKKSRKAYREVREKLSRLNAFLQESISGMSVIQLFN 197
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568980685 250 AQEKEIQRYTQHLKDAKDAGIKRATASKLSLGAVYFFMNGAYGLAFWYGTSLIFGGepGYTIGTILA 316
Cdd:cd18544 198 REKREFEEFDEINQEYRKANLKSIKLFALFRPLVELLSSLALALVLWYGGGQVLSG--AVTLGVLYA 262
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
727-941 |
3.77e-18 |
|
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: 86.44 E-value: 3.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 727 MLVVLGIVALVTYLMQGLFYGRAEENLAMRLRHSAFKAMLYQDMAWYDdkENNTGALTTTLAVDVAQIQGAATSRLGIVT 806
Cdd:cd18572 41 LLLLLSVLSGLFSGLRGGCFSYAGTRLVRRLRRDLFRSLLRQDIAFFD--ATKTGELTSRLTSDCQKVSDPLSTNLNVFL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 807 QDVSNMSLSILISFIYGWEMTLLILSFAPVLAVTgmiqTAAMAGF----ANRDKQALKRAGKIATEAVENIRTVVSLTRE 882
Cdd:cd18572 119 RNLVQLVGGLAFMFSLSWRLTLLAFITVPVIALI----TKVYGRYyrklSKEIQDALAEANQVAEEALSNIRTVRSFATE 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 568980685 883 RAFEQMYEETLQTQHRNALKRAHITGCCYAVSHAFVHFAHAAGFRFGAYLIQAGRMMPE 941
Cdd:cd18572 195 EREARRYERALDKALKLSVRQALAYAGYVAVNTLLQNGTQVLVLFYGGHLVLSGRMSAG 253
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
375-597 |
3.96e-18 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 84.54 E-value: 3.96e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 375 IEFKNVSFSYPSRPSAkvLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDI---RAQNVRHYRE 451
Cdd:PRK10908 2 IRFEHVSKAYLGGRQA--LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDItrlKNREVPFLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 452 QIGVVRQEP-VLFGTTIGNNIKFGREGVGEKEMEQAAREANAYDFIMAFPKKFNTLVgekgaQMSGGQKQRIAIARALVR 530
Cdd:PRK10908 80 QIGMIFQDHhLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPI-----QLSGGEQQRVGIARAVVN 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568980685 531 NPKILILDEATSALDTE-SESLVQTALEKASKGRTTIVVAHRLSTI-RGADLIVTMKDGMVVEkGTHAE 597
Cdd:PRK10908 155 KPAVLLADEPTGNLDDAlSEGILRLFEEFNRVGVTVLMATHDIGLIsRRSYRMLTLSDGHLHG-GVGGE 222
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
375-593 |
5.86e-18 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 88.69 E-value: 5.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 375 IEFKNVSFSYPSrpsAKVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVdeNDIRAQNVRH---YRE 451
Cdd:PRK09700 6 ISMAGIGKSFGP---VHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITI--NNINYNKLDHklaAQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 452 QIGVVRQE-PVLFGTTIGNNIKFGR---------EGVGEKEMEQAAREANaydFIMAFPKKFNTLVGEkgaqMSGGQKQR 521
Cdd:PRK09700 81 GIGIIYQElSVIDELTVLENLYIGRhltkkvcgvNIIDWREMRVRAAMML---LRVGLKVDLDEKVAN----LSISHKQM 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568980685 522 IAIARALVRNPKILILDEATSAL-DTESESLVQTALEKASKGRTTIVVAHRLSTIRG-ADLIVTMKDGMVVEKG 593
Cdd:PRK09700 154 LEIAKTLMLDAKVIIMDEPTSSLtNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRiCDRYTVMKDGSSVCSG 227
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
375-600 |
6.19e-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: 6.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 375 IEFKNVSFSYPS--RPSAKVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCIT-------VDENDIRAQN 445
Cdd:TIGR03269 280 IKVRNVSKRYISvdRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNvrvgdewVDMTKPGPDG 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 446 VRHYREQIGVVRQEPVLFG-TTIGNNIKfgrEGVGEKEMEQAAREANAYDFIMA-FPKKFNTLVGEK-GAQMSGGQKQRI 522
Cdd:TIGR03269 360 RGRAKRYIGILHQEYDLYPhRTVLDNLT---EAIGLELPDELARMKAVITLKMVgFDEEKAEEILDKyPDELSEGERHRV 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 523 AIARALVRNPKILILDEATSALDTESESLVQTALEKASK--GRTTIVVAHRLSTIRG-ADLIVTMKDGMVVEKGTHAELM 599
Cdd:TIGR03269 437 ALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREemEQTFIIVSHDMDFVLDvCDRAALMRDGKIVKIGDPEEIV 516
|
.
gi 568980685 600 A 600
Cdd:TIGR03269 517 E 517
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
1010-1224 |
9.25e-18 |
|
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: 83.92 E-value: 9.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1010 SFVYPCRPEVPVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVKELNVQWLRSQTAIVSQEP 1089
Cdd:cd03267 25 SLFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRIGVVFGQKT 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1090 VL-FNCSIAENIAYgdNSRMVPLEE------IKEVADAANIHSFIEGLPRkyntlvglrgvQLSGGQKQRLAIARALLRK 1162
Cdd:cd03267 105 QLwWDLPVIDSFYL--LAAIYDLPParfkkrLDELSELLDLEELLDTPVR-----------QLSLGQRMRAEIAAALLHE 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568980685 1163 PKILLLDEATSALDNESEKVVQQALDK--ARRGKTCLVVAHRLSTIQN-ADMIVVLQNGSIKEQG 1224
Cdd:cd03267 172 PEILFLDEPTIGLDVVAQENIRNFLKEynRERGTTVLLTSHYMKDIEAlARRVLVIDKGRLLYDG 236
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
392-615 |
9.59e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 84.76 E-value: 9.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 392 VLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDG------CITVDENDIRAQNVRHYREQIGVVRQEPVLFGT 465
Cdd:PRK14271 36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgdVLLGGRSIFNYRDVLEFRRRVGMLFQRPNPFPM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 466 TIGNNIKFGREG---VGEKEMEQAAR----EANAYDFImafpkkfNTLVGEKGAQMSGGQKQRIAIARALVRNPKILILD 538
Cdd:PRK14271 116 SIMDNVLAGVRAhklVPRKEFRGVAQarltEVGLWDAV-------KDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLD 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 539 EATSALDTESESLVQTALEKASKGRTTIVVAHRLS-TIRGADLIVTMKDGMVVEKGTHAELMAK----QGLYYSLAMAQD 613
Cdd:PRK14271 189 EPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAqAARISDRAALFFDGRLVEEGPTEQLFSSpkhaETARYVAGLSGD 268
|
..
gi 568980685 614 IK 615
Cdd:PRK14271 269 VK 270
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
378-545 |
1.05e-17 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 83.79 E-value: 1.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 378 KNVSFSYPSRpsaKVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDIRAQNVR-HYREQIGVV 456
Cdd:PRK10895 7 KNLAKAYKGR---RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHaRARRGIGYL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 457 RQEPVLFGT-TIGNNIKfgreGVGE--KEMEQAAREANAYDFIMAFpkKFNTLVGEKGAQMSGGQKQRIAIARALVRNPK 533
Cdd:PRK10895 84 PQEASIFRRlSVYDNLM----AVLQirDDLSAEQREDRANELMEEF--HIEHLRDSMGQSLSGGERRRVEIARALAANPK 157
|
170
....*....|..
gi 568980685 534 ILILDEATSALD 545
Cdd:PRK10895 158 FILLDEPFAGVD 169
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
666-1170 |
1.14e-17 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 87.93 E-value: 1.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 666 SLLKIfkLSKSEWPFVVLGTLASALNGsvhpVFSIIFGKLVtmfedkNKATLKQDAELYSMMLVVLGIVALV---TYLMQ 742
Cdd:COG4615 2 NLLRL--LLRESRWLLLLALLLGLLSG----LANAGLIALI------NQALNATGAALARLLLLFAGLLVLLllsRLASQ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 743 GLFYGRAEENLAmRLRHSAFKAMLyqdmawyddkenntgaltttlAVDVAQIQGAATSRL-GIVTQDVSNMS--LSILIS 819
Cdd:COG4615 70 LLLTRLGQHAVA-RLRLRLSRRIL---------------------AAPLERLERIGAARLlAALTEDVRTISqaFVRLPE 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 820 FIYGweMTLLILSFA-------PVLAVTGMIQTAAMAGF---ANRDKQALKRAGKIATEAVENIRTVVS------LTRER 883
Cdd:COG4615 128 LLQS--VALVLGCLAylawlspPLFLLTLVLLGLGVAGYrllVRRARRHLRRAREAEDRLFKHFRALLEgfkelkLNRRR 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 884 AfEQMYEETLQtQHRNALKRAHItgccyavsHAFVHFAHAAGFrfgayliqaGRMMpegMF-----IVFTAIAYG----A 954
Cdd:COG4615 206 R-RAFFDEDLQ-PTAERYRDLRI--------RADTIFALANNW---------GNLL---FFaliglILFLLPALGwadpA 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 955 MAIGETLV-------------WAPEYSKAKAGASHLFAL---LKNKPTINSCSQSGEKPDTCEGnLEFREVSFVYPCRPE 1018
Cdd:COG4615 264 VLSGFVLVllflrgplsqlvgALPTLSRANVALRKIEELelaLAAAEPAAADAAAPPAPADFQT-LELRGVTYRYPGEDG 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1019 VP--VLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVKELNVQWLRSQTAIVSQEPVLFNcsi 1096
Cdd:COG4615 343 DEgfTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQLFSAVFSDFHLFD--- 419
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1097 aeniaygdnsRMVPLEeikEVADAANIHSFIEGLprKYNTLVGLRG-----VQLSGGQKQRLAIARALL-RKPkILLLDE 1170
Cdd:COG4615 420 ----------RLLGLD---GEADPARARELLERL--ELDHKVSVEDgrfstTDLSQGQRKRLALLVALLeDRP-ILVFDE 483
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1016-1201 |
1.19e-17 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 87.81 E-value: 1.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1016 RPEVPVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLD-GVDVkelnvqwlrsqtAIVSQEPVLF-N 1093
Cdd:COG0488 8 FGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPkGLRI------------GYLPQEPPLDdD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1094 CSIAENIAYGDN-----------------------SRMVPLEEIKEVADAANIHSFIE------GLP-RKYNTLVGlrgv 1143
Cdd:COG0488 76 LTVLDTVLDGDAelraleaeleeleaklaepdedlERLAELQEEFEALGGWEAEARAEeilsglGFPeEDLDRPVS---- 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568980685 1144 QLSGGQKQRLAIARALLRKPKILLLDEATSALDNES----EKVVqqaldKARRGkTCLVVAH 1201
Cdd:COG0488 152 ELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESiewlEEFL-----KNYPG-TVLVVSH 207
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
1018-1224 |
1.20e-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: 82.57 E-value: 1.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1018 EVPVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRF--YDPMKGQVLLDGVDVKELNVQwLRSQTAI--VSQEPVlfn 1093
Cdd:cd03217 12 GKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPE-ERARLGIflAFQYPP--- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1094 csiaeniaygdnsrmvpleEIKEVadaaNIHSFIEGLprkyntlvglrGVQLSGGQKQRLAIARALLRKPKILLLDEATS 1173
Cdd:cd03217 88 -------------------EIPGV----KNADFLRYV-----------NEGFSGGEKKRNEILQLLLLEPDLAILDEPDS 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 568980685 1174 ALDNESEKVVQQALDKARR-GKTCLVVAH--RLSTIQNADMIVVLQNGSIKEQG 1224
Cdd:cd03217 134 GLDIDALRLVAEVINKLREeGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVKSG 187
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1004-1222 |
1.33e-17 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 87.81 E-value: 1.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1004 LEFREVSFVYPcrpEVPVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLdGVDVKelnvqwlrsqTA 1083
Cdd:COG0488 316 LELEGLSKSYG---DKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVK----------IG 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1084 IVSQEPVLFNcsiaeniayGDNSrmvPLEEIKEVADAAN---IHSFIEGL---PRKYNTLVGlrgvQLSGGQKQRLAIAR 1157
Cdd:COG0488 382 YFDQHQEELD---------PDKT---VLDELRDGAPGGTeqeVRGYLGRFlfsGDDAFKPVG----VLSGGEKARLALAK 445
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568980685 1158 ALLRKPKILLLDEATSALDNESEKVVQQALDkARRGkTCLVVAH-R--LSTIqnADMIVVLQNGSIKE 1222
Cdd:COG0488 446 LLLSPPNVLLLDEPTNHLDIETLEALEEALD-DFPG-TVLLVSHdRyfLDRV--ATRILEFEDGGVRE 509
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
37-316 |
1.64e-17 |
|
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: 84.76 E-value: 1.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 37 MTLGILASMINGATVPLMSLVLGEISDHLINGCLVQTNRTKyqncsqtqeklnEDIIVLTLYYIGIGAAALIFGYVQiSF 116
Cdd:cd18547 1 LILVIILAIISTLLSVLGPYLLGKAIDLIIEGLGGGGGVDF------------SGLLRILLLLLGLYLLSALFSYLQ-NR 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 117 WVITAARQTT-RIRKQFFHSILAQDISWFDGSDICELNTRMTGDINKLCDGIGDKIPLMFQNISGFSIGLVISLIKSWKL 195
Cdd:cd18547 68 LMARVSQRTVyDLRKDLFEKLQRLPLSYFDTHSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPLL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 196 SLVVLSTSPLIMassaLCSRMIISLTSKELDAYSKA-GAV---AEEALSSIQTVTAFGAQEKEIQRYTQHLKDAKDAGIK 271
Cdd:cd18547 148 TLIVLVTVPLSL----LVTKFIAKRSQKYFRKQQKAlGELngyIEEMISGQKVVKAFNREEEAIEEFDEINEELYKASFK 223
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 568980685 272 RATASKLSLGAVYFFMNGAYGLAFWYGTSLIFGGepGYTIGTILA 316
Cdd:cd18547 224 AQFYSGLLMPIMNFINNLGYVLVAVVGGLLVING--ALTVGVIQA 266
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
92-320 |
1.74e-17 |
|
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: 84.48 E-value: 1.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 92 IIVLTLyyIGIGAAALIFGYVQ--ISFWVitAARQTTRIRKQFFHSILAQDISWFDGSDICELNTRMTGDINKLCDGIGD 169
Cdd:cd18563 44 LLVLGL--AGAYVLSALLGILRgrLLARL--GERITADLRRDLYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDFLSD 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 170 KIPLMFQNISGFSIGLVISLIKSWKLSLVVLSTSPLIMASSALCSRMIISLTSKELDAYSKAGAVAEEALSSIQTVTAFG 249
Cdd:cd18563 120 GLPDFLTNILMIIGIGVVLFSLNWKLALLVLIPVPLVVWGSYFFWKKIRRLFHRQWRRWSRLNSVLNDTLPGIRVVKAFG 199
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568980685 250 AQEKEIQRYTQHLKDAKDAGIkRATASKLSLGAVYFFMNGAYGLAFWY-GTSLIFGGEpgYTIGTILAvFFS 320
Cdd:cd18563 200 QEKREIKRFDEANQELLDANI-RAEKLWATFFPLLTFLTSLGTLIVWYfGGRQVLSGT--MTLGTLVA-FLS 267
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1021-1225 |
1.93e-17 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 82.94 E-value: 1.93e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1021 VLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVKELNVQW---LRSQTA--IVSQEPVLFNCS 1095
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAkaeLRNQKLgfIYQFHHLLPDFT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1096 IAENIAY----GDNSRMVPLEEIKEVADAAnihsfieGLPRKYNTlvglRGVQLSGGQKQRLAIARALLRKPKILLLDEA 1171
Cdd:PRK11629 104 ALENVAMplliGKKKPAEINSRALEMLAAV-------GLEHRANH----RPSELSGGERQRVAIARALVNNPRLVLADEP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 568980685 1172 TSALDNESEKVVQQALDK--ARRGKTCLVVAHRLSTIQNADMIVVLQNGSIKEQGT 1225
Cdd:PRK11629 173 TGNLDARNADSIFQLLGElnRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRLTAELS 228
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
376-598 |
2.09e-17 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 86.89 E-value: 2.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 376 EFKNVSFSYPSrpsAKVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDIRAQNVRHYREQ-IG 454
Cdd:PRK11288 6 SFDGIGKTFPG---VKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAALAAgVA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 455 VVRQE----PVLfgtTIGNNIKFG----REG-VGEKEMEQAAREANAYDFIMAFPkkfNTLVGEkgaqMSGGQKQRIAIA 525
Cdd:PRK11288 83 IIYQElhlvPEM---TVAENLYLGqlphKGGiVNRRLLNYEAREQLEHLGVDIDP---DTPLKY----LSIGQRQMVEIA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568980685 526 RALVRNPKILILDEATSALDT-ESESLVQTALEKASKGRTTIVVAHRLSTI-RGADLIVTMKDGMVVEkgTHAEL 598
Cdd:PRK11288 153 KALARNARVIAFDEPTSSLSArEIEQLFRVIRELRAEGRVILYVSHRMEEIfALCDAITVFKDGRYVA--TFDDM 225
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
92-316 |
2.09e-17 |
|
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: 84.07 E-value: 2.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 92 IIVLTLYYIGIGAAALIFGYVQISFWVITAARQTTRIRKQFFHSILAQDISWFDGSDICELNTRMTGDINKLCDGIGDKI 171
Cdd:cd18550 38 LVLLALGMVAVAVASALLGVVQTYLSARIGQGVMYDLRVQLYAHLQRMSLAFFTRTRTGEIQSRLNNDVGGAQSVVTGTL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 172 PLMFQNISGFSIGLVISLIKSWKLSLVVLSTSPLIMASSALCSRMIISLTSKELDAYSKAGAVAEEALS--SIQTVTAFG 249
Cdd:cd18550 118 TSVVSNVVTLVATLVAMLALDWRLALLSLVLLPLFVLPTRRVGRRRRKLTREQQEKLAELNSIMQETLSvsGALLVKLFG 197
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568980685 250 AQEKEIQRYTQHLKDAKDAGIKRATASKLSLGAVYFFMNGAYGLAFWYGTSLIFGGEPgyTIGTILA 316
Cdd:cd18550 198 REDDEAARFARRSRELRDLGVRQALAGRWFFAALGLFTAIGPALVYWVGGLLVIGGGL--TIGTLVA 262
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
377-593 |
2.64e-17 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 83.05 E-value: 2.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 377 FKNVSFS-YPsrpsakvlkglnlkikaGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDIRAQNV--------R 447
Cdd:PRK11701 22 CRDVSFDlYP-----------------GEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLyalseaerR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 448 H-YREQIGVVRQEP---VLFGTTIGNNIkfgregvGEKEMEQAARE-----ANAYDF----------IMAFPKKFntlvg 508
Cdd:PRK11701 85 RlLRTEWGFVHQHPrdgLRMQVSAGGNI-------GERLMAVGARHygdirATAGDWlerveidaarIDDLPTTF----- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 509 ekgaqmSGGQKQRIAIARALVRNPKILILDEATSALDTEseslVQTALEKASKGRTT------IVVAHRLSTIRG-ADLI 581
Cdd:PRK11701 153 ------SGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVS----VQARLLDLLRGLVRelglavVIVTHDLAVARLlAHRL 222
|
250
....*....|..
gi 568980685 582 VTMKDGMVVEKG 593
Cdd:PRK11701 223 LVMKQGRVVESG 234
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
1016-1232 |
2.90e-17 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 83.35 E-value: 2.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1016 RPEVPVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVKELNVQWlRSQTA-IVSQEPvlfNC 1094
Cdd:COG4167 23 RQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDYKY-RCKHIrMIFQDP---NT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1095 SIAENIAYGD--------NSRMVPLEEIKEVadaanihsfieglprkYNTL--VGLRGVQ-------LSGGQKQRLAIAR 1157
Cdd:COG4167 99 SLNPRLNIGQileeplrlNTDLTAEEREERI----------------FATLrlVGLLPEHanfyphmLSSGQKQRVALAR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1158 ALLRKPKILLLDEATSALDnesEKVVQQALD-----KARRGKTCLVVAHRLSTIQN-ADMIVVLQNGSIKEQGTHQELLR 1231
Cdd:COG4167 163 ALILQPKIIIADEALAALD---MSVRSQIINlmlelQEKLGISYIYVSQHLGIVKHiSDKVLVMHQGEVVEYGKTAEVFA 239
|
.
gi 568980685 1232 N 1232
Cdd:COG4167 240 N 240
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
379-623 |
3.56e-17 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 84.39 E-value: 3.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 379 NVSFSYPSRPSAKVlKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPE---DGCITVDENDI-----RAQNvRHYR 450
Cdd:PRK09473 19 RVTFSTPDGDVTAV-NDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNGREIlnlpeKELN-KLRA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 451 EQIGVVRQEPVlfgTTIGNNIKFGRE---------GVGEKE-------MEQAAREANAYDFIMAFPKKFntlvgekgaqm 514
Cdd:PRK09473 97 EQISMIFQDPM---TSLNPYMRVGEQlmevlmlhkGMSKAEafeesvrMLDAVKMPEARKRMKMYPHEF----------- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 515 SGGQKQRIAIARALVRNPKILILDEATSALDTESESLVQTALEKASKGRTT--IVVAHRLSTIRG-ADLIVTMKDGMVVE 591
Cdd:PRK09473 163 SGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTaiIMITHDLGVVAGiCDKVLVMYAGRTME 242
|
250 260 270
....*....|....*....|....*....|..
gi 568980685 592 KGTHAELMAKQGLYYSLAMAQDIKKVDEQMES 623
Cdd:PRK09473 243 YGNARDVFYQPSHPYSIGLLNAVPRLDAEGES 274
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1020-1170 |
4.35e-17 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 82.00 E-value: 4.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1020 PVLQNMSLSIEKGKTVAFVGSSGCGKSTCvqllqrFY------DPMKGQVLLDGVDVKELNVqWLRSQTAI--VSQEPVL 1091
Cdd:COG1137 17 TVVKDVSLEVNQGEIVGLLGPNGAGKTTT------FYmivglvKPDSGRIFLDGEDITHLPM-HKRARLGIgyLPQEASI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1092 F-NCSIAENIaygdnsRMV------PLEEIKEVADAAnIHSF-IEGLpRKYntlvglRGVQLSGGQKQRLAIARALLRKP 1163
Cdd:COG1137 90 FrKLTVEDNI------LAVlelrklSKKEREERLEEL-LEEFgITHL-RKS------KAYSLSGGERRRVEIARALATNP 155
|
....*..
gi 568980685 1164 KILLLDE 1170
Cdd:COG1137 156 KFILLDE 162
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
388-591 |
4.61e-17 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 86.00 E-value: 4.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 388 PSAKVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYdPE---DGCITVDEN-----DIRAQnvrhyrEQIGVV--R 457
Cdd:NF040905 12 PGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PHgsyEGEILFDGEvcrfkDIRDS------EALGIViiH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 458 QE----PVLfgtTIGNNIKFGRE----GVGE-KEMEQAAREanaydfIMA------FPkkfNTLVGEKGAqmsgGQKQRI 522
Cdd:NF040905 85 QElaliPYL---SIAENIFLGNErakrGVIDwNETNRRARE------LLAkvgldeSP---DTLVTDIGV----GKQQLV 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568980685 523 AIARALVRNPKILILDEATSAL-DTESESLVQTALEKASKGRTTIVVAHRLSTIRG-ADLIVTMKDGMVVE 591
Cdd:NF040905 149 EIAKALSKDVKLLILDEPTAALnEEDSAALLDLLLELKAQGITSIIISHKLNEIRRvADSITVLRDGRTIE 219
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1021-1231 |
6.96e-17 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 85.53 E-value: 6.96e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1021 VLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYdPMKGQVLLDGVDVKELNVQWL---RSQTAIVSQEPvlfNCSIa 1097
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLHNLNRRQLlpvRHRIQVVFQDP---NSSL- 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1098 eniaygdNSRMVPLEEIKEvadaanihsfieGLPRKYNTL---------------VGLRGV-------QLSGGQKQRLAI 1155
Cdd:PRK15134 376 -------NPRLNVLQIIEE------------GLRVHQPTLsaaqreqqviavmeeVGLDPEtrhrypaEFSGGQRQRIAI 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1156 ARALLRKPKILLLDEATSALDneseKVVQQ---ALDKA---RRGKTCLVVAHRLSTIQN-ADMIVVLQNGSIKEQGTHQE 1228
Cdd:PRK15134 437 ARALILKPSLIILDEPTSSLD----KTVQAqilALLKSlqqKHQLAYLFISHDLHVVRAlCHQVIVLRQGEVVEQGDCER 512
|
...
gi 568980685 1229 LLR 1231
Cdd:PRK15134 513 VFA 515
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
374-601 |
7.38e-17 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 83.74 E-value: 7.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 374 NIEFKNVSFSYPSRpsAKVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDIraqNVRHYREQ- 452
Cdd:PRK11650 3 GLKLQAVRKSYDGK--TQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVV---NELEPADRd 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 453 IGVVRQEPVLF-GTTIGNNIKFG---ReGVGEKEMEQAAREAnaydfimAFPKKFNTLVGEKGAQMSGGQKQRIAIARAL 528
Cdd:PRK11650 78 IAMVFQNYALYpHMSVRENMAYGlkiR-GMPKAEIEERVAEA-------ARILELEPLLDRKPRELSGGQRQRVAMGRAI 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568980685 529 VRNPKILILDEATSALDTeseSL-VQTALE----KASKGRTTIVVAH-RLSTIRGADLIVTMKDGMVVEKGTHAELMAK 601
Cdd:PRK11650 150 VREPAVFLFDEPLSNLDA---KLrVQMRLEiqrlHRRLKTTSLYVTHdQVEAMTLADRVVVMNGGVAEQIGTPVEVYEK 225
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1004-1232 |
7.79e-17 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 81.46 E-value: 7.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1004 LEFREVSFVYPcrpEVPVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVKEL-NVQWLRSQT 1082
Cdd:PRK11614 6 LSFDKVSAHYG---KIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWqTAKIMREAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1083 AIVSQEPVLFN-CSIAENIAYGD--NSRMVPLEEIKEVADAanihsfiegLPRKYNTLVGLRGVqLSGGQKQRLAIARAL 1159
Cdd:PRK11614 83 AIVPEGRRVFSrMTVEENLAMGGffAERDQFQERIKWVYEL---------FPRLHERRIQRAGT-MSGGEQQMLAIGRAL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568980685 1160 LRKPKILLLDEATSALdneSEKVVQQALDKARR----GKTCLVVAHRLS-TIQNADMIVVLQNGSIKEQGTHQELLRN 1232
Cdd:PRK11614 153 MSQPRLLLLDEPSLGL---APIIIQQIFDTIEQlreqGMTIFLVEQNANqALKLADRGYVLENGHVVLEDTGDALLAN 227
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
379-594 |
8.64e-17 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 85.68 E-value: 8.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 379 NVSFSYPSRPSAKVlKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDIRAQN------------- 445
Cdd:PRK10261 19 NIAFMQEQQKIAAV-RNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRSrqvielseqsaaq 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 446 VRHYR-EQIGVVRQEPVL-------FGTTIGNNIKFgREGVGEkemEQAAREANAYDFIMAFPKKfNTLVGEKGAQMSGG 517
Cdd:PRK10261 98 MRHVRgADMAMIFQEPMTslnpvftVGEQIAESIRL-HQGASR---EEAMVEAKRMLDQVRIPEA-QTILSRYPHQLSGG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 518 QKQRIAIARALVRNPKILILDEATSALDTESES----LVQTALEKASKGrtTIVVAHRLSTIRG-ADLIVTMKDGMVVEK 592
Cdd:PRK10261 173 MRQRVMIAMALSCRPAVLIADEPTTALDVTIQAqilqLIKVLQKEMSMG--VIFITHDMGVVAEiADRVLVMYQGEAVET 250
|
..
gi 568980685 593 GT 594
Cdd:PRK10261 251 GS 252
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
375-594 |
9.59e-17 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 81.28 E-value: 9.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 375 IEFKNVSFSYPSRPSAK-------------------VLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCIT 435
Cdd:COG1134 5 IEVENVSKSYRLYHEPSrslkelllrrrrtrreefwALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 436 VDENdIRAqnvrhyreqigvvrqepvLFGTTIGNNIKF-GRE---------GVGEKEMEQaareanAYDFIMAF---PKK 502
Cdd:COG1134 85 VNGR-VSA------------------LLELGAGFHPELtGREniylngrllGLSRKEIDE------KFDEIVEFaelGDF 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 503 FNTLVGekgaQMSGGQKQRIAIARALVRNPKILILDEATSALDTE----SESLVQtalEKASKGRTTIVVAHRLSTIRG- 577
Cdd:COG1134 140 IDQPVK----TYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAfqkkCLARIR---ELRESGRTVIFVSHSMGAVRRl 212
|
250
....*....|....*..
gi 568980685 578 ADLIVTMKDGMVVEKGT 594
Cdd:COG1134 213 CDRAIWLEKGRLVMDGD 229
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
1017-1243 |
1.10e-16 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 81.28 E-value: 1.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1017 PEVPVLQNMSLSIEKGKTVAFVGSSGCGKS-TCVQLLQRFydP-----MKGQVLLDGvdvKELNVQWLRSQT-AIVSQEP 1089
Cdd:PRK10418 14 AAQPLVHGVSLTLQRGRVLALVGGSGSGKSlTCAAALGIL--PagvrqTAGRVLLDG---KPVAPCALRGRKiATIMQNP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1090 -VLFNcsIAENIAygDNSRMVPLEEIKEVADAANIHSFIE-GLPRKyNTLVGLRGVQLSGGQKQRLAIARALLRKPKILL 1167
Cdd:PRK10418 89 rSAFN--PLHTMH--THARETCLALGKPADDATLTAALEAvGLENA-ARVLKLYPFEMSGGMLQRMMIALALLCEAPFII 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1168 LDEATSALDnesekVVQQA--LD-----KARRGKTCLVVAHRLSTIQN-ADMIVVLQNGSIKEQGTHQELLRN--GDTYF 1237
Cdd:PRK10418 164 ADEPTTDLD-----VVAQAriLDllesiVQKRALGMLLVTHDMGVVARlADDVAVMSHGRIVEQGDVETLFNApkHAVTR 238
|
....*.
gi 568980685 1238 KLVAAH 1243
Cdd:PRK10418 239 SLVSAH 244
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
1021-1230 |
1.11e-16 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 81.57 E-value: 1.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1021 VLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVKELNVQWLRSQTAIVSQEPVL-FNCSIAEN 1099
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTpGDITVQEL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1100 IAYGDNSRMvPL--EEIKEVADAANIHSFIEGLprkynTLVGLRGVQ-LSGGQKQRLAIARALLRKPKILLLDEATSALD 1176
Cdd:PRK10253 102 VARGRYPHQ-PLftRWRKEDEEAVTKAMQATGI-----THLADQSVDtLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLD 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 568980685 1177 NESEKVVQQALDKARR--GKTCLVVAHRLS-TIQNADMIVVLQNGSIKEQGTHQELL 1230
Cdd:PRK10253 176 ISHQIDLLELLSELNRekGYTLAAVLHDLNqACRYASHLIALREGKIVAQGAPKEIV 232
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
390-587 |
1.15e-16 |
|
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: 79.40 E-value: 1.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 390 AKVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDIRAQNVRHYREQ-IGVV---RQepvlfgt 465
Cdd:cd03215 13 KGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAgIAYVpedRK------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 466 tignnikfgREGVgekemeqaareanaydfIMAFPKKFNTLVGekgAQMSGGQKQRIAIARALVRNPKILILDEATSALD 545
Cdd:cd03215 86 ---------REGL-----------------VLDLSVAENIALS---SLLSGGNQQKVVLARWLARDPRVLILDEPTRGVD 136
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 568980685 546 TES-ESLVQTALEKASKGRTTIVVAHRLSTIRG-ADLIVTMKDG 587
Cdd:cd03215 137 VGAkAEIYRLIRELADAGKAVLLISSELDELLGlCDRILVMYEG 180
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
392-600 |
1.35e-16 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 84.76 E-value: 1.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 392 VLKGLNLKIKAGETVALVGPSGSGKS-TTVQLLQRLYDPEdgcITVDENDIR----------AQNVRHYR-EQIGVVRQE 459
Cdd:PRK15134 24 VVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPP---VVYPSGDIRfhgesllhasEQTLRGVRgNKIAMIFQE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 460 PVLFGTTIGNNIK-----------FGREG-----------VGekeMEQAAREANAYdfimafPKkfntlvgekgaQMSGG 517
Cdd:PRK15134 101 PMVSLNPLHTLEKqlyevlslhrgMRREAargeilncldrVG---IRQAAKRLTDY------PH-----------QLSGG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 518 QKQRIAIARALVRNPKILILDEATSALDTESESLVQTALE--KASKGRTTIVVAHRLSTIRG-ADLIVTMKDGMVVEKGT 594
Cdd:PRK15134 161 ERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRelQQELNMGLLFITHNLSIVRKlADRVAVMQNGRCVEQNR 240
|
....*.
gi 568980685 595 HAELMA 600
Cdd:PRK15134 241 AATLFS 246
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
389-587 |
1.38e-16 |
|
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: 84.49 E-value: 1.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 389 SAKVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYdPE---DGCITVDENDIRAQNVRHYREQ-IGVVRQEPVLF- 463
Cdd:TIGR02633 13 GVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVY-PHgtwDGEIYWSGSPLKASNIRDTERAgIVIIHQELTLVp 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 464 GTTIGNNIKFGRE------GVGEKEMEQAAREANAYDFIMAFPkkfNTL-VGEKGaqmsGGQKQRIAIARALVRNPKILI 536
Cdd:TIGR02633 92 ELSVAENIFLGNEitlpggRMAYNAMYLRAKNLLRELQLDADN---VTRpVGDYG----GGQQQLVEIAKALNKQARLLI 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 568980685 537 LDEATSAL-DTESESLVQTALEKASKGRTTIVVAHRLSTIRG-ADLIVTMKDG 587
Cdd:TIGR02633 165 LDEPSSSLtEKETEILLDIIRDLKAHGVACVYISHKLNEVKAvCDTICVIRDG 217
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
991-1230 |
1.43e-16 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 82.57 E-value: 1.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 991 SQSGEKPDTCegnLEFREVSFVYPCRPevpVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDV 1070
Cdd:PRK13536 32 SIPGSMSTVA---IDLAGVSKSYGDKA---VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1071 KElNVQWLRSQTAIVSQEPVL-FNCSIAEN-IAYGDNSRMvPLEEIKEVadaanIHSFIE--GLPRKYNTLVGlrgvQLS 1146
Cdd:PRK13536 106 PA-RARLARARIGVVPQFDNLdLEFTVRENlLVFGRYFGM-STREIEAV-----IPSLLEfaRLESKADARVS----DLS 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1147 GGQKQRLAIARALLRKPKILLLDEATSALDNESEKVVQQALDK-ARRGKTCLVVAHRLSTIQN-ADMIVVLQNGSIKEQG 1224
Cdd:PRK13536 175 GGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSlLARGKTILLTTHFMEEAERlCDRLCVLEAGRKIAEG 254
|
....*.
gi 568980685 1225 THQELL 1230
Cdd:PRK13536 255 RPHALI 260
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
392-569 |
1.47e-16 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 79.53 E-value: 1.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 392 VLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDIRAQNVR---HYreqIGvvRQE---PVLfgt 465
Cdd:PRK13539 17 LFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAeacHY---LG--HRNamkPAL--- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 466 TIGNNIKFGREGVGEKEmEQAAREANAYDFIMAFPKKFNTLvgekgaqmSGGQKQRIAIARALVRNPKILILDEATSALD 545
Cdd:PRK13539 89 TVAENLEFWAAFLGGEE-LDIAAALEAVGLAPLAHLPFGYL--------SAGQKRRVALARLLVSNRPIWILDEPTAALD 159
|
170 180
....*....|....*....|....
gi 568980685 546 TESESLVQTALEKASKGRTTIVVA 569
Cdd:PRK13539 160 AAAVALFAELIRAHLAQGGIVIAA 183
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1004-1206 |
1.62e-16 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 79.92 E-value: 1.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1004 LEFREVSFVYPCRPEVpvLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVKELN---VQWLRS 1080
Cdd:PRK10908 2 IRFEHVSKAYLGGRQA--LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKnreVPFLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1081 QTAIVSQEP-VLFNCSIAENIAygdnsrmVPLeeIKEVADAANIHSFIEGLPRKYNTLVGLRG--VQLSGGQKQRLAIAR 1157
Cdd:PRK10908 80 QIGMIFQDHhLLMDRTVYDNVA-------IPL--IIAGASGDDIRRRVSAALDKVGLLDKAKNfpIQLSGGEQQRVGIAR 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 568980685 1158 ALLRKPKILLLDEATSALDNE-SEKVVQQALDKARRGKTCLVVAHRLSTI 1206
Cdd:PRK10908 151 AVVNKPAVLLADEPTGNLDDAlSEGILRLFEEFNRVGVTVLMATHDIGLI 200
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
365-669 |
1.66e-16 |
|
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: 85.84 E-value: 1.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 365 GFVPE-CIEGNIEFknvsFSYPSRPSakvLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDIRA 443
Cdd:TIGR01257 924 GLVPGvCVKNLVKI----FEPSGRPA---VDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET 996
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 444 qNVRHYREQIGVVRQEPVLFG-TTIGNNIKFGREGVGeKEMEQAAREANAYDFIMAFPKKFNtlvgEKGAQMSGGQKQRI 522
Cdd:TIGR01257 997 -NLDAVRQSLGMCPQHNILFHhLTVAEHILFYAQLKG-RSWEEAQLEMEAMLEDTGLHHKRN----EEAQDLSGGMQRKL 1070
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 523 AIARALVRNPKILILDEATSALDTESESLVQTALEKASKGRTTIVVAHRL--STIRGaDLIVTMKDGMVVEKGTHAELMA 600
Cdd:TIGR01257 1071 SVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMdeADLLG-DRIAIISQGRLYCSGTPLFLKN 1149
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568980685 601 KQGLYYSLAMAQDIKKVDEQMESR----TCSTAGNASYGSLCDVNSAKAPCTD----QLEEAVHHQktsLPEVSLLK 669
Cdd:TIGR01257 1150 CFGTGFYLTLVRKMKNIQSQRGGCegtcSCTSKGFSTRCPARVDEITPEQVLDgdvnELMDLVYHH---VPEAKLVE 1223
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
1021-1230 |
2.43e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 80.91 E-value: 2.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1021 VLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKG-----QVLLDGVDV-KELNVQWLRSQTAIVSQEPVLFNC 1094
Cdd:PRK14271 36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIfNYRDVLEFRRRVGMLFQRPNPFPM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1095 SIAENIAYGDNS-RMVPLEEIKEVADAANIHSfieGLPRKYNTLVGLRGVQLSGGQKQRLAIARALLRKPKILLLDEATS 1173
Cdd:PRK14271 116 SIMDNVLAGVRAhKLVPRKEFRGVAQARLTEV---GLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTS 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 568980685 1174 ALDNESEKVVQQALDKARRGKTCLVVAHRLSTIQN-ADMIVVLQNGSIKEQGTHQELL 1230
Cdd:PRK14271 193 ALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARiSDRAALFFDGRLVEEGPTEQLF 250
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
1018-1202 |
2.51e-16 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 79.23 E-value: 2.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1018 EVPVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRfydPMKGQVLLDGVDVKELnvQWLRsqtaivsqepvlfNCSIA 1097
Cdd:COG2401 42 ERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAG---ALKGTPVAGCVDVPDN--QFGR-------------EASLI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1098 ENIAygdnsRMVPLEEIKEV------ADAANihsfiegLPRKYNtlvglrgvQLSGGQKQRLAIARALLRKPKILLLDEA 1171
Cdd:COG2401 104 DAIG-----RKGDFKDAVELlnavglSDAVL-------WLRRFK--------ELSTGQKFRFRLALLLAERPKLLVIDEF 163
|
170 180 190
....*....|....*....|....*....|...
gi 568980685 1172 TSALDNESEKVVQQALDKA--RRGKTCLVVAHR 1202
Cdd:COG2401 164 CSHLDRQTAKRVARNLQKLarRAGITLVVATHH 196
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
375-604 |
2.54e-16 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 79.92 E-value: 2.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 375 IEFKNVSFSYPSrpsAKVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDIRA-QNVRHYREQI 453
Cdd:PRK11614 6 LSFDKVSAHYGK---IQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDwQTAKIMREAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 454 GVVRQEPVLFG-TTIGNNIKFGREGVGEKEMEQaaREANAYDFimaFPKKFNTLVGEKGAqMSGGQKQRIAIARALVRNP 532
Cdd:PRK11614 83 AIVPEGRRVFSrMTVEENLAMGGFFAERDQFQE--RIKWVYEL---FPRLHERRIQRAGT-MSGGEQQMLAIGRALMSQP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568980685 533 KILILDEATSAL-DTESESLVQTALEKASKGRTTIVVAHRLS-TIRGADLIVTMKDGMVVEKGTHAELMAKQGL 604
Cdd:PRK11614 157 RLLLLDEPSLGLaPIIIQQIFDTIEQLREQGMTIFLVEQNANqALKLADRGYVLENGHVVLEDTGDALLANEAV 230
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
375-601 |
3.41e-16 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 83.48 E-value: 3.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 375 IEFKNVSFSYPSRPSAkvLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDIRAQNVRHYREQIG 454
Cdd:PRK10522 323 LELRNVTFAYQDNGFS--VGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFS 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 455 VVRQEPVLFGTTIGnnikfgregvgeKEMEQAAREanAYDFIMAFPKKFNTLVGEKG----AQMSGGQKQRIAIARALVR 530
Cdd:PRK10522 401 AVFTDFHLFDQLLG------------PEGKPANPA--LVEKWLERLKMAHKLELEDGrisnLKLSKGQKKRLALLLALAE 466
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568980685 531 NPKILILDEATSALDTESESLVQTAL--EKASKGRTTIVVAHRLSTIRGADLIVTMKDGMVVE-KGTHAELMAK 601
Cdd:PRK10522 467 ERDILLLDEWAADQDPHFRREFYQVLlpLLQEMGKTIFAISHDDHYFIHADRLLEMRNGQLSElTGEERDAASR 540
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1004-1218 |
3.57e-16 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 83.04 E-value: 3.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1004 LEFREVSFVYPcrpEVPVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVKELNVQ-WLRSQT 1082
Cdd:PRK11288 5 LSFDGIGKTFP---GVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTaALAAGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1083 AIVSQE----PVLfncSIAENIAYG---------DNSRMVP-----LEEIKEVADAAnihsfiegLPRKYntlvglrgvq 1144
Cdd:PRK11288 82 AIIYQElhlvPEM---TVAENLYLGqlphkggivNRRLLNYeareqLEHLGVDIDPD--------TPLKY---------- 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568980685 1145 LSGGQKQRLAIARALLRKPKILLLDEATSALD-NESE---KVVQQALDKarrGKTCLVVAHRLSTI-QNADMIVVLQNG 1218
Cdd:PRK11288 141 LSIGQRQMVEIAKALARNARVIAFDEPTSSLSaREIEqlfRVIRELRAE---GRVILYVSHRMEEIfALCDAITVFKDG 216
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
681-955 |
4.18e-16 |
|
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: 80.16 E-value: 4.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 681 VVLGTLASALNGSVHPVFSIIFGKLV-TMFEDKNKATLKqdaeLYSMMLVVLGIVALVTYLMQGLFYGRAEENLAMRLRH 759
Cdd:cd18552 1 LALAILGMILVAATTAALAWLLKPLLdDIFVEKDLEALL----LVPLAIIGLFLLRGLASYLQTYLMAYVGQRVVRDLRN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 760 SAFKAMLYQDMAWYDdkENNTGALTTTLAVDVAQIQGAATSRLGIVTQDvsnmSLSILISFIY----GWEMTLLILSFAP 835
Cdd:cd18552 77 DLFDKLLRLPLSFFD--RNSSGDLISRITNDVNQVQNALTSALTVLVRD----PLTVIGLLGVlfylDWKLTLIALVVLP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 836 VLAVtgmiqtaAMAGFANRdkqaLKRAGK-----------IATEAVENIRTVVSLTRERAFEQMYEETLQTQHRNALKRA 904
Cdd:cd18552 151 LAAL-------PIRRIGKR----LRKISRrsqesmgdltsVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIA 219
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 568980685 905 HITgccyAVSHAFVHFAHAAGF----RFGAYLIQAGRMMPeGMFIVFTAIAYGAM 955
Cdd:cd18552 220 RAR----ALSSPLMELLGAIAIalvlWYGGYQVISGELTP-GEFISFITALLLLY 269
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
375-593 |
4.53e-16 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 78.73 E-value: 4.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 375 IEFKNVSFSYPS------------RPSAK-------VLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCIT 435
Cdd:cd03220 1 IELENVSKSYPTykggssslkklgILGRKgevgefwALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 436 VDeNDIRAqnvrhyreqigvvrqepvLFGTTIG--------NNIKF-GRE-GVGEKEMEQaareanAYDFIMAF---PKK 502
Cdd:cd03220 81 VR-GRVSS------------------LLGLGGGfnpeltgrENIYLnGRLlGLSRKEIDE------KIDEIIEFselGDF 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 503 FNTLVGEkgaqMSGGQKQRIAIARALVRNPKILILDEATSALDtesESLVQTAL----EKASKGRTTIVVAHRLSTIRG- 577
Cdd:cd03220 136 IDLPVKT----YSSGMKARLAFAIATALEPDILLIDEVLAVGD---AAFQEKCQrrlrELLKQGKTVILVSHDPSSIKRl 208
|
250
....*....|....*.
gi 568980685 578 ADLIVTMKDGMVVEKG 593
Cdd:cd03220 209 CDRALVLEKGKIRFDG 224
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1017-1218 |
4.69e-16 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 82.67 E-value: 4.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1017 PEVPVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYdP---MKGQVLLDGVDVKELNVQWL-RSQTAIVSQEPVLF 1092
Cdd:PRK13549 16 GGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PhgtYEGEIIFEGEELQASNIRDTeRAGIAIIHQELALV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1093 -NCSIAENIAYGdnsrmvplEEIKE--VADAANIHSFIEGLPR--KYNTLVGLRGVQLSGGQKQRLAIARALLRKPKILL 1167
Cdd:PRK13549 95 kELSVLENIFLG--------NEITPggIMDYDAMYLRAQKLLAqlKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLI 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 568980685 1168 LDEATSALdNESEKVVQQAL--DKARRGKTCLVVAHRLSTIQN-ADMIVVLQNG 1218
Cdd:PRK13549 167 LDEPTASL-TESETAVLLDIirDLKAHGIACIYISHKLNEVKAiSDTICVIRDG 219
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
392-599 |
4.93e-16 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 79.65 E-value: 4.93e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 392 VLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDIRAQNVRHYREQIGVVRQEPVLFG-TTIGNN 470
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTPGdITVQEL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 471 IKFGRE------GVGEKEMEQAAREANAYDFImafpkkfNTLVGEKGAQMSGGQKQRIAIARALVRNPKILILDEATSAL 544
Cdd:PRK10253 102 VARGRYphqplfTRWRKEDEEAVTKAMQATGI-------THLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 568980685 545 DTESE-SLVQTALE-KASKGRTTIVVAHRLS-TIRGADLIVTMKDGMVVEKGTHAELM 599
Cdd:PRK10253 175 DISHQiDLLELLSElNREKGYTLAAVLHDLNqACRYASHLIALREGKIVAQGAPKEIV 232
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
1004-1218 |
5.14e-16 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 76.33 E-value: 5.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1004 LEFREVSFVYPCRPevpVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLqrfydpmkgqvlldgvdvkelnvqwlrsqta 1083
Cdd:cd03221 1 IELENLSKTYGGKL---LLKDISLTINPGDRIGLVGRNGAGKSTLLKLI------------------------------- 46
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1084 ivsqepvlfncsiaeniaygdNSRMVPLEEIKEVADAANIHSFieglprkyntlvglrgVQLSGGQKQRLAIARALLRKP 1163
Cdd:cd03221 47 ---------------------AGELEPDEGIVTWGSTVKIGYF----------------EQLSGGEKMRLALAKLLLENP 89
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 568980685 1164 KILLLDEATSALDNESEKVVQQALdKARRGkTCLVVAHRLSTIQN-ADMIVVLQNG 1218
Cdd:cd03221 90 NLLLLDEPTNHLDLESIEALEEAL-KEYPG-TVILVSHDRYFLDQvATKIIELEDG 143
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
375-601 |
5.40e-16 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 82.54 E-value: 5.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 375 IEFKNVSFSYPSRpsaKVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRL--YDPEDG-----------CITVD---- 437
Cdd:TIGR03269 1 IEVKNLTKKFDGK---EVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGriiyhvalcekCGYVErpsk 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 438 --------ENDIRAQNV----------RHYREQIGVVRQEP-VLFGT-TIGNNIKFGREGVGEKEMEQAAREANAYDFIm 497
Cdd:TIGR03269 78 vgepcpvcGGTLEPEEVdfwnlsdklrRRIRKRIAIMLQRTfALYGDdTVLDNVLEALEEIGYEGKEAVGRAVDLIEMV- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 498 afpkKFNTLVGEKGAQMSGGQKQRIAIARALVRNPKILILDEATSALDTESESLVQTALEKASK--GRTTIVVAHRLSTI 575
Cdd:TIGR03269 157 ----QLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKasGISMVLTSHWPEVI 232
|
250 260
....*....|....*....|....*..
gi 568980685 576 RG-ADLIVTMKDGMVVEKGTHAELMAK 601
Cdd:TIGR03269 233 EDlSDKAIWLENGEIKEEGTPDEVVAV 259
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1017-1219 |
6.15e-16 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 82.52 E-value: 6.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1017 PEVPVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVKELNVQwLRSQ--TAIVSQE-PVLFN 1093
Cdd:PRK09700 16 GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHK-LAAQlgIGIIYQElSVIDE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1094 CSIAENIAYGdnsRM-------VPLEEIKEVADAANIHSFIEGLPRKYNTLVGlrgvQLSGGQKQRLAIARALLRKPKIL 1166
Cdd:PRK09700 95 LTVLENLYIG---RHltkkvcgVNIIDWREMRVRAAMMLLRVGLKVDLDEKVA----NLSISHKQMLEIAKTLMLDAKVI 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 568980685 1167 LLDEATSALDNESEKVVQQALDKARR-GKTCLVVAHRLSTIQN-ADMIVVLQNGS 1219
Cdd:PRK09700 168 IMDEPTSSLTNKEVDYLFLIMNQLRKeGTAIVYISHKLAEIRRiCDRYTVMKDGS 222
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
1022-1229 |
7.02e-16 |
|
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: 78.18 E-value: 7.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1022 LQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDV-KE-LNVqwlRSQTAIVSQEPVLFNCSIA-E 1098
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVvREpREV---RRRIGIVFQDLSVDDELTGwE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1099 NIA-----YGdNSRMVPLEEIKEVADAANIHSFIEGLPRKYntlvglrgvqlSGGQKQRLAIARALLRKPKILLLDEATS 1173
Cdd:cd03265 93 NLYiharlYG-VPGAERRERIDELLDFVGLLEAADRLVKTY-----------SGGMRRRLEIARSLVHRPEVLFLDEPTI 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 568980685 1174 ALDNESEKVVQQALDK--ARRGKTCLVVAHRLSTI-QNADMIVVLQNGSIKEQGTHQEL 1229
Cdd:cd03265 161 GLDPQTRAHVWEYIEKlkEEFGMTILLTTHYMEEAeQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
88-591 |
7.78e-16 |
|
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: 82.15 E-value: 7.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 88 LNEDIIVLTLYYIGIGAAALIFGYVQ-ISFWVITAARQTT--RIRKQFFHSILAQDISWFDGSDICELNTRMTGDINKLC 164
Cdd:COG4615 40 LNATGAALARLLLLFAGLLVLLLLSRlASQLLLTRLGQHAvaRLRLRLSRRILAAPLERLERIGAARLLAALTEDVRTIS 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 165 DGigdkiplmFQNISGFSIGLVISL-------IKSWKLSLVVLSTSPLIMASSALCSRMIISLTSKELDAyskagavaEE 237
Cdd:COG4615 120 QA--------FVRLPELLQSVALVLgclaylaWLSPPLFLLTLVLLGLGVAGYRLLVRRARRHLRRAREA--------ED 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 238 AL-SSIQTVTAfGAQEKEIQR------YTQHLKDAkdagIKRATASKLsLGAVYFFMNGAYGLAFWYGTS-LIFGGEPGY 309
Cdd:COG4615 184 RLfKHFRALLE-GFKELKLNRrrrrafFDEDLQPT----AERYRDLRI-RADTIFALANNWGNLLFFALIgLILFLLPAL 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 310 T-------IGTILAVFFSVIHSSYCIGSvaphLETFTVARGAAFNI---FQVIDKKPNIDNFSTAGFVPECIEGnIEFKN 379
Cdd:COG4615 258 GwadpavlSGFVLVLLFLRGPLSQLVGA----LPTLSRANVALRKIeelELALAAAEPAAADAAAPPAPADFQT-LELRG 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 380 VSFSYPSRPSAK--VLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDIRAQNVRHYREQIGVVR 457
Cdd:COG4615 333 VTYRYPGEDGDEgfTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQLFSAVF 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 458 QEPVLFGTTIGNNIKFGREGVGEK----EMEQAAREANaydfimafpKKFNTLvgekgaQMSGGQKQRIAIARALVRNPK 533
Cdd:COG4615 413 SDFHLFDRLLGLDGEADPARARELlerlELDHKVSVED---------GRFSTT------DLSQGQRKRLALLVALLEDRP 477
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568980685 534 ILILDEATSALD--------TEsesLVQtALeKAsKGRTTIVVAH-----RLstirgADLIVTMKDGMVVE 591
Cdd:COG4615 478 ILVFDEWAADQDpefrrvfyTE---LLP-EL-KA-RGKTVIAISHddryfDL-----ADRVLKMDYGKLVE 537
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
1015-1230 |
8.96e-16 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 82.40 E-value: 8.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1015 CRPEVPVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQrFYDP--MKGQ--VLLDGVDVkelNVQWLRSQTAIVSQEPV 1090
Cdd:TIGR00955 34 ERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALA-FRSPkgVKGSgsVLLNGMPI---DAKEMRAISAYVQQDDL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1091 LF-NCSIAENIAYGDNSRM-------VPLEEIKEVADAAnihsfieGLPRKYNTLVGLRGVQ--LSGGQKQRLAIARALL 1160
Cdd:TIGR00955 110 FIpTLTVREHLMFQAHLRMprrvtkkEKRERVDEVLQAL-------GLRKCANTRIGVPGRVkgLSGGERKRLAFASELL 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568980685 1161 RKPKILLLDEATSALDNESEKVVQQALDK-ARRGKTCLVVAHRLST--IQNADMIVVLQNGSIKEQGTHQELL 1230
Cdd:TIGR00955 183 TDPPLLFCDEPTSGLDSFMAYSVVQVLKGlAQKGKTIICTIHQPSSelFELFDKIILMAEGRVAYLGSPDQAV 255
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1021-1220 |
1.05e-15 |
|
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: 76.32 E-value: 1.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1021 VLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVKelnvqwLRSQTAivsqepvlfncSIAENI 1100
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVT------RRSPRD-----------AIRAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1101 AYgdnsrmVPlEEIKEvadaaniHSFIEGLPRKYNTLVGlrgVQLSGGQKQRLAIARALLRKPKILLLDEATSALDNES- 1179
Cdd:cd03215 78 AY------VP-EDRKR-------EGLVLDLSVAENIALS---SLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAk 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 568980685 1180 EKVVQQALDKARRGKTCLVVahrlST-----IQNADMIVVLQNGSI 1220
Cdd:cd03215 141 AEIYRLIRELADAGKAVLLI----SSeldelLGLCDRILVMYEGRI 182
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
387-598 |
1.06e-15 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 82.02 E-value: 1.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 387 RPSAKVLKGLNLKIKAGETVALVGPSGSGKSTtvqLLQRL--YDPED----GCITVDEndiRAQNVRHYREQIGVVRQEP 460
Cdd:TIGR00955 35 RPRKHLLKNVSGVAKPGELLAVMGSSGAGKTT---LMNALafRSPKGvkgsGSVLLNG---MPIDAKEMRAISAYVQQDD 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 461 VLFGT-------TIGNNIKFGREGVGEKEME--QAAREAnaydfiMAFPKKFNTLVGEKGAQ--MSGGQKQRIAIARALV 529
Cdd:TIGR00955 109 LFIPTltvrehlMFQAHLRMPRRVTKKEKRErvDEVLQA------LGLRKCANTRIGVPGRVkgLSGGERKRLAFASELL 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568980685 530 RNPKILILDEATSALDTES-ESLVQTALEKASKGRTTIVVAHRLST--IRGADLIVTMKDGMVVEKGTHAEL 598
Cdd:TIGR00955 183 TDPPLLFCDEPTSGLDSFMaYSVVQVLKGLAQKGKTIICTIHQPSSelFELFDKIILMAEGRVAYLGSPDQA 254
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
393-604 |
1.07e-15 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 78.34 E-value: 1.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 393 LKGLNLKIKAGETVALVGPSGSGKSTtvqLLQRLYD--PEDGCITVDENDIRAQNVRHYREQIGVVRQE-PVLFGTTIGN 469
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKST---LLARMAGllPGQGEILLNGRPLSDWSAAELARHRAYLSQQqSPPFAMPVFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 470 NIKFGREGVGEKEMEQAAREANAYDFIMAfpKKFNTLVGekgaQMSGGQKQRIAIARALVR-----NP--KILILDEATS 542
Cdd:COG4138 89 YLALHQPAGASSEAVEQLLAQLAEALGLE--DKLSRPLT----QLSGGEWQRVRLAAVLLQvwptiNPegQLLLLDEPMN 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568980685 543 ALDTESESLVQTALEK-ASKGRTTIVVAHRLS-TIRGADLIVTMKDGMVVEKGTHAELMAKQGL 604
Cdd:COG4138 163 SLDVAQQAALDRLLRElCQQGITVVMSSHDLNhTLRHADRVWLLKQGKLVASGETAEVMTPENL 226
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1018-1231 |
1.11e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 79.00 E-value: 1.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1018 EVPVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGvdvkelnvqwlrsqtaivsqEPvlFNCSIA 1097
Cdd:COG4152 13 DKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDG--------------------EP--LDPEDR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1098 ENIAY-----GDNSRM--------------VPLEEIKEVADAanihsFIE--GLPRKYNTLVGlrgvQLSGGQKQRLAIA 1156
Cdd:COG4152 71 RRIGYlpeerGLYPKMkvgeqlvylarlkgLSKAEAKRRADE-----WLErlGLGDRANKKVE----ELSKGNQQKVQLI 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568980685 1157 RALLRKPKILLLDEATSALD--NeSEKVVQQALDKARRGKTCLVVAHRLSTIQN-ADMIVVLQNGSIKEQGTHQELLR 1231
Cdd:COG4152 142 AALLHDPELLILDEPFSGLDpvN-VELLKDVIRELAAKGTTVIFSSHQMELVEElCDRIVIINKGRKVLSGSVDEIRR 218
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
1004-1222 |
1.25e-15 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 81.56 E-value: 1.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1004 LEFREVSFVYPCRP-EV-PVlqnmSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVKELNVQWLRSQ 1081
Cdd:PRK10522 323 LELRNVTFAYQDNGfSVgPI----NLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKL 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1082 TAIVSQEPVLFncsiaeniaygdnSRMvpLEEIKEVADAANIHSFIEGLPRKYN-TLVGLR--GVQLSGGQKQRLAIARA 1158
Cdd:PRK10522 399 FSAVFTDFHLF-------------DQL--LGPEGKPANPALVEKWLERLKMAHKlELEDGRisNLKLSKGQKKRLALLLA 463
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568980685 1159 LLRKPKILLLDEATSALDNESEKVVQQALDKARR--GKTCLVVAHRLSTIQNADMIVVLQNGSIKE 1222
Cdd:PRK10522 464 LAEERDILLLDEWAADQDPHFRREFYQVLLPLLQemGKTIFAISHDDHYFIHADRLLEMRNGQLSE 529
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
1026-1232 |
1.66e-15 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 79.37 E-value: 1.66e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1026 SLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVKELN-VQWL--RSQTAIVSQEPVlfnCSIaeniay 1102
Cdd:PRK15079 41 TLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKdDEWRavRSDIQMIFQDPL---ASL------ 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1103 gdNSRMV-------PLEEIKEVADAANIHSFIEGLPRKyntlVGLRGV-------QLSGGQKQRLAIARALLRKPKILLL 1168
Cdd:PRK15079 112 --NPRMTigeiiaePLRTYHPKLSRQEVKDRVKAMMLK----VGLLPNlinryphEFSGGQCQRIGIARALILEPKLIIC 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568980685 1169 DEATSALDNESEKVVQQALDKARR--GKTCLVVAHRLSTIQN-ADMIVVLQNGSIKEQGTHQELLRN 1232
Cdd:PRK15079 186 DEPVSALDVSIQAQVVNLLQQLQRemGLSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEVYHN 252
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1021-1229 |
1.68e-15 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 81.00 E-value: 1.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1021 VLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRF--YDPMKGQVLLD-----------------------GVDVKELNV 1075
Cdd:TIGR03269 15 VLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIYHvalcekcgyverpskvgepcpvcGGTLEPEEV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1076 Q-W---------LRSQTAIVSQ--------EPVLFNCSIA-ENIAY-GDNSRMVPLEEIKEVadaaNIHSFIEGLPRkyn 1135
Cdd:TIGR03269 95 DfWnlsdklrrrIRKRIAIMLQrtfalygdDTVLDNVLEAlEEIGYeGKEAVGRAVDLIEMV----QLSHRITHIAR--- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1136 tlvglrgvQLSGGQKQRLAIARALLRKPKILLLDEATSALDNESEKVVQQALDKA--RRGKTCLVVAHRLSTIQN-ADMI 1212
Cdd:TIGR03269 168 --------DLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAvkASGISMVLTSHWPEVIEDlSDKA 239
|
250
....*....|....*..
gi 568980685 1213 VVLQNGSIKEQGTHQEL 1229
Cdd:TIGR03269 240 IWLENGEIKEEGTPDEV 256
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
92-316 |
1.82e-15 |
|
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: 78.28 E-value: 1.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 92 IIVLTLYYIGIGAAALIFGYVQISFWVITAARQTTRIRKQFFHSILAQDISWFDGSDICELNTRMTGDINKLCDGIGDKI 171
Cdd:cd18545 39 LLIIALLFLALNLVNWVASRLRIYLMAKVGQRILYDLRQDLFSHLQKLSFSFFDSRPVGKILSRVINDVNSLSDLLSNGL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 172 PLMFQNISGFSIGLVISLIKSWKLSLVVLSTSPLIMASSALCSRMIISLTSKELDAYSKAGAVAEEALSSIQTVTAFGAQ 251
Cdd:cd18545 119 INLIPDLLTLVGIVIIMFSLNVRLALVTLAVLPLLVLVVFLLRRRARKAWQRVRKKISNLNAYLHESISGIRVIQSFARE 198
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 252 EKEIQRYTQHLKDAKDAGIKratASKLSlgAVYF----FMNG-AYGLAFWYGTSLIFGGEpgYTIGTILA 316
Cdd:cd18545 199 DENEEIFDELNRENRKANMR---AVRLN--ALFWplveLISAlGTALVYWYGGKLVLGGA--ITVGVLVA 261
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1016-1231 |
2.03e-15 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 81.05 E-value: 2.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1016 RPEVPVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVKELNVQW--LRSQT----------- 1082
Cdd:PRK10261 26 QQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRSRQVieLSEQSaaqmrhvrgad 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1083 -AIVSQEPV-----LFNC--SIAENIAYGDN-SRMVPLEEIKEVADAANIHSFIEGLPRKYNtlvglrgvQLSGGQKQRL 1153
Cdd:PRK10261 106 mAMIFQEPMtslnpVFTVgeQIAESIRLHQGaSREEAMVEAKRMLDQVRIPEAQTILSRYPH--------QLSGGMRQRV 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1154 AIARALLRKPKILLLDEATSALDNESE-------KVVQQALDKArrgktCLVVAHRLSTIQN-ADMIVVLQNGSIKEQGT 1225
Cdd:PRK10261 178 MIAMALSCRPAVLIADEPTTALDVTIQaqilqliKVLQKEMSMG-----VIFITHDMGVVAEiADRVLVMYQGEAVETGS 252
|
....*.
gi 568980685 1226 HQELLR 1231
Cdd:PRK10261 253 VEQIFH 258
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
994-1225 |
2.07e-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: 2.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 994 GEKPDTCEGNLefreVSFVYPC-RPEVpvlQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVkE 1072
Cdd:TIGR01257 924 GLVPGVCVKNL----VKIFEPSgRPAV---DRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-E 995
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1073 LNVQWLRSQTAIVSQEPVLFN-CSIAENIAYGDNSRMVPLEEIKevadaANIHSFIE--GLPRKYNTlvglRGVQLSGGQ 1149
Cdd:TIGR01257 996 TNLDAVRQSLGMCPQHNILFHhLTVAEHILFYAQLKGRSWEEAQ-----LEMEAMLEdtGLHHKRNE----EAQDLSGGM 1066
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568980685 1150 KQRLAIARALLRKPKILLLDEATSALDNESEKVVQQALDKARRGKTCLVVAHRLSTIQN-ADMIVVLQNGSIKEQGT 1225
Cdd:TIGR01257 1067 QRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEADLlGDRIAIISQGRLYCSGT 1143
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1018-1242 |
2.08e-15 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 81.05 E-value: 2.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1018 EVPVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVKELN---VQWLRSQTAIVSQEPVlfnC 1094
Cdd:PRK10261 336 EVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSpgkLQALRRDIQFIFQDPY---A 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1095 SIAENIAYGDnSRMVPLEeikevadaanIHSFIEG--LPRKYNTL---VGLRGV-------QLSGGQKQRLAIARALLRK 1162
Cdd:PRK10261 413 SLDPRQTVGD-SIMEPLR----------VHGLLPGkaAAARVAWLlerVGLLPEhawryphEFSGGQRQRICIARALALN 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1163 PKILLLDEATSALD-NESEKVVQQALDKARR-GKTCLVVAHRLSTIQN-ADMIVVLQNGSIKEQGTHQELLRNGDTYF-- 1237
Cdd:PRK10261 482 PKVIIADEAVSALDvSIRGQIINLLLDLQRDfGIAYLFISHDMAVVERiSHRVAVMYLGQIVEIGPRRAVFENPQHPYtr 561
|
....*
gi 568980685 1238 KLVAA 1242
Cdd:PRK10261 562 KLMAA 566
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
389-587 |
3.48e-15 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 76.39 E-value: 3.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 389 SAKVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDE---NDIRAQNVRHYR-EQIGVVRQ------ 458
Cdd:PRK11629 21 QTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGqpmSKLSSAAKAELRnQKLGFIYQfhhllp 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 459 -----EPVLFGTTIGnnikfgreGVGEKEMEQAAREANAydfIMAFPKKFNtlvgEKGAQMSGGQKQRIAIARALVRNPK 533
Cdd:PRK11629 101 dftalENVAMPLLIG--------KKKPAEINSRALEMLA---AVGLEHRAN----HRPSELSGGERQRVAIARALVNNPR 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 568980685 534 ILILDEATSALDTE-SESLVQTALE-KASKGRTTIVVAHRLSTIRGADLIVTMKDG 587
Cdd:PRK11629 166 LVLADEPTGNLDARnADSIFQLLGElNRLQGTAFLVVTHDLQLAKRMSRQLEMRDG 221
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
381-567 |
6.13e-15 |
|
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: 75.83 E-value: 6.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 381 SFSYPSRPSAKVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQrlydpedGCITVDENDIRAQNVRHYREQIGVVRQEP 460
Cdd:cd03267 25 SLFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILS-------GLLQPTSGEVRVAGLVPWKRRKKFLRRIG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 461 VLFGT--------TIGNNIKFGREGVGEKEMEQAAREANAYDFImafpkKFNTLVGEKGAQMSGGQKQRIAIARALVRNP 532
Cdd:cd03267 98 VVFGQktqlwwdlPVIDSFYLLAAIYDLPPARFKKRLDELSELL-----DLEELLDTPVRQLSLGQRMRAEIAAALLHEP 172
|
170 180 190
....*....|....*....|....*....|....*
gi 568980685 533 KILILDEATSALDTESESLVQTALEKASKGRTTIV 567
Cdd:cd03267 173 EILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTV 207
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1016-1243 |
6.68e-15 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 76.37 E-value: 6.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1016 RPEVPVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVKELNVQWlRSQ-TAIVSQEPvlfnc 1094
Cdd:PRK15112 23 RQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSY-RSQrIRMIFQDP----- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1095 SIAENiaygdnsrmvPLEEIKEVADAA-NIHSFIEGLPRK---YNTL--VGLRGVQ-------LSGGQKQRLAIARALLR 1161
Cdd:PRK15112 97 STSLN----------PRQRISQILDFPlRLNTDLEPEQREkqiIETLrqVGLLPDHasyyphmLAPGQKQRLGLARALIL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1162 KPKILLLDEATSALD-NESEKVVQQALD-KARRGKTCLVVAHRLSTIQN-ADMIVVLQNGSIKEQGTHQELLRN--GDTY 1236
Cdd:PRK15112 167 RPKVIIADEALASLDmSMRSQLINLMLElQEKQGISYIYVTQHLGMMKHiSDQVLVMHQGEVVERGSTADVLASplHELT 246
|
....*..
gi 568980685 1237 FKLVAAH 1243
Cdd:PRK15112 247 KRLIAGH 253
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
391-571 |
9.71e-15 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 74.61 E-value: 9.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 391 KVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLY--DPEDGCITVDENDIraqnvrhYREQIGVvrqEPVLFGTTIG 468
Cdd:COG2401 44 YVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPDNQF-------GREASLI---DAIGRKGDFK 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 469 NNIKF-GREGVGEkemeqaareanAYDFImafpKKFNTLvgekgaqmSGGQKQRIAIARALVRNPKILILDEATSALDTE 547
Cdd:COG2401 114 DAVELlNAVGLSD-----------AVLWL----RRFKEL--------STGQKFRFRLALLLAERPKLLVIDEFCSHLDRQ 170
|
170 180
....*....|....*....|....*.
gi 568980685 548 SESLVQTALEKASK--GRTTIVVAHR 571
Cdd:COG2401 171 TAKRVARNLQKLARraGITLVVATHH 196
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
403-593 |
1.03e-14 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 78.74 E-value: 1.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 403 GETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDI---RAQNVRHYREQIGVVRQEPV-------LFGTTIGNNIK 472
Cdd:PRK10261 350 GETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIdtlSPGKLQALRRDIQFIFQDPYasldprqTVGDSIMEPLR 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 473 FGREGVGEKEMEQAA----REANAYDFIMAFPKKFntlvgekgaqmSGGQKQRIAIARALVRNPKILILDEATSALDTES 548
Cdd:PRK10261 430 VHGLLPGKAAAARVAwlleRVGLLPEHAWRYPHEF-----------SGGQRQRICIARALALNPKVIIADEAVSALDVSI 498
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 568980685 549 ESLVQTALEKASK--GRTTIVVAHRLSTI-RGADLIVTMKDGMVVEKG 593
Cdd:PRK10261 499 RGQIINLLLDLQRdfGIAYLFISHDMAVVeRISHRVAVMYLGQIVEIG 546
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
392-570 |
1.14e-14 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 74.82 E-value: 1.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 392 VLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCI--------TVDEN---DIRAQNVrhyreqiGVVRQEP 460
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVslvgqplhQMDEEaraKLRAKHV-------GFVFQSF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 461 VLFGT-TIGNNIKFGREGVGEKEmEQAAREANAYDFIMAFPKKFNTLvgekGAQMSGGQKQRIAIARALVRNPKILILDE 539
Cdd:PRK10584 98 MLIPTlNALENVELPALLRGESS-RQSRNGAKALLEQLGLGKRLDHL----PAQLSGGEQQRVALARAFNGRPDVLFADE 172
|
170 180 190
....*....|....*....|....*....|...
gi 568980685 540 ATSALDTESESLVQTALEKASK--GRTTIVVAH 570
Cdd:PRK10584 173 PTGNLDRQTGDKIADLLFSLNRehGTTLILVTH 205
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
386-570 |
1.23e-14 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 73.93 E-value: 1.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 386 SRPSAKVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDIrAQNVRHYREQIGVVRQEPVLFGT 465
Cdd:TIGR01189 9 SRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPL-AEQRDEPHENILYLGHLPGLKPE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 466 -TIGNNIKFGRE--GVGEKEMEQAAREANAYDFImafpkkfNTLVgekgAQMSGGQKQRIAIARALVRNPKILILDEATS 542
Cdd:TIGR01189 88 lSALENLHFWAAihGGAQRTIEDALAAVGLTGFE-------DLPA----AQLSAGQQRRLALARLWLSRRPLWILDEPTT 156
|
170 180
....*....|....*....|....*....
gi 568980685 543 ALDTESESLVQTALEK-ASKGRTTIVVAH 570
Cdd:TIGR01189 157 ALDKAGVALLAGLLRAhLARGGIVLLTTH 185
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
386-556 |
2.19e-14 |
|
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: 73.30 E-value: 2.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 386 SRPSAKVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVdENDIRAQNVRHYREQIGVVRQEPVLFGT 465
Cdd:cd03231 9 ERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLL-NGGPLDFQRDSIARGLLYLGHAPGIKTT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 466 -TIGNNIKFGREGVGEKEMEQAAREAN--AYDFIMAfpkkfntlvgekgAQMSGGQKQRIAIARALVRNPKILILDEATS 542
Cdd:cd03231 88 lSVLENLRFWHADHSDEQVEEALARVGlnGFEDRPV-------------AQLSAGQQRRVALARLLLSGRPLWILDEPTT 154
|
170
....*....|....
gi 568980685 543 ALDTESESLVQTAL 556
Cdd:cd03231 155 ALDKAGVARFAEAM 168
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
403-592 |
2.54e-14 |
|
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: 71.64 E-value: 2.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 403 GETVALVGPSGSGKSTTVQLLQRLYDPED-GCITVDENDIRAQNVRHYReqigvvrqepvlfgttignnikfgregvgek 481
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGgGVIYIDGEDILEEVLDQLL------------------------------- 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 482 emeqaareanaydfimafpkkfNTLVGEKGAQMSGGQKQRIAIARALVRNPKILILDEATSALDTESESLVQTALE---- 557
Cdd:smart00382 51 ----------------------LIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElrll 108
|
170 180 190
....*....|....*....|....*....|....*..
gi 568980685 558 --KASKGRTTIVVAHRLSTIRGADLIVTMKDGMVVEK 592
Cdd:smart00382 109 llLKSEKNLTVILTTNDEKDLGPALLRRRFDRRIVLL 145
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1022-1229 |
3.18e-14 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 74.28 E-value: 3.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1022 LQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMK---GQVLLDGVDVKEL-----NVQWLRSQTAIVSQEPVLFN 1093
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKsagSHIELLGRTVQREgrlarDIRKSRANTGYIFQQFNLVN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1094 -CSIAENIAYGDNSRMVPLEEIKEVADAANIHSFIEGLPRkyntlVGL------RGVQLSGGQKQRLAIARALLRKPKIL 1166
Cdd:PRK09984 100 rLSVLENVLIGALGSTPFWRTCFSWFTREQKQRALQALTR-----VGMvhfahqRVSTLSGGQQQRVAIARALMQQAKVI 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568980685 1167 LLDEATSALDNESEKVVQQALDKARR--GKTCLVVAHRLS-TIQNADMIVVLQNGSIKEQGTHQEL 1229
Cdd:PRK09984 175 LADEPIASLDPESARIVMDTLRDINQndGITVVVTLHQVDyALRYCERIVALRQGHVFYDGSSQQF 240
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
1004-1201 |
3.25e-14 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 72.78 E-value: 3.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1004 LEFREVSFVypcRPEVPVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVKELNVQWlrsqta 1083
Cdd:TIGR01189 1 LAARNLACS---RGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEP------ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1084 ivsqepvlfncsiAENIAY-----GDNSRMVPLEEIKEVADaanIHSFIEGLPRKYNTLVGLRGV------QLSGGQKQR 1152
Cdd:TIGR01189 72 -------------HENILYlghlpGLKPELSALENLHFWAA---IHGGAQRTIEDALAAVGLTGFedlpaaQLSAGQQRR 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 568980685 1153 LAIARALLRKPKILLLDEATSALDNES-EKVVQQALDKARRGKTCLVVAH 1201
Cdd:TIGR01189 136 LALARLWLSRRPLWILDEPTTALDKAGvALLAGLLRAHLARGGIVLLTTH 185
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
34-322 |
3.61e-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: 74.44 E-value: 3.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 34 IVLMTLGILASMINGATVPLmslvlgeISDHLINGCLVQTNRTkyqncsqtqeklneDIIVLTLYYIGIGAAALIFGYVQ 113
Cdd:cd18543 1 LILALLAALLATLAGLAIPL-------LTRRAIDGPIAHGDRS--------------ALWPLVLLLLALGVAEAVLSFLR 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 114 ISFWVITAARQTTRIRKQFFHSILAQDISWFDGSDICELNTRMTGDINKLCDGIGdKIPLMFQNISGFSIGLVISLIKSW 193
Cdd:cd18543 60 RYLAGRLSLGVEHDLRTDLFAHLQRLDGAFHDRWQSGQLLSRATSDLSLVQRFLA-FGPFLLGNLLTLVVGLVVMLVLSP 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 194 KLSLVVLSTSPLIMASSALCSRMIISLTskeLDAYSKAGAVA---EEALSSIQTVTAFGAQEKEIQRYTQHLKDAKDAGI 270
Cdd:cd18543 139 PLALVALASLPPLVLVARRFRRRYFPAS---RRAQDQAGDLAtvvEESVTGIRVVKAFGRERRELDRFEAAARRLRATRL 215
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 568980685 271 KRATASKLSLGAVYFFMNGAYGLAFWYGTSLIFGGEpgYTIGTILAvFFSVI 322
Cdd:cd18543 216 RAARLRARFWPLLEALPELGLAAVLALGGWLVANGS--LTLGTLVA-FSAYL 264
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
92-317 |
3.77e-14 |
|
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: 74.36 E-value: 3.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 92 IIVLTLYYIGIGAAALIFGYVQISFWVITAARQTTRIRKQFFHSILAQDISWFD----GSdiceLNTRMTGDINKLCDGI 167
Cdd:cd18548 38 ILRTGLLMLLLALLGLIAGILAGYFAAKASQGFGRDLRKDLFEKIQSFSFAEIDkfgtSS----LITRLTNDVTQVQNFV 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 168 GD------KIPLMFqnisgfsIG-LVISLIKSWKLSLVVLSTSPLIMASSALCSRMIISLTSKELDAYSKAGAVAEEALS 240
Cdd:cd18548 114 MMllrmlvRAPIML-------IGaIIMAFRINPKLALILLVAIPILALVVFLIMKKAIPLFKKVQKKLDRLNRVVRENLT 186
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568980685 241 SIQTVTAFGAQEKEIQRYTQHLKDAKDAGIKRATASKLSLGAVYFFMNGAYGLAFWYGTSLIFGGEPgyTIGTILAV 317
Cdd:cd18548 187 GIRVIRAFNREDYEEERFDKANDDLTDTSLKAGRLMALLNPLMMLIMNLAIVAILWFGGHLINAGSL--QVGDLVAF 261
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1019-1218 |
6.11e-14 |
|
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: 76.02 E-value: 6.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1019 VPVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFY--DPMKGQVLLDGVDVKELNVQWL-RSQTAIVSQEPVLF-NC 1094
Cdd:TIGR02633 14 VKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYphGTWDGEIYWSGSPLKASNIRDTeRAGIVIIHQELTLVpEL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1095 SIAENIAYGDnsrmvpleeikEVADAANIHSFIEGLPRKYNTLVGL--------RGV-QLSGGQKQRLAIARALLRKPKI 1165
Cdd:TIGR02633 94 SVAENIFLGN-----------EITLPGGRMAYNAMYLRAKNLLRELqldadnvtRPVgDYGGGQQQLVEIAKALNKQARL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 568980685 1166 LLLDEATSAL-DNESEKVVQQALDKARRGKTCLVVAHRLSTIQN-ADMIVVLQNG 1218
Cdd:TIGR02633 163 LILDEPSSSLtEKETEILLDIIRDLKAHGVACVYISHKLNEVKAvCDTICVIRDG 217
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
1016-1201 |
7.01e-14 |
|
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: 71.76 E-value: 7.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1016 RPEVPVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVKELNVQWLRSQTAIVSQEPVLFNCS 1095
Cdd:cd03231 10 RDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1096 IAENIAY--GDNSRmvplEEIKEVADAANIHSFiEGLPrkyntlVGlrgvQLSGGQKQRLAIARALLRKPKILLLDEATS 1173
Cdd:cd03231 90 VLENLRFwhADHSD----EQVEEALARVGLNGF-EDRP------VA----QLSAGQQRRVALARLLLSGRPLWILDEPTT 154
|
170 180
....*....|....*....|....*....
gi 568980685 1174 ALDNES-EKVVQQALDKARRGKTCLVVAH 1201
Cdd:cd03231 155 ALDKAGvARFAEAMAGHCARGGMVVLTTH 183
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
92-326 |
9.63e-14 |
|
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: 73.70 E-value: 9.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 92 IIVLTLYYIGIGAAALIFGYVQISFWVITAARQTTRIRKQFFHSILAQDISWFDGSDICELNTRMTGDINKLCDGIGDKI 171
Cdd:cd18564 53 LLLAAAALVGIALLRGLASYAGTYLTALVGQRVVLDLRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGAIQDLLVSGV 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 172 PLMFQNISGFSIGLVISLIKSWKLSLVVLSTSPLIMASSALCSRMIISLTSKELDAYSKAGAVAEEALSSIQTVTAFGAQ 251
Cdd:cd18564 133 LPLLTNLLTLVGMLGVMFWLDWQLALIALAVAPLLLLAARRFSRRIKEASREQRRREGALASVAQESLSAIRVVQAFGRE 212
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568980685 252 EKEIQRYTQHLKDAKDAGIK-RATASKLSLgAVYFFMNGAYGLAFWYGTSLIFGGEpgYTIGTILaVFFSVIHSSY 326
Cdd:cd18564 213 EHEERRFARENRKSLRAGLRaARLQALLSP-VVDVLVAVGTALVLWFGAWLVLAGR--LTPGDLL-VFLAYLKNLY 284
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
391-602 |
1.39e-13 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 71.98 E-value: 1.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 391 KVLKGLNLKIKAGETVALVGPSGSGKSTTVQLL--QRLYDPEDGCITVDENDIRAQNVRHyREQIGVVR--QEPVlfgtT 466
Cdd:CHL00131 21 EILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIagHPAYKILEGDILFKGESILDLEPEE-RAHLGIFLafQYPI----E 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 467 IG--NNIKFGREGVGEKEMEQAAREANAYDFIMAFPKKFNtLVGEKGAQM--------SGGQKQRIAIARALVRNPKILI 536
Cdd:CHL00131 96 IPgvSNADFLRLAYNSKRKFQGLPELDPLEFLEIINEKLK-LVGMDPSFLsrnvnegfSGGEKKRNEILQMALLDSELAI 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568980685 537 LDEATSALDTESESLVQTALEK-ASKGRTTIVVAH--RLSTIRGADLIVTMKDGMVVEKGThAELmAKQ 602
Cdd:CHL00131 175 LDETDSGLDIDALKIIAEGINKlMTSENSIILITHyqRLLDYIKPDYVHVMQNGKIIKTGD-AEL-AKE 241
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
1022-1218 |
1.92e-13 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 70.35 E-value: 1.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1022 LQNMSLSIEKGKTVAFVGSSGCGKSTCVQLL-QRFYD-PMKGQVLLDGvdvKELNVQWLRSqTAIVSQEPVLFNCS-IAE 1098
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESGAGKTTLLDVLaGRKTAgVITGEILING---RPLDKNFQRS-TGYVEQQDVHSPNLtVRE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1099 NIAYgdnsrmvpleeikevadAANihsfieglprkyntlvgLRGvqLSGGQKQRLAIARALLRKPKILLLDEATSALDNE 1178
Cdd:cd03232 99 ALRF-----------------SAL-----------------LRG--LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQ 142
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 568980685 1179 SEKVVQQALDK-ARRGKTCLVVAHRLS--TIQNADMIVVLQNG 1218
Cdd:cd03232 143 AAYNIVRFLKKlADSGQAILCTIHQPSasIFEKFDRLLLLKRG 185
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
396-619 |
2.02e-13 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 71.50 E-value: 2.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 396 LNLKIKAGETVALVGPSGSGKSTtvqLLQRLYD--PEDGCITVDENDI---RAQNVRHYR----EQIGVVRQEPV----- 461
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKST---LLARMAGllPGSGSIQFAGQPLeawSAAELARHRaylsQQQTPPFAMPVfqylt 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 462 LFGTTIGNnikfgrEGVGEKEMEQAAREANAYDfimafpkKFNTLVGekgaQMSGGQKQRIAIARALVR-----NP--KI 534
Cdd:PRK03695 92 LHQPDKTR------TEAVASALNEVAEALGLDD-------KLGRSVN----QLSGGEWQRVRLAAVVLQvwpdiNPagQL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 535 LILDEATSALDTESESLVQTALEK-ASKGRTTIVVAHRLS-TIRGADLIVTMKDGMVVEKGTHAELMAKQGLyySLAMAQ 612
Cdd:PRK03695 155 LLLDEPMNSLDVAQQAALDRLLSElCQQGIAVVMSSHDLNhTLRHADRVWLLKQGKLLASGRRDEVLTPENL--AQVFGV 232
|
....*..
gi 568980685 613 DIKKVDE 619
Cdd:PRK03695 233 NFRRLDV 239
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
375-545 |
2.07e-13 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 71.68 E-value: 2.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 375 IEFKNVSFSYPSRpsaKVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCItvdendiraqnVRHYREQIG 454
Cdd:PRK09544 5 VSLENVSVSFGQR---RVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI-----------KRNGKLRIG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 455 VVRQEPVLFGT---TIGNNIKFgREGVGEKEMEQAAREANAYDFIMAFPKKfntlvgekgaqMSGGQKQRIAIARALVRN 531
Cdd:PRK09544 71 YVPQKLYLDTTlplTVNRFLRL-RPGTKKEDILPALKRVQAGHLIDAPMQK-----------LSGGETQRVLLARALLNR 138
|
170
....*....|....
gi 568980685 532 PKILILDEATSALD 545
Cdd:PRK09544 139 PQLLVLDEPTQGVD 152
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1019-1220 |
2.60e-13 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 73.93 E-value: 2.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1019 VPVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVKELNVQwLRSQTAI--VSQEPVLF-NCS 1095
Cdd:PRK15439 24 VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPA-KAHQLGIylVPQEPLLFpNLS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1096 IAENIAYGDNSRMVPLEEIKEVADAANIHsfieglpRKYNTLVGLrgvqLSGGQKQRLAIARALLRKPKILLLDEATSAL 1175
Cdd:PRK15439 103 VKENILFGLPKRQASMQKMKQLLAALGCQ-------LDLDSSAGS----LEVADRQIVEILRGLMRDSRILILDEPTASL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 568980685 1176 D-NESEKVVQQALDKARRGKTCLVVAHRLSTI-QNADMIVVLQNGSI 1220
Cdd:PRK15439 172 TpAETERLFSRIRELLAQGVGIVFISHKLPEIrQLADRISVMRDGTI 218
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1018-1238 |
2.83e-13 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 71.21 E-value: 2.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1018 EVPVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLL--QRFYDPMKGQVLLDGVDVKELNVQwLRSQTAI----------- 1084
Cdd:CHL00131 19 ENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIagHPAYKILEGDILFKGESILDLEPE-ERAHLGIflafqypieip 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1085 -VSQEPVLfncsiaeNIAYGDNSRMVPLEEIKEVadaanihSFIEGLPRKYNtLVGL------RGVQ--LSGGQKQRLAI 1155
Cdd:CHL00131 98 gVSNADFL-------RLAYNSKRKFQGLPELDPL-------EFLEIINEKLK-LVGMdpsflsRNVNegFSGGEKKRNEI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1156 ARALLRKPKILLLDEATSALDNESEKVVQQALDK-ARRGKTCLVVAH--RLSTIQNADMIVVLQNGSIKEQGT---HQEL 1229
Cdd:CHL00131 163 LQMALLDSELAILDETDSGLDIDALKIIAEGINKlMTSENSIILITHyqRLLDYIKPDYVHVMQNGKIIKTGDaelAKEL 242
|
....*....
gi 568980685 1230 LRNGDTYFK 1238
Cdd:CHL00131 243 EKKGYDWLK 251
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1016-1200 |
2.85e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 70.29 E-value: 2.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1016 RPEVPVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVKELNVqwlRSQTAIVSQ----EPVL 1091
Cdd:PRK13539 12 RGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDV---AEACHYLGHrnamKPAL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1092 fncSIAENIAYGDNSRMVPLEEIKEVADAANIHSfIEGLPRKYntlvglrgvqLSGGQKQRLAIARALLRKPKILLLDEA 1171
Cdd:PRK13539 89 ---TVAENLEFWAAFLGGEELDIAAALEAVGLAP-LAHLPFGY----------LSAGQKRRVALARLLVSNRPIWILDEP 154
|
170 180
....*....|....*....|....*....
gi 568980685 1172 TSALDNESEKVVqQALDKARRGKTCLVVA 1200
Cdd:PRK13539 155 TAALDAAAVALF-AELIRAHLAQGGIVIA 182
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
1031-1224 |
3.36e-13 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 72.60 E-value: 3.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1031 KGKTVAFvGSSGCGKSTCVQLLQRFYDPMKGQVLLDG---VDV-KELNVQWLRSQTAIVSQEPVLF-NCSIAENIAYGDN 1105
Cdd:PRK11144 24 QGITAIF-GRSGAGKTSLINAISGLTRPQKGRIVLNGrvlFDAeKGICLPPEKRRIGYVFQDARLFpHYKVRGNLRYGMA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1106 SRMVPleeikevadaanihsfieglprKYNTLVGLRGVQ---------LSGGQKQRLAIARALLRKPKILLLDEATSALD 1176
Cdd:PRK11144 103 KSMVA----------------------QFDKIVALLGIEplldrypgsLSGGEKQRVAIGRALLTAPELLLMDEPLASLD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 568980685 1177 NESEKVVQQALDK-ARRGKT-CLVVAHRLSTI-QNADMIVVLQNGSIKEQG 1224
Cdd:PRK11144 161 LPRKRELLPYLERlAREINIpILYVSHSLDEIlRLADRVVVLEQGKVKAFG 211
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
1017-1219 |
4.25e-13 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 73.29 E-value: 4.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1017 PEVPVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYdP---MKGQVLLDGvdvKELNVQWLRSQTA----IVSQE- 1088
Cdd:NF040905 12 PGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PhgsYEGEILFDG---EVCRFKDIRDSEAlgivIIHQEl 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1089 ---PVLfncSIAENIAYGDnsrmvpleeikEVA-------DAANIHSfIE-----GLPRKYNTLVGLRGVqlsgGQKQRL 1153
Cdd:NF040905 88 aliPYL---SIAENIFLGN-----------ERAkrgvidwNETNRRA-REllakvGLDESPDTLVTDIGV----GKQQLV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568980685 1154 AIARALLRKPKILLLDEATSAL-DNESEKVVQQALDKARRGKTCLVVAHRLSTI-QNADMIVVLQNGS 1219
Cdd:NF040905 149 EIAKALSKDVKLLILDEPTAALnEEDSAALLDLLLELKAQGITSIIISHKLNEIrRVADSITVLRDGR 216
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1004-1230 |
6.98e-13 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 70.99 E-value: 6.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1004 LEFREVSFVYPcrpEVPVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVKElNVQWLRSQTA 1083
Cdd:PRK13537 8 IDFRNVEKRYG---DKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPS-RARHARQRVG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1084 IVSQ----EPvlfNCSIAENI----------AYGDNSRMVPLEEIKEvadaanihsfiegLPRKYNTLVGlrgvQLSGGQ 1149
Cdd:PRK13537 84 VVPQfdnlDP---DFTVRENLlvfgryfglsAAAARALVPPLLEFAK-------------LENKADAKVG----ELSGGM 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1150 KQRLAIARALLRKPKILLLDEATSALDNESEKVVQQALDK-ARRGKTCLVVAHRLSTIQN-ADMIVVLQNGSIKEQGTHQ 1227
Cdd:PRK13537 144 KRRLTLARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSlLARGKTILLTTHFMEEAERlCDRLCVIEEGRKIAEGAPH 223
|
...
gi 568980685 1228 ELL 1230
Cdd:PRK13537 224 ALI 226
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
392-574 |
9.76e-13 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 72.60 E-value: 9.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 392 VLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQ-RLYDPE-DGCITVDENDIRAQNVRhyreQIGVVRQEPVLF-GTTIG 468
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAgRIQGNNfTGTILANNRKPTKQILK----RTGFVTQDDILYpHLTVR 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 469 NNIKFGREGVGEKEMEQAAREANAYDFI--MAFPKKFNTLVGEKGAQ-MSGGQKQRIAIARALVRNPKILILDEATSALD 545
Cdd:PLN03211 159 ETLVFCSLLRLPKSLTKQEKILVAESVIseLGLTKCENTIIGNSFIRgISGGERKRVSIAHEMLINPSLLILDEPTSGLD 238
|
170 180 190
....*....|....*....|....*....|
gi 568980685 546 -TESESLVQTALEKASKGRTTIVVAHRLST 574
Cdd:PLN03211 239 aTAAYRLVLTLGSLAQKGKTIVTSMHQPSS 268
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1006-1229 |
1.15e-12 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 69.57 E-value: 1.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1006 FREVSF-VYPcrpevpvlqnmslsiekGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVKELNVQWL------ 1078
Cdd:PRK11701 22 CRDVSFdLYP-----------------GEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALseaerr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1079 ---RSQTAIVSQEP---VLFNCSIAENIA----------YGdNSRMVPLEEIKEVADAAnihSFIEGLPRKYntlvglrg 1142
Cdd:PRK11701 85 rllRTEWGFVHQHPrdgLRMQVSAGGNIGerlmavgarhYG-DIRATAGDWLERVEIDA---ARIDDLPTTF-------- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1143 vqlSGGQKQRLAIARALLRKPKILLLDEATSALDnesekVVQQA--LDKARR-----GKTCLVVAHRLSTIQN-ADMIVV 1214
Cdd:PRK11701 153 ---SGGMQQRLQIARNLVTHPRLVFMDEPTGGLD-----VSVQArlLDLLRGlvrelGLAVVIVTHDLAVARLlAHRLLV 224
|
250
....*....|....*.
gi 568980685 1215 LQNGSIKEQG-THQEL 1229
Cdd:PRK11701 225 MKQGRVVESGlTDQVL 240
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1016-1231 |
1.20e-12 |
|
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: 72.14 E-value: 1.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1016 RPEVPVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLL----DGVDVKELNVQwLRSQT----AIVSQ 1087
Cdd:TIGR03269 294 RGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdEWVDMTKPGPD-GRGRAkryiGILHQ 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1088 EPVLF-NCSIAENIaygdnSRMVPLEEIKEVADAANIHSF-IEGLPRKY--NTLVGLRGvQLSGGQKQRLAIARALLRKP 1163
Cdd:TIGR03269 373 EYDLYpHRTVLDNL-----TEAIGLELPDELARMKAVITLkMVGFDEEKaeEILDKYPD-ELSEGERHRVALAQVLIKEP 446
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568980685 1164 KILLLDEATSALDNESEKVVQQALDKARR--GKTCLVVAHRLSTIQN-ADMIVVLQNGSIKEQGTHQELLR 1231
Cdd:TIGR03269 447 RIVILDEPTGTMDPITKVDVTHSILKAREemEQTFIIVSHDMDFVLDvCDRAALMRDGKIVKIGDPEEIVE 517
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
375-604 |
1.43e-12 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 71.85 E-value: 1.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 375 IEFKNVSFSYPSRPsakVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENdiraqnvrhyrEQIG 454
Cdd:PRK15064 320 LEVENLTKGFDNGP---LFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSEN-----------ANIG 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 455 VVRQEPVL-FGTTIgNNIKFGREGVGEKEMEQAAREA------NAYDFimafPKKFNTLvgekgaqmSGGQKQRIAIARA 527
Cdd:PRK15064 386 YYAQDHAYdFENDL-TLFDWMSQWRQEGDDEQAVRGTlgrllfSQDDI----KKSVKVL--------SGGEKGRMLFGKL 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 528 LVRNPKILILDEATSALDTES-ESLvQTALEKaSKGrTTIVVAH-R--LSTIrgADLIVTMK-DGMVVEKGTHAELMAKQ 602
Cdd:PRK15064 453 MMQKPNVLVMDEPTNHMDMESiESL-NMALEK-YEG-TLIFVSHdRefVSSL--ATRIIEITpDGVVDFSGTYEEYLRSQ 527
|
..
gi 568980685 603 GL 604
Cdd:PRK15064 528 GI 529
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
390-602 |
1.63e-12 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 71.59 E-value: 1.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 390 AKVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDIRAQNVRH-------Y----REQIGVVRQ 458
Cdd:COG1129 265 GGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDairagiaYvpedRKGEGLVLD 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 459 EPVLFGTTIGNNIKFGREG-VGEKEMEQAAREanaydFImafpKKFN-------TLVGekgaQMSGGQKQRIAIARALVR 530
Cdd:COG1129 345 LSIRENITLASLDRLSRGGlLDRRRERALAEE-----YI----KRLRiktpspeQPVG----NLSGGNQQKVVLAKWLAT 411
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568980685 531 NPKILILDEATSALDTESESLVQTALEK-ASKGRTTIVVAHRLSTIRG-ADLIVTMKDGMVVekgthAELMAKQ 602
Cdd:COG1129 412 DPKVLILDEPTRGIDVGAKAEIYRLIRElAAEGKAVIVISSELPELLGlSDRILVMREGRIV-----GELDREE 480
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
396-593 |
1.72e-12 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 70.29 E-value: 1.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 396 LNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDE---NDIRAQ-NVRHYREQIGVVRQEPVLF-GTTIGNN 470
Cdd:PRK11144 17 VNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGrvlFDAEKGiCLPPEKRRIGYVFQDARLFpHYKVRGN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 471 IKFGregVGEKEMEQaareanaydfimafpkkFNTLVGEKG---------AQMSGGQKQRIAIARALVRNPKILILDEAT 541
Cdd:PRK11144 97 LRYG---MAKSMVAQ-----------------FDKIVALLGieplldrypGSLSGGEKQRVAIGRALLTAPELLLMDEPL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 568980685 542 SALDTESESLVQTALEKASKG-RTTIV-VAHRLSTI-RGADLIVTMKDGMVVEKG 593
Cdd:PRK11144 157 ASLDLPRKRELLPYLERLAREiNIPILyVSHSLDEIlRLADRVVVLEQGKVKAFG 211
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1018-1223 |
1.94e-12 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 68.27 E-value: 1.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1018 EVPVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVKELNVQW---LRSQ-TAIVSQEPVLFN 1093
Cdd:PRK10584 22 ELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEArakLRAKhVGFVFQSFMLIP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1094 CSIA-ENIAY-----GDNSRMvPLEEIKEVADAANIHSFIEGLPrkyntlvglrgVQLSGGQKQRLAIARALLRKPKILL 1167
Cdd:PRK10584 102 TLNAlENVELpallrGESSRQ-SRNGAKALLEQLGLGKRLDHLP-----------AQLSGGEQQRVALARAFNGRPDVLF 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 568980685 1168 LDEATSALDNES-EKVVQQALDKARRGKTCLV-VAHRLSTIQNADMIVVLQNGSIKEQ 1223
Cdd:PRK10584 170 ADEPTGNLDRQTgDKIADLLFSLNREHGTTLIlVTHDLQLAARCDRRLRLVNGQLQEE 227
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1016-1239 |
2.86e-12 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 67.14 E-value: 2.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1016 RPEVPVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVKEL------NVQWLRSQTAIvsqEP 1089
Cdd:PRK13538 11 RDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQrdeyhqDLLYLGHQPGI---KT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1090 VLfncSIAENIAYgdnsrmvpLEEIKEVADAANIHSFIEGlprkyntlVGLRGV------QLSGGQKQRLAIARALLRKP 1163
Cdd:PRK13538 88 EL---TALENLRF--------YQRLHGPGDDEALWEALAQ--------VGLAGFedvpvrQLSAGQQRRVALARLWLTRA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568980685 1164 KILLLDEATSALDNESEKVVQQALDK-ARRGKtclvvahrlstiqnadmIVVLQngsikeqgTHQELLRNGDTYFKL 1239
Cdd:PRK13538 149 PLWILDEPFTAIDKQGVARLEALLAQhAEQGG-----------------MVILT--------THQDLPVASDKVRKL 200
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1018-1240 |
3.12e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 69.35 E-value: 3.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1018 EVPVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVKELNVQWLRSQTAIVSQE-------PV 1090
Cdd:COG4586 34 EVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFKRRKEFARRIGVVFGQRsqlwwdlPA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1091 LfncsiaeniaygDNSRMvpLEEIKEVADAA---NIHSFIE--GLPRKYNTLVglRgvQLSGGQKQRLAIARALLRKPKI 1165
Cdd:COG4586 114 I------------DSFRL--LKAIYRIPDAEykkRLDELVEllDLGELLDTPV--R--QLSLGQRMRCELAAALLHRPKI 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568980685 1166 LLLDEATSALDNESEKVVQQALDK--ARRGKTCLVVAHRLSTIQN-ADMIVVLQNGSIKEQGTHQELLRNGDTYFKLV 1240
Cdd:COG4586 176 LFLDEPTIGLDVVSKEAIREFLKEynRERGTTILLTSHDMDDIEAlCDRVIVIDHGRIIYDGSLEELKERFGPYKTIV 253
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
1031-1212 |
3.35e-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: 65.47 E-value: 3.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1031 KGKTVAFVGSSGCGKSTCVQLLQRFYDPmkgqvllDGVDVKELNVQWLRSQTAIvsqepvlfncsiaeniaygdnsrmvp 1110
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGP-------PGGGVIYIDGEDILEEVLD-------------------------- 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1111 leeikevadaanihsfieglpRKYNTLVGLRGVQLSGGQKQRLAIARALLRKPKILLLDEATSALDNESEKVVQQALD-- 1188
Cdd:smart00382 48 ---------------------QLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElr 106
|
170 180
....*....|....*....|....*....
gi 568980685 1189 -----KARRGKTCLVVAHRLSTIQNADMI 1212
Cdd:smart00382 107 lllllKSEKNLTVILTTNDEKDLGPALLR 135
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1024-1234 |
4.77e-12 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 67.71 E-value: 4.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1024 NMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVKEL---------------NVQWLRSQTAI---- 1084
Cdd:PRK11300 23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLpghqiarmgvvrtfqHVRLFREMTVIenll 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1085 VSQEPVLfncsiaeniaygdNSRMVP-LeeikeVADAANIHSFIEGLPRKYNTL--VGLRGV------QLSGGQKQRLAI 1155
Cdd:PRK11300 103 VAQHQQL-------------KTGLFSgL-----LKTPAFRRAESEALDRAATWLerVGLLEHanrqagNLAYGQQRRLEI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1156 ARALLRKPKILLLDEATSALDNESEKVVQQALDKARR--GKTCLVVAHRLSTIQN-ADMIVVLQNGSIKEQGTHQELLRN 1232
Cdd:PRK11300 165 ARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNehNVTVLLIEHDMKLVMGiSDRIYVVNQGTPLANGTPEEIRNN 244
|
..
gi 568980685 1233 GD 1234
Cdd:PRK11300 245 PD 246
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
375-574 |
5.66e-12 |
|
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: 66.11 E-value: 5.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 375 IEFKNVSFSYPSRPSAK-VLKGLNLKIKAGETVALVGPSGSGKSTTVQLL-QRlydPEDGCITvdeNDIRA---QNVRHY 449
Cdd:cd03232 4 LTWKNLNYTVPVKGGKRqLLNNISGYVKPGTLTALMGESGAGKTTLLDVLaGR---KTAGVIT---GEILIngrPLDKNF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 450 REQIGVVRQEPVLFGttignnikfgregvgekemEQAAREAnaydfiMAFPKKFNTLvgekgaqmSGGQKQRIAIARALV 529
Cdd:cd03232 78 QRSTGYVEQQDVHSP-------------------NLTVREA------LRFSALLRGL--------SVEQRKRLTIGVELA 124
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 568980685 530 RNPKILILDEATSALDTESESLVQTALEK-ASKGRTTIVVAHRLST 574
Cdd:cd03232 125 AKPSILFLDEPTSGLDSQAAYNIVRFLKKlADSGQAILCTIHQPSA 170
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
378-587 |
5.67e-12 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 69.76 E-value: 5.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 378 KNVSFSYPSrpsAKVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDIRAQNVRHYREQ-IGVV 456
Cdd:PRK10982 2 SNISKSFPG---VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALENgISMV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 457 RQE-PVLFGTTIGNNIKFGR---EG--VGEKEMEQAAREANAYDFIMAFPKkfntlvgEKGAQMSGGQKQRIAIARALVR 530
Cdd:PRK10982 79 HQElNLVLQRSVMDNMWLGRyptKGmfVDQDKMYRDTKAIFDELDIDIDPR-------AKVATLSVSQMQMIEIAKAFSY 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 568980685 531 NPKILILDEATSAL-DTESESLVQTALEKASKGRTTIVVAHRLSTI-RGADLIVTMKDG 587
Cdd:PRK10982 152 NAKIVIMDEPTSSLtEKEVNHLFTIIRKLKERGCGIVYISHKMEEIfQLCDEITILRDG 210
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
383-590 |
6.24e-12 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 69.67 E-value: 6.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 383 SYPSRPSAKVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDIRAQNVRHYREQ-IGVVRQEPV 461
Cdd:COG3845 264 SVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLgVAYIPEDRL 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 462 LFGT----TIGNNI--------KFGREGVgekeMEQAAREANAYDFIMAF---PKKFNTLVGekgaQMSGGQKQRIAIAR 526
Cdd:COG3845 344 GRGLvpdmSVAENLilgryrrpPFSRGGF----LDRKAIRAFAEELIEEFdvrTPGPDTPAR----SLSGGNQQKVILAR 415
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568980685 527 ALVRNPKILILDEATSALDTESESLVQTAL-EKASKGRTTIVVAHRLSTIRG-ADLIVTMKDGMVV 590
Cdd:COG3845 416 ELSRDPKLLIAAQPTRGLDVGAIEFIHQRLlELRDAGAAVLLISEDLDEILAlSDRIAVMYEGRIV 481
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1020-1210 |
8.15e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 65.74 E-value: 8.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1020 PVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVKELNVQWLRSQTAIVSQEPVLFNCSIAEN 1099
Cdd:PRK13540 15 PLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCFVGHRSGINPYLTLREN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1100 IAYGDNSRMVPLeEIKEVADAANIHSFIEgLPrkyntlVGLrgvqLSGGQKQRLAIARALLRKPKILLLDEATSALDNES 1179
Cdd:PRK13540 95 CLYDIHFSPGAV-GITELCRLFSLEHLID-YP------CGL----LSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELS 162
|
170 180 190
....*....|....*....|....*....|..
gi 568980685 1180 EKVVQQALDKAR-RGKTCLVVAHRLSTIQNAD 1210
Cdd:PRK13540 163 LLTIITKIQEHRaKGGAVLLTSHQDLPLNKAD 194
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1017-1218 |
1.13e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 68.88 E-value: 1.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1017 PEVPVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGvdvKELNVQWLR-SQTA---IVSQEPVLF 1092
Cdd:PRK10762 15 PGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLG---KEVTFNGPKsSQEAgigIIHQELNLI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1093 -NCSIAENIAYGDN--SRMVPLEEIKEVADAANIHSFIeGLPRKYNTLVGlrgvQLSGGQKQRLAIARALLRKPKILLLD 1169
Cdd:PRK10762 92 pQLTIAENIFLGREfvNRFGRIDWKKMYAEADKLLARL-NLRFSSDKLVG----ELSIGEQQMVEIAKVLSFESKVIIMD 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 568980685 1170 EATSAL-DNESE---KVVQQaLDKARRGktCLVVAHRLSTI-QNADMIVVLQNG 1218
Cdd:PRK10762 167 EPTDALtDTETEslfRVIRE-LKSQGRG--IVYISHRLKEIfEICDDVTVFRDG 217
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1007-1220 |
1.21e-11 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 68.51 E-value: 1.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1007 REVSFVYPCRPEVP--------------VLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVKe 1072
Cdd:COG1129 239 RELEDLFPKRAAAPgevvleveglsvggVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVR- 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1073 lnvqwLRS-QTAI------VS----QEPVLFNCSIAENI---AYGDNSRMVPLEEIKEVADAAnihSFIEGL---PRKYN 1135
Cdd:COG1129 318 -----IRSpRDAIragiayVPedrkGEGLVLDLSIRENItlaSLDRLSRGGLLDRRRERALAE---EYIKRLrikTPSPE 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1136 TLVGlrgvQLSGGQKQRLAIARALLRKPKILLLDEATSALD----NEsekvVQQALDK-ARRGKTCLVVahrlST----- 1205
Cdd:COG1129 390 QPVG----NLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDvgakAE----IYRLIRElAAEGKAVIVI----SSelpel 457
|
250
....*....|....*
gi 568980685 1206 IQNADMIVVLQNGSI 1220
Cdd:COG1129 458 LGLSDRILVMREGRI 472
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
395-570 |
1.34e-11 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 65.21 E-value: 1.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 395 GLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDIRAQNVRHYRE------QIGVvrqEPVLfgtTIG 468
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDllylghQPGI---KTEL---TAL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 469 NNIKFGREGVGEKEmEQAAREANAydfimafpkkfntLVGEKG------AQMSGGQKQRIAIARALVRNPKILILDEATS 542
Cdd:PRK13538 93 ENLRFYQRLHGPGD-DEALWEALA-------------QVGLAGfedvpvRQLSAGQQRRVALARLWLTRAPLWILDEPFT 158
|
170 180
....*....|....*....|....*....
gi 568980685 543 ALDTES-ESLVQTALEKASKGRTTIVVAH 570
Cdd:PRK13538 159 AIDKQGvARLEALLAQHAEQGGMVILTTH 187
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
375-576 |
1.43e-11 |
|
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: 69.01 E-value: 1.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 375 IEFKNVSFSYPSrpSAKVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDEndiraqnvrhyREQIG 454
Cdd:TIGR00954 452 IKFENIPLVTPN--GDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPA-----------KGKLF 518
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 455 VVRQEPVLFGTTIGNNI-------KFGREGVGEKEMEQAAREAnaydfimafpkKFNTLVGEKGA---------QMSGGQ 518
Cdd:TIGR00954 519 YVPQRPYMTLGTLRDQIiypdsseDMKRRGLSDKDLEQILDNV-----------QLTHILEREGGwsavqdwmdVLSGGE 587
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 568980685 519 KQRIAIARALVRNPKILILDEATSALDTESESLVQTALEKAskGRTTIVVAHRLSTIR 576
Cdd:TIGR00954 588 KQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCREF--GITLFSVSHRKSLWK 643
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
382-570 |
1.69e-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: 65.89 E-value: 1.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 382 FSYPSrpSAKVLKGLNLKIKAG-----ETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDI--RAQNVRhyREQIG 454
Cdd:cd03237 1 YTYPT--MKKTLGEFTLEVEGGsisesEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVsyKPQYIK--ADYEG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 455 VVRQepVLFGTTignnikfgregvgekemeQAAREANAYDFIMAFPKKFNTLVGEKGAQMSGGQKQRIAIARALVRNPKI 534
Cdd:cd03237 77 TVRD--LLSSIT------------------KDFYTHPYFKTEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADI 136
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 568980685 535 LILDEATSALDTESESLVQTAL----EKASKgrTTIVVAH 570
Cdd:cd03237 137 YLLDEPSAYLDVEQRLMASKVIrrfaENNEK--TAFVVEH 174
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
1026-1231 |
1.97e-11 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 65.72 E-value: 1.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1026 SLSIEKGKTVAFVGSSGCGKSTcvqLLQRFYD--PMKGQVLLDGVDVKELNVQWLRSQTAIVSQE-PVLFNCSIAENIAY 1102
Cdd:PRK03695 16 SAEVRAGEILHLVGPNGAGKST---LLARMAGllPGSGSIQFAGQPLEAWSAAELARHRAYLSQQqTPPFAMPVFQYLTL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1103 --GDNSRMVPLE-EIKEVADAANIHSFiegLPRKYNtlvglrgvQLSGGQKQRLAIARALLR-----KP--KILLLDEAT 1172
Cdd:PRK03695 93 hqPDKTRTEAVAsALNEVAEALGLDDK---LGRSVN--------QLSGGEWQRVRLAAVVLQvwpdiNPagQLLLLDEPM 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568980685 1173 SALDnesekVVQQ-ALDK-----ARRGKTCLVVAHRLS-TIQNADMIVVLQNGSIKEQGTHQELLR 1231
Cdd:PRK03695 162 NSLD-----VAQQaALDRllselCQQGIAVVMSSHDLNhTLRHADRVWLLKQGKLLASGRRDEVLT 222
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
753-938 |
2.30e-11 |
|
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: 66.21 E-value: 2.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 753 LAMRLRHSAFKAMLYQDMAWYDdkENNTGALTTTLAVDVAQIqgaatSRlgIVTQDVSNMSLSI-----LISFIYG--WE 825
Cdd:cd18590 67 LNLRLRHQLFSSLVQQDIGFFE--KTKTGDLTSRLSTDTTLM-----SR--SVALNANVLLRSLvktlgMLGFMLSlsWQ 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 826 MTLLILSFAPVLAVTGMIQTAAMAGFANRDKQALKRAGKIATEAVENIRTVVSLTRERAFEQMYEETLQTQHRNALKRAH 905
Cdd:cd18590 138 LTLLTLIEMPLTAIAQKVYNTYHQKLSQAVQDSIAKAGELAREAVSSIRTVRSFKAEEEEACRYSEALERTYNLKDRRDT 217
|
170 180 190
....*....|....*....|....*....|...
gi 568980685 906 ITGCCYAVSHAFVHFAHAAGFRFGAYLIQAGRM 938
Cdd:cd18590 218 VRAVYLLVRRVLQLGVQVLMLYCGRQLIQSGHL 250
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
375-600 |
4.68e-11 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 64.72 E-value: 4.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 375 IEFKNVSFsYPSRPsakVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDP----EDGCITVD-----ENDIRA-- 443
Cdd:PRK10418 5 IELRNIAL-QAAQP---LVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDgkpvaPCALRGrk 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 444 -----QNVR-----------HYRE---QIGVVRQEPVLFGTTignnikfgrEGVGekeMEQAAREANAYDFimafpkkfn 504
Cdd:PRK10418 81 iatimQNPRsafnplhtmhtHAREtclALGKPADDATLTAAL---------EAVG---LENAARVLKLYPF--------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 505 tlvgekgaQMSGGQKQRIAIARALVRNPKILILDEATSALDTESESLVQTALEK--ASKGRTTIVVAHRLSTI-RGADLI 581
Cdd:PRK10418 140 --------EMSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESivQKRALGMLLVTHDMGVVaRLADDV 211
|
250
....*....|....*....
gi 568980685 582 VTMKDGMVVEKGTHAELMA 600
Cdd:PRK10418 212 AVMSHGRIVEQGDVETLFN 230
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1009-1201 |
5.55e-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: 66.88 E-value: 5.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1009 VSFVYPcrPEVPVLQNMSLSIEKGKTVAFVGSSGCGKSTcvqLLQrfydpmkgqvLLDGVDvKELNVQWLRSQTAIV--- 1085
Cdd:TIGR03719 10 VSKVVP--PKKEILKDISLSFFPGAKIGVLGLNGAGKST---LLR----------IMAGVD-KDFNGEARPQPGIKVgyl 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1086 SQEPVL-FNCSIAENI-------------------AYGDNS--------RMVPLEEIKEVADAANIHSFIE------GLP 1131
Cdd:TIGR03719 74 PQEPQLdPTKTVRENVeegvaeikdaldrfneisaKYAEPDadfdklaaEQAELQEIIDAADAWDLDSQLEiamdalRCP 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1132 rKYNTLVGLrgvqLSGGQKQRLAIARALLRKPKILLLDEATSALDNESEKVVQQALdkARRGKTCLVVAH 1201
Cdd:TIGR03719 154 -PWDADVTK----LSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHL--QEYPGTVVAVTH 216
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
736-894 |
6.57e-11 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B member 8, mitochondrial, and similar proteins; This group includes ABCB8, which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. ABCB8 is essential for maintenance of normal cardiac function, involves mitochondrial iron export, and plays a role in the maturation of cytosolic Fe/S cluster-containing enzymes. ABCB8 is a half-molecule ABC protein that contains one TMD fused to a NBD, which dimerize to form a functional transporter.
Pssm-ID: 350018 [Multi-domain] Cd Length: 295 Bit Score: 64.87 E-value: 6.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 736 LVTYLMQGLF---Y----GRAEENLAMRLRHSAFKAMLYQDMAWYDdkENNTGALTTTLAVDVAQIQGAATSrlgIVTQD 808
Cdd:cd18574 49 LGLYLLQSLLtfaYisllSVVGERVAARLRNDLFSSLLRQDIAFFD--THRTGELVNRLTADVQEFKSSFKQ---CVSQG 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 809 VSNMSLSI-------LISFiygwEMTLLILSFAPVLAVTGMIQTAAMAGFANRDKQALKRAGKIATEAVENIRTVVSLTR 881
Cdd:cd18574 124 LRSVTQTVgcvvslyLISP----KLTLLLLVIVPVVVLVGTLYGSFLRKLSRRAQAQVAKATGVADEALGNIRTVRAFAM 199
|
170
....*....|...
gi 568980685 882 ERAFEQMYEETLQ 894
Cdd:cd18574 200 EDRELELYEEEVE 212
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
377-590 |
7.47e-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: 63.05 E-value: 7.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 377 FKNVSF-SYPSRPSAKVLKGLNLKIKAGETVALVGPSGSGKSTtvqLLQRLYDPEDGCITVdENDIR------AQNVRHY 449
Cdd:cd03233 6 WRNISFtTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCST---LLKALANRTEGNVSV-EGDIHyngipyKEFAEKY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 450 REQIGVVRQEPVLFGT-TIGNNIKFgregvgekemeqaAREANAYDFIMAFpkkfntlvgekgaqmSGGQKQRIAIARAL 528
Cdd:cd03233 82 PGEIIYVSEEDVHFPTlTVRETLDF-------------ALRCKGNEFVRGI---------------SGGERKRVSIAEAL 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568980685 529 VRNPKILILDEATSALDTeseslvQTALEKASKGRTtivVAH--RLSTIRGA-----------DLIVTMKDGMVV 590
Cdd:cd03233 134 VSRASVLCWDNSTRGLDS------STALEILKCIRT---MADvlKTTTFVSLyqasdeiydlfDKVLVLYEGRQI 199
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
1021-1231 |
8.37e-11 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 64.08 E-value: 8.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1021 VLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQ-RFYDP-------MKGQVLLDGVDVKELNVQWLRSQTAIVSQ--EPV 1090
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAgDLTGGgaprgarVTGDVTLNGEPLAAIDAPRLARLRAVLPQaaQPA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1091 lFNCSIAENIAYG--DNSRMVPLEEIK--EVADAAnihsfiegLPRK-YNTLVGLRGVQLSGGQKQRLAIARAL------ 1159
Cdd:PRK13547 96 -FAFSAREIVLLGryPHARRAGALTHRdgEIAWQA--------LALAgATALVGRDVTTLSGGELARVQFARVLaqlwpp 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1160 ---LRKPKILLLDEATSALDNESEkvvQQALDKARR-------GKTCLVVAHRLSTiQNADMIVVLQNGSIKEQGTHQEL 1229
Cdd:PRK13547 167 hdaAQPPRYLLLDEPTAALDLAHQ---HRLLDTVRRlardwnlGVLAIVHDPNLAA-RHADRIAMLADGAIVAHGAPADV 242
|
..
gi 568980685 1230 LR 1231
Cdd:PRK13547 243 LT 244
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
1021-1204 |
1.19e-10 |
|
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: 65.93 E-value: 1.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1021 VLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYdPMKGQVLLDGVDVKELnvqwlrsqtaIVSQEPVLFNCSIAENI 1100
Cdd:TIGR00954 467 LIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELW-PVYGGRLTKPAKGKLF----------YVPQRPYMTLGTLRDQI 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1101 AYGDNS--------RMVPLEEIKEVADAANIhsfiegLPRKyntlVGLRGVQ-----LSGGQKQRLAIARALLRKPKILL 1167
Cdd:TIGR00954 536 IYPDSSedmkrrglSDKDLEQILDNVQLTHI------LERE----GGWSAVQdwmdvLSGGEKQRIAMARLFYHKPQFAI 605
|
170 180 190
....*....|....*....|....*....|....*..
gi 568980685 1168 LDEATSALDNESEKVVQQALDKArrGKTCLVVAHRLS 1204
Cdd:TIGR00954 606 LDECTSAVSVDVEGYMYRLCREF--GITLFSVSHRKS 640
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
395-598 |
1.25e-10 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 63.47 E-value: 1.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 395 GLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDIRAQNvRHYREQIGVVR--QEPVLFG--TTIGN- 469
Cdd:PRK11300 23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLP-GHQIARMGVVRtfQHVRLFRemTVIENl 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 470 ------NIK-------FGREGVGEKEMEQAAREANAYDFIMAFPkkfntLVGEKGAQMSGGQKQRIAIARALVRNPKILI 536
Cdd:PRK11300 102 lvaqhqQLKtglfsglLKTPAFRRAESEALDRAATWLERVGLLE-----HANRQAGNLAYGQQRRLEIARCMVTQPEILM 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568980685 537 LDEATSALD-TESESLVQTALE-KASKGRTTIVVAHRLSTIRG-ADLIVTMKDGMVVEKGTHAEL 598
Cdd:PRK11300 177 LDEPAAGLNpKETKELDELIAElRNEHNVTVLLIEHDMKLVMGiSDRIYVVNQGTPLANGTPEEI 241
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1020-1218 |
1.43e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 65.74 E-value: 1.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1020 PVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQrfydpmkGQVLLD-GvdvkELNVQwlrsQTAIVS---QEP------ 1089
Cdd:PRK11147 17 PLLDNAELHIEDNERVCLVGRNGAGKSTLMKILN-------GEVLLDdG----RIIYE----QDLIVArlqQDPprnveg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1090 VLFNcSIAENIA--------YGDNSRMVP----------LEEIKEVADAAN-------IHSFIEGLPRKYNTLVGlrgvQ 1144
Cdd:PRK11147 82 TVYD-FVAEGIEeqaeylkrYHDISHLVEtdpseknlneLAKLQEQLDHHNlwqlenrINEVLAQLGLDPDAALS----S 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568980685 1145 LSGGQKQRLAIARALLRKPKILLLDEATSALDNESEKVVQQALdKARRGkTCLVVAHRLSTIQN-ADMIVVLQNG 1218
Cdd:PRK11147 157 LSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFL-KTFQG-SIIFISHDRSFIRNmATRIVDLDRG 229
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
994-1218 |
1.63e-10 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 65.29 E-value: 1.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 994 GEKPDTCEGNLEFREVSfvypcrpevpVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQ-RFY-DPMKGQVLLDGvdvK 1071
Cdd:PLN03211 66 GHKPKISDETRQIQERT----------ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAgRIQgNNFTGTILANN---R 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1072 ELNVQWLRsQTAIVSQEPVLF-NCSIAENIAYGDNSRMvPLEEIKEVADAANIHSFIE-GLPRKYNTLVG---LRGVqlS 1146
Cdd:PLN03211 133 KPTKQILK-RTGFVTQDDILYpHLTVRETLVFCSLLRL-PKSLTKQEKILVAESVISElGLTKCENTIIGnsfIRGI--S 208
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568980685 1147 GGQKQRLAIARALLRKPKILLLDEATSALDNESE-KVVQQALDKARRGKTCLVVAHRLST--IQNADMIVVLQNG 1218
Cdd:PLN03211 209 GGERKRVSIAHEMLINPSLLILDEPTSGLDATAAyRLVLTLGSLAQKGKTIVTSMHQPSSrvYQMFDSVLVLSEG 283
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1009-1179 |
1.76e-10 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 65.14 E-value: 1.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1009 VSFVYPcrPEVPVLQNMSLSIEKGKTVAFVGSSGCGKSTcvqLLQrfydpmkgqvLLDGVDvKELNVQWLRSQTAIV--- 1085
Cdd:PRK11819 12 VSKVVP--PKKQILKDISLSFFPGAKIGVLGLNGAGKST---LLR----------IMAGVD-KEFEGEARPAPGIKVgyl 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1086 SQEPVL-----------------------FNcSIAENIAYGDN------SRMVPLEEIKEVADAANIHSFIE------GL 1130
Cdd:PRK11819 76 PQEPQLdpektvrenveegvaevkaaldrFN-EIYAAYAEPDAdfdalaAEQGELQEIIDAADAWDLDSQLEiamdalRC 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 568980685 1131 PRKyNTLVGlrgvQLSGGQKQRLAIARALLRKPKILLLDEATSALDNES 1179
Cdd:PRK11819 155 PPW-DAKVT----KLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES 198
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
723-949 |
1.83e-10 |
|
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: 63.22 E-value: 1.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 723 LYSMMLVVLGIV-ALVTYLmQGLFYGRAEENLAMRLRHSAFKAMLYQDMAWYDDkeNNTGALTTTLAVDVAQIQGAATSR 801
Cdd:cd18542 40 LLALLILGVALLrGVFRYL-QGYLAEKASQKVAYDLRNDLYDHLQRLSFSFHDK--ARTGDLMSRCTSDVDTIRRFLAFG 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 802 LGIVTQDVSNMSLSILISFIYGWEMTLLILSFAPVLAVTGMIqtaamagFANRDKQALKRA----GKIATEAVENI---R 874
Cdd:cd18542 117 LVELVRAVLLFIGALIIMFSINWKLTLISLAIIPFIALFSYV-------FFKKVRPAFEEIreqeGELNTVLQENLtgvR 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568980685 875 TVVSLTRERA----FEQMYEETLQTQhrnaLKRAHITGCCYAVSHAFVHFAHAAGFRFGAYLIQAGRMMPeGMFIVFTA 949
Cdd:cd18542 190 VVKAFAREDYeiekFDKENEEYRDLN----IKLAKLLAKYWPLMDFLSGLQIVLVLWVGGYLVINGEITL-GELVAFIS 263
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1021-1232 |
1.94e-10 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 62.60 E-value: 1.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1021 VLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVKELNVQwLRSQTAI--VSQEPvlfncSIAE 1098
Cdd:PRK10895 18 VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLH-ARARRGIgyLPQEA-----SIFR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1099 NIAYGDNsrMVPLEEIKEVADAANIHSFIEGLPRKYNtLVGLR---GVQLSGGQKQRLAIARALLRKPKILLLDEATSAL 1175
Cdd:PRK10895 92 RLSVYDN--LMAVLQIRDDLSAEQREDRANELMEEFH-IEHLRdsmGQSLSGGERRRVEIARALAANPKFILLDEPFAGV 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568980685 1176 DNES----EKVVQQALDkarRGKTCLVVAHRL-STIQNADMIVVLQNGSIKEQGTHQELLRN 1232
Cdd:PRK10895 169 DPISvidiKRIIEHLRD---SGLGVLITDHNVrETLAVCERAYIVSQGHLIAHGTPTEILQD 227
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
399-598 |
2.35e-10 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 63.61 E-value: 2.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 399 KIKAGETVALVGPSGSGKSTTVQLLQRLYD-PedGCITVDE-----NDIRAQNVRHYREQIG----VVRQEPVL------ 462
Cdd:PRK11022 29 SVKQGEVVGIVGESGSGKSVSSLAIMGLIDyP--GRVMAEKlefngQDLQRISEKERRNLVGaevaMIFQDPMTslnpcy 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 463 -FGTTIGNNIKFGREGvgekemEQAAREANAYDFImafpkkfnTLVGEKGA---------QMSGGQKQRIAIARALVRNP 532
Cdd:PRK11022 107 tVGFQIMEAIKVHQGG------NKKTRRQRAIDLL--------NQVGIPDPasrldvyphQLSGGMSQRVMIAMAIACRP 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568980685 533 KILILDEATSALD-TESESLVQTALE-KASKGRTTIVVAHRLSTI-RGADLIVTMKDGMVVEKGTHAEL 598
Cdd:PRK11022 173 KLLIADEPTTALDvTIQAQIIELLLElQQKENMALVLITHDLALVaEAAHKIIVMYAGQVVETGKAHDI 241
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
392-575 |
2.82e-10 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 65.13 E-value: 2.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 392 VLKGLNLKIKAGETVALVGPSGSGKST-----TVQLLQRLYDpEDGCITVD---ENDIRaqnvRHYREQIGVVRQEPVLF 463
Cdd:TIGR00956 76 ILKPMDGLIKPGELTVVLGRPGSGCSTllktiASNTDGFHIG-VEGVITYDgitPEEIK----KHYRGDVVYNAETDVHF 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 464 GT-TIGNNIKF-------GREGVGEKEMEQAAREANAYDFIMAFPKKFNTLVGE---KGaqMSGGQKQRIAIARALVRNP 532
Cdd:TIGR00956 151 PHlTVGETLDFaarcktpQNRPDGVSREEYAKHIADVYMATYGLSHTRNTKVGNdfvRG--VSGGERKRVSIAEASLGGA 228
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 568980685 533 KILILDEATSALDTeseslvQTALEKASKGRTTIVVAHRLSTI 575
Cdd:TIGR00956 229 KIQCWDNATRGLDS------ATALEFIRALKTSANILDTTPLV 265
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
375-602 |
3.82e-10 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 62.09 E-value: 3.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 375 IEFKNVSFSYPSRPsakVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDIRA-QNVRHY--RE 451
Cdd:PRK11831 8 VDMRGVSFTRGNRC---IFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAmSRSRLYtvRK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 452 QIGVVRQEPVLF-GTTIGNNIKFGRegvgeKEMEQAAREANAYDFIMAFPKkfntlVGEKGA------QMSGGQKQRIAI 524
Cdd:PRK11831 85 RMSMLFQSGALFtDMNVFDNVAYPL-----REHTQLPAPLLHSTVMMKLEA-----VGLRGAaklmpsELSGGMARRAAL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 525 ARALVRNPKILILDEATSALDTESES-LVQTALE-KASKGRTTIVVAHRLSTIRG-ADLIVTMKDGMVVEKGTHAELMAK 601
Cdd:PRK11831 155 ARAIALEPDLIMFDEPFVGQDPITMGvLVKLISElNSALGVTCVVVSHDVPEVLSiADHAYIVADKKIVAHGSAQALQAN 234
|
.
gi 568980685 602 Q 602
Cdd:PRK11831 235 P 235
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
716-947 |
3.92e-10 |
|
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: 62.33 E-value: 3.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 716 TLKQDAELYSMMLVVLGIVALVTYL---MQGLFYGRAEENLAMRLRHSAFKAMLYQDMAWYDdkENNTGALTTTLAVDVA 792
Cdd:cd18784 27 VIEKSQDKFSRAIIIMGLLAIASSVaagIRGGLFTLAMARLNIRIRNLLFRSIVSQEIGFFD--TVKTGDITSRLTSDTT 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 793 QIQGAATSRLGIVTQDVSNMSLSILISFIYGWEMTLLILSFAPVLAVTGMIQTAAMAGFANRDKQALKRAGKIATEAVEN 872
Cdd:cd18784 105 TMSDTVSLNLNIFLRSLVKAIGVIVFMFKLSWQLSLVTLIGLPLIAIVSKVYGDYYKKLSKAVQDSLAKANEVAEETISS 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568980685 873 IRTVVSLTRERAFEQMYEETLQTQHRNALKRAHITGCCYAVSHAFVHFAHAAGFRFGAYLIQAGRmMPEGMFIVF 947
Cdd:cd18784 185 IRTVRSFANEDGEANRYSEKLKDTYKLKIKEALAYGGYVWSNELTELALTVSTLYYGGHLVITGQ-ISGGNLISF 258
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
391-567 |
4.31e-10 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 62.80 E-value: 4.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 391 KVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDI---RAQNVRhyreQIGVV---RQE----- 459
Cdd:COG4586 36 EAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPfkrRKEFAR----RIGVVfgqRSQlwwdl 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 460 PV-----LFG-------TTIGNNIKFGRE--GVGEKeMEQAAReanaydfimafpkkfntlvgekgaQMSGGQKQRIAIA 525
Cdd:COG4586 112 PAidsfrLLKaiyripdAEYKKRLDELVEllDLGEL-LDTPVR------------------------QLSLGQRMRCELA 166
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 568980685 526 RALVRNPKILILDEATSALDTESESLVQTALEKASKGR-TTIV 567
Cdd:COG4586 167 AALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERgTTIL 209
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
1017-1238 |
7.65e-10 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 63.59 E-value: 7.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1017 PEVPVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLL----QRFYDPMKGQVLLDGVDVKELnVQWLRSQTAIVSQEPVLF 1092
Cdd:TIGR00956 72 KTFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIasntDGFHIGVEGVITYDGITPEEI-KKHYRGDVVYNAETDVHF 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1093 -NCSIAENIAY-----GDNSRMVPLEEIKEVADAANIHSFIEGLPRKYNTLVG---LRGVqlSGGQKQRLAIARALLRKP 1163
Cdd:TIGR00956 151 pHLTVGETLDFaarckTPQNRPDGVSREEYAKHIADVYMATYGLSHTRNTKVGndfVRGV--SGGERKRVSIAEASLGGA 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1164 KILLLDEATSALDNESekvvqqALDKARRGKTCLVVAHRLSTI------QNA----DMIVVLQNGSIKEQGTHQELLrng 1233
Cdd:TIGR00956 229 KIQCWDNATRGLDSAT------ALEFIRALKTSANILDTTPLVaiyqcsQDAyelfDKVIVLYEGYQIYFGPADKAK--- 299
|
....*
gi 568980685 1234 dTYFK 1238
Cdd:TIGR00956 300 -QYFE 303
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
97-319 |
9.37e-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: 350051 [Multi-domain] Cd Length: 293 Bit Score: 61.40 E-value: 9.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 97 LYYIGIGAAALIFGYVQISFWVI----TAARQTTR-IRKQFFHSILAQDISWFDGSDICELNTRMTGDINKLCDGIGDKI 171
Cdd:cd18778 39 LLGLALLLLGAYLLRALLNFLRIylnhVAEQKVVAdLRSDLYDKLQRLSLRYFDDRQTGDLMSRVINDVANVERLIADGI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 172 PLMFQNISGFSIGLVISLIKSWKLSLVVLSTSPLIMASSALCSRMIISLTSKELDAYSKAGAVAEEALSSIQTVTAFGAQ 251
Cdd:cd18778 119 PQGITNVLTLVGVAIILFSINPKLALLTLIPIPFLALGAWLYSKKVRPRYRKVREALGELNALLQDNLSGIREIQAFGRE 198
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568980685 252 EKEIQRYtqhlkDAKDAGIKRATASKLSLGAVYF-FMNGA----YGLAFWYGTSLIFGGEpgYTIGTILAVFF 319
Cdd:cd18778 199 EEEAKRF-----EALSRRYRKAQLRAMKLWAIFHpLMEFLtslgTVLVLGFGGRLVLAGE--LTIGDLVAFLL 264
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
100-310 |
9.59e-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: 350009 [Multi-domain] Cd Length: 313 Bit Score: 61.43 E-value: 9.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 100 IGIGAAALIFGYVQISFWVITAARQTTRIRKQFFHSILAQDISWFDGSDICELNTRMTGDINKLCDGIGDKIPLMFQNIS 179
Cdd:cd18565 61 VAAFLLESLFQYLSGVLWRRFAQRVQHDLRTDTYDHVQRLDMAFFEDRQTGDLMSVLNNDVNQLERFLDDGANSIIRVVV 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 180 GFSIGLVISLIKSWKLSLVVLSTSPLIMASSALCSRMIislTSKELDAYSKAGAVA---EEALSSIQTVTAFGAQEKEIQ 256
Cdd:cd18565 141 TVLGIGAILFYLNWQLALVALLPVPLIIAGTYWFQRRI---EPRYRAVREAVGDLNarlENNLSGIAVIKAFTAEDFERE 217
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 568980685 257 RYTQHLKDAKDAGIKRATASKLSLGAVYFFMNGAYGLAFWYGTSLIFGGEPGYT 310
Cdd:cd18565 218 RVADASEEYRDANWRAIRLRAAFFPVIRLVAGAGFVATFVVGGYWVLDGPPLFT 271
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
96-316 |
9.61e-10 |
|
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: 61.07 E-value: 9.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 96 TLYYIGIG--AAAL---IFGYVQISFWVITAARQTTRIRKQFFHSILAQDISWFDGSDICELNTRmTGDINKLCDGIGDK 170
Cdd:cd18782 40 TLYVIGVVmlVAALleaVLTALRTYLFTDTANRIDLELGGTIIDHLLRLPLGFFDKRPVGELSTR-ISELDTIRGFLTGT 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 171 IPLMFQNIsGFSIGLVISLIK-SWKLSLVVLSTSPLIMASSALCSRMIISLTSKELDAYSKAGAVAEEALSSIQTVTAFG 249
Cdd:cd18782 119 ALTTLLDV-LFSVIYIAVLFSySPLLTLVVLATVPLQLLLTFLFGPILRRQIRRRAEASAKTQSYLVESLTGIQTVKAQN 197
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568980685 250 AQEKEIQRYTQHLKDAKDAGIKrATASKLSLGAVYFFMNGAYGLAF-WYGTSLIFGGEpgYTIGTILA 316
Cdd:cd18782 198 AELKARWRWQNRYARSLGEGFK-LTVLGTTSGSLSQFLNKLSSLLVlWVGAYLVLRGE--LTLGQLIA 262
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
375-602 |
9.96e-10 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 60.58 E-value: 9.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 375 IEFKNVSFSYPSRPsakVLKGLNLKIKAGETVALVGPSGSGKSTTVQLL--QRLYDPEDGCITVDENDIRAQNVRHYR-E 451
Cdd:PRK09580 2 LSIKDLHVSVEDKA---ILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLagREDYEVTGGTVEFKGKDLLELSPEDRAgE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 452 QIGVVRQEPV--------LFGTTIGNNIKFGREgvgekemEQAAREANAYDFI------MAFPKKFNTLVGEKGaqMSGG 517
Cdd:PRK09580 79 GIFMAFQYPVeipgvsnqFFLQTALNAVRSYRG-------QEPLDRFDFQDLMeekialLKMPEDLLTRSVNVG--FSGG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 518 QKQRIAIARALVRNPKILILDEATSALDTESESLVQTALEKASKG-RTTIVVAH--RLSTIRGADLIVTMKDGMVVEKGT 594
Cdd:PRK09580 150 EKKRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGkRSFIIVTHyqRILDYIKPDYVHVLYQGRIVKSGD 229
|
....*...
gi 568980685 595 HAelMAKQ 602
Cdd:PRK09580 230 FT--LVKQ 235
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1019-1220 |
1.02e-09 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 62.35 E-value: 1.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1019 VPVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLL--QRfyDPMKGQVLLDGVDVKELNV-QWLRSQTAIVSQEP-----V 1090
Cdd:COG3845 271 VPALKDVSLEVRAGEILGIAGVAGNGQSELAEALagLR--PPASGSIRLDGEDITGLSPrERRRLGVAYIPEDRlgrglV 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1091 LfNCSIAENIAYGDNSRmvpleeiKEVA-----DAANIHSFIEGLPRKY-------NTLVGLrgvqLSGGQKQRLAIARA 1158
Cdd:COG3845 349 P-DMSVAENLILGRYRR-------PPFSrggflDRKAIRAFAEELIEEFdvrtpgpDTPARS----LSGGNQQKVILARE 416
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568980685 1159 LLRKPKILLLDEATSALDNES-EKVVQQALDKARRGKTCLVVAHRLSTIQN-ADMIVVLQNGSI 1220
Cdd:COG3845 417 LSRDPKLLIAAQPTRGLDVGAiEFIHQRLLELRDAGAAVLLISEDLDEILAlSDRIAVMYEGRI 480
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
378-570 |
1.05e-09 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 62.65 E-value: 1.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 378 KNVSFSYPsrPSAKVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGcitvdenDIRAQ-NVRhyreqIGVV 456
Cdd:TIGR03719 8 NRVSKVVP--PKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNG-------EARPQpGIK-----VGYL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 457 RQEPVLFGT-TIGNNIKfgrEGVGEKEmeQAAREANAYDFIMAFP-KKFNTLVGEKG----------------------- 511
Cdd:TIGR03719 74 PQEPQLDPTkTVRENVE---EGVAEIK--DALDRFNEISAKYAEPdADFDKLAAEQAelqeiidaadawdldsqleiamd 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 512 -----------AQMSGGQKQRIAIARALVRNPKILILDEATSALDTESESLVQTALEKaSKGrTTIVVAH 570
Cdd:TIGR03719 149 alrcppwdadvTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQE-YPG-TVVAVTH 216
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
995-1221 |
1.10e-09 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 62.53 E-value: 1.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 995 EKPDTCEGNLEFREVSFVYPCRPEVPVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYD-PMKGQVLLDG--VDVK 1071
Cdd:TIGR02633 249 EPHEIGDVILEARNLTCWDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPgKFEGNVFINGkpVDIR 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1072 ELnVQWLRSQTAIVSQE-------PVLfncSIAENIAYGDNSRMVPLEEIKEVADAANIHSFIEGLPRKYNTlVGLRGVQ 1144
Cdd:TIGR02633 329 NP-AQAIRAGIAMVPEDrkrhgivPIL---GVGKNITLSVLKSFCFKMRIDAAAELQIIGSAIQRLKVKTAS-PFLPIGR 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1145 LSGGQKQRLAIARALLRKPKILLLDEATSALD----NESEKVVQQAldkARRGKTCLVVAHRLSTIQN-ADMIVVLQNGS 1219
Cdd:TIGR02633 404 LSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDvgakYEIYKLINQL---AQEGVAIIVVSSELAEVLGlSDRVLVIGEGK 480
|
..
gi 568980685 1220 IK 1221
Cdd:TIGR02633 481 LK 482
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1024-1231 |
2.27e-09 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 60.53 E-value: 2.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1024 NMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYD-P---MKGQVLLDGVDVKELNVQWLR----SQTAIVSQEP------ 1089
Cdd:PRK11022 25 RISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDyPgrvMAEKLEFNGQDLQRISEKERRnlvgAEVAMIFQDPmtslnp 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1090 ---VLFNCSIAENIAYGDN-----SRMVPLEEIKEVADAAnihSFIEGLPRkyntlvglrgvQLSGGQKQRLAIARALLR 1161
Cdd:PRK11022 105 cytVGFQIMEAIKVHQGGNkktrrQRAIDLLNQVGIPDPA---SRLDVYPH-----------QLSGGMSQRVMIAMAIAC 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568980685 1162 KPKILLLDEATSALD-NESEKVVQQALDKARRGKTCLV-VAHRLSTI-QNADMIVVLQNGSIKEQGTHQELLR 1231
Cdd:PRK11022 171 RPKLLIADEPTTALDvTIQAQIIELLLELQQKENMALVlITHDLALVaEAAHKIIVMYAGQVVETGKAHDIFR 243
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1020-1231 |
2.38e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 61.28 E-value: 2.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1020 PVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVKELN-----------VQWLRSQTAIVSQE 1088
Cdd:PRK10982 262 PSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNaneainhgfalVTEERRSTGIYAYL 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1089 PVLFNCSIAENIAYG------DNSRMVplEEIKEVADAANIHSfieglPrKYNTLVGlrgvQLSGGQKQRLAIARALLRK 1162
Cdd:PRK10982 342 DIGFNSLISNIRNYKnkvgllDNSRMK--SDTQWVIDSMRVKT-----P-GHRTQIG----SLSGGNQQKVIIGRWLLTQ 409
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568980685 1163 PKILLLDEATSALDNESE-KVVQQALDKARRGKTCLVVAHRLSTIQN-ADMIVVLQNGSI-----KEQGTHQELLR 1231
Cdd:PRK10982 410 PEILMLDEPTRGIDVGAKfEIYQLIAELAKKDKGIIIISSEMPELLGiTDRILVMSNGLVagivdTKTTTQNEILR 485
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1004-1229 |
2.48e-09 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 61.48 E-value: 2.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1004 LEFREVSFVYPCRPEVPVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMK-GQVLLDGVDVKELN-VQWLRSQ 1081
Cdd:PRK13549 260 LEVRNLTAWDPVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPGRWeGEIFIDGKPVKIRNpQQAIAQG 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1082 TAIVSQE-------PVLfncSIAENIAYGDNSRMVPLEEIKEVADAANIHSFIEGLPRKYNTLVgLRGVQLSGGQKQRLA 1154
Cdd:PRK13549 340 IAMVPEDrkrdgivPVM---GVGKNITLAALDRFTGGSRIDDAAELKTILESIQRLKVKTASPE-LAIARLSGGNQQKAV 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1155 IARALLRKPKILLLDEATSALD----NESEKVVQQAldkARRGKTCLVVAHRLSTIQN-ADMIVVLQNGSIKEQGTHQEL 1229
Cdd:PRK13549 416 LAKCLLLNPKILILDEPTRGIDvgakYEIYKLINQL---VQQGVAIIVISSELPEVLGlSDRVLVMHEGKLKGDLINHNL 492
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
386-599 |
2.67e-09 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 59.46 E-value: 2.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 386 SRPSAKVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQ-RLYDPED-------GCITVDENDIRAQNVRHYREQIGVVR 457
Cdd:PRK13547 10 ARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAgDLTGGGAprgarvtGDVTLNGEPLAAIDAPRLARLRAVLP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 458 Q--EPVlFGTTIGNNIKFGREGVGEKEMEQAAREANAYDFIMAFPKKfNTLVGEKGAQMSGGQKQRIAIARAL------- 528
Cdd:PRK13547 90 QaaQPA-FAFSAREIVLLGRYPHARRAGALTHRDGEIAWQALALAGA-TALVGRDVTTLSGGELARVQFARVLaqlwpph 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568980685 529 --VRNPKILILDEATSALD-TESESLVQTALEKASK---GRTTIVVAHRLSTiRGADLIVTMKDGMVVEKGTHAELM 599
Cdd:PRK13547 168 daAQPPRYLLLDEPTAALDlAHQHRLLDTVRRLARDwnlGVLAIVHDPNLAA-RHADRIAMLADGAIVAHGAPADVL 243
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
386-579 |
2.72e-09 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 58.71 E-value: 2.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 386 SRPSAKVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVD-ENDIRAQNVRH--YREQIGVVRQEpvl 462
Cdd:PRK13543 20 SRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDgKTATRGDRSRFmaYLGHLPGLKAD--- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 463 fgTTIGNNIKF--GREGVGEKEMEQAAREanaydfIMAFPKKFNTLVgekgAQMSGGQKQRIAIARALVRNPKILILDEA 540
Cdd:PRK13543 97 --LSTLENLHFlcGLHGRRAKQMPGSALA------IVGLAGYEDTLV----RQLSAGQKKRLALARLWLSPAPLWLLDEP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 568980685 541 TSALDTESESLVQ-----------TALEKASKGRTTIVVAHRLSTIRGAD 579
Cdd:PRK13543 165 YANLDLEGITLVNrmisahlrgggAALVTTHGAYAAPPVRTRMLTLEAAA 214
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
375-553 |
3.05e-09 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 61.41 E-value: 3.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 375 IEFKNVSFSYPSRPSakVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCItvdendIRAQNVRhyreqIG 454
Cdd:PLN03073 509 ISFSDASFGYPGGPL--LFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTV------FRSAKVR-----MA 575
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 455 VVRQEPVlFGTTIGNN--IKFGR--EGVGEKEMeqaarEANAYDFIMAfpkkfNTLVGEKGAQMSGGQKQRIAIARALVR 530
Cdd:PLN03073 576 VFSQHHV-DGLDLSSNplLYMMRcfPGVPEQKL-----RAHLGSFGVT-----GNLALQPMYTLSGGQKSRVAFAKITFK 644
|
170 180
....*....|....*....|....
gi 568980685 531 NPKILILDEATSALDTES-ESLVQ 553
Cdd:PLN03073 645 KPHILLLDEPSNHLDLDAvEALIQ 668
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
727-949 |
6.54e-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: 350008 [Multi-domain] Cd Length: 307 Bit Score: 58.68 E-value: 6.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 727 MLVVLGIVALVTYLMQGLFyGRAEENLAMRLRHSAFKAMLYQDMAWYDdkENNTGALTTTLAVDVAQIQGAATSrlgIVT 806
Cdd:cd18564 60 LVGIALLRGLASYAGTYLT-ALVGQRVVLDLRRDLFAHLQRLSLSFHD--RRRTGDLLSRLTGDVGAIQDLLVS---GVL 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 807 QDVSNMsLSIL----ISFIYGWEMTLLILSFAPVLAVtgmiqtaAMAGFANRDKQAL----KRAGKIAT---EAVENIRT 875
Cdd:cd18564 134 PLLTNL-LTLVgmlgVMFWLDWQLALIALAVAPLLLL-------AARRFSRRIKEASreqrRREGALASvaqESLSAIRV 205
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568980685 876 VVSLTRERAFEqmyeETLQTQHRNALK---RAHITGCCYA-VSHAFVHFAHAAGFRFGAYLIQAGRMMPeGMFIVFTA 949
Cdd:cd18564 206 VQAFGREEHEE----RRFARENRKSLRaglRAARLQALLSpVVDVLVAVGTALVLWFGAWLVLAGRLTP-GDLLVFLA 278
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
726-975 |
7.37e-09 |
|
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: 58.65 E-value: 7.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 726 MMLVVLGIVALVTYLMqglFY--GRAEENLAMRLRHSAFKAMLYQDMAWYDdkENNTGALTTTLAVDVAQIQGAATSRLG 803
Cdd:cd18575 41 LLLAVALVLALASALR---FYlvSWLGERVVADLRKAVFAHLLRLSPSFFE--TTRTGEVLSRLTTDTTLIQTVVGSSLS 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 804 IVTQDVSNMSLSILISFIYGWEMTLLIL-----SFAPVLAVTGMIQTAAMAgfaNRDKQAlkRAGKIATEAVENIRTVVS 878
Cdd:cd18575 116 IALRNLLLLIGGLVMLFITSPKLTLLVLlviplVVLPIILFGRRVRRLSRA---SQDRLA--DLSAFAEETLSAIKTVQA 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 879 LTRERAFEQMYEETLQTQHRNALKRAHITGCCYAVSHAFVHFAHAAGFRFGAYLIQAGRMMPE--GMFIVFTAIAYGAMA 956
Cdd:cd18575 191 FTREDAERQRFATAVEAAFAAALRRIRARALLTALVIFLVFGAIVFVLWLGAHDVLAGRMSAGelSQFVFYAVLAAGSVG 270
|
250 260
....*....|....*....|
gi 568980685 957 -IGEtlVWApEYSKAkAGAS 975
Cdd:cd18575 271 aLSE--VWG-DLQRA-AGAA 286
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1022-1224 |
9.00e-09 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 57.97 E-value: 9.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1022 LQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVKELNVQWLrsqTAIVSQE-------PVLfnc 1094
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNL---VAYVPQSeevdwsfPVL--- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1095 sIAENIAYGDNSRM----VPLEEIKEVADAAnihsfiegLPRKynTLVGLRGVQ---LSGGQKQRLAIARALLRKPKILL 1167
Cdd:PRK15056 97 -VEDVVMMGRYGHMgwlrRAKKRDRQIVTAA--------LARV--DMVEFRHRQigeLSGGQKKRVFLARAIAQQGQVIL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 568980685 1168 LDEATSALDNESEKVVQQALDKAR-RGKTCLVVAHRLSTIQNADMIVVLQNGSIKEQG 1224
Cdd:PRK15056 166 LDEPFTGVDVKTEARIISLLRELRdEGKTMLVSTHNLGSVTEFCDYTVMVKGTVLASG 223
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
376-570 |
1.21e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 59.19 E-value: 1.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 376 EFKNVSFSYPSRpsaKVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDG---CITVDENDIRAQnvrhYREQ 452
Cdd:PRK11147 321 EMENVNYQIDGK---QLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGrihCGTKLEVAYFDQ----HRAE 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 453 IGVVRqepvlfgtTIGNNIKfgrEGVGEKEMEQAAREANAY--DFIMAfPKKFNTLVgekgAQMSGGQKQRIAIARALVR 530
Cdd:PRK11147 394 LDPEK--------TVMDNLA---EGKQEVMVNGRPRHVLGYlqDFLFH-PKRAMTPV----KALSGGERNRLLLARLFLK 457
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 568980685 531 NPKILILDEATSALDTESESLVQTALEkASKGrTTIVVAH 570
Cdd:PRK11147 458 PSNLLILDEPTNDLDVETLELLEELLD-SYQG-TVLLVSH 495
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1029-1212 |
1.25e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 59.05 E-value: 1.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1029 IEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDgVDV----------KELNVQ-WLRSQTAIVSQEPvlFNCSIA 1097
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE-LKIsykpqyikpdYDGTVEdLLRSITDDLGSSY--YKSEII 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1098 EniaygdnsrmvPLeeikevadaanihsfieGLPRKYNTLVGlrgvQLSGGQKQRLAIARALLRKPKILLLDEATSALDN 1177
Cdd:PRK13409 439 K-----------PL-----------------QLERLLDKNVK----DLSGGELQRVAIAACLSRDADLYLLDEPSAHLDV 486
|
170 180 190
....*....|....*....|....*....|....*..
gi 568980685 1178 ESEKVVQQALDK--ARRGKTCLVVAHRLSTIqnaDMI 1212
Cdd:PRK13409 487 EQRLAVAKAIRRiaEEREATALVVDHDIYMI---DYI 520
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
393-598 |
1.47e-08 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 59.26 E-value: 1.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 393 LKGLNLKIKAGETVALVGPSGSGKSTTVQ------LLQRLYDPE---------------DGCITVDENDI-RAQ--NVRH 448
Cdd:TIGR00630 624 LKNITVSIPLGLFTCITGVSGSGKSTLINdtlypaLANRLNGAKtvpgrytsieglehlDKVIHIDQSPIgRTPrsNPAT 703
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 449 YreqIGV---VRQepvLF---------GTTIGN---NIKFGR------EGVGEKEM------------------------ 483
Cdd:TIGR00630 704 Y---TGVfdeIRE---LFaetpeakvrGYTPGRfsfNVKGGRceacqgDGVIKIEMhflpdvyvpcevckgkrynretle 777
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 484 ------------EQAAREAnaYDFIMAFPK---KFNTLV---------GEKGAQMSGGQKQRIAIARALVR---NPKILI 536
Cdd:TIGR00630 778 vkykgkniadvlDMTVEEA--YEFFEAVPSisrKLQTLCdvglgyirlGQPATTLSGGEAQRIKLAKELSKrstGRTLYI 855
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568980685 537 LDEATSALDTESESLVQTALEK-ASKGRTTIVVAHRLSTIRGADLIVTM------KDGMVVEKGTHAEL 598
Cdd:TIGR00630 856 LDEPTTGLHFDDIKKLLEVLQRlVDKGNTVVVIEHNLDVIKTADYIIDLgpeggdGGGTVVASGTPEEV 924
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
401-573 |
1.93e-08 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 56.61 E-value: 1.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 401 KAGETVALVGPSGSGKSTTVQLLQRLYDPEDGciTVDENDIRAQNVRHYR-------------EQIGVVR------QEPV 461
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAGKLKPNLG--KFDDPPDWDEILDEFRgselqnyftklleGDVKVIVkpqyvdLIPK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 462 LFGTTIGNNIKfgregvgekemeqAAREANAYDFIMAfPKKFNTLVGEKGAQMSGGQKQRIAIARALVRNPKILILDEAT 541
Cdd:cd03236 102 AVKGKVGELLK-------------KKDERGKLDELVD-QLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPS 167
|
170 180 190
....*....|....*....|....*....|...
gi 568980685 542 SALDTESE-SLVQTALEKASKGRTTIVVAHRLS 573
Cdd:cd03236 168 SYLDIKQRlNAARLIRELAEDDNYVLVVEHDLA 200
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
381-590 |
2.08e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 58.42 E-value: 2.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 381 SFSYpsrpsAKVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCItvdendIRAQNVRHYREQIGVVRQEP 460
Cdd:PRK11147 12 SFSD-----APLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRI------IYEQDLIVARLQQDPPRNVE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 461 vlfgttiGNNIKFGREGVGE---------------------KEMEQAAR------EANAYDF---IMAFPKKFNTLVGEK 510
Cdd:PRK11147 81 -------GTVYDFVAEGIEEqaeylkryhdishlvetdpseKNLNELAKlqeqldHHNLWQLenrINEVLAQLGLDPDAA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 511 GAQMSGGQKQRIAIARALVRNPKILILDEATSALDTESESLVQTALeKASKGrTTIVVAHRLSTIRG-ADLIVTMKDGMV 589
Cdd:PRK11147 154 LSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFL-KTFQG-SIIFISHDRSFIRNmATRIVDLDRGKL 231
|
.
gi 568980685 590 V 590
Cdd:PRK11147 232 V 232
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
340-575 |
2.21e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 58.97 E-value: 2.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 340 VARGAAFNIFQVIDKKPNIDNFStagFVPECIEGNI-EFKNVSFSYP-SRPSAKVLKGLNLKIKAGETVALVGPSGSGKS 417
Cdd:TIGR00956 727 IEAGEVLGSTDLTDESDDVNDEK---DMEKESGEDIfHWRNLTYEVKiKKEKRVILNNVDGWVKPGTLTALMGASGAGKT 803
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 418 TTVQLL-QRLydpEDGCITvdeNDIRAQNVR----HYREQIGVVRQEPVLFGT-TIGNNIKFgregvgEKEMEQAA---- 487
Cdd:TIGR00956 804 TLLNVLaERV---TTGVIT---GGDRLVNGRpldsSFQRSIGYVQQQDLHLPTsTVRESLRF------SAYLRQPKsvsk 871
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 488 REANAY-DFIM---AFPKKFNTLVGEKGAQMSGGQKQRIAIARALVRNPKILI-LDEATSALDTESE-SLVQTALEKASK 561
Cdd:TIGR00956 872 SEKMEYvEEVIkllEMESYADAVVGVPGEGLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAwSICKLMRKLADH 951
|
250
....*....|....
gi 568980685 562 GRTTIVVAHRLSTI 575
Cdd:TIGR00956 952 GQAILCTIHQPSAI 965
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
396-589 |
2.70e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 58.14 E-value: 2.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 396 LNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDIRAQNVRHyREQIGVV-----RQEPVLF------- 463
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQ-RLARGLVylpedRQSSGLYldaplaw 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 464 ---GTTIGNNIKFGREGVGEKEMEQAAREANAydfimafpkKFNTLvgEKGAQ-MSGGQKQRIAIARALVRNPKILILDE 539
Cdd:PRK15439 361 nvcALTHNRRGFWIKPARENAVLERYRRALNI---------KFNHA--EQAARtLSGGNQQKVLIAKCLEASPQLLIVDE 429
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 568980685 540 ATSALDTESES-LVQTALEKASKGRTTIVVAHRLSTIRG-ADLIVTMKDGMV 589
Cdd:PRK15439 430 PTRGVDVSARNdIYQLIRSIAAQNVAVLFISSDLEEIEQmADRVLVMHQGEI 481
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
375-608 |
2.92e-08 |
|
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: 57.91 E-value: 2.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 375 IEFKNVSFSYPSRPSAKVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPE-DGCITVDEN--DIR--AQNVRHY 449
Cdd:TIGR02633 258 LEARNLTCWDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKpvDIRnpAQAIRAG 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 450 -------REQIGVVrqePVLfgtTIGNNI------KFGREGVGEKEMEQAAREANAYDFIMAFPKKFNTLvgekgAQMSG 516
Cdd:TIGR02633 338 iamvpedRKRHGIV---PIL---GVGKNItlsvlkSFCFKMRIDAAAELQIIGSAIQRLKVKTASPFLPI-----GRLSG 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 517 GQKQRIAIARALVRNPKILILDEATSALDTESESLVQTALEK-ASKGRTTIVVAHRLSTIRG-ADLIVTMKDGMVVEKGT 594
Cdd:TIGR02633 407 GNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQlAQEGVAIIVVSSELAEVLGlSDRVLVIGEGKLKGDFV 486
|
250
....*....|....
gi 568980685 595 HAELMAKQGLYYSL 608
Cdd:TIGR02633 487 NHALTQEQVLAAAL 500
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1028-1201 |
3.37e-08 |
|
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: 55.88 E-value: 3.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1028 SIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVK----------ELNVQ-WLRSQTAIVSQEPvLFNCSI 1096
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSykpqyikadyEGTVRdLLSSITKDFYTHP-YFKTEI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1097 AEniaygdnsrmvPLEeikevadaanihsfIEGLprkYNTLVglrgVQLSGGQKQRLAIARALLRKPKILLLDEATSALD 1176
Cdd:cd03237 100 AK-----------PLQ--------------IEQI---LDREV----PELSGGELQRVAIAACLSKDADIYLLDEPSAYLD 147
|
170 180
....*....|....*....|....*....
gi 568980685 1177 NESE----KVVQQALDKARrgKTCLVVAH 1201
Cdd:cd03237 148 VEQRlmasKVIRRFAENNE--KTAFVVEH 174
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
942-1218 |
3.43e-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: 3.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 942 GMFIVFTAIAYGAMAIGETLVW----------APEYSKAKAGAshlfalLKNKPTINSCSQSGEKPD----------TCE 1001
Cdd:TIGR00956 684 FVYILLTEFNKGAKQKGEILVFrrgslkrakkAGETSASNKND------IEAGEVLGSTDLTDESDDvndekdmekeSGE 757
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1002 GNLEFREVSFVYPCRPEVPV-LQNMSLSIEKGKTVAFVGSSGCGKSTcvqLLQRFYDPMKGQVLLDG---VDVKELNVQW 1077
Cdd:TIGR00956 758 DIFHWRNLTYEVKIKKEKRViLNNVDGWVKPGTLTALMGASGAGKTT---LLNVLAERVTTGVITGGdrlVNGRPLDSSF 834
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1078 LRSqTAIVSQEPV-LFNCSIAENI---AYGDNSRMVPLEE----IKEVADAANIHSFIEGLprkyntlVGLRGVQLSGGQ 1149
Cdd:TIGR00956 835 QRS-IGYVQQQDLhLPTSTVRESLrfsAYLRQPKSVSKSEkmeyVEEVIKLLEMESYADAV-------VGVPGEGLNVEQ 906
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568980685 1150 KQRLAIARALLRKPKILL-LDEATSALDNESEKVVQQALDK-ARRGKTCLVVAHRLSTI--QNADMIVVLQNG 1218
Cdd:TIGR00956 907 RKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKlADHGQAILCTIHQPSAIlfEEFDRLLLLQKG 979
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
393-594 |
3.94e-08 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 56.04 E-value: 3.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 393 LKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDIRA---QNVRHYREQIGVVRQE-PVLfgttIG 468
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQalqKNLVAYVPQSEEVDWSfPVL----VE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 469 NNIKFGREG------VGEKEMEQAAREANAYDFIMAFPKKfntLVGEkgaqMSGGQKQRIAIARALVRNPKILILDEATS 542
Cdd:PRK15056 99 DVVMMGRYGhmgwlrRAKKRDRQIVTAALARVDMVEFRHR---QIGE----LSGGQKKRVFLARAIAQQGQVILLDEPFT 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 568980685 543 ALDTESESLVQTAL-EKASKGRTTIVVAHRLSTirgadlIVTMKDGMVVEKGT 594
Cdd:PRK15056 172 GVDVKTEARIISLLrELRDEGKTMLVSTHNLGS------VTEFCDYTVMVKGT 218
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1017-1218 |
4.12e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 57.43 E-value: 4.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1017 PEVPVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDV-----KELnvqwLRSQTAIVSQE-PV 1090
Cdd:PRK10982 9 PGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdfkssKEA----LENGISMVHQElNL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1091 LFNCSIAENIAYG---------DNSRMvpLEEIKEVADAANIHsfIEglPRKyntlvglRGVQLSGGQKQRLAIARALLR 1161
Cdd:PRK10982 85 VLQRSVMDNMWLGryptkgmfvDQDKM--YRDTKAIFDELDID--ID--PRA-------KVATLSVSQMQMIEIAKAFSY 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568980685 1162 KPKILLLDEATSALdneSEKVVQ---QALDKAR-RGKTCLVVAHRLSTI-QNADMIVVLQNG 1218
Cdd:PRK10982 152 NAKIVIMDEPTSSL---TEKEVNhlfTIIRKLKeRGCGIVYISHKMEEIfQLCDEITILRDG 210
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
34-320 |
4.84e-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: 349984 [Multi-domain] Cd Length: 295 Bit Score: 55.95 E-value: 4.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 34 IVLMTLGILASMINgATVPLMSlvlGEISDHLIngclvqTNRTkyqncsqtqeklNEDIIVLTLYYIGIgaaALIFGYVQ 113
Cdd:cd18540 5 ILLIILMLLVALLD-AVFPLLT---KYAIDHFI------TPGT------------LDGLTGFILLYLGL---ILIQALSV 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 114 ISFwVITAARQTTR----IRKQFFHSILAQDISWFDGSDICELNTRMTGDINKLCD----GIGDkiplMFQNISGFSIGL 185
Cdd:cd18540 60 FLF-IRLAGKIEMGvsydLRKKAFEHLQTLSFSYFDKTPVGWIMARVTSDTQRLGEiiswGLVD----LVWGITYMIGIL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 186 VISLIKSWKLSLVVLSTSPLIMASSALCSRMIISLTSKELDAYSKAGAVAEEALSSIQTVTAFGAQEKEIQRYTQHLKDA 265
Cdd:cd18540 135 IVMLILNWKLALIVLAVVPVLAVVSIYFQKKILKAYRKVRKINSRITGAFNEGITGAKTTKTLVREEKNLREFKELTEEM 214
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 568980685 266 KDAGIKRATASKLSLGAVYFFMNGAYGLAFWYGTSLIFGGepGYTIGTiLAVFFS 320
Cdd:cd18540 215 RRASVRAARLSALFLPIVLFLGSIATALVLWYGGILVLAG--AITIGT-LVAFIS 266
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
1026-1230 |
5.90e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 56.95 E-value: 5.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1026 SLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDV---------KELNVQWLRSQTAIVSQEPVLFNCSI 1096
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHItrlsfeqlqKLVSDEWQRNNTDMLSPGEDDTGRTT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1097 AENIAYG--DNSRMVPLEEIKEVADaanihsfieglprkyntLVGLRGVQLSGGQKQRLAIARALLRKPKILLLDEATSA 1174
Cdd:PRK10938 103 AEIIQDEvkDPARCEQLAQQFGITA-----------------LLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDG 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 568980685 1175 LDNESEKVVQQALDK-ARRGKTCLVVAHRLSTIQN-ADMIVVLQNGSIKEQGTHQELL 1230
Cdd:PRK10938 166 LDVASRQQLAELLASlHQSGITLVLVLNRFDEIPDfVQFAGVLADCTLAETGEREEIL 223
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1021-1203 |
5.91e-08 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 55.12 E-value: 5.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1021 VLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGqvlldgvdvkelnvqwlrsqtaIVSQEPVLfncsiaeNI 1100
Cdd:PRK09544 19 VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEG----------------------VIKRNGKL-------RI 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1101 AYgdnsrmVPLEEIKEVADAANIHSFIEGLP--RKYNTLVGLRGVQ-----------LSGGQKQRLAIARALLRKPKILL 1167
Cdd:PRK09544 70 GY------VPQKLYLDTTLPLTVNRFLRLRPgtKKEDILPALKRVQaghlidapmqkLSGGETQRVLLARALLNRPQLLV 143
|
170 180 190
....*....|....*....|....*....|....*...
gi 568980685 1168 LDEATSALDNESEKVVQQALDKARRGKTC--LVVAHRL 1203
Cdd:PRK09544 144 LDEPTQGVDVNGQVALYDLIDQLRRELDCavLMVSHDL 181
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
728-947 |
6.81e-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: 55.65 E-value: 6.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 728 LVVLGIVALVTYLMQGLF---YGRAEENLAMRLRHS----AFKAMLYQDMAWYDDKEnnTGALTTTLAVDVAQIQGAATS 800
Cdd:cd18565 53 LWLLGGLTVAAFLLESLFqylSGVLWRRFAQRVQHDlrtdTYDHVQRLDMAFFEDRQ--TGDLMSVLNNDVNQLERFLDD 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 801 RLGIVTQDVSNMSLSILISFIYGWEMTLLILSFAPVLAvtgmiqtAAMAGFANR--DKQALKR--AGKIATeAVEN---- 872
Cdd:cd18565 131 GANSIIRVVVTVLGIGAILFYLNWQLALVALLPVPLII-------AGTYWFQRRiePRYRAVReaVGDLNA-RLENnlsg 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 873 IRTVVSLTRErAFEQMYEETLQTQHRNALKRAHITGCCY-AVSHAFVHFAHAAGFRFGAYLIQAGRM-----MPEGMFIV 946
Cdd:cd18565 203 IAVIKAFTAE-DFERERVADASEEYRDANWRAIRLRAAFfPVIRLVAGAGFVATFVVGGYWVLDGPPlftgtLTVGTLVT 281
|
.
gi 568980685 947 F 947
Cdd:cd18565 282 F 282
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
378-548 |
9.66e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 56.28 E-value: 9.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 378 KNVSFSYPsrPSAKVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENdiraqnvrhYReqIGVVR 457
Cdd:PRK11819 10 NRVSKVVP--PKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPAPG---------IK--VGYLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 458 QEPVLFGT-TIGNNIKfgrEGVGEKEmeQAAREANAYDFIMAFPK-KFNTLVGEKG------------------------ 511
Cdd:PRK11819 77 QEPQLDPEkTVRENVE---EGVAEVK--AALDRFNEIYAAYAEPDaDFDALAAEQGelqeiidaadawdldsqleiamda 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 568980685 512 ----------AQMSGGQKQRIAIARALVRNPKILILDEATSALDTES 548
Cdd:PRK11819 152 lrcppwdakvTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES 198
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
375-559 |
1.02e-07 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 56.10 E-value: 1.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 375 IEFKNVSFSYPSRPsakVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDEndiraqNVrhyreQIG 454
Cdd:TIGR03719 323 IEAENLTKAFGDKL---LIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGE------TV-----KLA 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 455 VVRQepvlfgttignnikfGREGV------------GEKEMEQAAREANAYDFIMAFpkkfntlvGEKGA-------QMS 515
Cdd:TIGR03719 389 YVDQ---------------SRDALdpnktvweeisgGLDIIKLGKREIPSRAYVGRF--------NFKGSdqqkkvgQLS 445
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 568980685 516 GGQKQRIAIARALVRNPKILILDEATSALDTESESlvqtALEKA 559
Cdd:TIGR03719 446 GGERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLR----ALEEA 485
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
88-316 |
1.06e-07 |
|
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: 55.15 E-value: 1.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 88 LNEDIIVLTLYYIGIGAAALIFGYVqISFWV---------ITAARQTTRIRKQFFHSILAQDISWFDGSDICELNTRMTG 158
Cdd:cd18549 29 IDDLLPSKNLRLILIIGAILLALYI-LRTLLnyfvtywghVMGARIETDMRRDLFEHLQKLSFSFFDNNKTGQLMSRITN 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 159 DINKLCD----GIGDkiplMFqnISGFSI--GLVISLIKSWKLSLVVLSTSPLIMASSALCSR--MIISLTSKEldAYSK 230
Cdd:cd18549 108 DLFDISElahhGPED----LF--ISIITIigSFIILLTINVPLTLIVFALLPLMIIFTIYFNKkmKKAFRRVRE--KIGE 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 231 AGAVAEEALSSIQTVTAFGAQEKEIQRY---TQHLKDAKDAGIKratASKLSLGAVYFFMNGAYGLAFWYGTSLIFGGEp 307
Cdd:cd18549 180 INAQLEDSLSGIRVVKAFANEEYEIEKFdegNDRFLESKKKAYK---AMAYFFSGMNFFTNLLNLVVLVAGGYFIIKGE- 255
|
....*....
gi 568980685 308 gYTIGTILA 316
Cdd:cd18549 256 -ITLGDLVA 263
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
1117-1229 |
1.13e-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: 56.56 E-value: 1.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1117 VADAANIHSFIEGLPRKYNTL--VGLRGVQ-------LSGGQKQRLAIARALLRK---PKILLLDEATSALDNESEK--- 1181
Cdd:TIGR00630 793 VEEAYEFFEAVPSISRKLQTLcdVGLGYIRlgqpattLSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLHFDDIKkll 872
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 568980685 1182 -VVQQALDKarrGKTCLVVAHRLSTIQNADMIVVL------QNGSIKEQGTHQEL 1229
Cdd:TIGR00630 873 eVLQRLVDK---GNTVVVIEHNLDVIKTADYIIDLgpeggdGGGTVVASGTPEEV 924
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
1004-1187 |
1.41e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 56.02 E-value: 1.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1004 LEFREVSFVYPCRPevPVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVL--------------LDGVD 1069
Cdd:PLN03073 509 ISFSDASFGYPGGP--LLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFrsakvrmavfsqhhVDGLD 586
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1070 VkelnvqwlrsqtaivSQEPVLF--NCSIAeniaygdnsrmVPLEEIKevadaANIHSFieglprkynTLVGLRGVQ--- 1144
Cdd:PLN03073 587 L---------------SSNPLLYmmRCFPG-----------VPEQKLR-----AHLGSF---------GVTGNLALQpmy 626
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 568980685 1145 -LSGGQKQRLAIARALLRKPKILLLDEATSALDNESEKVVQQAL 1187
Cdd:PLN03073 627 tLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGL 670
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
379-579 |
1.46e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 53.42 E-value: 1.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 379 NVSFSYPSRPsakVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDIRaQNVRHYREQIGVVRQ 458
Cdd:PRK13540 6 ELDFDYHDQP---LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIK-KDLCTYQKQLCFVGH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 459 EpvlfgTTIGNNIKFGREGVGEKEMEQAAREANayDFIMAFpkKFNTLVGEKGAQMSGGQKQRIAIARALVRNPKILILD 538
Cdd:PRK13540 82 R-----SGINPYLTLRENCLYDIHFSPGAVGIT--ELCRLF--SLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLD 152
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 568980685 539 EATSALDTESESLVQTALEK-ASKGRTTIVVAHRLSTIRGAD 579
Cdd:PRK13540 153 EPLVALDELSLLTIITKIQEhRAKGGAVLLTSHQDLPLNKAD 194
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
1024-1176 |
1.79e-07 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 55.90 E-value: 1.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1024 NMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDG--VDVKELNVqwlRSQTAIVSQEPVLFN-CSIAENI 1100
Cdd:NF033858 284 HVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGqpVDAGDIAT---RRRVGYMSQAFSLYGeLTVRQNL 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1101 A-----YGdnsrmVPLEEIKE-VADAanIHSFieglprkyntlvGLRGVQ------LSGGQKQRLAIARALLRKPKILLL 1168
Cdd:NF033858 361 ElharlFH-----LPAAEIAArVAEM--LERF------------DLADVAdalpdsLPLGIRQRLSLAVAVIHKPELLIL 421
|
....*...
gi 568980685 1169 DEATSALD 1176
Cdd:NF033858 422 DEPTSGVD 429
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
1016-1201 |
2.04e-07 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 52.93 E-value: 2.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1016 RPEVPVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVKELNvqwlRSQ-TAIVSQEPVL-FN 1093
Cdd:PRK13543 21 RNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGD----RSRfMAYLGHLPGLkAD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1094 CSIAENIAY-----GDNSRMVPLEEIKevadaanihsfIEGLPRKYNTLVGlrgvQLSGGQKQRLAIARALLRKPKILLL 1168
Cdd:PRK13543 97 LSTLENLHFlcglhGRRAKQMPGSALA-----------IVGLAGYEDTLVR----QLSAGQKKRLALARLWLSPAPLWLL 161
|
170 180 190
....*....|....*....|....*....|....
gi 568980685 1169 DEATSALDNESEKVVQQALD-KARRGKTCLVVAH 1201
Cdd:PRK13543 162 DEPYANLDLEGITLVNRMISaHLRGGGAALVTTH 195
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
994-1236 |
2.31e-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: 55.79 E-value: 2.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 994 GEKPDTcegnLEFREVSFVYPCRPEvPVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVKEl 1073
Cdd:TIGR01257 1932 GNKTDI----LRLNELTKVYSGTSS-PAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT- 2005
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1074 NVQWLRSQTAIVSQEPVLFNCSIA-ENIAYGDNSRMVPLEEIKEVADAAnIHSFieGLPRKYNTLVGlrgvQLSGGQKQR 1152
Cdd:TIGR01257 2006 NISDVHQNMGYCPQFDAIDDLLTGrEHLYLYARLRGVPAEEIEKVANWS-IQSL--GLSLYADRLAG----TYSGGNKRK 2078
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1153 LAIARALLRKPKILLLDEATSALDNESEKVVQQAL-DKARRGKTCLVVAHRLSTIQN-ADMIVVLQNGSIKEQGTHQEL- 1229
Cdd:TIGR01257 2079 LSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIvSIIREGRAVVLTSHSMEECEAlCTRLAIMVKGAFQCLGTIQHLk 2158
|
....*..
gi 568980685 1230 LRNGDTY 1236
Cdd:TIGR01257 2159 SKFGDGY 2165
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
365-594 |
2.78e-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: 54.79 E-value: 2.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 365 GFVPEciEgNIEFKNVSFSYPSRPSAKVLKGLNL--------------------KIKAGETVALVGPSGSGKSTTVQLLQ 424
Cdd:COG1245 311 GYLPE--E-NVRIRDEPIEFEVHAPRREKEEETLveypdltksyggfsleveggEIREGEVLGIVGPNGIGKTTFAKILA 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 425 RLYDPEDGCITVDEnDI--RAQNVRHyrEQIGVVRQepvLFGTTIGNNI--KFGREGVG-----EKEMEQAAREanaydf 495
Cdd:COG1245 388 GVLKPDEGEVDEDL-KIsyKPQYISP--DYDGTVEE---FLRSANTDDFgsSYYKTEIIkplglEKLLDKNVKD------ 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 496 imafpkkfntlvgekgaqMSGGQKQRIAIARALVRNPKILILDEATSALDTESESLVQTALEK--ASKGRTTIVVAHRLS 573
Cdd:COG1245 456 ------------------LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRfaENRGKTAMVVDHDIY 517
|
250 260
....*....|....*....|.
gi 568980685 574 TIrgaDLIVtmkDGMVVEKGT 594
Cdd:COG1245 518 LI---DYIS---DRLMVFEGE 532
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
400-582 |
2.85e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 54.81 E-value: 2.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 400 IKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCitVDENDIRAQNVRHYReqigvvrqepvlfGTTIGNNIKfgreGVG 479
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSGELIPNLGD--YEEEPSWDEVLKRFR-------------GTELQNYFK----KLY 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 480 EKEMeQAAREANAYDFImafPKKFNTLVG-------EKGA-------------------QMSGGQKQRIAIARALVRNPK 533
Cdd:PRK13409 157 NGEI-KVVHKPQYVDLI---PKVFKGKVRellkkvdERGKldevverlglenildrdisELSGGELQRVAIAAALLRDAD 232
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 568980685 534 ILILDEATSALDTESESLVQTALEKASKGRTTIVVAHrlstirgaDLIV 582
Cdd:PRK13409 233 FYFFDEPTSYLDIRQRLNVARLIRELAEGKYVLVVEH--------DLAV 273
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
720-914 |
2.94e-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: 53.63 E-value: 2.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 720 DAELYSMMLVVL-GIVALVTYLMQGLFYGRAEENLAMRLRHSAFKAMLYQDMAWYDdkENNTGALTTTLAVDVAQIQGAA 798
Cdd:cd18589 33 EAFTAAITVMSLlTIASAVSEFVCDLIYNITMSRIHSRLQGLVFAAVLRQEIAFFD--SNQTGDIVSRVTTDTEDMSESL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 799 TSRLGIVTQDVSNMSLSILISFIYGWEMTLLILSFAPVLAVTGMIQTAAMAGFANRDKQALKRAGKIATEAVENIRTVVS 878
Cdd:cd18589 111 SENLSLLMWYLARGLFLFIFMLWLSPKLALLTALGLPLLLLVPKFVGKFQQSLAVQVQKSLARANQVAVETFSAMKTVRS 190
|
170 180 190
....*....|....*....|....*....|....*.
gi 568980685 879 LTRERAFEQMYEETLQTQHRNALKRAhitgCCYAVS 914
Cdd:cd18589 191 FANEEGEAQRYRQRLQKTYRLNKKEA----AAYAVS 222
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
393-594 |
3.06e-07 |
|
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: 53.39 E-value: 3.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 393 LKGLNLKIKAGETVALVGPSGSGKSTTVQ------LLQRLYDPEDGCITVDENDiRAQNVrhyrEQIGVVRQEPVlfGTT 466
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLINdtlypaLARRLHLKKEQPGNHDRIE-GLEHI----DKVIVIDQSPI--GRT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 467 IGNN----------I-----------KFGREGVGEK----------EMeqAAREAnaYDFIMAFPK---KFNTLV----- 507
Cdd:cd03271 84 PRSNpatytgvfdeIrelfcevckgkRYNRETLEVRykgksiadvlDM--TVEEA--LEFFENIPKiarKLQTLCdvglg 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 508 ----GEKGAQMSGGQKQRIAIARALVR---NPKILILDEATSALDTES-ESLVQTALEKASKGRTTIVVAHRLSTIRGAD 579
Cdd:cd03271 160 yiklGQPATTLSGGEAQRIKLAKELSKrstGKTLYILDEPTTGLHFHDvKKLLEVLQRLVDKGNTVVVIEHNLDVIKCAD 239
|
250 260
....*....|....*....|.
gi 568980685 580 LIVTM------KDGMVVEKGT 594
Cdd:cd03271 240 WIIDLgpeggdGGGQVVASGT 260
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
401-574 |
3.22e-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: 54.79 E-value: 3.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 401 KAGETVALVGPSGSGKSTTVQLLQ-----RLYDPEDGcitVDENDIraqnVRHYReqigvvrqepvlfGTTIGNNIKfgr 475
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSgelkpNLGDYDEE---PSWDEV----LKRFR-------------GTELQDYFK--- 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 476 eGVGEKEMEqAAREANAYDFImafPKKFNTLVG-------EKGA-------------------QMSGGQKQRIAIARALV 529
Cdd:COG1245 154 -KLANGEIK-VAHKPQYVDLI---PKVFKGTVRellekvdERGKldelaeklglenildrdisELSGGELQRVAIAAALL 228
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 568980685 530 RNPKILILDEATSALD----TESESLVQtalEKASKGRTTIVVAHRLST 574
Cdd:COG1245 229 RDADFYFFDEPSSYLDiyqrLNVARLIR---ELAEEGKYVLVVEHDLAI 274
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1032-1215 |
4.42e-07 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 52.75 E-value: 4.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1032 GKTVAFVGSSGCGKSTCVQLLQ--------RFYDPMKGQVLLD---GVDVKELNVQWLRSQTAI------VSQEPVLFNC 1094
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAgklkpnlgKFDDPPDWDEILDefrGSELQNYFTKLLEGDVKVivkpqyVDLIPKAVKG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1095 SIAENIAYGDNSRMvpLEEIKEVADAANIhsfiegLPRKYNtlvglrgvQLSGGQKQRLAIARALLRKPKILLLDEATSA 1174
Cdd:cd03236 106 KVGELLKKKDERGK--LDELVDQLELRHV------LDRNID--------QLSGGELQRVAIAAALARDADFYFFDEPSSY 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 568980685 1175 LDnesekvVQQALDKAR-------RGKTCLVVAHRLSTIQN-ADMIVVL 1215
Cdd:cd03236 170 LD------IKQRLNAARlirelaeDDNYVLVVEHDLAVLDYlSDYIHCL 212
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
95-262 |
4.49e-07 |
|
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group represents the six-transmembrane domain 2 (TMD2) of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. All ABC transporters share a common architecture of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. By contrast, bacterial ABC exporters are typically assembled from dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are comprised of two identical TMDs and two identical NBDs.
Pssm-ID: 350024 [Multi-domain] Cd Length: 294 Bit Score: 52.89 E-value: 4.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 95 LTLYYIGIGAAALIFGYVQISFWVITAARQTTRIRKQFFHSILAQDISWFDGSDICELNTRMTGDINkLCDgigDKIPLM 174
Cdd:cd18580 41 LGVYAALLVLASVLLVLLRWLLFVLAGLRASRRLHDKLLRSVLRAPMSFFDTTPSGRILNRFSKDIG-LID---EELPLA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 175 FQNISGFSIGLVISLIkswklslVVLSTSPLIMASSALCSRMIISL------TSKE---LDAYSKAGAVA--EEALSSIQ 243
Cdd:cd18580 117 LLDFLQSLFSVLGSLI-------VIAIVSPYFLIVLPPLLVVYYLLqryylrTSRQlrrLESESRSPLYShfSETLSGLS 189
|
170
....*....|....*....
gi 568980685 244 TVTAFGAQEKEIQRYTQHL 262
Cdd:cd18580 190 TIRAFGWQERFIEENLRLL 208
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
376-590 |
5.74e-07 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 53.64 E-value: 5.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 376 EFKNVSFSYPSRPSAKVLKGLNLKIKAGETVALVGPSGSGKS-TTVQLLQRLYDP-EDGCITVDENDIRAQNVRH----- 448
Cdd:NF040905 259 EVKNWTVYHPLHPERKVVDDVSLNVRRGEIVGIAGLMGAGRTeLAMSVFGRSYGRnISGTVFKDGKEVDVSTVSDaidag 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 449 --Y----REQIGVVRQEPVLFGTTIGNNIKFGREGV--GEKEMEQAAReanaydfimaFPKKFNTL---VGEKGAQMSGG 517
Cdd:NF040905 339 laYvtedRKGYGLNLIDDIKRNITLANLGKVSRRGVidENEEIKVAEE----------YRKKMNIKtpsVFQKVGNLSGG 408
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568980685 518 QKQRIAIARALVRNPKILILDEATSALDT----ESESLVQtalEKASKGRTTIVVAHRLSTIRG-ADLIVTMKDGMVV 590
Cdd:NF040905 409 NQQKVVLSKWLFTDPDVLILDEPTRGIDVgakyEIYTIIN---ELAAEGKGVIVISSELPELLGmCDRIYVMNEGRIT 483
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
92-316 |
5.80e-07 |
|
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: 52.88 E-value: 5.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 92 IIVLTLYYIGIGAAALIFGYVQISFWVITAARQTTRIRKQFFHSILAQDISWFDGSDICELNTRMTGDINKLCDGIGDKI 171
Cdd:cd18546 38 LLLAAAAYLAVVLAGWVAQRAQTRLTGRTGERLLYDLRLRVFAHLQRLSLDFHERETSGRIMTRMTSDIDALSELLQTGL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 172 PLMFQNISGFSIGLVISLIKSWKLSLVVLSTSPLIMASSALCSRmiislTSKEldAYSKA-GAVAE------EALSSIQT 244
Cdd:cd18546 118 VQLVVSLLTLVGIAVVLLVLDPRLALVALAALPPLALATRWFRR-----RSSR--AYRRArERIAAvnadlqETLAGIRV 190
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568980685 245 VTAFGAQEKEIQRYTQHLKDAKDAgikRATASKLSlgAVYF-FM----NGAYGLAFWYGTSLIFGGEpgYTIGTILA 316
Cdd:cd18546 191 VQAFRRERRNAERFAELSDDYRDA---RLRAQRLV--AIYFpGVellgNLATAAVLLVGAWRVAAGT--LTVGVLVA 260
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
1124-1215 |
7.01e-07 |
|
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: 52.23 E-value: 7.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1124 HSFIEGLP---RKYNTL--VGLRGVQ-------LSGGQKQRLAIARALLRK---PKILLLDEATSALDNESEKVVQQALD 1188
Cdd:cd03271 137 LEFFENIPkiaRKLQTLcdVGLGYIKlgqpattLSGGEAQRIKLAKELSKRstgKTLYILDEPTTGLHFHDVKKLLEVLQ 216
|
90 100
....*....|....*....|....*...
gi 568980685 1189 K-ARRGKTCLVVAHRLSTIQNADMIVVL 1215
Cdd:cd03271 217 RlVDKGNTVVVIEHNLDVIKCADWIIDL 244
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
1016-1176 |
7.20e-07 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 51.11 E-value: 7.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1016 RPEVPVLQNMSLSIEKGKTVAFVGSSGCGKST---CVQLLQRFYDPMKGQVLLDGVDVKELNVQWlRSQTAIVSQEPVLF 1092
Cdd:cd03233 17 RSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTllkALANRTEGNVSVEGDIHYNGIPYKEFAEKY-PGEIIYVSEEDVHF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1093 ncsiaeniaygdnsrmvPLEEIKEVADAA---NIHSFIeglprkyntlvglRGVqlSGGQKQRLAIARALLRKPKILLLD 1169
Cdd:cd03233 96 -----------------PTLTVRETLDFAlrcKGNEFV-------------RGI--SGGERKRVSIAEALVSRASVLCWD 143
|
....*..
gi 568980685 1170 EATSALD 1176
Cdd:cd03233 144 NSTRGLD 150
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
726-938 |
7.39e-07 |
|
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: 52.44 E-value: 7.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 726 MMLVVLGIVALVTYLMQGLFYGRAEENLAMRLRHSAFKAMLYQDMAWYDdkENNTGALTTTLAVDVAQIQGAATSRL--- 802
Cdd:cd18551 40 ALLVALFLLQAVLSALSSYLLGRTGERVVLDLRRRLWRRLLRLPVSFFD--RRRSGDLVSRVTNDTTLLRELITSGLpql 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 803 --GIVTqdvsnMSLSILISFIYGWEMTLLILSfapVLAVTGMIQTAAMAGFANRDKQALKRAGKIA---TEAVENIRTVV 877
Cdd:cd18551 118 vtGVLT-----VVGAVVLMFLLDWVLTLVTLA---VVPLAFLIILPLGRRIRKASKRAQDALGELSaalERALSAIRTVK 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568980685 878 SLTRERAFEQMYEETLQTQHRNALKRAHITGCCYAVSHAFVHFAHAAGFRFGAYLIQAGRM 938
Cdd:cd18551 190 ASNAEERETKRGGEAAERLYRAGLKAAKIEALIGPLMGLAVQLALLVVLGVGGARVASGAL 250
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
1144-1215 |
8.11e-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: 8.11e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568980685 1144 QLSGGQKQRLAIARALLRKPKILLLDEATSALD-NESEKVVQQALDKARRGKTCLVVAHRLSTIQN-ADMIVVL 1215
Cdd:COG1245 212 ELSGGELQRVAIAAALLRDADFYFFDEPSSYLDiYQRLNVARLIRELAEEGKYVLVVEHDLAILDYlADYVHIL 285
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1014-1230 |
8.23e-07 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 53.08 E-value: 8.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1014 PCRPEV-----PVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVKELNVQ-WLRSQTAIVSQ 1087
Cdd:PRK10762 255 EVRLKVdnlsgPGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQdGLANGIVYISE 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1088 EP----VLFNCSIAENI---AYGDNSR-MVPL---EEIKEVADaanihsFIEGLPRKYNTL---VGLrgvqLSGGQKQRL 1153
Cdd:PRK10762 335 DRkrdgLVLGMSVKENMsltALRYFSRaGGSLkhaDEQQAVSD------FIRLFNIKTPSMeqaIGL----LSGGNQQKV 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1154 AIARALLRKPKILLLDEATSALDNESEKVVQQALDKARR-GKTCLVVAHRLSTIQN-ADMIVVLQNGSI-----KEQGTH 1226
Cdd:PRK10762 405 AIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAeGLSIILVSSEMPEVLGmSDRILVMHEGRIsgeftREQATQ 484
|
....
gi 568980685 1227 QELL 1230
Cdd:PRK10762 485 EKLM 488
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
1145-1212 |
8.40e-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: 8.40e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1145 LSGGQKQRLAIARALLRKPKILLLDEATSALDNESEKVVQQALDK-AR-RGKTCLVVAHRLSTIqnaDMI 1212
Cdd:COG1245 456 LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRfAEnRGKTAMVVDHDIYLI---DYI 522
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1021-1176 |
8.42e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 53.25 E-value: 8.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1021 VLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLqrfydpmKGQVLLDGVDVKeLNVQWlrsQTAIVSQEPVLFNCSIAENI 1100
Cdd:PRK10636 16 LLDNATATINPGQKVGLVGKNGCGKSTLLALL-------KNEISADGGSYT-FPGNW---QLAWVNQETPALPQPALEYV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1101 AYGDNsRMVPLEEIKEVADAAN-------IHSFIEGL------PRKYNTLVGLRGVQ---------LSGGQKQRLAIARA 1158
Cdd:PRK10636 85 IDGDR-EYRQLEAQLHDANERNdghaiatIHGKLDAIdawtirSRAASLLHGLGFSNeqlerpvsdFSGGWRMRLNLAQA 163
|
170
....*....|....*...
gi 568980685 1159 LLRKPKILLLDEATSALD 1176
Cdd:PRK10636 164 LICRSDLLLLDEPTNHLD 181
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1019-1229 |
8.88e-07 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 52.42 E-value: 8.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1019 VPVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDP---MKGQVLLDGVDV-----KELNVqwLRS-QTAIVSQEP 1089
Cdd:PRK09473 29 VTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAngrIGGSATFNGREIlnlpeKELNK--LRAeQISMIFQDP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1090 ----------------VLF---NCSIAEniAYGDNSRMVPLEEIKEVADAANI--HSFieglprkyntlvglrgvqlSGG 1148
Cdd:PRK09473 107 mtslnpymrvgeqlmeVLMlhkGMSKAE--AFEESVRMLDAVKMPEARKRMKMypHEF-------------------SGG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1149 QKQRLAIARALLRKPKILLLDEATSALDNESEKVVQQALDKARR--GKTCLVVAHRLSTIQN-ADMIVVLQNGSIKEQGT 1225
Cdd:PRK09473 166 MRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKRefNTAIIMITHDLGVVAGiCDKVLVMYAGRTMEYGN 245
|
....
gi 568980685 1226 HQEL 1229
Cdd:PRK09473 246 ARDV 249
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
1143-1216 |
9.38e-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: 50.26 E-value: 9.38e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568980685 1143 VQLSGGQKQRLAIARALLRKPKILLLDEATSALDNE----SEKVVQQALDKARrgKTCLVVAHRLSTIQN-ADMIVVLQ 1216
Cdd:cd03222 70 IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEqrlnAARAIRRLSEEGK--KTALVVEHDLAVLDYlSDRIHVFE 146
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1144-1215 |
1.07e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 52.89 E-value: 1.07e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568980685 1144 QLSGGQKQRLAIARALLRKPKILLLDEATSALDnesekvVQQALDKAR------RGKTCLVVAHRLSTIQN-ADMIVVL 1215
Cdd:PRK13409 212 ELSGGELQRVAIAAALLRDADFYFFDEPTSYLD------IRQRLNVARlirelaEGKYVLVVEHDLAVLDYlADNVHIA 284
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
382-610 |
1.69e-06 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 52.22 E-value: 1.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 382 FSYPSRPSAKV---LKGL---------NLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDIRAQNVRHY 449
Cdd:PRK11288 246 YGYRPRPLGEVrlrLDGLkgpglrepiSFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDA 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 450 REQiGVV------RQEPVLFGTTIGNNI------KFGREGV---GEKEMEQAAReanaydFIMAFPKKF---NTLVGekg 511
Cdd:PRK11288 326 IRA-GIMlcpedrKAEGIIPVHSVADNInisarrHHLRAGClinNRWEAENADR------FIRSLNIKTpsrEQLIM--- 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 512 aQMSGGQKQRIAIARALVRNPKILILDEATSALDTESES-LVQTALEKASKGRTTIVVAHRLSTIRG-ADLIVTMKDGMV 589
Cdd:PRK11288 396 -NLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHeIYNVIYELAAQGVAVLFVSSDLPEVLGvADRIVVMREGRI 474
|
250 260
....*....|....*....|.
gi 568980685 590 VEKGTHAElmAKQGLYYSLAM 610
Cdd:PRK11288 475 AGELAREQ--ATERQALSLAL 493
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1023-1222 |
1.85e-06 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 52.09 E-value: 1.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1023 QNMSLSIEKGKTVAFVGSSGCGKStcvQLLQRFY--DPMK-GQVLLDGVDVKELN-VQWLRSQTAIVSQ---EPVLF-NC 1094
Cdd:PRK09700 280 RDISFSVCRGEILGFAGLVGSGRT---ELMNCLFgvDKRAgGEIRLNGKDISPRSpLDAVKKGMAYITEsrrDNGFFpNF 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1095 SIAENIA---------YGDNSRMVPLEEIKEVADAANihsfiEGLPRKYNTlVGLRGVQLSGGQKQRLAIARALLRKPKI 1165
Cdd:PRK09700 357 SIAQNMAisrslkdggYKGAMGLFHEVDEQRTAENQR-----ELLALKCHS-VNQNITELSGGNQQKVLISKWLCCCPEV 430
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568980685 1166 LLLDEATSALD----NESEKVVQQALDKarrGKTCLVVAHRLSTIQNA-DMIVVLQNGSIKE 1222
Cdd:PRK09700 431 IIFDEPTRGIDvgakAEIYKVMRQLADD---GKVILMVSSELPEIITVcDRIAVFCEGRLTQ 489
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1026-1230 |
1.90e-06 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 51.84 E-value: 1.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1026 SLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVKelnvqwLRSQTAIVSQEPVLfnC----------- 1094
Cdd:PRK11288 273 SFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPID------IRSPRDAIRAGIML--Cpedrkaegiip 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1095 --SIAENI---AYGDNSRMVPLeeIKEVADAANIHSFIEGLPRKY---NTLVGlrgvQLSGGQKQRLAIARALLRKPKIL 1166
Cdd:PRK11288 345 vhSVADNInisARRHHLRAGCL--INNRWEAENADRFIRSLNIKTpsrEQLIM----NLSGGNQQKAILGRWLSEDMKVI 418
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568980685 1167 LLDEATSALD----NESEKVVqqaLDKARRGKTCLVVAHRLSTIQN-ADMIVVLQNGSI-----KEQGTHQELL 1230
Cdd:PRK11288 419 LLDEPTRGIDvgakHEIYNVI---YELAAQGVAVLFVSSDLPEVLGvADRIVVMREGRIagelaREQATERQAL 489
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
393-584 |
2.19e-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: 49.24 E-value: 2.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 393 LKGLNLKIKAGETVALVGPSGSGKSTTVQllqrlydpeDGcitvdendIRAQNVRHYREQIGVVRQEPVLFGTTIGNNIK 472
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVN---------EG--------LYASGKARLISFLPKFSRNKLIFIDQLQFLID 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 473 FGregVGEKEMEQAAreanaydfimafpkkfNTLvgekgaqmSGGQKQRIAIARALVRNPK--ILILDEATSALDTES-E 549
Cdd:cd03238 74 VG---LGYLTLGQKL----------------STL--------SGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDiN 126
|
170 180 190
....*....|....*....|....*....|....*
gi 568980685 550 SLVQTALEKASKGRTTIVVAHRLSTIRGADLIVTM 584
Cdd:cd03238 127 QLLEVIKGLIDLGNTVILIEHNLDVLSSADWIIDF 161
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
1022-1225 |
2.36e-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: 49.24 E-value: 2.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1022 LQNMSLSIEKGKTVAFVGSSGCGKSTcvqLLQRFYDPMKGQVLLDGVDVKElnvqwlRSQTAIVSQEPVLfncsIAENIA 1101
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKST---LVNEGLYASGKARLISFLPKFS------RNKLIFIDQLQFL----IDVGLG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1102 YgdnsrmVPLEeikevadaanihsfieglpRKYNTLvglrgvqlSGGQKQRLAIARALLRKPK--ILLLDEATSALDNES 1179
Cdd:cd03238 78 Y------LTLG-------------------QKLSTL--------SGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQD 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 568980685 1180 ekvVQQALDKARR----GKTCLVVAHRLSTIQNADMIVVLQNGSIKEQGT 1225
Cdd:cd03238 125 ---INQLLEVIKGlidlGNTVILIEHNLDVLSSADWIIDFGPGSGKSGGK 171
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1022-1201 |
2.57e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 51.87 E-value: 2.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1022 LQNMSLSIEKGKTVAFVGSSGCGKSTCVQLlqrfydpMKGQVLLDGVDVK---ELNVQWLRSQTAIVSQEPvlfncSIAE 1098
Cdd:PRK11147 335 VKDFSAQVQRGDKIALIGPNGCGKTTLLKL-------MLGQLQADSGRIHcgtKLEVAYFDQHRAELDPEK-----TVMD 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1099 NIAYGDNSRMVpleeikevadaaN-----IHSFIEGL---PRKYNTLVGlrgvQLSGGQKQRLAIARALLRKPKILLLDE 1170
Cdd:PRK11147 403 NLAEGKQEVMV------------NgrprhVLGYLQDFlfhPKRAMTPVK----ALSGGERNRLLLARLFLKPSNLLILDE 466
|
170 180 190
....*....|....*....|....*....|.
gi 568980685 1171 ATSALDNESEKVVQQALDkARRGkTCLVVAH 1201
Cdd:PRK11147 467 PTNDLDVETLELLEELLD-SYQG-TVLLVSH 495
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
1020-1226 |
3.20e-06 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 49.79 E-value: 3.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1020 PVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLL--QRFYDPMKGQVLLDGVDVKELNVQWLRSQTAIVS-QEPV------ 1090
Cdd:PRK09580 15 AILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLagREDYEVTGGTVEFKGKDLLELSPEDRAGEGIFMAfQYPVeipgvs 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1091 ---LFNCSIAENIAYGDNSrmvPLEEIkEVADAanIHSFIEGLPRKYNTLVGLRGVQLSGGQKQRLAIARALLRKPKILL 1167
Cdd:PRK09580 95 nqfFLQTALNAVRSYRGQE---PLDRF-DFQDL--MEEKIALLKMPEDLLTRSVNVGFSGGEKKRNDILQMAVLEPELCI 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568980685 1168 LDEATSALDNESEKVVQQALDKARRGK-TCLVVAH--RLSTIQNADMIVVLQNGSIKEQGTH 1226
Cdd:PRK09580 169 LDESDSGLDIDALKIVADGVNSLRDGKrSFIIVTHyqRILDYIKPDYVHVLYQGRIVKSGDF 230
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
375-570 |
4.53e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 50.78 E-value: 4.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 375 IEFKNVSFSYPSRPsakVLKGLNLKIKAGETVALVGPSGSGKSTTVQLlqrlydpedgcITVDE-----NDI-------- 441
Cdd:PRK10938 261 IVLNNGVVSYNDRP---ILHNLSWQVNPGEHWQIVGPNGAGKSTLLSL-----------ITGDHpqgysNDLtlfgrrrg 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 442 RAQNVRHYREQIGVVRQEPVL---FGTTIGNNIK---FGREGVGEKEMEQAAREANAYDFIMAFPKK-----FNTLvgek 510
Cdd:PRK10938 327 SGETIWDIKKHIGYVSSSLHLdyrVSTSVRNVILsgfFDSIGIYQAVSDRQQKLAQQWLDILGIDKRtadapFHSL---- 402
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568980685 511 gaqmSGGQkQRIA-IARALVRNPKILILDEATSALDTESESLVQTALEK-ASKGRTTIV-VAH 570
Cdd:PRK10938 403 ----SWGQ-QRLAlIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVlISEGETQLLfVSH 460
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
375-559 |
5.47e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 50.50 E-value: 5.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 375 IEFKNVSFSYPSRpsakVL-KGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDEndiraqNVrhyreQI 453
Cdd:PRK11819 325 IEAENLSKSFGDR----LLiDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGE------TV-----KL 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 454 GVVRQ-----EPvlfGTTIGNNIKFGRE--GVGEKEMeqAAReanAYdfIMAFpkkfntlvGEKGA-------QMSGGQK 519
Cdd:PRK11819 390 AYVDQsrdalDP---NKTVWEEISGGLDiiKVGNREI--PSR---AY--VGRF--------NFKGGdqqkkvgVLSGGER 451
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 568980685 520 QRIAIARALVRNPKILILDEATSALDTESESlvqtALEKA 559
Cdd:PRK11819 452 NRLHLAKTLKQGGNVLLLDEPTNDLDVETLR----ALEEA 487
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
384-610 |
5.60e-06 |
|
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: 51.17 E-value: 5.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 384 YPSRPSAKVLKgLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDIrAQNVRHYREQIGVVRQEPVLf 463
Cdd:TIGR01257 1947 YSGTSSPAVDR-LCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSI-LTNISDVHQNMGYCPQFDAI- 2023
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 464 gttigNNIKFGRE---------GVGEKEMEqaaREANAYDFIMAFPKKFNTLVGekgaQMSGGQKQRIAIARALVRNPKI 534
Cdd:TIGR01257 2024 -----DDLLTGREhlylyarlrGVPAEEIE---KVANWSIQSLGLSLYADRLAG----TYSGGNKRKLSTAIALIGCPPL 2091
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568980685 535 LILDEATSALDTESESLV-QTALEKASKGRTTIVVAHRLSTIRG-ADLIVTMKDGMVVEKGTHAELMAKQGLYYSLAM 610
Cdd:TIGR01257 2092 VLLDEPTTGMDPQARRMLwNTIVSIIREGRAVVLTSHSMEECEAlCTRLAIMVKGAFQCLGTIQHLKSKFGDGYIVTM 2169
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
183-326 |
5.64e-06 |
|
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) and similar proteins. These transporter subunits include HylB, PrtD, CyaB, CvaB, RsaD, HasD, LipB, and LapB, among many others. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). Most targeted proteins are not cleaved at the N terminus, but rather carry signals located toward the extreme C terminus to direct type I secretion. However, the 10 kDa Escherichia coli colicin V (CvaB) targets the ABC transporter using a cleaved, N-terminal signal sequence. Almost all transport substrates of the type I system have critical functions in attacking host cells either directly or by being essential for host colonization. The ABC-dependent T1SS transports various molecules, from ions, drugs, to proteins of various sizes up to 900 kDa. The molecules secreted vary in size from the small Escherichia coli peptide colicin V, (10 kDa) to the Pseudomonas fluorescens cell adhesion protein LapA of 520 kDa. The best characterized are the RTX toxins such as the adenylate cyclase (CyaA) toxin from Bordetella pertussis, the causative agent of whooping cough, and the lipases such as LipA. Type I secretion is also involved in export of non-protein substrates such as cyclic beta-glucans and polysaccharides.
Pssm-ID: 349999 [Multi-domain] Cd Length: 294 Bit Score: 49.82 E-value: 5.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 183 IGLVISLIKSWKLSLVVLSTSPLIMASSALCSRMIISLTSKELDAYSKAGAVAEEALSSIQTVTAFGAQEKEIQRYTQHL 262
Cdd:cd18555 131 IYLIYMLYYSPLLTLIVLLLGLLIVLLLLLTRKKIKKLNQEEIVAQTKVQSYLTETLYGIETIKSLGSEKNIYKKWENLF 210
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568980685 263 KDAKDAGIKRA-TASKLS--LGAVYFFMNgayGLAFWYGTSLIFGGEpgYTIGTILAvfFSVIHSSY 326
Cdd:cd18555 211 KKQLKAFKKKErLSNILNsiSSSIQFIAP---LLILWIGAYLVINGE--LTLGELIA--FSSLAGSF 270
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
376-545 |
6.20e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 50.31 E-value: 6.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 376 EFKNVSFSYPSRPSAKVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPE-DGCITVD--ENDIR--AQNVRHY- 449
Cdd:PRK13549 261 EVRNLTAWDPVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPGRwEGEIFIDgkPVKIRnpQQAIAQGi 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 450 ------REQIGVVrqePVLfgtTIGNNI------KFGREGVGEKEMEQAAreanAYDFIMAFPKKFNTLVgEKGAQMSGG 517
Cdd:PRK13549 341 amvpedRKRDGIV---PVM---GVGKNItlaaldRFTGGSRIDDAAELKT----ILESIQRLKVKTASPE-LAIARLSGG 409
|
170 180
....*....|....*....|....*...
gi 568980685 518 QKQRIAIARALVRNPKILILDEATSALD 545
Cdd:PRK13549 410 NQQKAVLAKCLLLNPKILILDEPTRGID 437
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
400-575 |
6.51e-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: 47.95 E-value: 6.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 400 IKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDendiraqnvrhyreqigvvrqepvlfGTTIgnnikfgregvg 479
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWD--------------------------GITP------------ 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 480 ekemeqaareanAYDfimafPKKFNtlvgekgaqMSGGQKQRIAIARALVRNPKILILDEATSALDTESESLVQTALEKA 559
Cdd:cd03222 64 ------------VYK-----PQYID---------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRL 117
|
170
....*....|....*...
gi 568980685 560 SK--GRTTIVVAHRLSTI 575
Cdd:cd03222 118 SEegKKTALVVEHDLAVL 135
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
378-600 |
6.82e-06 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 50.39 E-value: 6.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 378 KNVSFSypsrpsakvlkglnlkIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDIraqNVRHYREQI--GV 455
Cdd:PRK10762 269 NDVSFT----------------LRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEV---VTRSPQDGLanGI 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 456 V------RQEPVLFGTTIGNNI------KFGREGVGEK-EMEQAAREanayDFIMAFPKK---FNTLVGEkgaqMSGGQK 519
Cdd:PRK10762 330 VyisedrKRDGLVLGMSVKENMsltalrYFSRAGGSLKhADEQQAVS----DFIRLFNIKtpsMEQAIGL----LSGGNQ 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 520 QRIAIARALVRNPKILILDEATSALDTES-ESLVQTALEKASKGRTTIVVAHRLSTIRG-ADLIVTMKDGMV-----VEK 592
Cdd:PRK10762 402 QKVAIARGLMTRPKVLILDEPTRGVDVGAkKEIYQLINQFKAEGLSIILVSSEMPEVLGmSDRILVMHEGRIsgeftREQ 481
|
....*...
gi 568980685 593 GTHAELMA 600
Cdd:PRK10762 482 ATQEKLMA 489
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
727-948 |
7.27e-06 |
|
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: 49.31 E-value: 7.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 727 MLVVLGIVALVTYLmQGLFYGRAEENLAMRLRHSAFKAMLYQDMAWYDdkENNTGALTTTLAVDVAQIQGAATSrlGIVT 806
Cdd:cd18544 47 YLGLLLLSFLLQYL-QTYLLQKLGQRIIYDLRRDLFSHIQRLPLSFFD--RTPVGRLVTRVTNDTEALNELFTS--GLVT 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 807 --QDVSNMSLSILISFIYGWEMTLLILSFAPVLAVtgmiqtaAMAGFANRDKQALKRA-GKIA------TEAVENIRTVV 877
Cdd:cd18544 122 liGDLLLLIGILIAMFLLNWRLALISLLVLPLLLL-------ATYLFRKKSRKAYREVrEKLSrlnaflQESISGMSVIQ 194
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568980685 878 SLTRERAFEQMYEETLQtQHRNALKRAHITgccYAVSHAFVHFAHAAG----FRFGAYLIQAGrMMPEGMFIVFT 948
Cdd:cd18544 195 LFNREKREFEEFDEINQ-EYRKANLKSIKL---FALFRPLVELLSSLAlalvLWYGGGQVLSG-AVTLGVLYAFI 264
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
513-570 |
7.53e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 50.24 E-value: 7.53e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 568980685 513 QMSGGQKQRIAIARALVRNPKILILDEATSALDTESESLVQTALEKASKgrTTIVVAH 570
Cdd:PLN03073 344 TFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPK--TFIVVSH 399
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
400-588 |
7.88e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 50.19 E-value: 7.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 400 IKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDEnDI--RAQNVRHyrEQIGVVRQepVLFGTT--IGNNI---- 471
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPEL-KIsyKPQYIKP--DYDGTVED--LLRSITddLGSSYykse 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 472 ---KFGREGVGEKEMeqaareanaydfimafpkkfNTLvgekgaqmSGGQKQRIAIARALVRNPKILILDEATSALDTES 548
Cdd:PRK13409 437 iikPLQLERLLDKNV--------------------KDL--------SGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQ 488
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568980685 549 ESLVQTALEK--ASKGRTTIVVAHRLSTIrgaDLI--------------------VTMKDGM 588
Cdd:PRK13409 489 RLAVAKAIRRiaEEREATALVVDHDIYMI---DYIsdrlmvfegepgkhghasgpMDMREGM 547
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
514-607 |
8.24e-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: 50.40 E-value: 8.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 514 MSGGQKQRIAIARAL------VrnpkILILDEATSAL---DTESesLVQTALEKASKGRTTIVVAHRLSTIRGADLIVTM 584
Cdd:TIGR00630 489 LSGGEAQRIRLATQIgsgltgV----LYVLDEPSIGLhqrDNRR--LINTLKRLRDLGNTLIVVEHDEDTIRAADYVIDI 562
|
90 100 110
....*....|....*....|....*....|...
gi 568980685 585 ------KDGMVVEKGTHAELMAKQ----GLYYS 607
Cdd:TIGR00630 563 gpgageHGGEVVASGTPEEILANPdsltGQYLS 595
|
|
| ABC_6TM_T1SS_like |
cd18779 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding ... |
185-316 |
1.01e-05 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) and similar proteins. These transporter subunits include HylB, PrtD, CyaB, CvaB, RsaD, HasD, LipB, and LapB, among many others. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). Most targeted proteins are not cleaved at the N terminus, but rather carry signals located toward the extreme C terminus to direct type I secretion. However, the 10 kDa Escherichia coli colicin V (CvaB) targets the ABC transporter using a cleaved, N-terminal signal sequence. Almost all transport substrates of the type I system have critical functions in attacking host cells either directly or by being essential for host colonization. The ABC-dependent T1SS transports various molecules, from ions, drugs, to proteins of various sizes up to 900 kDa. The molecules secreted vary in size from the small Escherichia coli peptide colicin V, (10 kDa) to the Pseudomonas fluorescens cell adhesion protein LapA of 520 kDa. The best characterized are the RTX toxins such as the adenylate cyclase (CyaA) toxin from Bordetella pertussis, the causative agent of whooping cough, and the lipases such as LipA. Type I secretion is also involved in export of non-protein substrates such as cyclic beta-glucans and polysaccharides.
Pssm-ID: 350052 [Multi-domain] Cd Length: 294 Bit Score: 48.70 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 185 LVISLIKSWKLSLVVLSTSPLIMASSALCSRMIISLTSKELDAYSKAGAVAEEALSSIQTVTAFGAQEKEIQRYTQHLKD 264
Cdd:cd18779 133 LALLFAQSPLLGLVVLGLAALQVALLLATRRRVRELMARELAAQAEAQSYLVEALSGIETLKASGAEDRALDRWSNLFVD 212
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 568980685 265 AKDAGIKRATASKLSLGAVYFFMNGAYGLAFWYGTSLIFGGEpgYTIGTILA 316
Cdd:cd18779 213 QLNASLRRGRLDALVDALLATLRLAAPLVLLWVGAWQVLDGQ--LSLGTMLA 262
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
514-605 |
1.37e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 49.34 E-value: 1.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 514 MSGGQKQRIAIARALVRNPKILILDEATSALDTESE-SLVQTALEKASKGRTTIVVAHRLSTIRG-ADLIVTMKDGMVV- 590
Cdd:PRK10982 392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKfEIYQLIAELAKKDKGIIIISSEMPELLGiTDRILVMSNGLVAg 471
|
90
....*....|....*....
gi 568980685 591 ----EKGTHAELMAKQGLY 605
Cdd:PRK10982 472 ivdtKTTTQNEILRLASLH 490
|
|
| ABC_6TM_ATM1_ABCB7 |
cd18582 |
Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1 ... |
34-317 |
2.22e-05 |
|
Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1/ABCB7 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. Yeast ATM1 and human ABCB7 (ABC transporter subfamily B, member 7), which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria. In eukaryotes, the Atm1/ABCB7 is present in the inner membrane of mitochondria and is required for the formation of cytosolic iron sulfur cluster containing proteins; mutations of ABCB7 gene result in mitochondrial iron accumulation and are responsible for X-linked sideroblastic anemia.
Pssm-ID: 350026 [Multi-domain] Cd Length: 292 Bit Score: 47.88 E-value: 2.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 34 IVLMTLGILASmingATVPLMslvLGEISDHLingclvqtnrtkyqncSQTQEKLNEDIIVLTLYYIGIGAAALIFGYVQ 113
Cdd:cd18582 2 LLLLVLAKLLN----VAVPFL---LKYAVDAL----------------SAPASALLAVPLLLLLAYGLARILSSLFNELR 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 114 ISFWVITAARQTTRIRKQFFHSILAQDISWFdgsdiceLNTRmTG----DINKLCDGIGDKIPLMFQNI--SGFSIGLVI 187
Cdd:cd18582 59 DALFARVSQRAVRRLALRVFRHLHSLSLRFH-------LSRK-TGalsrAIERGTRGIEFLLRFLLFNIlpTILELLLVC 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 188 SLIK---SWKLSLVVLSTSPLIMASSALCSRMIISLTSKELDAYSKAGAVAEEALSSIQTVTAFGAQEKEIQRYTQHLKD 264
Cdd:cd18582 131 GILWylyGWSYALITLVTVALYVAFTIKVTEWRTKFRREMNEADNEANAKAVDSLLNYETVKYFNNEEYEAERYDKALAK 210
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 568980685 265 AKDAGIKrataSKLSLGAVYFfmngayglafwyGTSLIFGGepGYTIGTILAV 317
Cdd:cd18582 211 YEKAAVK----SQTSLALLNI------------GQALIISL--GLTAIMLLAA 245
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
1032-1204 |
2.40e-05 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 49.07 E-value: 2.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1032 GKTVAFVGSSGCGKSTCVQLL--QRFYDPMKGQVLLDGVDVKE---LNVQWLRSQTAIVS-----QEPVLFNCSIAENIA 1101
Cdd:PLN03140 906 GVLTALMGVSGAGKTTLMDVLagRKTGGYIEGDIRISGFPKKQetfARISGYCEQNDIHSpqvtvRESLIYSAFLRLPKE 985
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1102 YGDNSRMVPLEEIKEVADAANIHSFIEGLPrkyntlvGLRGvqLSGGQKQRLAIARALLRKPKILLLDEATSALDNESEK 1181
Cdd:PLN03140 986 VSKEEKMMFVDEVMELVELDNLKDAIVGLP-------GVTG--LSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAA 1056
|
170 180
....*....|....*....|....
gi 568980685 1182 VVQQAL-DKARRGKTCLVVAHRLS 1204
Cdd:PLN03140 1057 IVMRTVrNTVDTGRTVVCTIHQPS 1080
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
393-584 |
2.95e-05 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 46.87 E-value: 2.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 393 LKGLNLKIKAGETVALVGPSGSGKSTTV---------------------QLLQRLYDPE----DG---CITVDENDIRaq 444
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLAfdtiyaegqrryveslsayarQFLGQMDKPDvdsiEGlspAIAIDQKTTS-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 445 nvRHYREQIGVVrqepvlfgTTIGNNIK--FGREGVGEKemeqaareanaYDFIMAFPKKFNTLVGEKGAqMSGGQKQRI 522
Cdd:cd03270 89 --RNPRSTVGTV--------TEIYDYLRllFARVGIRER-----------LGFLVDVGLGYLTLSRSAPT-LSGGEAQRI 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568980685 523 AIARALVRNPK--ILILDEATSAL-DTESESLVQTALEKASKGRTTIVVAHRLSTIRGADLIVTM 584
Cdd:cd03270 147 RLATQIGSGLTgvLYVLDEPSIGLhPRDNDRLIETLKRLRDLGNTVLVVEHDEDTIRAADHVIDI 211
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
1004-1232 |
4.06e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 47.58 E-value: 4.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1004 LEFREVSFVYPCRPevpVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVlldgvdvkelnvQWlrsqta 1083
Cdd:PRK15064 320 LEVENLTKGFDNGP---LFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV------------KW------ 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1084 ivsqepvlfncsiAENIAYG----DNSrmvpleeikevADAANIHSFIEGLPR----KYNTLVgLRGV------------ 1143
Cdd:PRK15064 379 -------------SENANIGyyaqDHA-----------YDFENDLTLFDWMSQwrqeGDDEQA-VRGTlgrllfsqddik 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1144 ----QLSGGQKQRLAIARALLRKPKILLLDEATSALDNESEKVVQQALDKARrgKTCLVVAH------RLSTiqnaDMIV 1213
Cdd:PRK15064 434 ksvkVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESIESLNMALEKYE--GTLIFVSHdrefvsSLAT----RIIE 507
|
250
....*....|....*....
gi 568980685 1214 VLQNGSIKEQGTHQELLRN 1232
Cdd:PRK15064 508 ITPDGVVDFSGTYEEYLRS 526
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
1022-1238 |
4.27e-05 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 46.73 E-value: 4.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1022 LQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDG-VDVKELNVQWLRSQTAIvsqepvlfncsiaENI 1100
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGeVSVIAISAGLSGQLTGI-------------ENI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1101 AYgdnsRMVPL----EEIK----EVADAANIHSFIEGLPRKYntlvglrgvqlSGGQKQRLAIARALLRKPKILLLDEAT 1172
Cdd:PRK13546 107 EF----KMLCMgfkrKEIKamtpKIIEFSELGEFIYQPVKKY-----------SSGMRAKLGFSINITVNPDILVIDEAL 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568980685 1173 SALDnesEKVVQQALDK----ARRGKTCLVVAHRLSTIQN-ADMIVVLQNGSIKEQGTHQELLRNGDTYFK 1238
Cdd:PRK13546 172 SVGD---QTFAQKCLDKiyefKEQNKTIFFVSHNLGQVRQfCTKIAWIEGGKLKDYGELDDVLPKYEAFLN 239
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1021-1187 |
4.69e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 47.86 E-value: 4.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1021 VLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQV-LLDGVDV---KELNVQWLRSqtaivsqepvlfncsi 1096
Cdd:PRK10636 327 ILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIgLAKGIKLgyfAQHQLEFLRA---------------- 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1097 aeniaygDNSrmvPLEEIKEVADAAnihsfIEGLPRKYNTLVGLRGVQL-------SGGQKQRLAIARALLRKPKILLLD 1169
Cdd:PRK10636 391 -------DES---PLQHLARLAPQE-----LEQKLRDYLGGFGFQGDKVteetrrfSGGEKARLVLALIVWQRPNLLLLD 455
|
170
....*....|....*...
gi 568980685 1170 EATSALDNESEKVVQQAL 1187
Cdd:PRK10636 456 EPTNHLDLDMRQALTEAL 473
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
407-585 |
4.98e-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: 45.04 E-value: 4.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 407 ALVGPSGSGKSTTVqllqrlydpedgcitvdendiraqnvrhyrEQIGVVrqepvlfgtTIGNNIKFGREGVGEKEMEQA 486
Cdd:cd03227 25 IITGPNGSGKSTIL------------------------------DAIGLA---------LGGAQSATRRRSGVKAGCIVA 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 487 AREANAYDFIMafpkkfntlvgekgaQMSGGQKQRIAIARAL----VRNPKILILDEATSALDTES-ESLVQTALEKASK 561
Cdd:cd03227 66 AVSAELIFTRL---------------QLSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDgQALAEAILEHLVK 130
|
170 180
....*....|....*....|....
gi 568980685 562 GRTTIVVAHRLSTIRGADLIVTMK 585
Cdd:cd03227 131 GAQVIVITHLPELAELADKLIHIK 154
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
680-839 |
6.09e-05 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349994 [Multi-domain] Cd Length: 294 Bit Score: 46.32 E-value: 6.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 680 FVVLGTLASALNGSVHPvfsIIFGKLVtmfedkNKATLKQDAEL---YSMMLVVLGIVALVTYLMQGLFYGRAEENLAMR 756
Cdd:cd18550 3 LVLLLILLSALLGLLPP---LLLREII------DDALPQGDLGLlvlLALGMVAVAVASALLGVVQTYLSARIGQGVMYD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 757 LRHSAFKAMLYQDMAWYddKENNTGALTTTLAVDVAQIQGAATSRLGIVTQDVSNMSLSILISFIYGWEMTLLILSFAPV 836
Cdd:cd18550 74 LRVQLYAHLQRMSLAFF--TRTRTGEIQSRLNNDVGGAQSVVTGTLTSVVSNVVTLVATLVAMLALDWRLALLSLVLLPL 151
|
...
gi 568980685 837 LAV 839
Cdd:cd18550 152 FVL 154
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
727-938 |
6.26e-05 |
|
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: 46.29 E-value: 6.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 727 MLVVLGIVALVTYLMQglFYGRaeeNLAMR----LRHSAFKAMLYQDMAWYDdkENNTGALTttlavdvaqiqgaatSRL 802
Cdd:cd18549 48 LLALYILRTLLNYFVT--YWGH---VMGARietdMRRDLFEHLQKLSFSFFD--NNKTGQLM---------------SRI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 803 givTQDVSNMS--------------LSILISFIY----GWEMTLLILSFAPVLAVTGMIQTAAMagfanrdKQALKRA-G 863
Cdd:cd18549 106 ---TNDLFDISelahhgpedlfisiITIIGSFIIlltiNVPLTLIVFALLPLMIIFTIYFNKKM-------KKAFRRVrE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 864 KIA--TEAVEN----IRTVVSLTRErAFEQMYEETLQTQHRNALKRAH-ITGCCYAVSHAFVHFAHAAGFRFGAYLIQAG 936
Cdd:cd18549 176 KIGeiNAQLEDslsgIRVVKAFANE-EYEIEKFDEGNDRFLESKKKAYkAMAYFFSGMNFFTNLLNLVVLVAGGYFIIKG 254
|
..
gi 568980685 937 RM 938
Cdd:cd18549 255 EI 256
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
504-587 |
7.37e-05 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 47.15 E-value: 7.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 504 NTLVGEKGAQ-MSGGQKQRIAIARALVRNPKILILDEATSALDTESESLV-QTALEKASKGRTTIVVAHRLS--TIRGAD 579
Cdd:PLN03140 1009 DAIVGLPGVTgLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVmRTVRNTVDTGRTVVCTIHQPSidIFEAFD 1088
|
....*...
gi 568980685 580 LIVTMKDG 587
Cdd:PLN03140 1089 ELLLMKRG 1096
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
410-581 |
7.54e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 45.25 E-value: 7.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 410 GPSGSGKSTTVQLLQRLYDPEDGCITVDENDIraQNV-RHYREQIGvvRQEPVLFGTTIGNNIKFGREGVGEKEMEQAAr 488
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGNIYYKNCNI--NNIaKPYCTYIG--HNLGLKLEMTVFENLKFWSEIYNSAETLYAA- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 489 eanaydfIMAFpkKFNTLVGEKGAQMSGGQKQRIAIARALVRNPKILILDEATSALDTESESLVQTALE-KASKGRTTIV 567
Cdd:PRK13541 108 -------IHYF--KLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLIVmKANSGGIVLL 178
|
170
....*....|....
gi 568980685 568 VAHRLSTIRGADLI 581
Cdd:PRK13541 179 SSHLESSIKSAQIL 192
|
|
| ABC_6TM_VMR1_D2_like |
cd18604 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
99-262 |
7.59e-05 |
|
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: 46.31 E-value: 7.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 99 YIGIGAAALIFGYVQISFWV---ITAARqttRIRKQFFHSILAQDISWFD---GSDIceLNtRMTGDINKLcDGigdKIP 172
Cdd:cd18604 49 YALISLLSVLLGTLRYLLFFfgsLRASR---KLHERLLHSVLRAPLRWLDttpVGRI--LN-RFSKDIETI-DS---ELA 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 173 LMFQNISGFSIGLVISLIkswklslVVLSTSP-------LIMASSALCSR--MIISLTSKELDAYSKA------GavaeE 237
Cdd:cd18604 119 DSLSSLLESTLSLLVILI-------AIVVVSPafllpavVLAALYVYIGRlyLRASRELKRLESVARSpilshfG----E 187
|
170 180
....*....|....*....|....*
gi 568980685 238 ALSSIQTVTAFGAQEkeiqRYTQHL 262
Cdd:cd18604 188 TLAGLVTIRAFGAEE----RFIEEM 208
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1021-1188 |
1.49e-04 |
|
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: 46.08 E-value: 1.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1021 VLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLdGVDVKelnvqwlrsqtaivsqepvlfncsiaenI 1100
Cdd:TIGR03719 337 LIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETVK----------------------------L 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1101 AYGDNSR--MVP----LEEIKEVADAANIHSFiEGLPRKYNTLVGLRGV-------QLSGGQKQRLAIARALLRKPKILL 1167
Cdd:TIGR03719 388 AYVDQSRdaLDPnktvWEEISGGLDIIKLGKR-EIPSRAYVGRFNFKGSdqqkkvgQLSGGERNRVHLAKTLKSGGNVLL 466
|
170 180
....*....|....*....|.
gi 568980685 1168 LDEATSALDNESEKVVQQALD 1188
Cdd:TIGR03719 467 LDEPTNDLDVETLRALEEALL 487
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
391-603 |
1.80e-04 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 45.11 E-value: 1.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 391 KVLKGLNLKIKAGETVALVGPSGSGKSTTVqLLQRLYDPEDGcitvdENDIR----AQNVRHYREQIGVVRqePVLFGTT 466
Cdd:NF000106 27 KAVDGVDLDVREGTVLGVLGP*GAA**RGA-LPAHV*GPDAG-----RRPWRf*twCANRRALRRTIG*HR--PVR*GRR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 467 IGNNikfGREG---VGEK-EMEQAAREANAYDFIMAFpkKFNTLVGEKGAQMSGGQKQRIAIARALVRNPKILILDEATS 542
Cdd:NF000106 99 ESFS---GRENlymIGR*lDLSRKDARARADELLERF--SLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTT 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568980685 543 ALDTESESLVQTALEKASK-GRTTIVVAHRLSTIRG-ADLIVTMKDGMVVEKGTHAELMAKQG 603
Cdd:NF000106 174 GLDPRTRNEVWDEVRSMVRdGATVLLTTQYMEEAEQlAHELTVIDRGRVIADGKVDELKTKVG 236
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
513-614 |
1.91e-04 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 45.18 E-value: 1.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 513 QMSGGQKQRIAIARALVRNPKILILDEATSALDTESESLVQTALEKASK--GRTTIVVAHRLSTI-RGADLIVTMKDGMV 589
Cdd:PRK15093 158 ELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQnnNTTILLISHDLQMLsQWADKINVLYCGQT 237
|
90 100
....*....|....*....|....*
gi 568980685 590 VEKGTHAELMAKQGLYYSLAMAQDI 614
Cdd:PRK15093 238 VETAPSKELVTTPHHPYTQALIRAI 262
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
729-938 |
1.97e-04 |
|
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: 44.79 E-value: 1.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 729 VVLGIVALVTYLMQGLFY---GRAEENLAMRLRHSAFKAMLYQDMAWYDdkENNTGALTTTLAVDVAQIQGAATSrlGIV 805
Cdd:cd18546 43 AAYLAVVLAGWVAQRAQTrltGRTGERLLYDLRLRVFAHLQRLSLDFHE--RETSGRIMTRMTSDIDALSELLQT--GLV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 806 TQDVSNMSLS-ILIS-FIYGWEMTLLILSFAPVLAVTGMI-QTAAMAGFAnrdkQALKRAGKIATEAVEN---IRTVVSL 879
Cdd:cd18546 119 QLVVSLLTLVgIAVVlLVLDPRLALVALAALPPLALATRWfRRRSSRAYR----RARERIAAVNADLQETlagIRVVQAF 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568980685 880 TRERAFEQMYEEtLQTQHRNALKRAHITGCCYAvshAFVHF----AHAAGFRFGAYLIQAGRM 938
Cdd:cd18546 195 RRERRNAERFAE-LSDDYRDARLRAQRLVAIYF---PGVELlgnlATAAVLLVGAWRVAAGTL 253
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
407-570 |
2.31e-04 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 43.75 E-value: 2.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 407 ALVGPSGSGKSTTVQ-LLQRLY---DPEDGCITVDENDIRAQNVRhyreqiGVVRQEpvlFGTTIGNNIKfgregvgeke 482
Cdd:cd03240 26 LIVGQNGAGKTTIIEaLKYALTgelPPNSKGGAHDPKLIREGEVR------AQVKLA---FENANGKKYT---------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 483 meqAAREANAYDF-IMAFPKKFNTLVGEKGAQMSGGQKQ------RIAIARALVRNPKILILDEATSALDTES--ESLVQ 553
Cdd:cd03240 87 ---ITRSLAILENvIFCHQGESNWPLLDMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENieESLAE 163
|
170
....*....|....*...
gi 568980685 554 -TALEKASKGRTTIVVAH 570
Cdd:cd03240 164 iIEERKSQKNFQLIVITH 181
|
|
| ABC_6TM_CyaB_HlyB_like |
cd18588 |
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ... |
192-316 |
2.34e-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: 44.80 E-value: 2.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 192 SWKLSLVVLSTSPLIMASSALCSRMIISLTSKELDAYSKAGAVAEEALSSIQTVTAFGAQEKEIQRYTQHLKDAKDAGIK 271
Cdd:cd18588 140 SPTLTLIVLASLPLYALLSLLVTPILRRRLEEKFQRGAENQSFLVETVTGIETVKSLAVEPQFQRRWEELLARYVKASFK 219
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 568980685 272 ratASKLSLGAVYF--FMNGAYGLA-FWYGTSLIFGGEpgYTIGTILA 316
Cdd:cd18588 220 ---TANLSNLASQIvqLIQKLTTLAiLWFGAYLVMDGE--LTIGQLIA 262
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1144-1230 |
2.98e-04 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 44.41 E-value: 2.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1144 QLSGGQKQRLAIARALLRKPKILLLDEATSALDNESEKVVQQALDKARR--GKTCLVVAHRLSTI-QNADMIVVLQNGSI 1220
Cdd:PRK15093 158 ELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQnnNTTILLISHDLQMLsQWADKINVLYCGQT 237
|
90
....*....|
gi 568980685 1221 KEQGTHQELL 1230
Cdd:PRK15093 238 VETAPSKELV 247
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
724-963 |
3.06e-04 |
|
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349985 [Multi-domain] Cd Length: 293 Bit Score: 44.32 E-value: 3.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 724 YSMMLVVLGIV-ALVTYLMQGLFYGrAEENLAMRLRHSAFKAMLYQDMAWYDdkENNTGALTTTLAVDVAQIQGAATsrL 802
Cdd:cd18541 42 YALLILLLALLiGIFRFLWRYLIFG-ASRRIEYDLRNDLFAHLLTLSPSFYQ--KNRTGDLMARATNDLNAVRMALG--P 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 803 GIVT--QDVSNMSLSILISFIYGWEMTLLILSFAPVLAVTGMIQTAAMagfANRDKQALKRAGKIATEAVEN---IRTVV 877
Cdd:cd18541 117 GILYlvDALFLGVLVLVMMFTISPKLTLIALLPLPLLALLVYRLGKKI---HKRFRKVQEAFSDLSDRVQESfsgIRVIK 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 878 SLTRERAF-EQMYEETLQTQHRNaLKRAHITGCCYAVSHAFVHFAHAAGFRFGAYLIQAGRMMPeGMFIVFtaIAYGAMa 956
Cdd:cd18541 194 AFVQEEAEiERFDKLNEEYVEKN-LRLARVDALFFPLIGLLIGLSFLIVLWYGGRLVIRGTITL-GDLVAF--NSYLGM- 268
|
....*..
gi 568980685 957 igetLVW 963
Cdd:cd18541 269 ----LIW 271
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
1022-1209 |
3.43e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 43.32 E-value: 3.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1022 LQNMSLSIEKG-----------KTVAFV-GSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVKELNVQWLrsqTAIVSQEP 1089
Cdd:PRK13541 4 LHQLQFNIEQKnlfdlsitflpSAITYIkGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPYC---TYIGHNLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1090 VLFNCSIAENIAYgdnsrmvpLEEIKEVADA--ANIHSFieglprKYNTLVGLRGVQLSGGQKQRLAIARALLRKPKILL 1167
Cdd:PRK13541 81 LKLEMTVFENLKF--------WSEIYNSAETlyAAIHYF------KLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWL 146
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 568980685 1168 LDEATSALDNESEKVVQQALD-KARRGKTCLVVAHRLSTIQNA 1209
Cdd:PRK13541 147 LDEVETNLSKENRDLLNNLIVmKANSGGIVLLSSHLESSIKSA 189
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
1144-1201 |
3.84e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 44.85 E-value: 3.84e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 568980685 1144 QLSGGQKQRLAIARALLRKPKILLLDEATSALDNESEKVVQQALDKARrgKTCLVVAH 1201
Cdd:PLN03073 344 TFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWP--KTFIVVSH 399
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
513-602 |
3.84e-04 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 44.39 E-value: 3.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 513 QMSGGQKQRIAIARALVRNPKILILDEATSALDTESESLVQTALEK-ASKGRTTIVVAHRLSTIRGA-DLIVTMKDGMVV 590
Cdd:PRK09700 409 ELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQlADDGKVILMVSSELPEIITVcDRIAVFCEGRLT 488
|
90
....*....|..
gi 568980685 591 EKGTHAELMAKQ 602
Cdd:PRK09700 489 QILTNRDDMSEE 500
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
393-545 |
4.02e-04 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 44.22 E-value: 4.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 393 LKGLNLKIKAGETVaLVGPSGSGKSTTVQLLQRLYDPEDGcITVDENDI-RAQNVRHYREQIGVVrqepvlFGTTIGNNI 471
Cdd:COG3593 14 IKDLSIELSDDLTV-LVGENNSGKSSILEALRLLLGPSSS-RKFDEEDFyLGDDPDLPEIEIELT------FGSLLSRLL 85
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568980685 472 KFGREGVGEKEMEQAAREANAyDFIMAFpKKFNTLVGEKGAQMSGGQKQRIAIA----RALVRNPKILILDEATSALD 545
Cdd:COG3593 86 RLLLKEEDKEELEEALEELNE-ELKEAL-KALNELLSEYLKELLDGLDLELELSldelEDLLKSLSLRIEDGKELPLD 161
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
492-594 |
4.67e-04 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 44.68 E-value: 4.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 492 AYDFIMAFPK---KFNTLV---------GEKGAQMSGGQKQRIAIARALVRNP--KIL-ILDEATSALDTES-------- 548
Cdd:PRK00349 797 ALEFFEAIPKiarKLQTLVdvglgyiklGQPATTLSGGEAQRVKLAKELSKRStgKTLyILDEPTTGLHFEDirkllevl 876
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 568980685 549 ESLVQtalekasKGRTTIVVAHRLSTIRGADLIVTM------KDGMVVEKGT 594
Cdd:PRK00349 877 HRLVD-------KGNTVVVIEHNLDVIKTADWIIDLgpeggdGGGEIVATGT 921
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
1145-1201 |
6.17e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 43.85 E-value: 6.17e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1145 LSGGQkQRLA-IARALLRKPKILLLDEATSALDNESEKVVQQALDK-ARRGKTCLV-VAH 1201
Cdd:PRK10938 402 LSWGQ-QRLAlIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVlISEGETQLLfVSH 460
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
727-962 |
7.22e-04 |
|
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: 42.96 E-value: 7.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 727 MLVVLGIVALVTYLMQGLF-YGRAE------ENLAMRLRHSAFKAMLYQDMAWYDdkENNTGALTTTLAvDVAQIQGAAT 799
Cdd:cd18566 40 TLQVLVIGVVIAILLESLLrLLRSYilawigARFDHRLSNAAFEHLLSLPLSFFE--REPSGAHLERLN-SLEQIREFLT 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 800 SRLGIVTQDVSNMSLSILISFIYGWEMTLLILSFAPVLAVTGMIQTAAM-AGFANRDKQALKRAGKIaTEAVENIRTVVS 878
Cdd:cd18566 117 GQALLALLDLPFVLIFLGLIWYLGGKLVLVPLVLLGLFVLVAILLGPILrRALKERSRADERRQNFL-IETLTGIHTIKA 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 879 LTRE----RAFEQMYEETLQTQHRNALKRAHITGCcyavSHAFVHFAHAAGFRFGAYLIQAGRMMpEGMFIVFTAIAYGA 954
Cdd:cd18566 196 MAMEpqmlRRYERLQANAAYAGFKVAKINAVAQTL----GQLFSQVSMVAVVAFGALLVINGDLT-VGALIACTMLSGRV 270
|
....*...
gi 568980685 955 MAIGETLV 962
Cdd:cd18566 271 LQPLQRAF 278
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
513-617 |
7.32e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 43.46 E-value: 7.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 513 QMSGGQKQRIAIARALVRNPKILILDEATSALDTESESLVQTALEK-ASKGRTTIVVAHRLSTIRG-ADLIVTMKDGMVV 590
Cdd:PRK10938 135 YLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASlHQSGITLVLVLNRFDEIPDfVQFAGVLADCTLA 214
|
90 100
....*....|....*....|....*..
gi 568980685 591 EKGTHAELMAkQGLYYSLAMAQDIKKV 617
Cdd:PRK10938 215 ETGEREEILQ-QALVAQLAHSEQLEGV 240
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
94-324 |
8.91e-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: 42.93 E-value: 8.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 94 VLTLYYIGIGAaaLIFGYVQIsfwVITAARQ----------TTRIRKQFFHSILAQDISWFDgsdicelnTRMTGDI--- 160
Cdd:cd18568 38 ISLLNLILIGL--LIVGIFQI---LLSAVRQylldyfanriDLSLLSDFYKHLLSLPLSFFA--------SRKVGDIitr 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 161 ---NklcdgigDKIPLMFQNiSGFSIGL-----VISLI----KSWKLSLVVLSTSPLIMASSALCSRMIISLTSKELDAY 228
Cdd:cd18568 105 fqeN-------QKIRRFLTR-SALTTILdllmvFIYLGlmfyYNLQLTLIVLAFIPLYVLLTLLSSPKLKRNSREIFQAN 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 229 SKAGAVAEEALSSIQTVTAFGAQEKEIQRYTQHLKDAKDA---GIKRATASKLSLGAVYFFMNGAyglAFWYGTSLIFGG 305
Cdd:cd18568 177 AEQQSFLVEALTGIATIKALAAERPIRWRWENKFAKALNTrfrGQKLSIVLQLISSLINHLGTIA---VLWYGAYLVISG 253
|
250 260
....*....|....*....|..
gi 568980685 306 EpgYTIGTILA---VFFSVIHS 324
Cdd:cd18568 254 Q--LTIGQLVAfnmLFGSVINP 273
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
723-904 |
9.38e-04 |
|
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: 42.84 E-value: 9.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 723 LYSMMLVVLGIVALVTYLMQGLFYGRAEENLAMRLRHSAFKAMLYQDMAWYDDKEnnTGALTTTLAVDVAQIQGAATSrl 802
Cdd:cd18545 41 IIALLFLALNLVNWVASRLRIYLMAKVGQRILYDLRQDLFSHLQKLSFSFFDSRP--VGKILSRVINDVNSLSDLLSN-- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 803 GIVT--QDVSNMSLSILISFIYGWEMTLLILSFAPVLAVtgmiqtaAMAGFANRDKQALKRA-GKIAT------EAVENI 873
Cdd:cd18545 117 GLINliPDLLTLVGIVIIMFSLNVRLALVTLAVLPLLVL-------VVFLLRRRARKAWQRVrKKISNlnaylhESISGI 189
|
170 180 190
....*....|....*....|....*....|.
gi 568980685 874 RTVVSLTRERAFEQMYEEtLQTQHRNALKRA 904
Cdd:cd18545 190 RVIQSFAREDENEEIFDE-LNRENRKANMRA 219
|
|
| ABC_6TM_AarD_CydDC_like |
cd18561 |
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and ... |
120-321 |
1.11e-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: 42.65 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 120 TAARQTTRIRKQFFHSILAQDISWFDGSDICELNTRMTGDINKLCDGIGDKIPLMFQNISG-FSIGLVISLIkSWKLSLV 198
Cdd:cd18561 63 AAQRVKQHLRRRLFAKLLKLGPGYLEGERTGELQTTVVDGVEALEAYYGRYLPQLLVALLGpLLILIYLFFL-DPLVALI 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 199 VLSTSPLIMASSALCSRMIISLTSKELDAYSKAGAVAEEALSSIQTVTAFGAQEKEIQRYTQHLKDAKDAGIKRATASKL 278
Cdd:cd18561 142 LLVFALLIPLSPALWDRLAKDTGRRHWAAYGRLSAQFLDSLQGMTTLKAFGASKRRGNELAARAEDLRQATMKVLAVSLL 221
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 568980685 279 SLGAVYFFMNGAYGLAFWYGTSLIFGGEPGYTIGtILAVFFSV 321
Cdd:cd18561 222 SSGIMGLATALGTALALGVGALRVLGGQLTLSSL-LLILFLSR 263
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
1139-1229 |
1.12e-03 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 42.80 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1139 GLRGVQLSGGQKQRLAIARALLRKPKILLLDEATSALDNESE-KVVQQALDKARRGKTCLVVAHRLSTI-QNADMIVVLQ 1216
Cdd:NF000106 139 GRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRnEVWDEVRSMVRDGATVLLTTQYMEEAeQLAHELTVID 218
|
90
....*....|...
gi 568980685 1217 NGSIKEQGTHQEL 1229
Cdd:NF000106 219 RGRVIADGKVDEL 231
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
393-576 |
1.26e-03 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 42.11 E-value: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 393 LKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITvdendiraqnvRHyrEQIGVVRQEPVLFGTTIG-NNI 471
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVD-----------RN--GEVSVIAISAGLSGQLTGiENI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 472 KFGR--EGVGEKEMEQAAREANAY----DFIMAFPKKFntlvgekgaqmSGGQKQRIAIARALVRNPKILILDEATSALD 545
Cdd:PRK13546 107 EFKMlcMGFKRKEIKAMTPKIIEFselgEFIYQPVKKY-----------SSGMRAKLGFSINITVNPDILVIDEALSVGD 175
|
170 180 190
....*....|....*....|....*....|....*
gi 568980685 546 tesESLVQTALEK----ASKGRTTIVVAHRLSTIR 576
Cdd:PRK13546 176 ---QTFAQKCLDKiyefKEQNKTIFFVSHNLGQVR 207
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
483-584 |
1.37e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 43.28 E-value: 1.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 483 MEQAAREANayDFIMAFPK---KFNTL---------VGEKGAQMSGGQKQRIAIARAL---VRNPKILILDEATSALDTE 547
Cdd:PRK00635 769 LEMTAYEAE--KFFLDEPSiheKIHALcslgldylpLGRPLSSLSGGEIQRLKLAYELlapSKKPTLYVLDEPTTGLHTH 846
|
90 100 110
....*....|....*....|....*....|....*...
gi 568980685 548 S-ESLVQTALEKASKGRTTIVVAHRLSTIRGADLIVTM 584
Cdd:PRK00635 847 DiKALIYVLQSLTHQGHTVVIIEHNMHVVKVADYVLEL 884
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
501-584 |
1.65e-03 |
|
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a tight junction-associated protein expressed in rat epithelial cells which is thought to have an important regulatory role in tight junction barrier function. Barmotin belongs to the SMC protein family. SMC proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213245 [Multi-domain] Cd Length: 197 Bit Score: 40.91 E-value: 1.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 501 KKFNTLvgekgAQMSGGQKQRIAIAR--ALVR-NPK-ILILDEATSALDTESESLVQTALEKASKGRTTIVVAHRLSTIR 576
Cdd:cd03278 106 KKVQRL-----SLLSGGEKALTALALlfAIFRvRPSpFCVLDEVDAALDDANVERFARLLKEFSKETQFIVITHRKGTME 180
|
90
....*....|
gi 568980685 577 GADLI--VTM 584
Cdd:cd03278 181 AADRLygVTM 190
|
|
| ABC_6TM_ABCC_D1 |
cd18579 |
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ... |
700-952 |
1.91e-03 |
|
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group represents the six-transmembrane domain 1 (TMD1)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. ABC transporters typically consist 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: 350023 [Multi-domain] Cd Length: 289 Bit Score: 41.70 E-value: 1.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 700 IIFGKLVTMFEDKNKATLKQdaelysmmLVVLGIVALVTYLMQGLFYGRAE---ENLAMRLRhSAFKAMLYQ---DMAWY 773
Cdd:cd18579 18 LLLGLLISYLSSYPDEPLSE--------GYLLALALFLVSLLQSLLLHQYFflsFRLGMRVR-SALSSLIYRkalRLSSS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 774 DDKENNTGALTTTLAVDVAQIQGAATSrlgivTQDVSNMSLSILISFIYGWeMTLLILSFAP--VLAVTGMIQTAAMAGF 851
Cdd:cd18579 89 ARQETSTGEIVNLMSVDVQRIEDFFLF-----LHYLWSAPLQIIVALYLLY-RLLGWAALAGlgVLLLLIPLQAFLAKLI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 852 ANRDKQALKRAG---KIATEAVENIRTVVSLTRERAFEQMYEETLQTQHRNALKRAHITGCCYAVSHAFVHFAHAAGfrF 928
Cdd:cd18579 163 SKLRKKLMKATDervKLTNEILSGIKVIKLYAWEKPFLKRIEELRKKELKALRKFGYLRALNSFLFFSTPVLVSLAT--F 240
|
250 260
....*....|....*....|....
gi 568980685 929 GAYLIQAGRMMPEgmfIVFTAIAY 952
Cdd:cd18579 241 ATYVLLGNPLTAA---KVFTALSL 261
|
|
| ABC_6TM_MRP7_D2_like |
cd18605 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ... |
99-264 |
2.33e-03 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and similar proteins; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated protein 7 (MRP7), which belongs to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350049 [Multi-domain] Cd Length: 300 Bit Score: 41.36 E-value: 2.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 99 YIGIGAAALIFGYVQISFWVITAARQTTRIRKQFFHSILAQDISWFDGSDICELNTRMTGDINKlcdgIGDKIPLMFQ-- 176
Cdd:cd18605 48 YGFLAGLNSLFTLLRAFLFAYGGLRAARRLHNKLLSSILFAKMSFFDKTPVGRILNRFSSDVYT----IDDSLPFILNil 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 177 --NISGFSIGLVISLIKSWKLSLVVLstsPLIMASSAL------CSRMIisltsKELDA--YSKAGAVAEEALSSIQTVT 246
Cdd:cd18605 124 laQLFGLLGYLVVICYQLPWLLLLLL---PLAFIYYRIqryyraTSREL-----KRLNSvnLSPLYTHFSETLKGLVTIR 195
|
170
....*....|....*...
gi 568980685 247 AFGAQEKEIQRYTQHLKD 264
Cdd:cd18605 196 AFRKQERFLKEYLEKLEN 213
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
1117-1236 |
2.37e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 42.37 E-value: 2.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1117 VADAAnihSFIEGLP---RKYNTL--VGLRGVQ-------LSGGQKQRLAIARALLRKP--KIL-LLDEATSALDNES-- 1179
Cdd:PRK00349 794 VEEAL---EFFEAIPkiaRKLQTLvdVGLGYIKlgqpattLSGGEAQRVKLAKELSKRStgKTLyILDEPTTGLHFEDir 870
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568980685 1180 --EKVVQQALDKarrGKTCLVVAHRLSTIQNADMIVVL------QNGSIKEQGTHQELLRNGDTY 1236
Cdd:PRK00349 871 klLEVLHRLVDK---GNTVVVIEHNLDVIKTADWIIDLgpeggdGGGEIVATGTPEEVAKVEASY 932
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
513-589 |
2.92e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 41.88 E-value: 2.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 513 QMSGGQKQRIAIAraLV-----RNPK-ILILDEATSALDTESESLVQTALEKASKGRTTIVVAHRLSTIRGAD-LI-VTM 584
Cdd:pfam02463 1077 LLSGGEKTLVALA--LIfaiqkYKPApFYLLDEIDAALDDQNVSRVANLLKELSKNAQFIVISLREEMLEKADkLVgVTM 1154
|
....*
gi 568980685 585 KDGMV 589
Cdd:pfam02463 1155 VENGV 1159
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
1110-1224 |
3.00e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 42.12 E-value: 3.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 1110 PLEEIkevadaANIHSFIEGLPRKYNTLV---------GLRGVQLSGGQKQRLAIARALLRKPK---ILLLDEATSALDN 1177
Cdd:PRK00635 1662 PIEEV------AETFPFLKKIQKPLQALIdnglgylplGQNLSSLSLSEKIAIKIAKFLYLPPKhptLFLLDEIATSLDN 1735
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 568980685 1178 ESEKVVQQALDK-ARRGKTCLVVAHRLSTIQNADMIVVLQNGSIKEQG 1224
Cdd:PRK00635 1736 QQKSALLVQLRTlVSLGHSVIYIDHDPALLKQADYLIEMGPGSGKTGG 1783
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
397-545 |
3.13e-03 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 42.03 E-value: 3.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 397 NLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCIT-----VDENDIRAqnvrhyREQIG------------VVRQE 459
Cdd:NF033858 286 SFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWlfgqpVDAGDIAT------RRRVGymsqafslygelTVRQN 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 460 PVL----FGttignnikfgregVGEKEMEQAAREAnAYDFIMAfpkkfnTLVGEKGAQMSGGQKQRIAIARALVRNPKIL 535
Cdd:NF033858 360 LELharlFH-------------LPAAEIAARVAEM-LERFDLA------DVADALPDSLPLGIRQRLSLAVAVIHKPELL 419
|
170
....*....|
gi 568980685 536 ILDEATSALD 545
Cdd:NF033858 420 ILDEPTSGVD 429
|
|
| Zeta_toxin |
pfam06414 |
Zeta toxin; This family consists of several bacterial zeta toxin proteins. Zeta toxin is ... |
408-497 |
3.17e-03 |
|
Zeta toxin; This family consists of several bacterial zeta toxin proteins. Zeta toxin is thought to be part of a postregulational killing system in bacteria. It relies on antitoxin/toxin systems that secure stable inheritance of low and medium copy number plasmids during cell division and kill cells that have lost the plasmid.
Pssm-ID: 428926 Cd Length: 192 Bit Score: 40.04 E-value: 3.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 408 LVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDIRAQNvRHYREQIGV-VRQEPVLFGttignniKFGREgVGEKeMEQA 486
Cdd:pfam06414 16 LGGQPGAGKTELARALLDELGRQGNVVRIDPDDFRELH-PHYRELQAAdPKTASEYTQ-------PDASR-WVEK-LLQH 85
|
90
....*....|.
gi 568980685 487 AREaNAYDFIM 497
Cdd:pfam06414 86 AIE-NGYNIIL 95
|
|
| ABC_6TM_SUR1_D2_like |
cd18602 |
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group ... |
85-262 |
3.19e-03 |
|
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group represents the six-transmembrane domain 2 (TMD2) of the sulphonylurea receptors SUR1/2 (ABCC8), which function as a modulator of ATP-sensitive potassium channels and insulin release, and belong to the ABCC subfamily. The ATP-sensitive (K-ATP) channel is an octameric complex of four pore-forming Kir6.2 subunits and four regulatory SUR subunits. Thus, in contrast to other ABC transporters, the SUR serves as the regulatory subunit of an ion channel. Mutations and deficiencies in the SUR proteins have been observed in patients with hyperinsulinemic hypoglycemia of infancy, an autosomal recessive disorder of unregulated and high insulin secretion. Mutations have also been associated with non-insulin-dependent diabetes mellitus type 2, an autosomal dominant disease of defective insulin secretion.
Pssm-ID: 350046 [Multi-domain] Cd Length: 307 Bit Score: 41.05 E-value: 3.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 85 QEKLNEDIIVLTLYYIGIGAAALIFGYVQISFWVITAARQTTRIRKQFFHSILAQDISWFDGSDICELNTRMTGDINKlc 164
Cdd:cd18602 42 SSLEDDEVSYYISVYAGLSLGAVILSLVTNLAGELAGLRAARRLHDRMLRNIVRAPMRFFDTTPIGRILNRFSSDTNV-- 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 165 dgIGDKIPLMFQNISGFSIgLVISLIkswklsLVVLSTSP--LIMASSALCSRMIIS----LTSKEL---DAYSKAGAVA 235
Cdd:cd18602 120 --IDQKLPTTLERLLRFLL-LCLSAI------IVNAIVTPyfLIALIPIIIVYYFLQkfyrASSRELqrlDNITKSPVFS 190
|
170 180
....*....|....*....|....*....
gi 568980685 236 E--EALSSIQTVTAFGAQEKEIQRYTQHL 262
Cdd:cd18602 191 HfsETLGGLTTIRAFRQQARFTQQMLELI 219
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1144-1213 |
3.80e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 41.50 E-value: 3.80e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568980685 1144 QLSGGQKQRLAIA--RALLR-KPK-ILLLDEATSALDNESEKVVQQALDKARRGKTCLVVAHRLSTIQNADMIV 1213
Cdd:pfam02463 1077 LLSGGEKTLVALAliFAIQKyKPApFYLLDEIDAALDDQNVSRVANLLKELSKNAQFIVISLREEMLEKADKLV 1150
|
|
| ABC_6TM_HMT1 |
cd18583 |
Six-transmembrane helical domain of the heavy metal tolerance protein; This group represents ... |
193-264 |
3.81e-03 |
|
Six-transmembrane helical domain of the heavy metal tolerance protein; This group represents the HMT1 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. Heavy Metal Tolerance Factor-1 (HMT1) proteins are required for cadmium resistance in Caenorhabditis elegans and Drosophila melanogaster. HMT1 is closely related to Yeast ATM1 and human ABCB7 (ABC transporter subfamily B, member 7), which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria.
Pssm-ID: 350027 [Multi-domain] Cd Length: 290 Bit Score: 40.97 E-value: 3.81e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568980685 193 WKLSLVVLSTSPLIMASSALCSRMIISLTSKELDAYSKAGAVAEEALSSIQTVTAFGAQEKEIQRYTQHLKD 264
Cdd:cd18583 137 PYMGLIVAVVMVLYVWSTIKLTSWRTKLRRDMIDADREERSILTESLLNWETVKYFNREPYEKERYREAVKN 208
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
1145-1215 |
5.15e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 41.35 E-value: 5.15e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568980685 1145 LSGGQKQRLAIARALL---RKPKILLLDEATSAL-DNESEKVVQQALDKARRGKTCLVVAHRLSTIQNADMIVVL 1215
Cdd:PRK00635 810 LSGGEIQRLKLAYELLapsKKPTLYVLDEPTTGLhTHDIKALIYVLQSLTHQGHTVVIIEHNMHVVKVADYVLEL 884
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
715-838 |
5.56e-03 |
|
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: 40.19 E-value: 5.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 715 ATLKQDAELYSMMLVVLGIVALVTYLMQ---GLFYGRAEENLAMRLRHSAFKAMLYQDMAWYDDKenNTGALTTTLAVDV 791
Cdd:cd18563 33 LGPGGNTSLLLLLVLGLAGAYVLSALLGilrGRLLARLGERITADLRRDLYEHLQRLSLSFFDKR--QTGSLMSRVTSDT 110
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 568980685 792 AQIQGAATSRLGIVTQDVSNMSLSILISFIYGWEMTLLILSFAPVLA 838
Cdd:cd18563 111 DRLQDFLSDGLPDFLTNILMIIGIGVVLFSLNWKLALLVLIPVPLVV 157
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|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
507-587 |
6.81e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 40.97 E-value: 6.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 507 VGEKGAQMSGGQKQRIAIARALVRNPK---ILILDEATSALDTESESLVQTALEK-ASKGRTTIVVAHRLSTIRGADLIV 582
Cdd:PRK00635 1693 LGQNLSSLSLSEKIAIKIAKFLYLPPKhptLFLLDEIATSLDNQQKSALLVQLRTlVSLGHSVIYIDHDPALLKQADYLI 1772
|
....*
gi 568980685 583 TMKDG 587
Cdd:PRK00635 1773 EMGPG 1777
|
|
| ABC_6TM_CyaB_HlyB_like |
cd18588 |
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ... |
808-951 |
7.44e-03 |
|
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: 39.79 E-value: 7.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568980685 808 DVSNMSLSILISFIYGWEMTLLILSFAPV-----LAVTGMIQTAAMAGF-ANRDKQALkragkiATEAVENIRTVVSLTR 881
Cdd:cd18588 125 DLVFSVVFLAVMFYYSPTLTLIVLASLPLyallsLLVTPILRRRLEEKFqRGAENQSF------LVETVTGIETVKSLAV 198
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568980685 882 ERAFEQMYEETLQTQHRNALKRAHITgccyAVSHAFVHFAH----AAGFRFGAYLIQAGRMMPeGMFIVFTAIA 951
Cdd:cd18588 199 EPQFQRRWEELLARYVKASFKTANLS----NLASQIVQLIQklttLAILWFGAYLVMDGELTI-GQLIAFNMLA 267
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