|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
51-1259 |
0e+00 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 608.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 51 LLGT--LAAIIHGIALPLMMLVFGDMTDSFaNVGNNrsmsfynATDIYAKLedemttyayyyTGIGAGVLIVAYIqvSLW 128
Cdd:PTZ00265 61 LLGVsfVCATISGGTLPFFVSVFGVIMKNM-NLGEN-------VNDIIFSL-----------VLIGIFQFILSFI--SSF 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 129 CL--AAGRQIHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFFQAMATFFGGFIIGFTRGWKL 206
Cdd:PTZ00265 120 CMdvVTTKILKTLKLEFLKSVFYQDGQFHDNNPGSKLTSDLDFYLEQVNAGIGTKFITIFTYASAFLGLYIWSLFKNARL 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 207 TLVILAISPVLGLSAGIWAKILSSFTDKELQAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNNNLEEAKRLGIKKAIT 286
Cdd:PTZ00265 200 TLCITCVFPLIYICGVICNKKVKINKKTSLLYNNNTMSIIEEALVGIRTVVSYCGEKTILKKFNLSEKLYSKYILKANFM 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 287 ANISMGAAFLLIYASYALAFWYGTSLVIS--------KEYTIGQVLTVFFSVLIGAFSVGQASPNIEAFANARGAAYEVF 358
Cdd:PTZ00265 280 ESLHIGMINGFILASYAFGFWYGTRIIISdlsnqqpnNDFHGGSVISILLGVLISMFMLTIILPNITEYMKSLEATNSLY 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 359 SIIDNKPSIDSfSKSGHKPDNIQgNLEFKNIHFSYPSRKDVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDP 438
Cdd:PTZ00265 360 EIINRKPLVEN-NDDGKKLKDIK-KIQFKNVRFHYDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDP 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 439 IEGEVSI-DGQDIRTINVRYLREIIGVVSQEPVLFATTIAENIRYG---------------------------------- 483
Cdd:PTZ00265 438 TEGDIIInDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKYSlyslkdlealsnyynedgndsqenknkrnscrak 517
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 484 --------RENVTMDEIEKAVKEANA---------------YDFIMKLPHKFDTLVGERGAQLSGGQKQRIAIARALVRN 540
Cdd:PTZ00265 518 cagdlndmSNTTDSNELIEMRKNYQTikdsevvdvskkvliHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRN 597
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 541 PKILLLDEATSALDTESEAVVQAALD--KAREGRTTIVIAHRLSTVRNADVI---------------------------- 590
Cdd:PTZ00265 598 PKILILDEATSSLDNKSEYLVQKTINnlKGNENRITIIIAHRLSTIRYANTIfvlsnrergstvdvdiigedptkdnken 677
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 591 -------------------AGFDGGVIVEQGNHDELMREK-GIYFKLVMTQTA--------GNEIELGNEACESKDG--- 639
Cdd:PTZ00265 678 nnknnkddnnnnnnnnnnkINNAGSYIIEQGTHDALMKNKnGIYYTMINNQKVsskkssnnDNDKDSDMKSSAYKDSerg 757
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 640 --IDNVDMSSKDSGSSLIRRRSTRKSIRGPHDQD--GELSTKEALDDDVPPA-SFWRILKLNSTEWPYFVVGVFCAII-N 713
Cdd:PTZ00265 758 ydPDEMNGNSKHENESASNKKSCKMSDENASENNagGKLPFLRNLFKRKPKApNNLRIVYREIFSYKKDVTIIALSILvA 837
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 714 GGLQPAFSIIFSKVVGvfTKNDTPEIQrQNSNLFSLLFLILGIISFITFFLQGFTFGKAGEILTKRLRYMVFKSMLRQDI 793
Cdd:PTZ00265 838 GGLYPVFALLYAKYVS--TLFDFANLE-ANSNKYSLYILVIAIAMFISETLKNYYNNVIGEKVEKTMKRRLFENILYQEI 914
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 794 SWFDDPKNTTGALTTRLANDAAQVKGATGSRLAVITQNIANLGTGIIISLIYGWQLTLLLLAIVPIIAIAGVVEMKMLSG 873
Cdd:PTZ00265 915 SFFDQDKHAPGLLSAHINRDVHLLKTGLVNNIVIFTHFIVLFLVSMVMSFYFCPIVAAVLTGTYFIFMRVFAIRARLTAN 994
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 874 QALkDKKELEGSGKI----------------ATEAIENFRTVVSLTREQKFETMYAQSLQIPYRNALKKAHVFGITFSFT 937
Cdd:PTZ00265 995 KDV-EKKEINQPGTVfaynsddeifkdpsflIQEAFYNMNTVIIYGLEDYFCNLIEKAIDYSNKGQKRKTLVNSMLWGFS 1073
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 938 QAMMYFSYAACFRFGAYLVARELMTFENVLLVFSAIVFGAMAVGQVSSFAPDYAKAKVSASHIIRIIEKIPEIDSYSTEG 1017
Cdd:PTZ00265 1074 QSAQLFINSFAYWFGSFLIRRGTILVDDFMKSLFTFLFTGSYAGKLMSLKGDSENAKLSFEKYYPLIIRKSNIDVRDNGG 1153
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1018 LK---PNMLEGNVKFNGVMFNYPTRPNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYD-------------- 1080
Cdd:PTZ00265 1154 IRiknKNDIKGKIEIMDVNFRYISRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDlkndhhivfkneht 1233
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1081 ----------------------------------------PMAGTVFLDGKEIKQLNVQWLRAHLGIVSQEPILFDCSIA 1120
Cdd:PTZ00265 1234 ndmtneqdyqgdeeqnvgmknvnefsltkeggsgedstvfKNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIY 1313
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1121 ENIAYGDNSrvVSHEEIVKAAKEANIHQFIDSLPEKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDT 1200
Cdd:PTZ00265 1314 ENIKFGKED--ATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDS 1391
|
1370 1380 1390 1400 1410 1420
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 25453402 1201 ESEKVVQEAL----DKAreGRTCIVIAHRLSTIQNADLIVVIQNGQ-----VKEHGTHQQLL-AQKGIY 1259
Cdd:PTZ00265 1392 NSEKLIEKTIvdikDKA--DKTIITIAHRIASIKRSDKIVVFNNPDrtgsfVQAHGTHEELLsVQDGVY 1458
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
38-624 |
0e+00 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 552.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 38 MFRYAgWLDRFYMLLGTLAAIIHGIALPLMMLVFGDMTDSFANVGNnrsmsfynatdiyaklEDEMTTYAYYYTGIGAGV 117
Cdd:COG1132 12 LLRYL-RPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGGD----------------LSALLLLLLLLLGLALLR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 118 LIVAYIQVSLWCLAAGRQIHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFFQAMATFFGGFI 197
Cdd:COG1132 75 ALLSYLQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 198 IGFTRGWKLTLVILAISPVLGLSAGIWAKILSSFTDKELQAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNNNLEEAK 277
Cdd:COG1132 155 VLFVIDWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELR 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 278 RLGIKKAITANISMGAAFLLIYASYALAFWYGTSLVISKEYTIGQVLTVFFSVLIGAFSVGQASPNIEAFANARGAAYEV 357
Cdd:COG1132 235 RANLRAARLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERI 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 358 FSIIDNKPSIDSfSKSGHKPDNIQGNLEFKNIHFSYPSRKDVqiLKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYD 437
Cdd:COG1132 315 FELLDEPPEIPD-PPGAVPLPPVRGEIEFENVSFSYPGDRPV--LKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYD 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 438 PIEGEVSIDGQDIRTINVRYLREIIGVVSQEPVLFATTIAENIRYGRENVTMDEIEKAVKEANAYDFIMKLPHKFDTLVG 517
Cdd:COG1132 392 PTSGRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVG 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 518 ERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFDGGV 597
Cdd:COG1132 472 ERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGR 551
|
570 580
....*....|....*....|....*..
gi 25453402 598 IVEQGNHDELMREKGIYFKLVMTQTAG 624
Cdd:COG1132 552 IVEQGTHEELLARGGLYARLYRLQFGE 578
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
685-1269 |
8.60e-169 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 513.94 E-value: 8.60e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 685 PPASFWRILKLNSTEWPYFVVGVFCAIINGGLQPAFSIIFSKVV-GVFTKNDTPEIqrqnsNLFSLLFLILGIISFITFF 763
Cdd:COG1132 5 PRKLLRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIdALLAGGDLSAL-----LLLLLLLLGLALLRALLSY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 764 LQGFTFGKAGEILTKRLRYMVFKSMLRQDISWFDdpKNTTGALTTRLANDAAQVKGATGSRLAVITQNIANLGTGIIISL 843
Cdd:COG1132 80 LQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFD--RRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 844 IYGWQLTLLLLAIVPIIAIAGVVEMKMLSGQALKDKKELEGSGKIATEAIENFRTVVSLTREQKFETMYAQSLQIPYRNA 923
Cdd:COG1132 158 VIDWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRAN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 924 LKKAHVFGITFSFTQAMMYFSYAACFRFGAYLVARELMTFENVLLVFSAIVFGAMAVGQVSSFAPDYAKAKVSASHIIRI 1003
Cdd:COG1132 238 LRAARLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFEL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1004 IEKIPEIDSySTEGLKPNMLEGNVKFNGVMFNYPtrPNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMA 1083
Cdd:COG1132 318 LDEPPEIPD-PPGAVPLPPVRGEIEFENVSFSYP--GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTS 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1084 GTVFLDGKEIKQLNVQWLRAHLGIVSQEPILFDCSIAENIAYGDNSrvVSHEEIVKAAKEANIHQFIDSLPEKYNTRVGD 1163
Cdd:COG1132 395 GRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPD--ATDEEVEEAAKAAQAHEFIEALPDGYDTVVGE 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1164 KGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIQNGQV 1243
Cdd:COG1132 473 RGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRI 552
|
570 580
....*....|....*....|....*.
gi 25453402 1244 KEHGTHQQLLAQKGIYFSMVSVQAGA 1269
Cdd:COG1132 553 VEQGTHEELLARGGLYARLYRLQFGE 578
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
50-357 |
9.61e-167 |
|
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: 497.95 E-value: 9.61e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 50 MLLGTLAAIIHGIALPLMMLVFGDMTDSFANVG----NNRSMSFYNATDIYAKLEDEMTTYAYYYTGIGAGVLIVAYIQV 125
Cdd:cd18558 1 MVVGILCAIIHGGLLPAFMVIFGDMTDSFTNGGmtniTGNSSGLNSSAGPFEKLEEEMTLYAYYYLIIGAIVLITAYIQG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 126 SLWCLAAGRQIHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFFQAMATFFGGFIIGFTRGWK 205
Cdd:cd18558 81 SFWGLAAGRQTKKIRYKFFHAIMRQEIGWFDVNDTGELNTRLADDVSKINEGIGDKIGVIFQNIATFGTGFIIGFIRGWK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 206 LTLVILAISPVLGLSAGIWAKILSSFTDKELQAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNNNLEEAKRLGIKKAI 285
Cdd:cd18558 161 LTLVILAISPVLGLSAVVWAKILSGFTDKEKKAYAKAGAVAEEVLEAFRTVIAFGGQQKEETRYAQNLEIAKRNGIKKAI 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 25453402 286 TANISMGAAFLLIYASYALAFWYGTSLVISKEYTIGQVLTVFFSVLIGAFSVGQASPNIEAFANARGAAYEV 357
Cdd:cd18558 241 TFNISMGAAFLLIYASYALAFWYGTYLVTQQEYSIGEVLTVFFSVLIGAFSAGQQVPSIEAFANARGAAYHI 312
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
385-621 |
1.13e-153 |
|
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: 460.85 E-value: 1.13e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 385 EFKNIHFSYPSRKDVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRTINVRYLREIIGV 464
Cdd:cd03249 2 EFKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 465 VSQEPVLFATTIAENIRYGRENVTMDEIEKAVKEANAYDFIMKLPHKFDTLVGERGAQLSGGQKQRIAIARALVRNPKIL 544
Cdd:cd03249 82 VSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKIL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 25453402 545 LLDEATSALDTESEAVVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFDGGVIVEQGNHDELMREKGIYFKLVMTQ 621
Cdd:cd03249 162 LLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKAQ 238
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
1027-1266 |
4.18e-152 |
|
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: 456.62 E-value: 4.18e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1027 VKFNGVMFNYPTRPNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIKQLNVQWLRAHLG 1106
Cdd:cd03249 1 IEFKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1107 IVSQEPILFDCSIAENIAYGDNSRVVshEEIVKAAKEANIHQFIDSLPEKYNTRVGDKGTQLSGGQKQRIAIARALVRQP 1186
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYGKPDATD--EEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1187 HILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIQNGQVKEHGTHQQLLAQKGIYFSMVSVQ 1266
Cdd:cd03249 159 KILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKAQ 238
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
113-622 |
2.44e-145 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 456.99 E-value: 2.44e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 113 IGAGVLIVAYIQVSL-----WCLA-AGRQI-HKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDdVSKINEGIGDKIGMF 185
Cdd:COG2274 198 LAIGLLLALLFEGLLrllrsYLLLrLGQRIdLRLSSRFFRHLLRLPLSFFESRSVGDLASRFRD-VESIREFLTGSLLTA 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 186 FQAMATFFGGFIIGFTRGWKLTLVILAISPVLGLSAGIWAKILSSFTDKELQAYAKAGAVAEEVLAAIRTVIAFGGQKKE 265
Cdd:COG2274 277 LLDLLFVLIFLIVLFFYSPPLALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRF 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 266 LERYNNNLEEAKRLGIKKAITANISMGAAFLLIYASYALAFWYGTSLVISKEYTIGQVLTvfFSVLIGAF--SVGQASPN 343
Cdd:COG2274 357 RRRWENLLAKYLNARFKLRRLSNLLSTLSGLLQQLATVALLWLGAYLVIDGQLTLGQLIA--FNILSGRFlaPVAQLIGL 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 344 IEAFANARGAAYEVFSIIDNKPSIDSFSKSGHKPdNIQGNLEFKNIHFSYPSRkDVQILKGLNLKVKSGQTVALVGNSGC 423
Cdd:COG2274 435 LQRFQDAKIALERLDDILDLPPEREEGRSKLSLP-RLKGDIELENVSFRYPGD-SPPVLDNISLTIKPGERVAIVGRSGS 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 424 GKSTTVQLLQRLYDPIEGEVSIDGQDIRTINVRYLREIIGVVSQEPVLFATTIAENIRYGRENVTMDEIEKAVKEANAYD 503
Cdd:COG2274 513 GKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPDATDEEIIEAARLAGLHD 592
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 504 FIMKLPHKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDKAREGRTTIVIAHRLST 583
Cdd:COG2274 593 FIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLST 672
|
490 500 510
....*....|....*....|....*....|....*....
gi 25453402 584 VRNADVIAGFDGGVIVEQGNHDELMREKGIYFKLVMTQT 622
Cdd:COG2274 673 IRLADRIIVLDKGRIVEDGTHEELLARKGLYAELVQQQL 711
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
693-1010 |
2.71e-145 |
|
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: 441.89 E-value: 2.71e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 693 LKLNSTEWPYFVVGVFCAIINGGLQPAFSIIFSKVVGVFTKNDTPEIQRQnSNLFSLLFLILGIISFITFFLQGFTFGKA 772
Cdd:cd18578 1 LKLNKPEWPLLLLGLIGAIIAGAVFPVFAILFSKLISVFSLPDDDELRSE-ANFWALMFLVLAIVAGIAYFLQGYLFGIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 773 GEILTKRLRYMVFKSMLRQDISWFDDPKNTTGALTTRLANDAAQVKGATGSRLAVITQNIANLGTGIIISLIYGWQLTLL 852
Cdd:cd18578 80 GERLTRRLRKLAFRAILRQDIAWFDDPENSTGALTSRLSTDASDVRGLVGDRLGLILQAIVTLVAGLIIAFVYGWKLALV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 853 LLAIVPIIAIAGVVEMKMLSGQALKDKKELEGSGKIATEAIENFRTVVSLTREQKFETMYAQSLQIPYRNALKKAHVFGI 932
Cdd:cd18578 160 GLATVPLLLLAGYLRMRLLSGFEEKNKKAYEESSKIASEAVSNIRTVASLTLEDYFLEKYEEALEEPLKKGLRRALISGL 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 25453402 933 TFSFTQAMMYFSYAACFRFGAYLVARELMTFENVLLVFSAIVFGAMAVGQVSSFAPDYAKAKVSASHIIRIIEKIPEI 1010
Cdd:cd18578 240 GFGLSQSLTFFAYALAFWYGGRLVANGEYTFEQFFIVFMALIFGAQSAGQAFSFAPDIAKAKAAAARIFRLLDRKPEI 317
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
131-618 |
2.51e-143 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 451.87 E-value: 2.51e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 131 AAGRQIHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFFQAMATFFGGFIIGFTRGWKLTLVI 210
Cdd:TIGR00958 228 TMARINLRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLVMLLGLLGFMLWLSPRLTMVT 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 211 LAISPVLGLSAGIWAKILSSFTDKELQAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNNNLEEAKRLGIKKAITANIS 290
Cdd:TIGR00958 308 LINLPLVFLAEKVFGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFAAEEGEASRFKEALEETLQLNKRKALAYAGY 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 291 MGAAFLLIYASYALAFWYGTSLVISKEYTIGQVLtvffSVLIGAFSVGQASPNIEAFAN----ARGAAYEVFSIIDNKPS 366
Cdd:TIGR00958 388 LWTTSVLGMLIQVLVLYYGGQLVLTGKVSSGNLV----SFLLYQEQLGEAVRVLSYVYSgmmqAVGASEKVFEYLDRKPN 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 367 IDSfsKSGHKPDNIQGNLEFKNIHFSYPSRKDVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSID 446
Cdd:TIGR00958 464 IPL--TGTLAPLNLEGLIEFQDVSFSYPNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLD 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 447 GQDIRTINVRYLREIIGVVSQEPVLFATTIAENIRYGRENVTMDEIEKAVKEANAYDFIMKLPHKFDTLVGERGAQLSGG 526
Cdd:TIGR00958 542 GVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGG 621
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 527 QKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAalDKAREGRTTIVIAHRLSTVRNADVIAGFDGGVIVEQGNHDE 606
Cdd:TIGR00958 622 QKQRIAIARALVRKPRVLILDEATSALDAECEQLLQE--SRSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQ 699
|
490
....*....|..
gi 25453402 607 LMREKGIYFKLV 618
Cdd:TIGR00958 700 LMEDQGCYKHLV 711
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
703-1000 |
1.20e-142 |
|
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: 435.17 E-value: 1.20e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 703 FVVGVFCAIINGGLQPAFSIIFSKVVGVFT----------------KNDTPEIQRQNSNLFSLLFLILGIISFITFFLQG 766
Cdd:cd18558 1 MVVGILCAIIHGGLLPAFMVIFGDMTDSFTnggmtnitgnssglnsSAGPFEKLEEEMTLYAYYYLIIGAIVLITAYIQG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 767 FTFGKAGEILTKRLRYMVFKSMLRQDISWFddPKNTTGALTTRLANDAAQVKGATGSRLAVITQNIANLGTGIIISLIYG 846
Cdd:cd18558 81 SFWGLAAGRQTKKIRYKFFHAIMRQEIGWF--DVNDTGELNTRLADDVSKINEGIGDKIGVIFQNIATFGTGFIIGFIRG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 847 WQLTLLLLAIVPIIAIAGVVEMKMLSGQALKDKKELEGSGKIATEAIENFRTVVSLTREQKFETMYAQSLQIPYRNALKK 926
Cdd:cd18558 159 WKLTLVILAISPVLGLSAVVWAKILSGFTDKEKKAYAKAGAVAEEVLEAFRTVIAFGGQQKEETRYAQNLEIAKRNGIKK 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 25453402 927 AHVFGITFSFTQAMMYFSYAACFRFGAYLV-ARELMTFENVLLVFSAIVFGAMAVGQVSSFAPdYAKAKVSASHI 1000
Cdd:cd18558 239 AITFNISMGAAFLLIYASYALAFWYGTYLVtQQEYSIGEVLTVFFSVLIGAFSAGQQVPSIEA-FANARGAAYHI 312
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
685-1267 |
1.96e-133 |
|
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: 425.40 E-value: 1.96e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 685 PPASFWRILKLNSTEWPYFVVGVFCAIINGGLQPAFSIIFSKVVG-VFTKNDTPEIqrqnsNLFSLLFLILGIISFITFF 763
Cdd:COG2274 140 KPFGLRWFLRLLRRYRRLLLQVLLASLLINLLALATPLFTQVVIDrVLPNQDLSTL-----WVLAIGLLLALLFEGLLRL 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 764 LQGFTFGKAGEILTKRLRYMVFKSMLRQDISWFDdpKNTTGALTTRLaNDAAQVKGATGSRLAVITQNIANLGTGIIISL 843
Cdd:COG2274 215 LRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFE--SRSVGDLASRF-RDVESIREFLTGSLLTALLDLLFVLIFLIVLF 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 844 IYGWQLTLLLLAIVPIIAIAGVV---EMKMLSGQALKDKKELEGsgkIATEAIENFRTVVSLTRE----QKFETMYAQSL 916
Cdd:COG2274 292 FYSPPLALVVLLLIPLYVLLGLLfqpRLRRLSREESEASAKRQS---LLVETLRGIETIKALGAEsrfrRRWENLLAKYL 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 917 qipyRNALKKAHVFGITFSFTQAMMYFSYAACFRFGAYLVARELMTFeNVLLVFSAIVFGAMA-VGQVSSFAPDYAKAKV 995
Cdd:COG2274 369 ----NARFKLRRLSNLLSTLSGLLQQLATVALLWLGAYLVIDGQLTL-GQLIAFNILSGRFLApVAQLIGLLQRFQDAKI 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 996 SASHIIRIIEKIPEIDSYSTEGLKPNmLEGNVKFNGVMFNYPTRpNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLL 1075
Cdd:COG2274 444 ALERLDDILDLPPEREEGRSKLSLPR-LKGDIELENVSFRYPGD-SPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLL 521
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1076 ERFYDPMAGTVFLDGKEIKQLNVQWLRAHLGIVSQEPILFDCSIAENIAYGDNSrvVSHEEIVKAAKEANIHQFIDSLPE 1155
Cdd:COG2274 522 LGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPD--ATDEEIIEAARLAGLHDFIEALPM 599
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1156 KYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLI 1235
Cdd:COG2274 600 GYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRI 679
|
570 580 590
....*....|....*....|....*....|..
gi 25453402 1236 VVIQNGQVKEHGTHQQLLAQKGIYFSMVSVQA 1267
Cdd:COG2274 680 IVLDKGRIVEDGTHEELLARKGLYAELVQQQL 711
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
50-357 |
9.97e-132 |
|
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: 405.70 E-value: 9.97e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 50 MLLGTLAAIIHGIALPLMMLVFGDMTDSFANvgnnrsmsFYNATDIYAKLEDEMTTYAYYYTGIGAGVLIVAYIQVSLWC 129
Cdd:cd18577 1 LIIGLLAAIAAGAALPLMTIVFGDLFDAFTD--------FGSGESSPDEFLDDVNKYALYFVYLGIGSFVLSYIQTACWT 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 130 LAAGRQIHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFFQAMATFFGGFIIGFTRGWKLTLV 209
Cdd:cd18577 73 ITGERQARRIRKRYLKALLRQDIAWFDKNGAGELTSRLTSDTNLIQDGIGEKLGLLIQSLSTFIAGFIIAFIYSWKLTLV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 210 ILAISPVLGLSAGIWAKILSSFTDKELQAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNNNLEEAKRLGIKKAITANI 289
Cdd:cd18577 153 LLATLPLIAIVGGIMGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKALEKARKAGIKKGLVSGL 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 25453402 290 SMGAAFLLIYASYALAFWYGTSLVISKEYTIGQVLTVFFSVLIGAFSVGQASPNIEAFANARGAAYEV 357
Cdd:cd18577 233 GLGLLFFIIFAMYALAFWYGSRLVRDGEISPGDVLTVFFAVLIGAFSLGQIAPNLQAFAKARAAAAKI 300
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
134-621 |
7.98e-129 |
|
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: 408.32 E-value: 7.98e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 134 RQIHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFFQAMATFFGGFIIGFTRGWKLTLVILAI 213
Cdd:TIGR02204 88 RVVADIRRAVFAHLISLSPSFFDKNRSGEVVSRLTTDTTLLQSVIGSSLSMALRNALMCIGGLIMMFITSPKLTSLVLLA 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 214 SPVLGLSAGIWAKILSSFTDKELQAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNNNLEEAKRLGIKKAITANISMGA 293
Cdd:TIGR02204 168 VPLVLLPILLFGRRVRKLSRESQDRIADAGSYAGETLGAIRTVQAFGHEDAERSRFGGAVEKAYEAARQRIRTRALLTAI 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 294 AFLLIYASYALAFWYGTSLVISKEYTIGQVLTVFFSVLIGAFSVGQASPNIEAFANARGAAYEVFSIIDNKPSIDSFSKS 373
Cdd:TIGR02204 248 VIVLVFGAIVGVLWVGAHDVIAGKMSAGTLGQFVFYAVMVAGSIGTLSEVWGELQRAAGAAERLIELLQAEPDIKAPAHP 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 374 GHKPDNIQGNLEFKNIHFSYPSRKDVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRTI 453
Cdd:TIGR02204 328 KTLPVPLRGEIEFEQVNFAYPARPDQPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDLRQL 407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 454 NVRYLREIIGVVSQEPVLFATTIAENIRYGRENVTMDEIEKAVKEANAYDFIMKLPHKFDTLVGERGAQLSGGQKQRIAI 533
Cdd:TIGR02204 408 DPAELRARMALVPQDPVLFAASVMENIRYGRPDATDEEVEAAARAAHAHEFISALPEGYDTYLGERGVTLSGGQRQRIAI 487
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 534 ARALVRNPKILLLDEATSALDTESEAVVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFDGGVIVEQGNHDELMREKGI 613
Cdd:TIGR02204 488 ARAILKDAPILLLDEATSALDAESEQLVQQALETLMKGRTTLIIAHRLATVLKADRIVVMDQGRIVAQGTHAELIAKGGL 567
|
....*...
gi 25453402 614 YFKLVMTQ 621
Cdd:TIGR02204 568 YARLARLQ 575
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
675-1263 |
7.22e-125 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 402.56 E-value: 7.22e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 675 STKEALDDDVPPAS-FWRILKLNSTEWPYFVVG---VFCAIINGGLQPAFS-IIFSKVVGVFTkndtpeIQRQNSNLFSL 749
Cdd:TIGR00958 134 SEKEAEQGQSETADlLFRLLGLSGRDWPWLISAfvfLTLSSLGEMFIPFYTgRVIDTLGGDKG------PPALASAIFFM 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 750 LflILGIISFITFFLQGFTFGKAGEILTKRLRYMVFKSMLRQDISWFDdpKNTTGALTTRLANDAAQVKGATGSRLAVIT 829
Cdd:TIGR00958 208 C--LLSIASSVSAGLRGGSFNYTMARINLRIREDLFRSLLRQDLGFFD--ENKTGELTSRLSSDTQTMSRSLSLNVNVLL 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 830 QNIANLGTGIIISLIYGWQLTLLLLAIVPIIAIAGVVEMKMLSGQALKDKKELEGSGKIATEAIENFRTVVSLTRE---- 905
Cdd:TIGR00958 284 RNLVMLLGLLGFMLWLSPRLTMVTLINLPLVFLAEKVFGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFAAEegea 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 906 QKFETMYAQSLQIPYRNALKKAhVFGITFSFTQAMMYFSYAACfrfGAYLVARELMTFENvLLVFsaiVFGAMAVGQ--- 982
Cdd:TIGR00958 364 SRFKEALEETLQLNKRKALAYA-GYLWTTSVLGMLIQVLVLYY---GGQLVLTGKVSSGN-LVSF---LLYQEQLGEavr 435
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 983 -VSSFAPDYAKAKVSASHIIRIIEKIPEIDSysTEGLKPNMLEGNVKFNGVMFNYPTRPNIPVLQGLSLEVKKGQTLALV 1061
Cdd:TIGR00958 436 vLSYVYSGMMQAVGASEKVFEYLDRKPNIPL--TGTLAPLNLEGLIEFQDVSFSYPNRPDVPVLKGLTFTLHPGEVVALV 513
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1062 GSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIKQLNVQWLRAHLGIVSQEPILFDCSIAENIAYGDNSrvVSHEEIVKAA 1141
Cdd:TIGR00958 514 GPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTD--TPDEEIMAAA 591
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1142 KEANIHQFIDSLPEKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEalDKAREGRTCIV 1221
Cdd:TIGR00958 592 KAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQE--SRSRASRTVLL 669
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 25453402 1222 IAHRLSTIQNADLIVVIQNGQVKEHGTHQQLLAQKGIYFSMV 1263
Cdd:TIGR00958 670 IAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQGCYKHLV 711
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
731-1266 |
1.95e-116 |
|
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: 375.19 E-value: 1.95e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 731 FTKNDTPEIQRqnsnLFSLLFLILGIISFITFFlQGFTFGKAGEILTKRLRYMVFKSMLRQDISWFDdpKNTTGALTTRL 810
Cdd:TIGR02204 49 FSKDSSGLLNR----YFAFLLVVALVLALGTAA-RFYLVTWLGERVVADIRRAVFAHLISLSPSFFD--KNRSGEVVSRL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 811 ANDAAQVKGATGSRLAVITQNIANLGTGIIISLIYGWQLTLLLLAIVPIIAIAGVVEMKMLSGQALKDKKELEGSGKIAT 890
Cdd:TIGR02204 122 TTDTTLLQSVIGSSLSMALRNALMCIGGLIMMFITSPKLTSLVLLAVPLVLLPILLFGRRVRKLSRESQDRIADAGSYAG 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 891 EAIENFRTVVSLTREQKFETMYAQSLQIPYRNALKKAHVFGITFSFTQAMMYFSYAACFRFGAYLV------ARELMTFe 964
Cdd:TIGR02204 202 ETLGAIRTVQAFGHEDAERSRFGGAVEKAYEAARQRIRTRALLTAIVIVLVFGAIVGVLWVGAHDViagkmsAGTLGQF- 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 965 nvllVFSAiVFGAMAVGQVSSFAPDYAKAKVSASHIIRIIEKIPEIDSYSTEGLKPNMLEGNVKFNGVMFNYPTRPNIPV 1044
Cdd:TIGR02204 281 ----VFYA-VMVAGSIGTLSEVWGELQRAAGAAERLIELLQAEPDIKAPAHPKTLPVPLRGEIEFEQVNFAYPARPDQPA 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1045 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIKQLNVQWLRAHLGIVSQEPILFDCSIAENIA 1124
Cdd:TIGR02204 356 LDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDLRQLDPAELRARMALVPQDPVLFAASVMENIR 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1125 YGdnsRV-VSHEEIVKAAKEANIHQFIDSLPEKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESE 1203
Cdd:TIGR02204 436 YG---RPdATDEEVEAAARAAHAHEFISALPEGYDTYLGERGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDAESE 512
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 25453402 1204 KVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIQNGQVKEHGTHQQLLAQKGIYFSMVSVQ 1266
Cdd:TIGR02204 513 QLVQQALETLMKGRTTLIIAHRLATVLKADRIVVMDQGRIVAQGTHAELIAKGGLYARLARLQ 575
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
119-617 |
5.15e-116 |
|
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: 374.05 E-value: 5.15e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 119 IVAYIQVSLWCLAAGRQIHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFFQAMATFFGGFII 198
Cdd:TIGR02203 69 ICSFVSTYLLSWVSNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIV 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 199 GFTRGWKLTLVILAISPVLGLSAGIWAKILSSFTDKELQAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNNNLEEAKR 278
Cdd:TIGR02203 149 LLYYSWQLTLIVVVMLPVLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFDAVSNRNRR 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 279 LGIKKAITANISMGAAFLLIYASYALAFWYGTSLVISKEYTIGQvLTVFFSVLIGAFSVGQASPNIEA-FANARGAAYEV 357
Cdd:TIGR02203 229 LAMKMTSAGSISSPITQLIASLALAVVLFIALFQAQAGSLTAGD-FTAFITAMIALIRPLKSLTNVNApMQRGLAAAESL 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 358 FSIIDNKPSIDsfsKSGHKPDNIQGNLEFKNIHFSYPSRkDVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYD 437
Cdd:TIGR02203 308 FTLLDSPPEKD---TGTRAIERARGDVEFRNVTFRYPGR-DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYE 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 438 PIEGEVSIDGQDIRTINVRYLREIIGVVSQEPVLFATTIAENIRYGR-ENVTMDEIEKAVKEANAYDFIMKLPHKFDTLV 516
Cdd:TIGR02203 384 PDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRtEQADRAEIERALAAAYAQDFVDKLPLGLDTPI 463
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 517 GERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFDGG 596
Cdd:TIGR02203 464 GENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDG 543
|
490 500
....*....|....*....|.
gi 25453402 597 VIVEQGNHDELMREKGIYFKL 617
Cdd:TIGR02203 544 RIVERGTHNELLARNGLYAQL 564
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
255-628 |
1.63e-114 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 371.07 E-value: 1.63e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 255 TVIAFGGQKKELERYNNNLEEAKRLGIKKAITANISMGAAFLLIYASYALAFWYGTSLVISKEYTIGQVltvffsVLIGA 334
Cdd:COG5265 230 TVKYFGNEAREARRYDEALARYERAAVKSQTSLALLNFGQALIIALGLTAMMLMAAQGVVAGTMTVGDF------VLVNA 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 335 F----------------SVGQASPNIEAfanargaayeVFSIIDNKPSIDSfsksghKPDNI-----QGNLEFKNIHFSY 393
Cdd:COG5265 304 YliqlyiplnflgfvyrEIRQALADMER----------MFDLLDQPPEVAD------APDAPplvvgGGEVRFENVSFGY 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 394 -PSRkdvQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRTINVRYLREIIGVVSQEPVLF 472
Cdd:COG5265 368 dPER---PILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLF 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 473 ATTIAENIRYGRENVTMDEIEKAVKEANAYDFIMKLPHKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSA 552
Cdd:COG5265 445 NDTIAYNIAYGRPDASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSA 524
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 25453402 553 LDTESEAVVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFDGGVIVEQGNHDELMREKGIYFKLVMTQTAGNEIE 628
Cdd:COG5265 525 LDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLYAQMWARQQEEEEAE 600
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
125-621 |
7.15e-114 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 368.58 E-value: 7.15e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 125 VSLWCLA--AGRQIHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDD------------VSKINEGigdkigmffqamA 190
Cdd:PRK11176 84 ISSYCISwvSGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDseqvassssgalITVVREG------------A 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 191 TFFGGFIIGFTRGWKLTLVILAISPVLGLSAGIWAKILSSFTDKELQAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYN 270
Cdd:PRK11176 152 SIIGLFIMMFYYSWQLSLILIVIAPIVSIAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFD 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 271 NNLEEAKRLGIKKAITANISMGAAFLLiyASYALAF-WYGTSL-VISKEYTIGQVlTVFFSVLIGAFSVGQASPNIEA-F 347
Cdd:PRK11176 232 KVSNRMRQQGMKMVSASSISDPIIQLI--ASLALAFvLYAASFpSVMDTLTAGTI-TVVFSSMIALMRPLKSLTNVNAqF 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 348 ANARGAAYEVFSIIDNKPSIDSfskSGHKPDNIQGNLEFKNIHFSYPSrKDVQILKGLNLKVKSGQTVALVGNSGCGKST 427
Cdd:PRK11176 309 QRGMAACQTLFAILDLEQEKDE---GKRVIERAKGDIEFRNVTFTYPG-KEVPALRNINFKIPAGKTVALVGRSGSGKST 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 428 TVQLLQRLYDPIEGEVSIDGQDIRTINVRYLREIIGVVSQEPVLFATTIAENIRYGRENV-TMDEIEKAVKEANAYDFIM 506
Cdd:PRK11176 385 IANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYARTEQySREQIEEAARMAYAMDFIN 464
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 507 KLPHKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDKAREGRTTIVIAHRLSTVRN 586
Cdd:PRK11176 465 KMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEK 544
|
490 500 510
....*....|....*....|....*....|....*
gi 25453402 587 ADVIAGFDGGVIVEQGNHDELMREKGIYFKLVMTQ 621
Cdd:PRK11176 545 ADEILVVEDGEIVERGTHAELLAQNGVYAQLHKMQ 579
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
688-1266 |
1.15e-110 |
|
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: 359.42 E-value: 1.15e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 688 SFWRILKLNSTEWPYFVVGVFCAIINGGLQPAFSIIFSKVV-GVFTKNDTPEIQRQNSNLFsLLFLILGIISFITFFLQG 766
Cdd:TIGR02203 1 TFRRLWSYVRPYKAGLVLAGVAMILVAATESTLAALLKPLLdDGFGGRDRSVLWWVPLVVI-GLAVLRGICSFVSTYLLS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 767 FTFGKageiLTKRLRYMVFKSMLRQDISWFDdpKNTTGALTTRLANDAAQVKGATGSRLAVITQNIANLGTGIIISLIYG 846
Cdd:TIGR02203 80 WVSNK----VVRDIRVRMFEKLLGLPVSFFD--RQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIVLLYYS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 847 WQLTLLLLAIVPIIAIAGVVEMKMLSGQALKDKKELEGSGKIATEAIENFRtVVSLTREQKFET-MYAQSLQIPYRNALK 925
Cdd:TIGR02203 154 WQLTLIVVVMLPVLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYR-VVKLFGGQAYETrRFDAVSNRNRRLAMK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 926 KAHVFGITFSFTQ-----AMMYFSYAACFRFGA-YLVARELMTF-ENVLLVFSAIvfgamavGQVSSFAPDYAKAKVSAS 998
Cdd:TIGR02203 233 MTSAGSISSPITQliaslALAVVLFIALFQAQAgSLTAGDFTAFiTAMIALIRPL-------KSLTNVNAPMQRGLAAAE 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 999 HIIRIIEKIPEIDsysTEGLKPNMLEGNVKFNGVMFNYPTRpNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERF 1078
Cdd:TIGR02203 306 SLFTLLDSPPEKD---TGTRAIERARGDVEFRNVTFRYPGR-DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRF 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1079 YDPMAGTVFLDGKEIKQLNVQWLRAHLGIVSQEPILFDCSIAENIAYGDNSRVVShEEIVKAAKEANIHQFIDSLPEKYN 1158
Cdd:TIGR02203 382 YEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRTEQADR-AEIERALAAAYAQDFVDKLPLGLD 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1159 TRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVI 1238
Cdd:TIGR02203 461 TPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVM 540
|
570 580
....*....|....*....|....*...
gi 25453402 1239 QNGQVKEHGTHQQLLAQKGIYFSMVSVQ 1266
Cdd:TIGR02203 541 DDGRIVERGTHNELLARNGLYAQLHNMQ 568
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
384-617 |
2.94e-108 |
|
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: 339.98 E-value: 2.94e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 384 LEFKNIHFSYPSrKDVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRTINVRYLREIIG 463
Cdd:cd03251 1 VEFKNVTFRYPG-DGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 464 VVSQEPVLFATTIAENIRYGRENVTMDEIEKAVKEANAYDFIMKLPHKFDTLVGERGAQLSGGQKQRIAIARALVRNPKI 543
Cdd:cd03251 80 LVSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 25453402 544 LLLDEATSALDTESEAVVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFDGGVIVEQGNHDELMREKGIYFKL 617
Cdd:cd03251 160 LILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKL 233
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
1027-1259 |
4.96e-106 |
|
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: 334.20 E-value: 4.96e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1027 VKFNGVMFNYPTRPNiPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIKQLNVQWLRAHLG 1106
Cdd:cd03251 1 VEFKNVTFRYPGDGP-PVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1107 IVSQEPILFDCSIAENIAYGDnsRVVSHEEIVKAAKEANIHQFIDSLPEKYNTRVGDKGTQLSGGQKQRIAIARALVRQP 1186
Cdd:cd03251 80 LVSQDVFLFNDTVAENIAYGR--PGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 25453402 1187 HILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIQNGQVKEHGTHQQLLAQKGIY 1259
Cdd:cd03251 158 PILILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVY 230
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
384-617 |
1.08e-104 |
|
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: 330.73 E-value: 1.08e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 384 LEFKNIHFSYPSRKdvQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRTINVRYLREIIG 463
Cdd:cd03253 1 IEFENVTFAYDPGR--PVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 464 VVSQEPVLFATTIAENIRYGRENVTMDEIEKAVKEANAYDFIMKLPHKFDTLVGERGAQLSGGQKQRIAIARALVRNPKI 543
Cdd:cd03253 79 VVPQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPI 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 25453402 544 LLLDEATSALDTESEAVVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFDGGVIVEQGNHDELMREKGIYFKL 617
Cdd:cd03253 159 LLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEM 232
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
1024-1272 |
5.62e-102 |
|
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: 336.79 E-value: 5.62e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1024 EGNVKFNGVMFNYptRPNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIKQLNVQWLRA 1103
Cdd:COG5265 355 GGEVRFENVSFGY--DPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRA 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1104 HLGIVSQEPILFDCSIAENIAYGDNSrvVSHEEIVKAAKEANIHQFIDSLPEKYNTRVGDKGTQLSGGQKQRIAIARALV 1183
Cdd:COG5265 433 AIGIVPQDTVLFNDTIAYNIAYGRPD--ASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLL 510
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1184 RQPHILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIQNGQVKEHGTHQQLLAQKGIYFSMV 1263
Cdd:COG5265 511 KNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLYAQMW 590
|
....*....
gi 25453402 1264 SVQAGAKRS 1272
Cdd:COG5265 591 ARQQEEEEA 599
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
382-612 |
1.35e-101 |
|
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: 321.87 E-value: 1.35e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 382 GNLEFKNIHFSYpsRKDVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRTINVRYLREI 461
Cdd:cd03254 1 GEIEFENVNFSY--DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 462 IGVVSQEPVLFATTIAENIRYGRENVTMDEIEKAVKEANAYDFIMKLPHKFDTLVGERGAQLSGGQKQRIAIARALVRNP 541
Cdd:cd03254 79 IGVVLQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 25453402 542 KILLLDEATSALDTESEAVVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFDGGVIVEQGNHDELMREKG 612
Cdd:cd03254 159 KILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
119-621 |
6.75e-100 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 330.77 E-value: 6.75e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 119 IVAYIQVSLwclAAGRQIHKIRQ----KFFHAIMNQEIGWFDVHDVGE-LNTRL--TDDVSKInegigdKIGMFFQAMAT 191
Cdd:PRK13657 70 IIAGVLVAR---HADRLAHRRRLavltEYFERIIQLPLAWHSQRGSGRaLHTLLrgTDALFGL------WLEFMREHLAT 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 192 FFGGFI---IGFTRGWKLTLVILaispVLGLSAGIWAKILSSFTdKELQA-----YAKAGAVAEEVLAAIRTVIAF---G 260
Cdd:PRK13657 141 LVALVVllpLALFMNWRLSLVLV----VLGIVYTLITTLVMRKT-KDGQAaveehYHDLFAHVSDAIGNVSVVQSYnriE 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 261 GQKKELERYNNNLEEAKR-----LGIKKAIT---ANISMGAAFLLiyasyalafwyGTSLVISKEYTIGQVLTV--FFSV 330
Cdd:PRK13657 216 AETQALRDIADNLLAAQMpvlswWALASVLNraaSTITMLAILVL-----------GAALVQKGQLRVGEVVAFvgFATL 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 331 LIGAFSvgqaspNIEAFAN----ARGAAYEVFSIIDNKPSIDsfsKSGHKPD--NIQGNLEFKNIHFSYPSRKdvQILKG 404
Cdd:PRK13657 285 LIGRLD------QVVAFINqvfmAAPKLEEFFEVEDAVPDVR---DPPGAIDlgRVKGAVEFDDVSFSYDNSR--QGVED 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 405 LNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRTINVRYLREIIGVVSQEPVLFATTIAENIRYGR 484
Cdd:PRK13657 354 VSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGR 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 485 ENVTMDEIEKAVKEANAYDFIMKLPHKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAA 564
Cdd:PRK13657 434 PDATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAA 513
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 25453402 565 LDKAREGRTTIVIAHRLSTVRNADVIAGFDGGVIVEQGNHDELMREKGIYFKLVMTQ 621
Cdd:PRK13657 514 LDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVARGGRFAALLRAQ 570
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
1027-1266 |
3.04e-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: 315.71 E-value: 3.04e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1027 VKFNGVMFNYPtrPNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIKQLNVQWLRAHLG 1106
Cdd:cd03253 1 IEFENVTFAYD--PGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1107 IVSQEPILFDCSIAENIAYGDNSrvVSHEEIVKAAKEANIHQFIDSLPEKYNTRVGDKGTQLSGGQKQRIAIARALVRQP 1186
Cdd:cd03253 79 VVPQDTVLFNDTIGYNIRYGRPD--ATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1187 HILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIQNGQVKEHGTHQQLLAQKGIYFSMVSVQ 1266
Cdd:cd03253 157 PILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMWKAQ 236
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
131-612 |
2.97e-98 |
|
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: 325.17 E-value: 2.97e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 131 AAGRQIHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFFQAMATFFGGFIIGFTRGWKLTLVI 210
Cdd:COG4988 85 AAARVKRRLRRRLLEKLLALGPAWLRGKSTGELATLLTEGVEALDGYFARYLPQLFLAALVPLLILVAVFPLDWLSGLIL 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 211 LAISPVLGLSAGIWAKILSSFTDKELQAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNNNLEEAKRlgikkaitanIS 290
Cdd:COG4988 165 LVTAPLIPLFMILVGKGAAKASRRQWRALARLSGHFLDRLRGLTTLKLFGRAKAEAERIAEASEDFRK----------RT 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 291 MGA---AFL-------LIYASYALAFWY-GTSLVIskeytiGQV-LTVFFSVLIgafsvgqASPniEAF----------- 347
Cdd:COG4988 235 MKVlrvAFLssavlefFASLSIALVAVYiGFRLLG------GSLtLFAALFVLL-------LAP--EFFlplrdlgsfyh 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 348 --ANARGAAYEVFSIIDnKPSIDSFSKSGHKPDNIQGNLEFKNIHFSYPSRKdvQILKGLNLKVKSGQTVALVGNSGCGK 425
Cdd:COG4988 300 arANGIAAAEKIFALLD-APEPAAPAGTAPLPAAGPPSIELEDVSFSYPGGR--PALDGLSLTIPPGERVALVGPSGAGK 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 426 STTVQLLQRLYDPIEGEVSIDGQDIRTINVRYLREIIGVVSQEPVLFATTIAENIRYGRENVTMDEIEKAVKEANAYDFI 505
Cdd:COG4988 377 STLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPDASDEELEAALEAAGLDEFV 456
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 506 MKLPHKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDKAREGRTTIVIAHRLSTVR 585
Cdd:COG4988 457 AALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLA 536
|
490 500
....*....|....*....|....*..
gi 25453402 586 NADVIAGFDGGVIVEQGNHDELMREKG 612
Cdd:COG4988 537 QADRILVLDDGRIVEQGTHEELLAKNG 563
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
750-1268 |
7.68e-98 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 324.66 E-value: 7.68e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 750 LFLILGIISFITFFLQGFTFGKageiLTKRLRYMVFKSMLRQDISWFDdpKNTTGALTTRLANDAAQVKGATGSRLAVIT 829
Cdd:PRK11176 74 LMILRGITSFISSYCISWVSGK----VVMTMRRRLFGHMMGMPVSFFD--KQSTGTLLSRITYDSEQVASSSSGALITVV 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 830 QNIANLGTGIIISLIYGWQLTLLLLAIVPIIAIA-GVVE-------------MKMLSG---QALKDKKELEGSGKIATEa 892
Cdd:PRK11176 148 REGASIIGLFIMMFYYSWQLSLILIVIAPIVSIAiRVVSkrfrnisknmqntMGQVTTsaeQMLKGHKEVLIFGGQEVE- 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 893 IENFRTVVSLTREQKFETMYAQSLQIPyrnalkkahVFGITFSFtqAMMYFSYAACFRfgaylVARELMTFENVLLVFSA 972
Cdd:PRK11176 227 TKRFDKVSNRMRQQGMKMVSASSISDP---------IIQLIASL--ALAFVLYAASFP-----SVMDTLTAGTITVVFSS 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 973 IvFGAM----AVGQVSSfapDYAKAKVSASHIIRIIEKIPEIDsystEG-LKPNMLEGNVKFNGVMFNYPTRpNIPVLQG 1047
Cdd:PRK11176 291 M-IALMrplkSLTNVNA---QFQRGMAACQTLFAILDLEQEKD----EGkRVIERAKGDIEFRNVTFTYPGK-EVPALRN 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1048 LSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIKQLNVQWLRAHLGIVSQEPILFDCSIAENIAYGD 1127
Cdd:PRK11176 362 INFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYAR 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1128 NSRVvSHEEIVKAAKEANIHQFIDSLPEKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQ 1207
Cdd:PRK11176 442 TEQY-SREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQ 520
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 25453402 1208 EALDKAREGRTCIVIAHRLSTIQNADLIVVIQNGQVKEHGTHQQLLAQKGIYFSMVSVQAG 1268
Cdd:PRK11176 521 AALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQNGVYAQLHKMQFG 581
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
1025-1257 |
5.73e-96 |
|
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: 306.46 E-value: 5.73e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1025 GNVKFNGVMFNYptRPNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIKQLNVQWLRAH 1104
Cdd:cd03254 1 GEIEFENVNFSY--DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1105 LGIVSQEPILFDCSIAENIAYGDNSrvVSHEEIVKAAKEANIHQFIDSLPEKYNTRVGDKGTQLSGGQKQRIAIARALVR 1184
Cdd:cd03254 79 IGVVLQDTFLFSGTIMENIRLGRPN--ATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLR 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 25453402 1185 QPHILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIQNGQVKEHGTHQQLLAQKG 1257
Cdd:cd03254 157 DPKILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
131-617 |
1.73e-90 |
|
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: 304.00 E-value: 1.73e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 131 AAGRQIHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVskinegigDKIGMFF-QAMATFFGGFIIGFTrgwkLTLV 209
Cdd:COG4987 82 ATLRLLADLRVRLYRRLEPLAPAGLARLRSGDLLNRLVADV--------DALDNLYlRVLLPLLVALLVILA----AVAF 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 210 ILAISPVLGLS-------AGIWAKILSSFTDKELQAYAKA--GAVAEEVLAAIR---TVIAFGGQKKELERYNNNLEEAK 277
Cdd:COG4987 150 LAFFSPALALVlalglllAGLLLPLLAARLGRRAGRRLAAarAALRARLTDLLQgaaELAAYGALDRALARLDAAEARLA 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 278 RLGIKKAITANISMGAAFLLIYASYALAFWYGTSLVISKEYTIGQVLTVFFSVLiGAFSVgqASPNIEAFAN---ARGAA 354
Cdd:COG4987 230 AAQRRLARLSALAQALLQLAAGLAVVAVLWLAAPLVAAGALSGPLLALLVLAAL-ALFEA--LAPLPAAAQHlgrVRAAA 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 355 YEVFSIIDNKPSIDSFSKSGHKPDniQGNLEFKNIHFSYPSRkDVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQR 434
Cdd:COG4987 307 RRLNELLDAPPAVTEPAEPAPAPG--GPSLELEDVSFRYPGA-GRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLR 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 435 LYDPIEGEVSIDGQDIRTINVRYLREIIGVVSQEPVLFATTIAENIRYGRENVTMDEIEKAVKEANAYDFIMKLPHKFDT 514
Cdd:COG4987 384 FLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPDATDEELWAALERVGLGDWLAALPDGLDT 463
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 515 LVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFD 594
Cdd:COG4987 464 WLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLE 543
|
490 500
....*....|....*....|...
gi 25453402 595 GGVIVEQGNHDELMREKGIYFKL 617
Cdd:COG4987 544 DGRIVEQGTHEELLAQNGRYRQL 566
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
1018-1243 |
1.12e-88 |
|
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: 286.29 E-value: 1.12e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1018 LKPNMLEGNVKFNGVMFNYPTRPNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIKQLN 1097
Cdd:cd03248 3 LAPDHLKGIVKFQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1098 VQWLRAHLGIVSQEPILFDCSIAENIAYGDNSrvVSHEEIVKAAKEANIHQFIDSLPEKYNTRVGDKGTQLSGGQKQRIA 1177
Cdd:cd03248 83 HKYLHSKVSLVGQEPVLFARSLQDNIAYGLQS--CSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 25453402 1178 IARALVRQPHILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIQNGQV 1243
Cdd:cd03248 161 IARALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
691-1257 |
1.12e-87 |
|
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: 295.90 E-value: 1.12e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 691 RILKLNSTEWPYFVVGVFCAIINGGLQPAFSIIFSKVV-GVFTKNDTPeiqrqnSNLFSLLFLILGII---SFITFFLQG 766
Cdd:COG4988 7 RLKRLARGARRWLALAVLLGLLSGLLIIAQAWLLASLLaGLIIGGAPL------SALLPLLGLLLAVLllrALLAWLRER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 767 FTFgKAGEILTKRLRYMVFKSMLRQDISWFDdpknttgalttrlandaaqvKGATGSRLAVITQNIANLGT--------- 837
Cdd:COG4988 81 AAF-RAAARVKRRLRRRLLEKLLALGPAWLR--------------------GKSTGELATLLTEGVEALDGyfarylpql 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 838 --GIIISLI-------YGWQLTLLLLAIVPII----AIAGV----------VEMKMLSGQ---ALK----------DKKE 881
Cdd:COG4988 140 flAALVPLLilvavfpLDWLSGLILLVTAPLIplfmILVGKgaakasrrqwRALARLSGHfldRLRglttlklfgrAKAE 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 882 LEgsgKIATEAiENFRTvvsltreqkfETMyaqslqipyrNALKKAhvFGITFsftqAMMYFSYaacfrFGAYLVArelm 961
Cdd:COG4988 220 AE---RIAEAS-EDFRK----------RTM----------KVLRVA--FLSSA----VLEFFAS-----LSIALVA---- 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 962 tfenVLLVFSAI-----VFGAMAV-----------GQVSSFAPDYAKAKVSASHIIRIIEKIPEIDSYSTEGLkPNMLEG 1025
Cdd:COG4988 261 ----VYIGFRLLggsltLFAALFVlllapefflplRDLGSFYHARANGIAAAEKIFALLDAPEPAAPAGTAPL-PAAGPP 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1026 NVKFNGVMFNYPTRPniPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIKQLNVQWLRAHL 1105
Cdd:COG4988 336 SIELEDVSFSYPGGR--PALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQI 413
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1106 GIVSQEPILFDCSIAENIAYGDnsRVVSHEEIVKAAKEANIHQFIDSLPEKYNTRVGDKGTQLSGGQKQRIAIARALVRQ 1185
Cdd:COG4988 414 AWVPQNPYLFAGTIRENLRLGR--PDASDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRD 491
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 25453402 1186 PHILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIQNGQVKEHGTHQQLLAQKG 1257
Cdd:COG4988 492 APLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQADRILVLDDGRIVEQGTHEELLAKNG 563
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
142-622 |
3.24e-87 |
|
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: 298.58 E-value: 3.24e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 142 KFFHAIMNQEIGWFDVHDVGELNTRLTDdVSKINEGIGDK-----IGMFFqaMATFFGgfiIGFTRGWKLTLVILAISPV 216
Cdd:TIGR01846 217 RLYRHLLGLPLGYFESRRVGDTVARVRE-LEQIRNFLTGSaltvvLDLLF--VVVFLA---VMFFYSPTLTGVVIGSLVC 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 217 LGLSAGIWAKILSSFTDKELQAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNNNLEEAKRLGIKKAITANISMGAAFL 296
Cdd:TIGR01846 291 YALLSVFVGPILRKRVEDKFERSAAATSFLVESVTGIETIKATATEPQFQNRWDRQLAAYVAASFRVTNLGNIAGQAIEL 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 297 LIYASYALAFWYGTSLVISKEYTIGQVltVFFSVLIGAFS--VGQASPNIEAFANARGAAYEVFSIIdNKPSiDSFSKSG 374
Cdd:TIGR01846 371 IQKLTFAILLWFGAHLVIGGALSPGQL--VAFNMLAGRVTqpVLRLAQLWQDFQQTGIALERLGDIL-NSPT-EPRSAGL 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 375 HKPDNIQGNLEFKNIHFSYpsRKDV-QILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRTI 453
Cdd:TIGR01846 447 AALPELRGAITFENIRFRY--APDSpEVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIA 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 454 NVRYLREIIGVVSQEPVLFATTIAENIRYGRENVTMDEIEKAVKEANAYDFIMKLPHKFDTLVGERGAQLSGGQKQRIAI 533
Cdd:TIGR01846 525 DPAWLRRQMGVVLQENVLFSRSIRDNIALCNPGAPFEHVIHAAKLAGAHDFISELPQGYNTEVGEKGANLSGGQRQRIAI 604
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 534 ARALVRNPKILLLDEATSALDTESEAVVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFDGGVIVEQGNHDELMREKGI 613
Cdd:TIGR01846 605 ARALVGNPRILIFDEATSALDYESEALIMRNMREICRGRTVIIIAHRLSTVRACDRIIVLEKGQIAESGRHEELLALQGL 684
|
....*....
gi 25453402 614 YFKLVMTQT 622
Cdd:TIGR01846 685 YARLWQQQS 693
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
46-367 |
5.95e-87 |
|
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: 285.11 E-value: 5.95e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 46 DRFYMLLGTLAAIIHGIALPLMMLVFGDMTDSFANVGNNrsmsfynatdiyaKLEDEMTTYAYYYTGIGAGVLIVAYIQV 125
Cdd:cd18578 7 EWPLLLLGLIGAIIAGAVFPVFAILFSKLISVFSLPDDD-------------ELRSEANFWALMFLVLAIVAGIAYFLQG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 126 SLWCLAAGRQIHKIRQKFFHAIMNQEIGWFD--VHDVGELNTRLTDDVSKINEGIGDKIGMFFQAMATFFGGFIIGFTRG 203
Cdd:cd18578 74 YLFGIAGERLTRRLRKLAFRAILRQDIAWFDdpENSTGALTSRLSTDASDVRGLVGDRLGLILQAIVTLVAGLIIAFVYG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 204 WKLTLVILAISPVLGLSAGIWAKILSSFTDKELQAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNNNLEEAKRLGIKK 283
Cdd:cd18578 154 WKLALVGLATVPLLLLAGYLRMRLLSGFEEKNKKAYEESSKIASEAVSNIRTVASLTLEDYFLEKYEEALEEPLKKGLRR 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 284 AITANISMGAAFLLIYASYALAFWYGTSLVISKEYTIGQVLTVFFSVLIGAFSVGQASPNIEAFANARGAAYEVFSIIDN 363
Cdd:cd18578 234 ALISGLGFGLSQSLTFFAYALAFWYGGRLVANGEYTFEQFFIVFMALIFGAQSAGQAFSFAPDIAKAKAAAARIFRLLDR 313
|
....
gi 25453402 364 KPSI 367
Cdd:cd18578 314 KPEI 317
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
377-598 |
3.81e-86 |
|
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: 279.36 E-value: 3.81e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 377 PDNIQGNLEFKNIHFSYPSRKDVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRTINVR 456
Cdd:cd03248 5 PDHLKGIVKFQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 457 YLREIIGVVSQEPVLFATTIAENIRYGRENVTMDEIEKAVKEANAYDFIMKLPHKFDTLVGERGAQLSGGQKQRIAIARA 536
Cdd:cd03248 85 YLHSKVSLVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 25453402 537 LVRNPKILLLDEATSALDTESEAVVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFDGGVI 598
Cdd:cd03248 165 LIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
384-621 |
2.65e-85 |
|
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: 277.45 E-value: 2.65e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 384 LEFKNIHFSYpsRKD-VQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRTINVRYLREII 462
Cdd:cd03252 1 ITFEHVRFRY--KPDgPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 463 GVVSQEPVLFATTIAENIRYGRENVTMDEIEKAVKEANAYDFIMKLPHKFDTLVGERGAQLSGGQKQRIAIARALVRNPK 542
Cdd:cd03252 79 GVVLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 25453402 543 ILLLDEATSALDTESEAVVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFDGGVIVEQGNHDELMREKGIYFKLVMTQ 621
Cdd:cd03252 159 ILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQLQ 237
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
50-335 |
1.42e-83 |
|
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: 274.13 E-value: 1.42e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 50 MLLGTLAAIIHGIALPLMMLVFGDMTDSFANVGNNRSMsfynatdiyakledEMTTYAYYYTGIGAGVLIVAYIQVSLWC 129
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLPDGDPETQ--------------ALNVYSLALLLLGLAQFILSFLQSYLLN 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 130 LAAGRQIHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFFQAMATFFGGFIIGFTRGWKLTLV 209
Cdd:pfam00664 67 HTGERLSRRLRRKLFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 210 ILAISPVLGLSAGIWAKILSSFTDKELQAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNNNLEEAKRLGIKKAITANI 289
Cdd:pfam00664 147 LLAVLPLYILVSAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGL 226
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 25453402 290 SMGAAFLLIYASYALAFWYGTSLVISKEYTIGQ--VLTVFFSVLIGAF 335
Cdd:pfam00664 227 SFGITQFIGYLSYALALWFGAYLVISGELSVGDlvAFLSLFAQLFGPL 274
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
776-1264 |
3.68e-82 |
|
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: 280.50 E-value: 3.68e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 776 LTKRLRYMVFKSMLRQDISWFDDPKntTGALTTRLANDAAQVKGATgsrLAVITQNIANLGTGIIISLIYGWQLTLLLLA 855
Cdd:COG4987 86 LLADLRVRLYRRLEPLAPAGLARLR--SGDLLNRLVADVDALDNLY---LRVLLPLLVALLVILAAVAFLAFFSPALALV 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 856 IVPIIAIAGVVeMKMLSGQALK--DKKELEGSGKIATEAIENFRTVVSLT---REQKFETMYAQSLQIPYRNALKKAHVF 930
Cdd:COG4987 161 LALGLLLAGLL-LPLLAARLGRraGRRLAAARAALRARLTDLLQGAAELAaygALDRALARLDAAEARLAAAQRRLARLS 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 931 GITFSFTQAMMYFSYAACFRFGAYLVARElmTFENVLLVfsAIVFGAMA----VGQVSSFAPDYAKAKVSASHIIRIIEK 1006
Cdd:COG4987 240 ALAQALLQLAAGLAVVAVLWLAAPLVAAG--ALSGPLLA--LLVLAALAlfeaLAPLPAAAQHLGRVRAAARRLNELLDA 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1007 IPEIDSYSTEGLKPNmlEGNVKFNGVMFNYPTRPNiPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTV 1086
Cdd:COG4987 316 PPAVTEPAEPAPAPG--GPSLELEDVSFRYPGAGR-PVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSI 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1087 FLDGKEIKQLNVQWLRAHLGIVSQEPILFDCSIAENIAYGDNSrvVSHEEIVKAAKEANIHQFIDSLPEKYNTRVGDKGT 1166
Cdd:COG4987 393 TLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPD--ATDEELWAALERVGLGDWLAALPDGLDTWLGEGGR 470
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1167 QLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIQNGQVKEH 1246
Cdd:COG4987 471 RLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQ 550
|
490
....*....|....*...
gi 25453402 1247 GTHQQLLAQKGIYFSMVS 1264
Cdd:COG4987 551 GTHEELLAQNGRYRQLYQ 568
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
703-1000 |
6.90e-82 |
|
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: 270.50 E-value: 6.90e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 703 FVVGVFCAIINGGLQPAFSIIFSKVVGVFTK----NDTPEIQRQNSNLFSLLFLILGIISFITFFLQGFTFGKAGEILTK 778
Cdd:cd18577 1 LIIGLLAAIAAGAALPLMTIVFGDLFDAFTDfgsgESSPDEFLDDVNKYALYFVYLGIGSFVLSYIQTACWTITGERQAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 779 RLRYMVFKSMLRQDISWFDdpKNTTGALTTRLANDAAQVKGATGSRLAVITQNIANLGTGIIISLIYGWQLTLLLLAIVP 858
Cdd:cd18577 81 RIRKRYLKALLRQDIAWFD--KNGAGELTSRLTSDTNLIQDGIGEKLGLLIQSLSTFIAGFIIAFIYSWKLTLVLLATLP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 859 IIAIAGVVEMKMLSGQALKDKKELEGSGKIATEAIENFRTVVSLTREQKFETMYAQSLQIPYRNALKKAHVFGITFSFTQ 938
Cdd:cd18577 159 LIAIVGGIMGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKALEKARKAGIKKGLVSGLGLGLLF 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 25453402 939 AMMYFSYAACFRFGAYLVARELMTFENVLLVFSAIVFGAMAVGQVSSFAPDYAKAKVSASHI 1000
Cdd:cd18577 239 FIIFAMYALAFWYGSRLVRDGEISPGDVLTVFFAVLIGAFSLGQIAPNLQAFAKARAAAAKI 300
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
841-1257 |
1.77e-81 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 279.54 E-value: 1.77e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 841 ISLIYGWQLTLLLLAIVPI-IAIAGVVEMKMLSGQALKDKKELEGSGKiATEAIENFRTVVSLTR-EQKFETM--YAQSL 916
Cdd:PRK13657 150 LALFMNWRLSLVLVVLGIVyTLITTLVMRKTKDGQAAVEEHYHDLFAH-VSDAIGNVSVVQSYNRiEAETQALrdIADNL 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 917 ---QIPYRN--ALkkahVFGIT-FSFTQAMMyfsyaACFRFGAYLVARELMTfenVLLVFSAIVFGAMAVG---QVSSFA 987
Cdd:PRK13657 229 laaQMPVLSwwAL----ASVLNrAASTITML-----AILVLGAALVQKGQLR---VGEVVAFVGFATLLIGrldQVVAFI 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 988 PDYAKAKVSASHIIRIIEKIPEIDSysTEGLK-PNMLEGNVKFNGVMFNYPTRPniPVLQGLSLEVKKGQTLALVGSSGC 1066
Cdd:PRK13657 297 NQVFMAAPKLEEFFEVEDAVPDVRD--PPGAIdLGRVKGAVEFDDVSFSYDNSR--QGVEDVSFEAKPGQTVAIVGPTGA 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1067 GKSTVVQLLERFYDPMAGTVFLDGKEIKQLNVQWLRAHLGIVSQEPILFDCSIAENIAYGDNSrvVSHEEIVKAAKEANI 1146
Cdd:PRK13657 373 GKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRPD--ATDEEMRAAAERAQA 450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1147 HQFIDSLPEKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRL 1226
Cdd:PRK13657 451 HDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRL 530
|
410 420 430
....*....|....*....|....*....|.
gi 25453402 1227 STIQNADLIVVIQNGQVKEHGTHQQLLAQKG 1257
Cdd:PRK13657 531 STVRNADRILVFDNGRVVESGSFDELVARGG 561
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
384-596 |
8.04e-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: 262.32 E-value: 8.04e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 384 LEFKNIHFSYPSRkDVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRTINVRYLREIIG 463
Cdd:cd03228 1 IEFKNVSFSYPGR-PKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 464 VVSQEPVLFATTIAENIrygrenvtmdeiekavkeanaydfimklphkfdtlvgergaqLSGGQKQRIAIARALVRNPKI 543
Cdd:cd03228 80 YVPQDPFLFSGTIRENI------------------------------------------LSGGQRQRIAIARALLRDPPI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 25453402 544 LLLDEATSALDTESEAVVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFDGG 596
Cdd:cd03228 118 LILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDG 170
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
1027-1266 |
3.04e-79 |
|
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: 260.50 E-value: 3.04e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1027 VKFNGVMFNYptRPNIP-VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIKQLNVQWLRAHL 1105
Cdd:cd03252 1 ITFEHVRFRY--KPDGPvILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1106 GIVSQEPILFDCSIAENIAYGDNSrvVSHEEIVKAAKEANIHQFIDSLPEKYNTRVGDKGTQLSGGQKQRIAIARALVRQ 1185
Cdd:cd03252 79 GVVLQENVLFNRSIRDNIALADPG--MSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1186 PHILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIQNGQVKEHGTHQQLLAQKGIYFSMVSV 1265
Cdd:cd03252 157 PRILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQL 236
|
.
gi 25453402 1266 Q 1266
Cdd:cd03252 237 Q 237
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
686-1259 |
3.76e-78 |
|
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: 273.36 E-value: 3.76e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 686 PASFWRILK--LNSTE--WPYFVVGVFCAIINGGLQPAFSIIFSkvvgvftknDTPEIQRQNSNLFSLLflilgIISFIT 761
Cdd:TIGR03796 138 KPSLLRALWrrLRGSRgaLLYLLLAGLLLVLPGLVIPAFSQIFV---------DEILVQGRQDWLRPLL-----LGMGLT 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 762 FFLQGFtfgkageiLTK-RLRYMV--------------FKSMLRQDISWFDdpKNTTGALTTRLANdAAQVKGATGSRLA 826
Cdd:TIGR03796 204 ALLQGV--------LTWlQLYYLRrleiklavgmsarfLWHILRLPVRFFA--QRHAGDIASRVQL-NDQVAEFLSGQLA 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 827 VITQNIANLGTGIIISLIYGWQLTLLLLAIVPIIAIAGVVEMKMLSGQALKDKKELEGSGKIATEAIENFRTVVSLTREQ 906
Cdd:TIGR03796 273 TTALDAVMLVFYALLMLLYDPVLTLIGIAFAAINVLALQLVSRRRVDANRRLQQDAGKLTGVAISGLQSIETLKASGLES 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 907 ----KFETMYAQSLqipyrNALKKAHVFGITFS-FTQAMMYFSYAACFRFGAYLVARELMT------FENVLLVFSAIVF 975
Cdd:TIGR03796 353 dffsRWAGYQAKLL-----NAQQELGVLTQILGvLPTLLTSLNSALILVVGGLRVMEGQLTigmlvaFQSLMSSFLEPVN 427
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 976 GAMAVGQ-VSSFAPDYAKAKVSASHIIRIIEKIPEIDSYSTEglKPNMLEGNVKFNGVMFNYpTRPNIPVLQGLSLEVKK 1054
Cdd:TIGR03796 428 NLVGFGGtLQELEGDLNRLDDVLRNPVDPLLEEPEGSAATSE--PPRRLSGYVELRNITFGY-SPLEPPLIENFSLTLQP 504
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1055 GQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIKQLNVQWLRAHLGIVSQEPILFDCSIAENIAYGDNSrvVSH 1134
Cdd:TIGR03796 505 GQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIPREVLANSVAMVDQDIFLFEGTVRDNLTLWDPT--IPD 582
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1135 EEIVKAAKEANIHQFIDSLPEKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALdkAR 1214
Cdd:TIGR03796 583 ADLVRACKDAAIHDVITSRPGGYDAELAEGGANLSGGQRQRLEIARALVRNPSILILDEATSALDPETEKIIDDNL--RR 660
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 25453402 1215 EGRTCIVIAHRLSTIQNADLIVVIQNGQVKEHGTHQQLLAQKGIY 1259
Cdd:TIGR03796 661 RGCTCIIVAHRLSTIRDCDEIIVLERGKVVQRGTHEELWAVGGAY 705
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
1027-1242 |
4.96e-78 |
|
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: 254.23 E-value: 4.96e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1027 VKFNGVMFNYPTRPNiPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIKQLNVQWLRAHLG 1106
Cdd:cd03228 1 IEFKNVSFSYPGRPK-PVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1107 IVSQEPILFDCSIAENIaygdnsrvvsheeivkaakeanihqfidslpekyntrvgdkgtqLSGGQKQRIAIARALVRQP 1186
Cdd:cd03228 80 YVPQDPFLFSGTIRENI--------------------------------------------LSGGQRQRIAIARALLRDP 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 25453402 1187 HILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIQNGQ 1242
Cdd:cd03228 116 PILILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
187-620 |
9.09e-78 |
|
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: 268.68 E-value: 9.09e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 187 QAMATFFGGFII---GFTRGWKLTLVILaispVLGLSAGIWAKILSSFTdKELQA-----YAKAGAVAEEVLAAIRTVIA 258
Cdd:TIGR01192 136 QHLATFVALFLLiptAFAMDWRLSIVLM----VLGILYILIAKLVMQRT-KNGQAavehhYHNVFKHVSDSISNVSVVHS 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 259 FG---GQKKELERYNNNLEEAK---------RLGIKKaITANISMGAAFLLiyasyalafwyGTSLVISKEYTIGQVLTV 326
Cdd:TIGR01192 211 YNrieAETSALKQFTNNLLSAQypvldwwalASGLNR-MASTISMMCILVI-----------GTVLVIKGELSVGEVIAF 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 327 --FFSVLIGAFSvgQASPNIEAFANARGAAYEVFSIIDNKPSIDSFSKSGHKPdNIQGNLEFKNIHFSYPSRKdvQILKG 404
Cdd:TIGR01192 279 igFANLLIGRLD--QMSGFITQIFEARAKLEDFFDLEDSVFQREEPADAPELP-NVKGAVEFRHITFEFANSS--QGVFD 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 405 LNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRTINVRYLREIIGVVSQEPVLFATTIAENIRYGR 484
Cdd:TIGR01192 354 VSFEAKAGQTVAIVGPTGAGKTTLINLLQRVYDPTVGQILIDGIDINTVTRESLRKSIATVFQDAGLFNRSIRENIRLGR 433
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 485 ENVTMDEIEKAVKEANAYDFIMKLPHKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAA 564
Cdd:TIGR01192 434 EGATDEEVYEAAKAAAAHDFILKRSNGYDTLVGERGNRLSGGERQRLAIARAILKNAPILVLDEATSALDVETEARVKNA 513
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 25453402 565 LDKAREGRTTIVIAHRLSTVRNADVIAGFDGGVIVEQGNHDELMREKGIYFKLVMT 620
Cdd:TIGR01192 514 IDALRKNRTTFIIAHRLSTVRNADLVLFLDQGRLIEKGSFQELIQKDGRFYKLLRR 569
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
971-1268 |
5.01e-75 |
|
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: 263.91 E-value: 5.01e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 971 SAIVFGAMAVGQVSSF--------AP---------DYAKAKVSASHIIRIIEKIPEIDSYSTEGLkPNmLEGNVKFNGVM 1033
Cdd:TIGR01846 385 HLVIGGALSPGQLVAFnmlagrvtQPvlrlaqlwqDFQQTGIALERLGDILNSPTEPRSAGLAAL-PE-LRGAITFENIR 462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1034 FNYptRPNIP-VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIKQLNVQWLRAHLGIVSQEP 1112
Cdd:TIGR01846 463 FRY--APDSPeVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAWLRRQMGVVLQEN 540
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1113 ILFDCSIAENIAYGDNSrvVSHEEIVKAAKEANIHQFIDSLPEKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLD 1192
Cdd:TIGR01846 541 VLFSRSIRDNIALCNPG--APFEHVIHAAKLAGAHDFISELPQGYNTEVGEKGANLSGGQRQRIAIARALVGNPRILIFD 618
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 25453402 1193 EATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIQNGQVKEHGTHQQLLAQKGIYFSMVSVQAG 1268
Cdd:TIGR01846 619 EATSALDYESEALIMRNMREICRGRTVIIIAHRLSTVRACDRIIVLEKGQIAESGRHEELLALQGLYARLWQQQSG 694
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
661-1266 |
2.47e-74 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 272.29 E-value: 2.47e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 661 RKSIRGPHDQD---GELSTKEALDDDVPPASFWRIL-KLNSTEWPYFV--------------VGVFCAIINGGLQPAFSI 722
Cdd:PTZ00265 2 KKDQRQKKDNNsggGNLSIKDEVEKELNKKGTFELYkKIKTQKIPFFLpfkclpashrkllgVSFVCATISGGTLPFFVS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 723 IFskvvGVFTKNDTPEiQRQNSNLFSLLflILGIISFITFFLQGFTFGKAGEILTKRLRYMVFKSMLRQDISWFDDpkNT 802
Cdd:PTZ00265 82 VF----GVIMKNMNLG-ENVNDIIFSLV--LIGIFQFILSFISSFCMDVVTTKILKTLKLEFLKSVFYQDGQFHDN--NP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 803 TGALTTRLANDAAQVKGATGSR-LAVITQNIANLGTgIIISLIYGWQLTLLLLAIVPIIAIAGVVEMKMLSgqaLKDKKE 881
Cdd:PTZ00265 153 GSKLTSDLDFYLEQVNAGIGTKfITIFTYASAFLGL-YIWSLFKNARLTLCITCVFPLIYICGVICNKKVK---INKKTS 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 882 L---EGSGKIATEAIENFRTVVSLTREQKFETMYAQSLQIPYRNALKKAHVFGITFSFTQAMMYFSYAACFRFGAYLVAR 958
Cdd:PTZ00265 229 LlynNNTMSIIEEALVGIRTVVSYCGEKTILKKFNLSEKLYSKYILKANFMESLHIGMINGFILASYAFGFWYGTRIIIS 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 959 ELMTFE--------NVLLVFSAIVFGAMAVGQVSSFAPDYAKAKVSASHIIRIIEKIPEIDSYSTEGLKPNMLEgnVKFN 1030
Cdd:PTZ00265 309 DLSNQQpnndfhggSVISILLGVLISMFMLTIILPNITEYMKSLEATNSLYEIINRKPLVENNDDGKKLKDIKK--IQFK 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1031 GVMFNYPTRPNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFL-DGKEIKQLNVQWLRAHLGIVS 1109
Cdd:PTZ00265 387 NVRFHYDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRSKIGVVS 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1110 QEPILFDCSIAENIAY------------------------GDNSR-------------------------------VVSH 1134
Cdd:PTZ00265 467 QDPLLFSNSIKNNIKYslyslkdlealsnyynedgndsqeNKNKRnscrakcagdlndmsnttdsneliemrknyqTIKD 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1135 EEIVKAAKEANIHQFIDSLPEKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALD--K 1212
Cdd:PTZ00265 547 SEVVDVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINnlK 626
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1213 AREGRTCIVIAHRLSTIQNADLIVVIQNGQ-----------------------------------------------VKE 1245
Cdd:PTZ00265 627 GNENRITIIIAHRLSTIRYANTIFVLSNRErgstvdvdiigedptkdnkennnknnkddnnnnnnnnnnkinnagsyIIE 706
|
730 740
....*....|....*....|..
gi 25453402 1246 HGTHQQLLAQK-GIYFSMVSVQ 1266
Cdd:PTZ00265 707 QGTHDALMKNKnGIYYTMINNQ 728
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
802-1266 |
4.32e-73 |
|
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: 257.96 E-value: 4.32e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 802 TTGALTTRlANDAAQVKgatgSRLAVITQNIANLGTGIIISL----IYGWQLTL--LLLAIVpIIAIAGVVEMKMLSgqa 875
Cdd:TIGR03797 231 STGDLASR-AMGISQIR----RILSGSTLTTLLSGIFALLNLglmfYYSWKLALvaVALALV-AIAVTLVLGLLQVR--- 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 876 lKDKKELEGSGKIATEAIENFRTVVSLtR----EQKFETMYAQ--SLQIpyRNALKKAHVFGITFSFTQAMMYFSYAACF 949
Cdd:TIGR03797 302 -KERRLLELSGKISGLTVQLINGISKL-RvagaENRAFARWAKlfSRQR--KLELSAQRIENLLTVFNAVLPVLTSAALF 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 950 RFGAYLVARELMTFENVLLVFSAIVFGAMAVGQVS-------SFAPDYAKAKvsashiiRIIEKIPEIDSYSTEglkPNM 1022
Cdd:TIGR03797 378 AAAISLLGGAGLSLGSFLAFNTAFGSFSGAVTQLSntlisilAVIPLWERAK-------PILEALPEVDEAKTD---PGK 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1023 LEGNVKFNGVMFNYptRPNIP-VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIKQLNVQWL 1101
Cdd:TIGR03797 448 LSGAIEVDRVTFRY--RPDGPlILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLDVQAV 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1102 RAHLGIVSQEPILFDCSIAENIAYGDnsrVVSHEEIVKAAKEANIHQFIDSLPEKYNTRVGDKGTQLSGGQKQRIAIARA 1181
Cdd:TIGR03797 526 RRQLGVVLQNGRLMSGSIFENIAGGA---PLTLDEAWEAARMAGLAEDIRAMPMGMHTVISEGGGTLSGGQRQRLLIARA 602
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1182 LVRQPHILLLDEATSALDTESEKVVQEALDKAREGRtcIVIAHRLSTIQNADLIVVIQNGQVKEHGTHQQLLAQKGIYFS 1261
Cdd:TIGR03797 603 LVRKPRILLFDEATSALDNRTQAIVSESLERLKVTR--IVIAHRLSTIRNADRIYVLDAGRVVQQGTYDELMAREGLFAQ 680
|
....*
gi 25453402 1262 MVSVQ 1266
Cdd:TIGR03797 681 LARRQ 685
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
703-978 |
2.61e-72 |
|
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: 242.55 E-value: 2.61e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 703 FVVGVFCAIINGGLQPAFSIIFSKVVGVFTKNDTPEiqRQNSNLFSLLFLILGIISFITFFLQGFTFGKAGEILTKRLRY 782
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLPDGDPE--TQALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 783 MVFKSMLRQDISWFDdpKNTTGALTTRLANDAAQVKGATGSRLAVITQNIANLGTGIIISLIYGWQLTLLLLAIVPIIAI 862
Cdd:pfam00664 79 KLFKKILRQPMSFFD--TNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYIL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 863 AGVVEMKMLSGQALKDKKELEGSGKIATEAIENFRTVVSLTREQKFETMYAQSLQIPYRNALKKAHVFGITFSFTQAMMY 942
Cdd:pfam00664 157 VSAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGY 236
|
250 260 270
....*....|....*....|....*....|....*...
gi 25453402 943 FSYAACFRFGAYLVARELMTFEN--VLLVFSAIVFGAM 978
Cdd:pfam00664 237 LSYALALWFGAYLVISGELSVGDlvAFLSLFAQLFGPL 274
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
387-1262 |
1.55e-69 |
|
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: 257.18 E-value: 1.55e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 387 KNIHFSYpSRKDVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGqdirtiNVRYlreiigvVS 466
Cdd:TIGR00957 640 HNATFTW-ARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG------SVAY-------VP 705
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 467 QEPVLFATTIAENIRYGREnvTMDEIEKAVKEANAY--DFIMkLPHKFDTLVGERGAQLSGGQKQRIAIARALVRNPKIL 544
Cdd:TIGR00957 706 QQAWIQNDSLRENILFGKA--LNEKYYQQVLEACALlpDLEI-LPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIY 782
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 545 LLDEATSALDTEseaVVQAALDKA------REGRTTIVIAHRLSTVRNADVIAGFDGGVIVEQGNHDELMREKGIYFKLV 618
Cdd:TIGR00957 783 LFDDPLSAVDAH---VGKHIFEHVigpegvLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAFAEFL 859
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 619 MTQtAGNEIELGNE----ACESKDG-----IDNVDMSSKDSGSSLIRRRSTRKSIRGphDQDGELSTKEALDDDVPPASF 689
Cdd:TIGR00957 860 RTY-APDEQQGHLEdswtALVSGEGkeaklIENGMLVTDVVGKQLQRQLSASSSDSG--DQSRHHGSSAELQKAEAKEET 936
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 690 WRILKLN---------STEWPYF-VVGVFCAIINGGL---QPAFSIIFSKVVGVFTKNDTPEIQRQNSNLFSLLFLILGI 756
Cdd:TIGR00957 937 WKLMEADkaqtgqvelSVYWDYMkAIGLFITFLSIFLfvcNHVSALASNYWLSLWTDDPMVNGTQNNTSLRLSVYGALGI 1016
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 757 ISFITFFLQGFTFGKAGEILTKRLRYMVFKSMLRQDISWFDdpKNTTGALTTRLANDAAQVKGATGSRLAVITQNIAN-L 835
Cdd:TIGR00957 1017 LQGFAVFGYSMAVSIGGIQASRVLHQDLLHNKLRSPMSFFE--RTPSGNLVNRFSKELDTVDSMIPPVIKMFMGSLFNvI 1094
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 836 GTGIIISLIygwqlTLLLLAIVPIIAIAGVVEMKMLSGQAlKDKKELEgsgkiateaienfrtvvSLTREQKF----ETM 911
Cdd:TIGR00957 1095 GALIVILLA-----TPIAAVIIPPLGLLYFFVQRFYVASS-RQLKRLE-----------------SVSRSPVYshfnETL 1151
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 912 YAQSLQIPYRNALKKAHVFGITFSFTQAMMYFSYAAcfrfGAYLVAReLMTFENVLLVFSAIvfgaMAVGQVSSFAPDYA 991
Cdd:TIGR00957 1152 LGVSVIRAFEEQERFIHQSDLKVDENQKAYYPSIVA----NRWLAVR-LECVGNCIVLFAAL----FAVISRHSLSAGLV 1222
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 992 KAKVSAS--------HIIRI-------IEKIPEIDSYS-TEGLKPNMLE-----------GNVKFNGVMFNYptRPNIP- 1043
Cdd:TIGR00957 1223 GLSVSYSlqvtfylnWLVRMssemetnIVAVERLKEYSeTEKEAPWQIQetappsgwpprGRVEFRNYCLRY--REDLDl 1300
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1044 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIKQLNVQWLRAHLGIVSQEPILFDCSIAENI 1123
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNL 1380
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1124 aygDNSRVVSHEEIVKAAKEANIHQFIDSLPEKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESE 1203
Cdd:TIGR00957 1381 ---DPFSQYSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETD 1457
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|....*....
gi 25453402 1204 KVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIQNGQVKEHGTHQQLLAQKGIYFSM 1262
Cdd:TIGR00957 1458 NLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRGIFYSM 1516
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
382-602 |
1.01e-68 |
|
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: 230.17 E-value: 1.01e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 382 GNLEFKNIHFSYPSRKdVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRTINVRYLREI 461
Cdd:cd03245 1 GRIEFRNVSFSYPNQE-IPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 462 IGVVSQEPVLFATTIAENIRYGRENVTMDEIEKAVKEANAYDFIMKLPHKFDTLVGERGAQLSGGQKQRIAIARALVRNP 541
Cdd:cd03245 80 IGYVPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 25453402 542 KILLLDEATSALDTESEAVVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFDGGVIVEQG 602
Cdd:cd03245 160 PILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
153-621 |
3.51e-68 |
|
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: 243.71 E-value: 3.51e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 153 GWFDVHDVGELNTRlTDDVSKINEGIGDKigMFFQAMATFFGGFIIG--FTRGWKLTLVILAISPVLGLSAGIWAKILss 230
Cdd:TIGR03797 225 SFFRQYSTGDLASR-AMGISQIRRILSGS--TLTTLLSGIFALLNLGlmFYYSWKLALVAVALALVAIAVTLVLGLLQ-- 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 231 fTDKELQAYAKAGAVAEEVLAAIRTVIAF---GGQKKELERYNNNLEEAKRLGIKKAITANI--SMGAAFLLIyASYALa 305
Cdd:TIGR03797 300 -VRKERRLLELSGKISGLTVQLINGISKLrvaGAENRAFARWAKLFSRQRKLELSAQRIENLltVFNAVLPVL-TSAAL- 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 306 FWYGTSLVISKEYTIGQVLTvfFSVLIGAFSVGqaspnIEAFANARGAAYEVF-------SIIDNKPSIDSfskSGHKPD 378
Cdd:TIGR03797 377 FAAAISLLGGAGLSLGSFLA--FNTAFGSFSGA-----VTQLSNTLISILAVIplwerakPILEALPEVDE---AKTDPG 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 379 NIQGNLEFKNIHFSYpsRKD-VQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRTINVRY 457
Cdd:TIGR03797 447 KLSGAIEVDRVTFRY--RPDgPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLDVQA 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 458 LREIIGVVSQEPVLFATTIAENIrYGRENVTMDEIEKAVKEANAYDFIMKLPHKFDTLVGERGAQLSGGQKQRIAIARAL 537
Cdd:TIGR03797 525 VRRQLGVVLQNGRLMSGSIFENI-AGGAPLTLDEAWEAARMAGLAEDIRAMPMGMHTVISEGGGTLSGGQRQRLLIARAL 603
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 538 VRNPKILLLDEATSALDTESEAVVQAALDKAREGRttIVIAHRLSTVRNADVIAGFDGGVIVEQGNHDELMREKGIYFKL 617
Cdd:TIGR03797 604 VRKPRILLFDEATSALDNRTQAIVSESLERLKVTR--IVIAHRLSTIRNADRIYVLDAGRVVQQGTYDELMAREGLFAQL 681
|
....
gi 25453402 618 VMTQ 621
Cdd:TIGR03797 682 ARRQ 685
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
1025-1243 |
3.66e-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: 225.55 E-value: 3.66e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1025 GNVKFNGVMFNYPTRPnIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIKQLNVQWLRAH 1104
Cdd:cd03245 1 GRIEFRNVSFSYPNQE-IPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1105 LGIVSQEPILFDCSIAENIAYGDnsRVVSHEEIVKAAKEANIHQFIDSLPEKYNTRVGDKGTQLSGGQKQRIAIARALVR 1184
Cdd:cd03245 80 IGYVPQDVTLFYGTLRDNITLGA--PLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLN 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 25453402 1185 QPHILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIQNGQV 1243
Cdd:cd03245 158 DPPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
382-603 |
6.64e-67 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 225.07 E-value: 6.64e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 382 GNLEFKNIHFSYPSRKDVqILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRTINVRYLREI 461
Cdd:cd03244 1 GDIEFKNVSLRYRPNLPP-VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 462 IGVVSQEPVLFATTIAENI----RYgrenvTMDEIEKAVKEANAYDFIMKLPHKFDTLVGERGAQLSGGQKQRIAIARAL 537
Cdd:cd03244 80 ISIIPQDPVLFSGTIRSNLdpfgEY-----SDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARAL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 25453402 538 VRNPKILLLDEATSALDTESEAVVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFDGGVIVEQGN 603
Cdd:cd03244 155 LRKSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
1024-1255 |
4.55e-66 |
|
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: 234.26 E-value: 4.55e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1024 EGNVKFNGVMFNYPTRPNiPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIKQLNVQWLRA 1103
Cdd:COG4618 328 KGRLSVENLTVVPPGSKR-PILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGR 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1104 HLGIVSQEPILFDCSIAENIA-YGDnsrvVSHEEIVKAAKEANIHQFIDSLPEKYNTRVGDKGTQLSGGQKQRIAIARAL 1182
Cdd:COG4618 407 HIGYLPQDVELFDGTIAENIArFGD----ADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARAL 482
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 25453402 1183 VRQPHILLLDEATSALDTESEKVVQEALDKARE-GRTCIVIAHRLSTIQNADLIVVIQNGQVKEHGTHQQLLAQ 1255
Cdd:COG4618 483 YGDPRLVVLDEPNSNLDDEGEAALAAAIRALKArGATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
96-618 |
8.06e-66 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 245.32 E-value: 8.06e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 96 YAKLEDEMTTYAYYYTGIGAGVLIVAYIQvSLWCLAAGRQIHK-IRQKFFHAIMNQEIGWFD--VHDVGELNTRLTDDVS 172
Cdd:PTZ00265 858 FANLEANSNKYSLYILVIAIAMFISETLK-NYYNNVIGEKVEKtMKRRLFENILYQEISFFDqdKHAPGLLSAHINRDVH 936
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 173 KINEGIGDKIGMFFQAMATFFGGFIIGF----------TRGWKLTLVILAISPVLGLSAGIWAK-------ILSSFTDKE 235
Cdd:PTZ00265 937 LLKTGLVNNIVIFTHFIVLFLVSMVMSFyfcpivaavlTGTYFIFMRVFAIRARLTANKDVEKKeinqpgtVFAYNSDDE 1016
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 236 LqaYAKAGAVAEEVLAAIRTVIAFGgqkkeLERYNNNLEEA----KRLGIKKAITAN-----ISMGAAFLLiyasYALAF 306
Cdd:PTZ00265 1017 I--FKDPSFLIQEAFYNMNTVIIYG-----LEDYFCNLIEKaidySNKGQKRKTLVNsmlwgFSQSAQLFI----NSFAY 1085
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 307 WYGTSLVISKEYTIGQVLTVFFSVLIGAFSVGQASPNIEAFANARGAAYEVFSIIDNKPSIDSFSKSGHKPDN---IQGN 383
Cdd:PTZ00265 1086 WFGSFLIRRGTILVDDFMKSLFTFLFTGSYAGKLMSLKGDSENAKLSFEKYYPLIIRKSNIDVRDNGGIRIKNkndIKGK 1165
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 384 LEFKNIHFSYPSRKDVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYD-------------------------- 437
Cdd:PTZ00265 1166 IEIMDVNFRYISRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDlkndhhivfknehtndmtneqdyqgd 1245
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 438 ----------------------------PIEGEVSIDGQDIRTINVRYLREIIGVVSQEPVLFATTIAENIRYGRENVTM 489
Cdd:PTZ00265 1246 eeqnvgmknvnefsltkeggsgedstvfKNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKEDATR 1325
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 490 DEIEKAVKEANAYDFIMKLPHKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAAL---- 565
Cdd:PTZ00265 1326 EDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIvdik 1405
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 25453402 566 DKAreGRTTIVIAHRLSTVRNADVIAGFD-----GGVIVEQGNHDELMR-EKGIYFKLV 618
Cdd:PTZ00265 1406 DKA--DKTIITIAHRIASIKRSDKIVVFNnpdrtGSFVQAHGTHEELLSvQDGVYKKYV 1462
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
346-590 |
2.36e-65 |
|
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: 231.41 E-value: 2.36e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 346 AFANARGAAYEVFSIIDNKPSIDSFSKSGHKPDNIQgnLEFKNIHFSYPSRKDVqiLKGLNLKVKSGQTVALVGNSGCGK 425
Cdd:TIGR02857 286 ARADGVAAAEALFAVLDAAPRPLAGKAPVTAAPASS--LEFSGVSVAYPGRRPA--LRPVSFTVPPGERVALVGPSGAGK 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 426 STTVQLLQRLYDPIEGEVSIDGQDIRTINVRYLREIIGVVSQEPVLFATTIAENIRYGRENVTMDEIEKAVKEANAYDFI 505
Cdd:TIGR02857 362 STLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLARPDASDAEIREALERAGLDEFV 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 506 MKLPHKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDKAREGRTTIVIAHRLSTVR 585
Cdd:TIGR02857 442 AALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAA 521
|
....*
gi 25453402 586 NADVI 590
Cdd:TIGR02857 522 LADRI 526
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
127-614 |
8.22e-64 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 228.06 E-value: 8.22e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 127 LWCLAAGRQIH-KIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFFQAMATFFGGFIIGFTR-GW 204
Cdd:PRK10789 58 VLLFGASYQLAvELREDFYRQLSRQHPEFYLRHRTGDLMARATNDVDRVVFAAGEGVLTLVDSLVMGCAVLIVMSTQiSW 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 205 KLTLVILAISPVLGLsagiwakILSSFTDKELQAYAKAGAV-------AEEVLAAIRTVIAFGgqkkeLERYNNNL--EE 275
Cdd:PRK10789 138 QLTLLALLPMPVMAI-------MIKRYGDQLHERFKLAQAAfsslndrTQESLTSIRMIKAFG-----LEDRQSALfaAD 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 276 AKRLGIKKAITANISM---GAAFLLIYASYALAFWYGTSLVISKEYTIGQvLTVFFSVLigafsvGQASPNIEAFA---N 349
Cdd:PRK10789 206 AEDTGKKNMRVARIDArfdPTIYIAIGMANLLAIGGGSWMVVNGSLTLGQ-LTSFVMYL------GLMIWPMLALAwmfN 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 350 --ARG-AAY-EVFSIIDNKPSIdsfsKSGHKP-DNIQGNLEFKNIHFSYPsRKDVQILKGLNLKVKSGQTVALVGNSGCG 424
Cdd:PRK10789 279 ivERGsAAYsRIRAMLAEAPVV----KDGSEPvPEGRGELDVNIRQFTYP-QTDHPALENVNFTLKPGQMLGICGPTGSG 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 425 KSTTVQLLQRLYDPIEGEVSIDGQDIRTINVRYLREIIGVVSQEPVLFATTIAENIRYGRENVTMDEIEKAVKEANAYDF 504
Cdd:PRK10789 354 KSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNIALGRPDATQQEIEHVARLASVHDD 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 505 IMKLPHKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDKAREGRTTIVIAHRLSTV 584
Cdd:PRK10789 434 ILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSAL 513
|
490 500 510
....*....|....*....|....*....|
gi 25453402 585 RNADVIAGFDGGVIVEQGNHDELMREKGIY 614
Cdd:PRK10789 514 TEASEILVMQHGHIAQRGNHDQLAQQSGWY 543
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
384-1263 |
1.71e-63 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 237.95 E-value: 1.71e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 384 LEFKNIHFSYPSRKDVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEgEVSIDgqdirtinvryLREIIG 463
Cdd:PLN03232 615 ISIKNGYFSWDSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAE-TSSVV-----------IRGSVA 682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 464 VVSQEPVLFATTIAENIRYGRENvtmdEIEKAVKeanAYDfIMKLPHKFD-------TLVGERGAQLSGGQKQRIAIARA 536
Cdd:PLN03232 683 YVPQVSWIFNATVRENILFGSDF----ESERYWR---AID-VTALQHDLDllpgrdlTEIGERGVNISGGQKQRVSMARA 754
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 537 LVRNPKILLLDEATSALDTE-SEAVVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFDGGVIVEQGNHDELMREkGIYF 615
Cdd:PLN03232 755 VYSNSDIYIFDDPLSALDAHvAHQVFDSCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELSKS-GSLF 833
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 616 KLVMtQTAGnEIELGNEACESKDGIDN------VDMSSKDSGSSLIRRRSTRKSIRGPHDQDGELStkealdddvppasf 689
Cdd:PLN03232 834 KKLM-ENAG-KMDATQEVNTNDENILKlgptvtIDVSERNLGSTKQGKRGRSVLVKQEERETGIIS-------------- 897
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 690 WRIL-KLNSTEWPYFVVGVF--CAIinggLQPAFSIIFSKVVGVFTKNDTPEIQRqnSNLFSLLFLILGIISFITFFLQG 766
Cdd:PLN03232 898 WNVLmRYNKAVGGLWVVMILlvCYL----TTEVLRVSSSTWLSIWTDQSTPKSYS--PGFYIVVYALLGFGQVAVTFTNS 971
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 767 FTFGKAGEILTKRLRYMVFKSMLRQDISWFDdpKNTTGALTTRLANDAAQvkgatgsrlavITQNIANLGTGIIISLiyg 846
Cdd:PLN03232 972 FWLISSSLHAAKRLHDAMLNSILRAPMLFFH--TNPTGRVINRFSKDIGD-----------IDRNVANLMNMFMNQL--- 1035
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 847 WQL--TLLLLAIVPIIAIAGVVEMKMLSGQAL-------KDKKELEGSGKIAT-----EAIENFRTVVSLTREQKFETMY 912
Cdd:PLN03232 1036 WQLlsTFALIGTVSTISLWAIMPLLILFYAAYlyyqstsREVRRLDSVTRSPIyaqfgEALNGLSSIRAYKAYDRMAKIN 1115
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 913 AQSLQIPYRNALKKAHVFG---ITFSFTQAMMYFSYA--ACFRFGAYLVARELMTFENVLLVFSAIVfgamaVGQVSSFA 987
Cdd:PLN03232 1116 GKSMDNNIRFTLANTSSNRwltIRLETLGGVMIWLTAtfAVLRNGNAENQAGFASTMGLLLSYTLNI-----TTLLSGVL 1190
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 988 PDYAKAKVSASHIIRIIEKIpEIDSYSTEGLKPNM------LEGNVKFNGVMFNYptRPNIP-VLQGLSLEVKKGQTLAL 1060
Cdd:PLN03232 1191 RQASKAENSLNSVERVGNYI-DLPSEATAIIENNRpvsgwpSRGSIKFEDVHLRY--RPGLPpVLHGLSFFVSPSEKVGV 1267
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1061 VGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIKQLNVQWLRAHLGIVSQEPILFDCSIAENIaygDNSRVVSHEEIVKA 1140
Cdd:PLN03232 1268 VGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNI---DPFSEHNDADLWEA 1344
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1141 AKEANIHQFIDSLPEKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKAREGRTCI 1220
Cdd:PLN03232 1345 LERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTML 1424
|
890 900 910 920
....*....|....*....|....*....|....*....|....
gi 25453402 1221 VIAHRLSTIQNADLIVVIQNGQVKEHGTHQQLLAQKG-IYFSMV 1263
Cdd:PLN03232 1425 VIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTsAFFRMV 1468
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
1025-1248 |
3.26e-62 |
|
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: 211.58 E-value: 3.26e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1025 GNVKFNGVMFNYptRPNI-PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIKQLNVQWLRA 1103
Cdd:cd03244 1 GDIEFKNVSLRY--RPNLpPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1104 HLGIVSQEPILFDCSIAENIaygDNSRVVSHEEIVKAAKEANIHQFIDSLPEKYNTRVGDKGTQLSGGQKQRIAIARALV 1183
Cdd:cd03244 79 RISIIPQDPVLFSGTIRSNL---DPFGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 25453402 1184 RQPHILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIQNGQVKEHGT 1248
Cdd:cd03244 156 RKSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
751-1266 |
4.29e-62 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 223.44 E-value: 4.29e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 751 FLILGIISFITFFLQGFTFGKAGEILTKRLRYMVFKSMLRQDISWFDdpKNTTGALTTRLANDAAQVKGATGSRLAVITQ 830
Cdd:PRK10790 71 YVGLQLLAAGLHYAQSLLFNRAAVGVVQQLRTDVMDAALRQPLSAFD--TQPVGQLISRVTNDTEVIRDLYVTVVATVLR 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 831 NIANLGTGIIISLIYGWQLTLLLLAIVPIIAIAGVVEMKMLSGQALKDKKELEGSGKIATEAIeNFRTVVSLTREQ-KF- 908
Cdd:PRK10790 149 SAALIGAMLVAMFSLDWRMALVAIMIFPAVLVVMVIYQRYSTPIVRRVRAYLADINDGFNEVI-NGMSVIQQFRQQaRFg 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 909 ETMYAQSlqipyrnalkKAHvfgitfsftqammYFSYAACFRFGAYLVaRELMTFenvllvFSAIVF------------G 976
Cdd:PRK10790 228 ERMGEAS----------RSH-------------YMARMQTLRLDGFLL-RPLLSL------FSALILcgllmlfgfsasG 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 977 AMAVGQVSSFApDY------------------AKAKVSASHIIRIIEKIPEidSYSTEGlKPnMLEGNVKFNGVMFNYpt 1038
Cdd:PRK10790 278 TIEVGVLYAFI-SYlgrlneplielttqqsmlQQAVVAGERVFELMDGPRQ--QYGNDD-RP-LQSGRIDIDNVSFAY-- 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1039 RPNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIKQLNVQWLRAHLGIVSQEPILFDCS 1118
Cdd:PRK10790 351 RDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADT 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1119 IAENIAYGdnsRVVSHEEIVKAAKEANIHQFIDSLPEKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSAL 1198
Cdd:PRK10790 431 FLANVTLG---RDISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANI 507
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 25453402 1199 DTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIQNGQVKEHGTHQQLLAQKGIYFSMVSVQ 1266
Cdd:PRK10790 508 DSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQGRYWQMYQLQ 575
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
119-618 |
1.33e-61 |
|
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: 225.00 E-value: 1.33e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 119 IVAYIQVSLWCLAAGRQIHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDdVSKINEGIGDKIGMFFQAMATFFG-GFI 197
Cdd:TIGR01193 211 ILSYIQIFLLNVLGQRLSIDIILSYIKHLFELPMSFFSTRRTGEIVSRFTD-ASSIIDALASTILSLFLDMWILVIvGLF 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 198 IGFtRGWKLTLVILAISPVLGLSAGIWAKILSSFTDKELQAYAKAGAVAEEVLAAIRTVIAFGGQ----KKELERYNNNL 273
Cdd:TIGR01193 290 LVR-QNMLLFLLSLLSIPVYAVIIILFKRTFNKLNHDAMQANAVLNSSIIEDLNGIETIKSLTSEaerySKIDSEFGDYL 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 274 EEAKRLGIKKAITANISMGAAFLLIyasyALAFWYGTSLVISKEYTIGQVLTvfFSVLIGAF-----SVGQASPNIEA-- 346
Cdd:TIGR01193 369 NKSFKYQKADQGQQAIKAVTKLILN----VVILWTGAYLVMRGKLTLGQLIT--FNALLSYFltpleNIINLQPKLQAar 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 347 FANAR-GAAYEVFSIIDNKPSIDSFSksghkpdNIQGNLEFKNIHFSYPSRKDvqILKGLNLKVKSGQTVALVGNSGCGK 425
Cdd:TIGR01193 443 VANNRlNEVYLVDSEFINKKKRTELN-------NLNGDIVINDVSYSYGYGSN--ILSDISLTIKMNSKTTIVGMSGSGK 513
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 426 STTVQLLQRLYDPIEGEVSIDGQDIRTINVRYLREIIGVVSQEPVLFATTIAENIRYG-RENVTMDEIEKAVKEANAYDF 504
Cdd:TIGR01193 514 STLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLGaKENVSQDEIWAACEIAEIKDD 593
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 505 IMKLPHKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDKAREgRTTIVIAHRLSTV 584
Cdd:TIGR01193 594 IENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQD-KTIIFVAHRLSVA 672
|
490 500 510
....*....|....*....|....*....|....
gi 25453402 585 RNADVIAGFDGGVIVEQGNHDELMREKGIYFKLV 618
Cdd:TIGR01193 673 KQSDKIIVLDHGKIIEQGSHDELLDRNGFYASLI 706
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
982-1238 |
5.29e-61 |
|
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: 218.70 E-value: 5.29e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 982 QVSSFAPDYAKAKVSASHIIRIIEKIPEIDSYSTEGLKPNMLEgnVKFNGVMFNYPTRPniPVLQGLSLEVKKGQTLALV 1061
Cdd:TIGR02857 279 QLGAQYHARADGVAAAEALFAVLDAAPRPLAGKAPVTAAPASS--LEFSGVSVAYPGRR--PALRPVSFTVPPGERVALV 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1062 GSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIKQLNVQWLRAHLGIVSQEPILFDCSIAENIAYGDnsRVVSHEEIVKAA 1141
Cdd:TIGR02857 355 GPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLAR--PDASDAEIREAL 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1142 KEANIHQFIDSLPEKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKAREGRTCIV 1221
Cdd:TIGR02857 433 ERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLL 512
|
250
....*....|....*..
gi 25453402 1222 IAHRLSTIQNADLIVVI 1238
Cdd:TIGR02857 513 VTHRLALAALADRIVVL 529
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
381-610 |
1.13e-60 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 218.46 E-value: 1.13e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 381 QGNLEFKNIHFSYPSRKDVqILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRTINVRYLRE 460
Cdd:COG4618 328 KGRLSVENLTVVPPGSKRP-ILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGR 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 461 IIGVVSQEPVLFATTIAENI-RYGreNVTMDEIEKAVKEANAYDFIMKLPHKFDTLVGERGAQLSGGQKQRIAIARALVR 539
Cdd:COG4618 407 HIGYLPQDVELFDGTIAENIaRFG--DADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYG 484
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 25453402 540 NPKILLLDEATSALDTESEAVVQAALDKARE-GRTTIVIAHRLSTVRNADVIAGFDGGVIVEQGNHDELMRE 610
Cdd:COG4618 485 DPRLVVLDEPNSNLDDEGEAALAAAIRALKArGATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
973-1262 |
2.51e-60 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 217.77 E-value: 2.51e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 973 IVFGAMA--------------VGQVSSfapdyakakvSASHIIRIIEKIPEIDSYSTEGLKPNmlEGNVKFNGVMFNYPT 1038
Cdd:PRK11160 283 FVFAALAafealmpvagafqhLGQVIA----------SARRINEITEQKPEVTFPTTSTAAAD--QVSLTLNNVSFTYPD 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1039 RPNiPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIKQLNVQWLRAHLGIVSQEPILFDCS 1118
Cdd:PRK11160 351 QPQ-PVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSAT 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1119 IAENIAYgdnsrvvsheeivkAAKEANIHQFIDSL-----------PEKYNTRVGDKGTQLSGGQKQRIAIARALVRQPH 1187
Cdd:PRK11160 430 LRDNLLL--------------AAPNASDEALIEVLqqvgleklledDKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAP 495
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 25453402 1188 ILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIQNGQVKEHGTHQQLLAQKGIYFSM 1262
Cdd:PRK11160 496 LLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQGRYYQL 570
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
803-1266 |
3.00e-60 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 217.66 E-value: 3.00e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 803 TGALTTRLANDAAQVKGATGSR-LAVITQNIANLGTGIIISLIYGWQLTLLLLAIVPIIAIA-----GVVEMKMLSGQA- 875
Cdd:PRK10789 92 TGDLMARATNDVDRVVFAAGEGvLTLVDSLVMGCAVLIVMSTQISWQLTLLALLPMPVMAIMikrygDQLHERFKLAQAa 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 876 ---LKDKkelegsgkiATEAIENFRTVVSLTREQKFETMYAQslqIPYRNALKKAHVFGITFSFTQAMmyfsYAAcfrfg 952
Cdd:PRK10789 172 fssLNDR---------TQESLTSIRMIKAFGLEDRQSALFAA---DAEDTGKKNMRVARIDARFDPTI----YIA----- 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 953 aylvarelMTFENVLLVFSA---IVFGAMAVGQVSSFA--------PDYAKA-------KVSA--SHIIRIIEKIPEIDs 1012
Cdd:PRK10789 231 --------IGMANLLAIGGGswmVVNGSLTLGQLTSFVmylglmiwPMLALAwmfniveRGSAaySRIRAMLAEAPVVK- 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1013 ystEGLKPNMLE-GNVKFNGVMFNYPTRPNiPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGK 1091
Cdd:PRK10789 302 ---DGSEPVPEGrGELDVNIRQFTYPQTDH-PALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDI 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1092 EIKQLNVQWLRAHLGIVSQEPILFDCSIAENIAYGDNSrvVSHEEIVKAAKEANIHQFIDSLPEKYNTRVGDKGTQLSGG 1171
Cdd:PRK10789 378 PLTKLQLDSWRSRLAVVSQTPFLFSDTVANNIALGRPD--ATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGG 455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1172 QKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIQNGQVKEHGTHQQ 1251
Cdd:PRK10789 456 QKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQ 535
|
490
....*....|....*
gi 25453402 1252 LLAQKGIYFSMVSVQ 1266
Cdd:PRK10789 536 LAQQSGWYRDMYRYQ 550
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
353-617 |
4.22e-60 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 217.39 E-value: 4.22e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 353 AAYEVFSIIDNKPSIdSFSKSgHKPDNIQGNLEFKNIHFSYPSRKDvQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLL 432
Cdd:PRK11160 310 SARRINEITEQKPEV-TFPTT-STAAADQVSLTLNNVSFTYPDQPQ-PVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLL 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 433 QRLYDPIEGEVSIDGQDIRTINVRYLREIIGVVSQEPVLFATTIAENIRYGRENVTmDEIEKAVKEANAYDFIMKLPHKF 512
Cdd:PRK11160 387 TRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLLAAPNAS-DEALIEVLQQVGLEKLLEDDKGL 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 513 DTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDKAREGRTTIVIAHRLSTVRNADVIAG 592
Cdd:PRK11160 466 NAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRICV 545
|
250 260
....*....|....*....|....*
gi 25453402 593 FDGGVIVEQGNHDELMREKGIYFKL 617
Cdd:PRK11160 546 MDNGQIIEQGTHQELLAQQGRYYQL 570
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
210-581 |
1.77e-57 |
|
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: 208.37 E-value: 1.77e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 210 ILAISPVLGLSAGIWAKILSSFTDKELQAYAKaGAVAEEVLAAIR---TVIAFGGQKKELERYNNNLEEAKRLGIKKAIT 286
Cdd:TIGR02868 158 ILAAGLLLAGFVAPLVSLRAARAAEQALARLR-GELAAQLTDALDgaaELVASGALPAALAQVEEADRELTRAERRAAAA 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 287 ANISMGAAFLLIYASYALAFWYGTSLVISKEYTiGQVLTVFFSVLIGAFSVGQASPN-IEAFANARGAAYEVFSIIDNKP 365
Cdd:TIGR02868 237 TALGAALTLLAAGLAVLGALWAGGPAVADGRLA-PVTLAVLVLLPLAAFEAFAALPAaAQQLTRVRAAAERIVEVLDAAG 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 366 SIDSFSKSGHKPDNIQG-NLEFKNIHFSYPSRKDVqiLKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVS 444
Cdd:TIGR02868 316 PVAEGSAPAAGAVGLGKpTLELRDLSAGYPGAPPV--LDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVT 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 445 IDGQDIRTINVRYLREIIGVVSQEPVLFATTIAENIRYGRENVTMDEIEKAVKEANAYDFIMKLPHKFDTLVGERGAQLS 524
Cdd:TIGR02868 394 LDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPDATDEELWAALERVGLADWLRALPDGLDTVLGEGGARLS 473
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 25453402 525 GGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDKAREGRTTIVIAHRL 581
Cdd:TIGR02868 474 GGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
101-628 |
1.95e-57 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 209.96 E-value: 1.95e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 101 DEMTTYAYYYTGIGAGvLIVAYI------------QVSLWCLAAGRQIHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLT 168
Cdd:PRK10790 51 DNMVAKGNLPLGLVAG-LAAAYVglqllaaglhyaQSLLFNRAAVGVVQQLRTDVMDAALRQPLSAFDTQPVGQLISRVT 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 169 DDVSKINEGIGDKIGMFFQAMATFFGGFIIGFTRGWKLTLVILAISPVLGLSAGIWAKiLSSFTDKELQAY-AKAGAVAE 247
Cdd:PRK10790 130 NDTEVIRDLYVTVVATVLRSAALIGAMLVAMFSLDWRMALVAIMIFPAVLVVMVIYQR-YSTPIVRRVRAYlADINDGFN 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 248 EVLAAIrTVIAfggQKKELERYNNNLEEAKRLGIKKAITA----------NISMGAAFLLIyasyALAFWYGtslvISKE 317
Cdd:PRK10790 209 EVINGM-SVIQ---QFRQQARFGERMGEASRSHYMARMQTlrldgfllrpLLSLFSALILC----GLLMLFG----FSAS 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 318 YTIG-QVLTVFFSVLiGAFSvgqaSPNIE------AFANARGAAYEVFSIIDNkpsidsfSKSGHKPDNI---QGNLEFK 387
Cdd:PRK10790 277 GTIEvGVLYAFISYL-GRLN----EPLIElttqqsMLQQAVVAGERVFELMDG-------PRQQYGNDDRplqSGRIDID 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 388 NIHFSYpsRKDVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRTINVRYLREIIGVVSQ 467
Cdd:PRK10790 345 NVSFAY--RDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQ 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 468 EPVLFATTIAENIRYGReNVTMDEIEKAVKEANAYDFIMKLPHKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLD 547
Cdd:PRK10790 423 DPVVLADTFLANVTLGR-DISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILD 501
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 548 EATSALDTESEAVVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFDGGVIVEQGNHDELMREKGIYFKLVMTQTAGNEI 627
Cdd:PRK10790 502 EATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQGRYWQMYQLQLAGEEL 581
|
.
gi 25453402 628 E 628
Cdd:PRK10790 582 A 582
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
707-1265 |
9.91e-57 |
|
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: 210.37 E-value: 9.91e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 707 VFCAIINGGLQPAFSIIFSKVVGVFTkndtPEIQRQNSNLFSLLFLILGIISFITFFLQGFTFGKAGEILTKRLRYMVFK 786
Cdd:TIGR01193 162 VIAAIIVTLISIAGSYYLQKIIDTYI----PHKMMGTLGIISIGLIIAYIIQQILSYIQIFLLNVLGQRLSIDIILSYIK 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 787 SMLRQDISWFDDPKntTGALTTRLAnDAAQVKGATGSrlaVITQNIANLGTGIIISLIYGWQ---LTLLLLAIVPIIAIA 863
Cdd:TIGR01193 238 HLFELPMSFFSTRR--TGEIVSRFT-DASSIIDALAS---TILSLFLDMWILVIVGLFLVRQnmlLFLLSLLSIPVYAVI 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 864 GVVEMKMLSGQalkDKKELEGSGKIATEAIENF---RTVVSLTREQ--------KFETMYAQSLQIPYRNALKKAHVFGI 932
Cdd:TIGR01193 312 IILFKRTFNKL---NHDAMQANAVLNSSIIEDLngiETIKSLTSEAeryskidsEFGDYLNKSFKYQKADQGQQAIKAVT 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 933 TFSFTQAMMYFsyaacfrfGAYLVARELMTFENvLLVFSAIV-FGAMAVGQVSSFAPDYAKAKVsASHIIRIIEKIPEID 1011
Cdd:TIGR01193 389 KLILNVVILWT--------GAYLVMRGKLTLGQ-LITFNALLsYFLTPLENIINLQPKLQAARV-ANNRLNEVYLVDSEF 458
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1012 SYSTEGLKPNMLEGNVKFNGVMFNYPTrpNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGK 1091
Cdd:TIGR01193 459 INKKKRTELNNLNGDIVINDVSYSYGY--GSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGF 536
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1092 EIKQLNVQWLRAHLGIVSQEPILFDCSIAENIAYGdNSRVVSHEEIVKAAKEANIHQFIDSLPEKYNTRVGDKGTQLSGG 1171
Cdd:TIGR01193 537 SLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLG-AKENVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGG 615
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1172 QKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKAREgRTCIVIAHRLSTIQNADLIVVIQNGQVKEHGTHQQ 1251
Cdd:TIGR01193 616 QKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQD-KTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDE 694
|
570
....*....|....
gi 25453402 1252 LLAQKGIYFSMVSV 1265
Cdd:TIGR01193 695 LLDRNGFYASLIHN 708
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
387-1263 |
2.24e-56 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 215.37 E-value: 2.24e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 387 KNIHFSYPSRKDVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQ-LLQRLYDPIEGEVSIDGqdirtiNVRYlreiigvV 465
Cdd:PLN03130 618 KNGYFSWDSKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISaMLGELPPRSDASVVIRG------TVAY-------V 684
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 466 SQEPVLFATTIAENIRYGREnVTMDEIEKAVKEANAYDFIMKLPHKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILL 545
Cdd:PLN03130 685 PQVSWIFNATVRDNILFGSP-FDPERYERAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYI 763
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 546 LDEATSALDTE-SEAVVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFDGGVIVEQGNHDELMREkGIYFKLVMtQTAG 624
Cdd:PLN03130 764 FDDPLSALDAHvGRQVFDKCIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSNN-GPLFQKLM-ENAG 841
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 625 NEIELGNEACESKDGIDNVDMSSKDSGSSLIRRRSTRKSirgPHDQDGELSTKEALDDDVPPasfWRIL-KLNSTEWPYF 703
Cdd:PLN03130 842 KMEEYVEENGEEEDDQTSSKPVANGNANNLKKDSSSKKK---SKEGKSVLIKQEERETGVVS---WKVLeRYKNALGGAW 915
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 704 VVGV--FCAIinggLQPAFSIIFSKVVGVFTKNDTPEIQRqnSNLFSLLFLILGIISFITFFLQGFTFGKAGEILTKRLR 781
Cdd:PLN03130 916 VVMIlfLCYV----LTEVFRVSSSTWLSEWTDQGTPKTHG--PLFYNLIYALLSFGQVLVTLLNSYWLIMSSLYAAKRLH 989
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 782 YMVFKSMLRQDISWFDdpKNTTGALTTRLANDaaqvkgatgsrLAVITQNIANLGTGIIISLiygWQL--TLLLLAIVPI 859
Cdd:PLN03130 990 DAMLGSILRAPMSFFH--TNPLGRIINRFAKD-----------LGDIDRNVAVFVNMFLGQI---FQLlsTFVLIGIVST 1053
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 860 IAIAGVVEMKML----------SGQALKDKKELEGSGKIAT--EAIENFRTVVSLTREQKFETMYAQSLQIPYRNAL--- 924
Cdd:PLN03130 1054 ISLWAIMPLLVLfygaylyyqsTAREVKRLDSITRSPVYAQfgEALNGLSTIRAYKAYDRMAEINGRSMDNNIRFTLvnm 1133
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 925 KKAHVFGITFSFTQAMMYFsYAACFRFGAYLVARELMTFEN---VLLVFSAIVFGAM-AVGQVSSFAPDYAKAKVSASHI 1000
Cdd:PLN03130 1134 SSNRWLAIRLETLGGLMIW-LTASFAVMQNGRAENQAAFAStmgLLLSYALNITSLLtAVLRLASLAENSLNAVERVGTY 1212
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1001 IRIIEKIPEIdsysTEGLKPNM---LEGNVKFNGVMFNYptRPNIP-VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLE 1076
Cdd:PLN03130 1213 IDLPSEAPLV----IENNRPPPgwpSSGSIKFEDVVLRY--RPELPpVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALF 1286
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1077 RFYDPMAGTVFLDGKEIKQLNVQWLRAHLGIVSQEPILFDCSIAENIaygDNSRVVSHEEIVKAAKEANIHQFIDSLPEK 1156
Cdd:PLN03130 1287 RIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNL---DPFNEHNDADLWESLERAHLKDVIRRNSLG 1363
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1157 YNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKarEGRTC--IVIAHRLSTIQNADL 1234
Cdd:PLN03130 1364 LDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIRE--EFKSCtmLIIAHRLNTIIDCDR 1441
|
890 900 910
....*....|....*....|....*....|
gi 25453402 1235 IVVIQNGQVKEHGTHQQLLAQKGIYFS-MV 1263
Cdd:PLN03130 1442 ILVLDAGRVVEFDTPENLLSNEGSAFSkMV 1471
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
346-614 |
4.77e-55 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 202.77 E-value: 4.77e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 346 AFANARGAAYEVFSIIDnkpSIDSFSKSGHKPDNIQGNLEFKNIHFSYPSRKDVQILKGLNLKVKSGQTVALVGNSGCGK 425
Cdd:PRK11174 313 AKAQAVGAAESLVTFLE---TPLAHPQQGEKELASNDPVTIEAEDLEILSPDGKTLAGPLNFTLPAGQRIALVGPSGAGK 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 426 STTVQLLqrL-YDPIEGEVSIDGQDIRTINVRYLREIIGVVSQEPVLFATTIAENIRYGRENVTMDEIEKAVKEANAYDF 504
Cdd:PRK11174 390 TSLLNAL--LgFLPYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGNPDASDEQLQQALENAWVSEF 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 505 IMKLPHKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDKAREGRTTIVIAHRLSTV 584
Cdd:PRK11174 468 LPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLEDL 547
|
250 260 270
....*....|....*....|....*....|
gi 25453402 585 RNADVIAGFDGGVIVEQGNHDELMREKGIY 614
Cdd:PRK11174 548 AQWDQIWVMQDGQIVQQGDYAELSQAGGLF 577
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
1037-1255 |
2.56e-53 |
|
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: 196.41 E-value: 2.56e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1037 PTRPNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIKQLNVQWLRAHLGIVSQEPILFD 1116
Cdd:TIGR01842 326 PPGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKHIGYLPQDVELFP 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1117 CSIAENIA-YGDNsrvVSHEEIVKAAKEANIHQFIDSLPEKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEAT 1195
Cdd:TIGR01842 406 GTVAENIArFGEN---ADPEKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPN 482
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 25453402 1196 SALDTESEKVVQEALDKAR-EGRTCIVIAHRLSTIQNADLIVVIQNGQVKEHGTHQQLLAQ 1255
Cdd:TIGR01842 483 SNLDEEGEQALANAIKALKaRGITVVVITHRPSLLGCVDKILVLQDGRIARFGERDEVLAK 543
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
384-611 |
4.86e-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: 185.61 E-value: 4.86e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 384 LEFKNIHFSYPsrKDVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRTINVRYLREIIG 463
Cdd:COG1122 1 IELENLSFSYP--GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 464 VVSQEPV--LFATTIAENIRYGREN--VTMDEIEKAVKEA----NAYDFIMKLPHkfdtlvgergaQLSGGQKQRIAIAR 535
Cdd:COG1122 79 LVFQNPDdqLFAPTVEEDVAFGPENlgLPREEIRERVEEAlelvGLEHLADRPPH-----------ELSGGQKQRVAIAG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 25453402 536 ALVRNPKILLLDEATSALDTESEAVVQAALDK-AREGRTTIVIAHRLSTV-RNADVIAGFDGGVIVEQGNHDELMREK 611
Cdd:COG1122 148 VLAMEPEVLVLDEPTAGLDPRGRRELLELLKRlNKEGKTVIIVTHDLDLVaELADRVIVLDDGRIVADGTPREVFSDY 225
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
384-609 |
2.81e-52 |
|
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: 192.81 E-value: 2.81e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 384 LEFKNIHFSYPSRK--DVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRTINVRYLREI 461
Cdd:COG1123 261 LEVRNLSKRYPVRGkgGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 462 ---IGVVSQEPV--LFAT-TIAENIRYGREN---VTMDEIEKAVKEANA-----YDFIMKLPHkfdtlvgergaQLSGGQ 527
Cdd:COG1123 341 rrrVQMVFQDPYssLNPRmTVGDIIAEPLRLhglLSRAERRERVAELLErvglpPDLADRYPH-----------ELSGGQ 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 528 KQRIAIARALVRNPKILLLDEATSALDteseAVVQAA-LD-----KAREGRTTIVIAHRLSTVRN-ADVIAGFDGGVIVE 600
Cdd:COG1123 410 RQRVAIARALALEPKLLILDEPTSALD----VSVQAQiLNllrdlQRELGLTYLFISHDLAVVRYiADRVAVMYDGRIVE 485
|
....*....
gi 25453402 601 QGNHDELMR 609
Cdd:COG1123 486 DGPTEEVFA 494
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1048-1262 |
3.61e-52 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 194.29 E-value: 3.61e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1048 LSLEVKKGQTLALVGSSGCGKSTVVQLLERFYdPMAGTVFLDGKEIKQLNVQWLRAHLGIVSQEPILFDCSIAENIAYGD 1127
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGN 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1128 NSrvVSHEEIVKAAKEANIHQFIDSLPEKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQ 1207
Cdd:PRK11174 448 PD--ASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVM 525
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 25453402 1208 EALDKAREGRTCIVIAHRLSTIQNADLIVVIQNGQVKEHGTHQQLLAQKGIYFSM 1262
Cdd:PRK11174 526 QALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATL 580
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
384-607 |
1.38e-51 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 181.22 E-value: 1.38e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 384 LEFKNIHFSYpsrKDVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYD-----PIEGEVSIDGQDIRTINVR-- 456
Cdd:cd03260 1 IELRDLNVYY---GDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDLDVDvl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 457 YLREIIGVVSQEPVLFATTIAENIRYG------RENVTMDEI-EKAVKEANAYDFIMKLPHkfdtlvgerGAQLSGGQKQ 529
Cdd:cd03260 78 ELRRRVGMVFQKPNPFPGSIYDNVAYGlrlhgiKLKEELDERvEEALRKAALWDEVKDRLH---------ALGLSGGQQQ 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 25453402 530 RIAIARALVRNPKILLLDEATSALDTESEAVVQAALDKAREGRTTIVIAHRLSTV-RNADVIAGFDGGVIVEQGNHDEL 607
Cdd:cd03260 149 RLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAaRVADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
385-596 |
1.49e-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: 180.74 E-value: 1.49e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 385 EFKNIHFSYPSRkDVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRTINVRYLREIIGV 464
Cdd:cd03225 1 ELKNLSFSYPDG-ARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 465 VSQEP--VLFATTIAENIRYGREN--VTMDEIEKAVKEANAydfIMKLPHKFDTLVgergAQLSGGQKQRIAIARALVRN 540
Cdd:cd03225 80 VFQNPddQFFGPTVEEEVAFGLENlgLPEEEIEERVEEALE---LVGLEGLRDRSP----FTLSGGQKQRVAIAGVLAMD 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 25453402 541 PKILLLDEATSALDTESEAVVQAALDK-AREGRTTIVIAHRLSTVRN-ADVIAGFDGG 596
Cdd:cd03225 153 PDILLLDEPTAGLDPAGRRELLELLKKlKAEGKTIIIVTHDLDLLLElADRVIVLEDG 210
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
309-610 |
4.92e-51 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 189.87 E-value: 4.92e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 309 GTSLVISKEYTIGQVLTVffSVLIG-AFS-VGQASPNIEAFANARGAAYEVFSIIDNKPSIDSfsksgHKP-DNIQGNLE 385
Cdd:TIGR01842 246 GAYLAIDGEITPGMMIAG--SILVGrALApIDGAIGGWKQFSGARQAYKRLNELLANYPSRDP-----AMPlPEPEGHLS 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 386 FKNIHFSYPSRKDVqILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRTINVRYLREIIGVV 465
Cdd:TIGR01842 319 VENVTIVPPGGKKP-TLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKHIGYL 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 466 SQEPVLFATTIAENIRYGRENVTMDEIEKAVKEANAYDFIMKLPHKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILL 545
Cdd:TIGR01842 398 PQDVELFPGTVAENIARFGENADPEKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVV 477
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 25453402 546 LDEATSALDTESEAVVQAALDKAR-EGRTTIVIAHRLSTVRNADVIAGFDGGVIVEQGNHDELMRE 610
Cdd:TIGR01842 478 LDEPNSNLDEEGEQALANAIKALKaRGITVVVITHRPSLLGCVDKILVLQDGRIARFGERDEVLAK 543
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
95-357 |
1.09e-48 |
|
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: 175.44 E-value: 1.09e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 95 IYAKLEDEMTTYAYYYTGIGAGVLIVAYIQVSLWCLAAGRQIHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKI 174
Cdd:cd18557 27 IKGGDLDVLNELALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFSSLLRQEIAFFDKHKTGELTSRLSSDTSVL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 175 NEGIGDKIGMFFQAMATFFGGFIIGFTRGWKLTLVILAISPVLGLSAGIWAKILSSFTDKELQAYAKAGAVAEEVLAAIR 254
Cdd:cd18557 107 QSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASKIYGRYIRKLSKEVQDALAKAGQVAEESLSNIR 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 255 TVIAFGGQKKELERYNNNLEEAKRLGIKKAITANISMGAAFLLIYASYALAFWYGTSLVISKEYTIGQVLT-VFFSVLIg 333
Cdd:cd18557 187 TVRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQGITSLLIYLSLLLVLWYGGYLVLSGQLTVGELTSfILYTIMV- 265
|
250 260
....*....|....*....|....
gi 25453402 334 AFSVGQASPNIEAFANARGAAYEV 357
Cdd:cd18557 266 ASSVGGLSSLLADIMKALGASERV 289
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
384-598 |
3.38e-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: 169.32 E-value: 3.38e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 384 LEFKNIHFSYPSRKDVqILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRTINVRYLREIIG 463
Cdd:cd03246 1 LEVENVSFRYPGAEPP-VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 464 VVSQEPVLFATTIAENIrygrenvtmdeiekavkeanaydfimklphkfdtlvgergaqLSGGQKQRIAIARALVRNPKI 543
Cdd:cd03246 80 YLPQDDELFSGSIAENI------------------------------------------LSGGQRQRLGLARALYGNPRI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 25453402 544 LLLDEATSALDTESEAVVQAALDKARE-GRTTIVIAHRLSTVRNADVIAGFDGGVI 598
Cdd:cd03246 118 LVLDEPNSHLDVEGERALNQAIAALKAaGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
402-551 |
4.22e-48 |
|
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: 168.21 E-value: 4.22e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 402 LKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRTINVRYLREIIGVVSQEPVLF-ATTIAENI 480
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFpRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 25453402 481 RYGREnvtMDEIEKAVKEANAYDFI--MKLPHKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATS 551
Cdd:pfam00005 81 RLGLL---LKGLSKREKDARAEEALekLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
1031-1243 |
8.90e-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: 168.16 E-value: 8.90e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1031 GVMFNYPTRPNiPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIKQLNVQWLRAHLGIVSQ 1110
Cdd:cd03246 5 NVSFRYPGAEP-PVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGYLPQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1111 EPILFDCSIAENIaygdnsrvvsheeivkaakeanihqfidslpekyntrvgdkgtqLSGGQKQRIAIARALVRQPHILL 1190
Cdd:cd03246 84 DDELFSGSIAENI--------------------------------------------LSGGQRQRLGLARALYGNPRILV 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 25453402 1191 LDEATSALDTESEKVVQEALDKARE-GRTCIVIAHRLSTIQNADLIVVIQNGQV 1243
Cdd:cd03246 120 LDEPNSHLDVEGERALNQAIAALKAaGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
384-602 |
1.21e-47 |
|
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: 169.99 E-value: 1.21e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 384 LEFKNIHFSYPSRKD-VQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRTINVRYLREI- 461
Cdd:cd03257 2 LEVKNLSVSFPTGGGsVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIRr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 462 --IGVVSQEPVL-------FATTIAENIRYGRENVTMDEIEKAVKEA-----NAYDFIMKLPHkfdtlvgergaQLSGGQ 527
Cdd:cd03257 82 keIQMVFQDPMSslnprmtIGEQIAEPLRIHGKLSKKEARKEAVLLLlvgvgLPEEVLNRYPH-----------ELSGGQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 25453402 528 KQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDKARE--GRTTIVIAHRLSTVRN-ADVIAGFDGGVIVEQG 602
Cdd:cd03257 151 RQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEelGLTLLFITHDLGVVAKiADRVAVMYAGKIVEEG 228
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
384-579 |
1.45e-47 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 169.23 E-value: 1.45e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 384 LEFKNIHFSYPSRKdvqILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRTINVRYLREIIG 463
Cdd:COG4619 1 LELEGLSFRVGGKP---ILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 464 VVSQEPVLFATTIAENI----RYGRENVTMDEIEKAVKEANaydfimkLPHKF-DTLVGErgaqLSGGQKQRIAIARALV 538
Cdd:COG4619 78 YVPQEPALWGGTVRDNLpfpfQLRERKFDRERALELLERLG-------LPPDIlDKPVER----LSGGERQRLALIRALL 146
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 25453402 539 RNPKILLLDEATSALDTESEAVVQAALDK--AREGRTTIVIAH 579
Cdd:COG4619 147 LQPDVLLLDEPTSALDPENTRRVEELLREylAEEGRAVLWVSH 189
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
1027-1256 |
2.08e-47 |
|
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: 169.44 E-value: 2.08e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1027 VKFNGVMFNYPtrPNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIKQLNVQWLRAHLG 1106
Cdd:COG1122 1 IELENLSFSYP--GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1107 IVSQEPI--LFDCSIAENIAYGDNSRVVSHEEIVKAAKEA----NIHQFIDSLPekyntrvgdkgTQLSGGQKQRIAIAR 1180
Cdd:COG1122 79 LVFQNPDdqLFAPTVEEDVAFGPENLGLPREEIRERVEEAlelvGLEHLADRPP-----------HELSGGQKQRVAIAG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 25453402 1181 ALVRQPHILLLDEATSALDTESEKVVQEALDK-AREGRTCIVIAHRLSTI-QNADLIVVIQNGQVKEHGTHQQLLAQK 1256
Cdd:COG1122 148 VLAMEPEVLVLDEPTAGLDPRGRRELLELLKRlNKEGKTVIIVTHDLDLVaELADRVIVLDDGRIVADGTPREVFSDY 225
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1027-1255 |
1.55e-46 |
|
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: 175.86 E-value: 1.55e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1027 VKFNGVMFNYPTRPN--IPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIKQLN---VQWL 1101
Cdd:COG1123 261 LEVRNLSKRYPVRGKggVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSrrsLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1102 RAHLGIVSQEPIL-FDC--SIAENIAYG-DNSRVVSHEEIVKAAKEAnIHQFidSLPEKYNTRvgdKGTQLSGGQKQRIA 1177
Cdd:COG1123 341 RRRVQMVFQDPYSsLNPrmTVGDIIAEPlRLHGLLSRAERRERVAEL-LERV--GLPPDLADR---YPHELSGGQRQRVA 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1178 IARALVRQPHILLLDEATSALDTESEKVVQEALD--KAREGRTCIVIAHRLSTIQN-ADLIVVIQNGQVKEHGTHQQLLA 1254
Cdd:COG1123 415 IARALALEPKLLILDEPTSALDVSVQAQILNLLRdlQRELGLTYLFISHDLAVVRYiADRVAVMYDGRIVEDGPTEEVFA 494
|
.
gi 25453402 1255 Q 1255
Cdd:COG1123 495 N 495
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
1043-1243 |
1.57e-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: 1.57e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1043 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIKQLNVQWLRAHLGIVSQEPILFDCSIAEN 1122
Cdd:COG4619 14 PILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYVPQEPALWGGTVRDN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1123 IA--YGDNSRVVSHEEIVKAAKEANihqfidsLPEKY-NTRVgdkgTQLSGGQKQRIAIARALVRQPHILLLDEATSALD 1199
Cdd:COG4619 94 LPfpFQLRERKFDRERALELLERLG-------LPPDIlDKPV----ERLSGGERQRLALIRALLLQPDVLLLDEPTSALD 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 25453402 1200 TESEKVVQEALDK--AREGRTCIVIAHRLSTIQN-ADLIVVIQNGQV 1243
Cdd:COG4619 163 PENTRRVEELLREylAEEGRAVLWVSHDPEQIERvADRVLTLEAGRL 209
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
1044-1252 |
1.79e-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: 166.59 E-value: 1.79e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1044 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYD-----PMAGTVFLDGKEI--KQLNVQWLRAHLGIVSQEPILFD 1116
Cdd:cd03260 15 ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIydLDVDVLELRRRVGMVFQKPNPFP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1117 CSIAENIAYGDN-----SRVVSHEEIVKAAKEANihqfidsLPEKYNTRVgdKGTQLSGGQKQRIAIARALVRQPHILLL 1191
Cdd:cd03260 95 GSIYDNVAYGLRlhgikLKEELDERVEEALRKAA-------LWDEVKDRL--HALGLSGGQQQRLCLARALANEPEVLLL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 25453402 1192 DEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVIQNGQVKEHGTHQQL 1252
Cdd:cd03260 166 DEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARvADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
384-607 |
2.83e-46 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 166.22 E-value: 2.83e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 384 LEFKNIHFSYPSR-KDVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRTINVRYLREI- 461
Cdd:cd03258 2 IELKNVSKVFGDTgGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKAr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 462 --IGVVSQEPVLFAT-TIAENIRYGRE--NVTMDEIEKAVKEANAydfIMKLPHKFDTlvgeRGAQLSGGQKQRIAIARA 536
Cdd:cd03258 82 rrIGMIFQHFNLLSSrTVFENVALPLEiaGVPKAEIEERVLELLE---LVGLEDKADA----YPAQLSGGQKQRVGIARA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 25453402 537 LVRNPKILLLDEATSALDTES-EAVVQAALDKAREGRTTIV-IAHRLSTVRN-ADVIAGFDGGVIVEQGNHDEL 607
Cdd:cd03258 155 LANNPKVLLCDEATSALDPETtQSILALLRDINRELGLTIVlITHEMEVVKRiCDRVAVMEKGEVVEEGTVEEV 228
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
384-609 |
2.92e-46 |
|
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: 174.71 E-value: 2.92e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 384 LEFKNIHFSYPSRkDVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDP---IEGEVSIDGQDIRTINVRYLRE 460
Cdd:COG1123 5 LEVRDLSVRYPGG-DVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHggrISGEVLLDGRDLLELSEALRGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 461 IIGVVSQEP--VLFATTIAENIRYGREN--VTMDEIEKAVKEANAydfIMKLPHKFDtlvgERGAQLSGGQKQRIAIARA 536
Cdd:COG1123 84 RIGMVFQDPmtQLNPVTVGDQIAEALENlgLSRAEARARVLELLE---AVGLERRLD----RYPHQLSGGQRQRVAIAMA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 25453402 537 LVRNPKILLLDEATSALDTESEAVVQAALDK--AREGRTTIVIAHRLSTV-RNADVIAGFDGGVIVEQGNHDELMR 609
Cdd:COG1123 157 LALDPDLLIADEPTTALDVTTQAEILDLLRElqRERGTTVLLITHDLGVVaEIADRVVVMDDGRIVEDGPPEEILA 232
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
384-603 |
3.56e-46 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 169.49 E-value: 3.56e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 384 LEFKNIHFSYPSRK-DVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRTINVRYLREI- 461
Cdd:COG1135 2 IELENLSKTFPTKGgPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAAr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 462 --IGVVSQEPVLFAT-TIAENIRYGRE--NVTMDEIEKAVKE----------ANAYdfimklPhkfdtlvgergAQLSGG 526
Cdd:COG1135 82 rkIGMIFQHFNLLSSrTVAENVALPLEiaGVPKAEIRKRVAEllelvglsdkADAY------P-----------SQLSGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 527 QKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDKARE--GRTTIVIAHRLSTVRN-ADVIAGFDGGVIVEQGN 603
Cdd:COG1135 145 QKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRelGLTIVLITHEMDVVRRiCDRVAVLENGRIVEQGP 224
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
53-340 |
7.40e-46 |
|
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: 167.43 E-value: 7.40e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 53 GTLAAIIHGIALPLMMLVFGDMTDSFANVgnnrsmsfynATDIYAKLEDEMTTYAYYYTGIGAGVLIVAYIQVSLWCLAA 132
Cdd:cd18780 1 GTIALLVSSGTNLALPYFFGQVIDAVTNH----------SGSGGEEALRALNQAVLILLGVVLIGSIATFLRSWLFTLAG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 133 GRQIHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFFQAMATFFGGFIIGFTRGWKLTLVILA 212
Cdd:cd18780 71 ERVVARLRKRLFSAIIAQEIAFFDVTRTGELLNRLSSDTQVLQNAVTVNLSMLLRYLVQIIGGLVFMFTTSWKLTLVMLS 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 213 ISPVLGLSAGIWAKILSSFTDKELQAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNNNLEEAKRLGIKKAITANISMG 292
Cdd:cd18780 151 VVPPLSIGAVIYGKYVRKLSKKFQDALAAASTVAEESISNIRTVRSFAKETKEVSRYSEKINESYLLGKKLARASGGFNG 230
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 25453402 293 AAFLLIYASYALAFWYGTSLVISKEYTIGQvLTVFfsvLIGAFSVGQA 340
Cdd:cd18780 231 FMGAAAQLAIVLVLWYGGRLVIDGELTTGL-LTSF---LLYTLTVAMS 274
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
384-607 |
1.15e-45 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 164.78 E-value: 1.15e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 384 LEFKNIHFSYpsrKDVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDI--RTINVRYLREI 461
Cdd:COG1126 2 IEIENLHKSF---GDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLtdSKKDINKLRRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 462 IGVVSQEPVLFA-TTIAENIRYGRENVT-MDEiEKAVKEANAYDFIMKLPHKFDtlvgERGAQLSGGQKQRIAIARALVR 539
Cdd:COG1126 79 VGMVFQQFNLFPhLTVLENVTLAPIKVKkMSK-AEAEERAMELLERVGLADKAD----AYPAQLSGGQQQRVAIARALAM 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 25453402 540 NPKILLLDEATSALDTE--SEaVVQAALDKAREGRTTIVIAHRLSTVRN-ADVIAGFDGGVIVEQGNHDEL 607
Cdd:COG1126 154 EPKVMLFDEPTSALDPElvGE-VLDVMRDLAKEGMTMVVVTHEMGFAREvADRVVFMDGGRIVEEGPPEEF 223
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
384-602 |
1.24e-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: 162.48 E-value: 1.24e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 384 LEFKNIHFSYPSrKDVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRTINvRYLREIIG 463
Cdd:cd03247 1 LSINNVSFSYPE-QEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 464 VVSQEPVLFATTIAENIrygrenvtmdeiekavkeanaydfimklphkfdtlvgerGAQLSGGQKQRIAIARALVRNPKI 543
Cdd:cd03247 79 VLNQRPYLFDTTLRNNL---------------------------------------GRRFSGGERQRLALARILLQDAPI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 25453402 544 LLLDEATSALDTESEAVVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFDGGVIVEQG 602
Cdd:cd03247 120 VLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
384-609 |
1.50e-45 |
|
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: 164.59 E-value: 1.50e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 384 LEFKNIHFSYPSR-KDVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRTINVRYLREII 462
Cdd:COG1124 2 LEVRNLSVSYGQGgRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 463 GVVSQEP---------VlfATTIAENIRYGRENVTMDEIEKAVKEAN-AYDFIMKLPHkfdtlvgergaQLSGGQKQRIA 532
Cdd:COG1124 82 QMVFQDPyaslhprhtV--DRILAEPLRIHGLPDREERIAELLEQVGlPPSFLDRYPH-----------QLSGGQRQRVA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 533 IARALVRNPKILLLDEATSALDteseAVVQAA-LD-----KAREGRTTIVIAHRLSTV-RNADVIAGFDGGVIVEQGNHD 605
Cdd:COG1124 149 IARALILEPELLLLDEPTSALD----VSVQAEiLNllkdlREERGLTYLFVSHDLAVVaHLCDRVAVMQNGRIVEELTVA 224
|
....
gi 25453402 606 ELMR 609
Cdd:COG1124 225 DLLA 228
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
966-1226 |
2.72e-45 |
|
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: 172.55 E-value: 2.72e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 966 VLLVFSAivFGAMAVgqVSSFAPDYAKAKVSASHIIRIIEKIPEIDSYSTEGLKPNMLEG-NVKFNGVMFNYPTRPniPV 1044
Cdd:TIGR02868 277 VLLPLAA--FEAFAA--LPAAAQQLTRVRAAAERIVEVLDAAGPVAEGSAPAAGAVGLGKpTLELRDLSAGYPGAP--PV 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1045 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIKQLNVQWLRAHLGIVSQEPILFDCSIAEN-- 1122
Cdd:TIGR02868 351 LDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENlr 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1123 IAYGDnsrvVSHEEIVKAAKEANIHQFIDSLPEKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTES 1202
Cdd:TIGR02868 431 LARPD----ATDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAET 506
|
250 260
....*....|....*....|....
gi 25453402 1203 EKVVQEALDKAREGRTCIVIAHRL 1226
Cdd:TIGR02868 507 ADELLEDLLAALSGRTVVLITHHL 530
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
1028-1242 |
2.99e-45 |
|
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: 162.64 E-value: 2.99e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1028 KFNGVMFNYPTRpNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIKQLNVQWLRAHLGI 1107
Cdd:cd03225 1 ELKNLSFSYPDG-ARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1108 VSQEP--ILFDCSIAENIAYGDNSRVVSHEEIVKAAKEA----NIHQFIDSLPEkyntrvgdkgtQLSGGQKQRIAIARA 1181
Cdd:cd03225 80 VFQNPddQFFGPTVEEEVAFGLENLGLPEEEIEERVEEAlelvGLEGLRDRSPF-----------TLSGGQKQRVAIAGV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 25453402 1182 LVRQPHILLLDEATSALDTESEKVVQEALDK-AREGRTCIVIAHRLSTIQN-ADLIVVIQNGQ 1242
Cdd:cd03225 149 LAMDPDILLLDEPTAGLDPAGRRELLELLKKlKAEGKTIIIVTHDLDLLLElADRVIVLEDGK 211
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
384-610 |
3.01e-45 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 163.31 E-value: 3.01e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 384 LEFKNIHFSYpsrKDVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRTINVRYlREIIG 463
Cdd:COG1131 1 IEVRGLTKRY---GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEV-RRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 464 VVSQEPVLFAT-TIAENIRYGRE--NVTMDEIEKAVKEANAydfIMKLPHKFDTLVGergaQLSGGQKQRIAIARALVRN 540
Cdd:COG1131 77 YVPQEPALYPDlTVRENLRFFARlyGLPRKEARERIDELLE---LFGLTDAADRKVG----TLSGGMKQRLGLALALLHD 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 25453402 541 PKILLLDEATSALDTESEAVVQAALDKAREGRTTIVIA-HRLSTV-RNADVIAGFDGGVIVEQGNHDELMRE 610
Cdd:COG1131 150 PELLILDEPTSGLDPEARRELWELLRELAAEGKTVLLStHYLEEAeRLCDRVAIIDKGRIVADGTPDELKAR 221
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
384-613 |
3.01e-45 |
|
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: 164.53 E-value: 3.01e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 384 LEFKNIHFSYPSRkDVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRTI-NVRYLREII 462
Cdd:TIGR04520 1 IEVENVSFSYPES-EKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEeNLWEIRKKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 463 GVVSQEP--VLFATTIAENIRYGREN--VTMDEIEKAVKEA----NAYDFIMKLPHKfdtlvgergaqLSGGQKQRIAIA 534
Cdd:TIGR04520 80 GMVFQNPdnQFVGATVEDDVAFGLENlgVPREEMRKRVDEAlklvGMEDFRDREPHL-----------LSGGQKQRVAIA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 535 RALVRNPKILLLDEATSALDTES-EAVVQAALD-KAREGRTTIVIAHRLSTVRNADVIAGFDGGVIVEQG------NHDE 606
Cdd:TIGR04520 149 GVLAMRPDIIILDEATSMLDPKGrKEVLETIRKlNKEEGITVISITHDMEEAVLADRVIVMNKGKIVAEGtpreifSQVE 228
|
....*..
gi 25453402 607 LMREKGI 613
Cdd:TIGR04520 229 LLKEIGL 235
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
382-602 |
4.70e-45 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 161.81 E-value: 4.70e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 382 GNLEFKNIHFSYPSRKDvQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRTINVRYLREI 461
Cdd:cd03369 5 GEIEVENLSVRYAPDLP-PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 462 IGVVSQEPVLFATTIAENI-RYGREnvTMDEIEKAVKeanaydfimklphkfdtlVGERGAQLSGGQKQRIAIARALVRN 540
Cdd:cd03369 84 LTIIPQDPTLFSGTIRSNLdPFDEY--SDEEIYGALR------------------VSEGGLNLSQGQRQLLCLARALLKR 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 25453402 541 PKILLLDEATSALDTESEAVVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFDGGVIVEQG 602
Cdd:cd03369 144 PRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYD 205
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
1025-1248 |
1.16e-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: 160.66 E-value: 1.16e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1025 GNVKFNGVMFNYptRPNIP-VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIKQLNVQWLRA 1103
Cdd:cd03369 5 GEIEVENLSVRY--APDLPpVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1104 HLGIVSQEPILFDCSIAENIaygDNSRVVSHEEIVKAakeanihqfidslpekynTRVGDKGTQLSGGQKQRIAIARALV 1183
Cdd:cd03369 83 SLTIIPQDPTLFSGTIRSNL---DPFDEYSDEEIYGA------------------LRVSEGGLNLSQGQRQLLCLARALL 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 25453402 1184 RQPHILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIQNGQVKEHGT 1248
Cdd:cd03369 142 KRPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
384-609 |
3.05e-44 |
|
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: 160.53 E-value: 3.05e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 384 LEFKNIHFSYPSRkdvQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRTINVRYLREI-- 461
Cdd:COG1127 6 IEVRNLTKSFGDR---VVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYELrr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 462 -IGVVSQEPVLF-ATTIAENIRYG-RENVTM--DEIEKAVkeanaydfIMKLphkfdTLVGERGA------QLSGGQKQR 530
Cdd:COG1127 83 rIGMLFQGGALFdSLTVFENVAFPlREHTDLseAEIRELV--------LEKL-----ELVGLPGAadkmpsELSGGMRKR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 531 IAIARALVRNPKILLLDEATSALDTESEAVVQAALDKARE--GRTTIVIAHRLSTVRN-ADVIAGFDGGVIVEQGNHDEL 607
Cdd:COG1127 150 VALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDelGLTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPEEL 229
|
..
gi 25453402 608 MR 609
Cdd:COG1127 230 LA 231
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
384-602 |
6.00e-44 |
|
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: 158.84 E-value: 6.00e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 384 LEFKNIHFSYpsrKDVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRTINVRylREIIG 463
Cdd:cd03259 1 LELKGLSKTY---GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE--RRNIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 464 VVSQEPVLFAT-TIAENIRYGRENVTM--DEIEKAVKEANAydfIMKLPHkfdtLVGERGAQLSGGQKQRIAIARALVRN 540
Cdd:cd03259 76 MVFQDYALFPHlTVAENIAFGLKLRGVpkAEIRARVRELLE---LVGLEG----LLNRYPHELSGGQQQRVALARALARE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 25453402 541 PKILLLDEATSALDTESEAVVQAALDK--AREGRTTIVIAHRLS-TVRNADVIAGFDGGVIVEQG 602
Cdd:cd03259 149 PSLLLLDEPLSALDAKLREELREELKElqRELGITTIYVTHDQEeALALADRIAVMNEGRIVQVG 213
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
384-610 |
6.46e-44 |
|
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: 162.53 E-value: 6.46e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 384 LEFKNIHFSYPSRK-DVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDP---IEGEVSIDGQDIRTINVRYLR 459
Cdd:COG0444 2 LEVRNLKVYFPTRRgVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 460 EI----IGVVSQEPvlFA---------TTIAENIRYgRENVTMDEIEKAVKEA-------NAYDFIMKLPHkfdtlvger 519
Cdd:COG0444 82 KIrgreIQMIFQDP--MTslnpvmtvgDQIAEPLRI-HGGLSKAEARERAIELlervglpDPERRLDRYPH--------- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 520 gaQLSGGQKQRIAIARALVRNPKILLLDEATSALDteseAVVQAA-LD-----KAREGRTTIVIAHRLSTVRN-ADVIAG 592
Cdd:COG0444 150 --ELSGGMRQRVMIARALALEPKLLIADEPTTALD----VTIQAQiLNllkdlQRELGLAILFITHDLGVVAEiADRVAV 223
|
250
....*....|....*...
gi 25453402 593 FDGGVIVEQGNHDELMRE 610
Cdd:COG0444 224 MYAGRIVEEGPVEELFEN 241
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
1029-1247 |
6.62e-44 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 157.47 E-value: 6.62e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1029 FNGVMFNYPTRpNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIKQLNVQwLRAHLGIV 1108
Cdd:cd03247 3 INNVSFSYPEQ-EQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKA-LSSLISVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1109 SQEPILFDCSIAENIaygdnsrvvsheeivkaakeanihqfidslpekyntrvgdkGTQLSGGQKQRIAIARALVRQPHI 1188
Cdd:cd03247 81 NQRPYLFDTTLRNNL-----------------------------------------GRRFSGGERQRLALARILLQDAPI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 25453402 1189 LLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIQNGQVKEHG 1247
Cdd:cd03247 120 VLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
384-601 |
8.29e-44 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 159.05 E-value: 8.29e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 384 LEFKNIHFSYPSRK-DVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRTIN----VRYL 458
Cdd:COG1136 5 LELRNLTKSYGTGEgEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSerelARLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 459 REIIGVVSQEPVLFAT-TIAENIRYGRE--NVTMDEIEKAVKEANAYdfiMKLPHKFDTLVgergAQLSGGQKQRIAIAR 535
Cdd:COG1136 85 RRHIGFVFQFFNLLPElTALENVALPLLlaGVSRKERRERARELLER---VGLGDRLDHRP----SQLSGGQQQRVAIAR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 25453402 536 ALVRNPKILLLDEATSALDTESEAVVQAALDK-AREGRTTIVIA-HRLSTVRNADVIAGFDGGVIVEQ 601
Cdd:COG1136 158 ALVNRPKLILADEPTGNLDSKTGEEVLELLRElNRELGTTIVMVtHDPELAARADRVIRLRDGRIVSD 225
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
384-598 |
1.02e-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: 158.42 E-value: 1.02e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 384 LEFKNIHFSYPSRKD-VQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRTIN----VRYL 458
Cdd:cd03255 1 IELKNLSKTYGGGGEkVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSekelAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 459 REIIGVVSQEPVLFAT-TIAENIRYGrenVTMDEIEKAVKEANAYDFI--MKLPHKFDTLVgergAQLSGGQKQRIAIAR 535
Cdd:cd03255 81 RRHIGFVFQSFNLLPDlTALENVELP---LLLAGVPKKERRERAEELLerVGLGDRLNHYP----SELSGGQQQRVAIAR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 25453402 536 ALVRNPKILLLDEATSALDTE-SEAVVQAALDKAREGRTTIVIA-HRLSTVRNADVIAGFDGGVI 598
Cdd:cd03255 154 ALANDPKIILADEPTGNLDSEtGKEVMELLRELNKEAGTTIVVVtHDPELAEYADRIIELRDGKI 218
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
384-579 |
1.04e-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: 159.87 E-value: 1.04e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 384 LEFKNIHFSYPSRK-DVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRTINVRylreiI 462
Cdd:COG1116 8 LELRGVSKRFPTGGgGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPD-----R 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 463 GVVSQEPVLFA-TTIAENIRYGRENVTMDEiEKAVKEANAY-------DFIMKLPHkfdtlvgergaQLSGGQKQRIAIA 534
Cdd:COG1116 83 GVVFQEPALLPwLTVLDNVALGLELRGVPK-AERRERARELlelvglaGFEDAYPH-----------QLSGGMRQRVAIA 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 25453402 535 RALVRNPKILLLDEATSALDTESEAVVQAALDK--AREGRTTIVIAH 579
Cdd:COG1116 151 RALANDPEVLLMDEPFGALDALTRERLQDELLRlwQETGKTVLFVTH 197
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
50-357 |
1.13e-43 |
|
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: 160.79 E-value: 1.13e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 50 MLLGTLAAIIHGIALPLMMLVFGDMTDsfaNVGNNRSMSFYNAtdiyakledemttYAYYYTGIGAGVLIVAYIQVSLWC 129
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLLID---DVIPAGDLSLLLW-------------IALLLLLLALLRALLSYLRRYLAA 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 130 LAAGRQIHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFFQAMATFFGGFIIGFTRGWKLTLV 209
Cdd:cd07346 65 RLGQRVVFDLRRDLFRHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 210 ILAISPVLGLSAGIWAKILSSFTDKELQAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNNNLEEAKRLGIKKAITANI 289
Cdd:cd07346 145 ALLLLPLYVLILRYFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSAL 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 25453402 290 SMGAAFLLIYASYALAFWYGTSLVISKEYTIGQvLTVFFSVLIGAFS-VGQASPNIEAFANARGAAYEV 357
Cdd:cd07346 225 FSPLIGLLTALGTALVLLYGGYLVLQGSLTIGE-LVAFLAYLGMLFGpIQRLANLYNQLQQALASLERI 292
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
101-357 |
4.13e-43 |
|
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: 159.25 E-value: 4.13e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 101 DEMTTYAYYYTGIGAGVLIVAYIQVSLWCLAAGRQIHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINEGIGD 180
Cdd:cd18572 33 EAFYRAVLLLLLLSVLSGLFSGLRGGCFSYAGTRLVRRLRRDLFRSLLRQDIAFFDATKTGELTSRLTSDCQKVSDPLST 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 181 KIGMFFQAMATFFGGFIIGFTRGWKLTLVILAISPVLGLSAGIWAKILSSFTDKELQAYAKAGAVAEEVLAAIRTVIAFG 260
Cdd:cd18572 113 NLNVFLRNLVQLVGGLAFMFSLSWRLTLLAFITVPVIALITKVYGRYYRKLSKEIQDALAEANQVAEEALSNIRTVRSFA 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 261 GQKKELERYNNNLEEAKRLGIKKAITANISMGAAFLLIYASYALAFWYGTSLVISKEYTIGQVLTVFF--SVLIGAF-SV 337
Cdd:cd18572 193 TEEREARRYERALDKALKLSVRQALAYAGYVAVNTLLQNGTQVLVLFYGGHLVLSGRMSAGQLVTFMLyqQQLGEAFqSL 272
|
250 260
....*....|....*....|
gi 25453402 338 GQaspNIEAFANARGAAYEV 357
Cdd:cd18572 273 GD---VFSSLMQAVGAAEKV 289
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
384-609 |
5.45e-43 |
|
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: 157.08 E-value: 5.45e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 384 LEFKNIHFSYPSRKDVqiLKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRTINVRYLREIIG 463
Cdd:cd03295 1 IEFENVTKRYGGGKKA--VNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 464 VVSQEPVLFA-TTIAENI-------RYGREnvtmdEIEKAVKEANAydfIMKLPHKfdTLVGERGAQLSGGQKQRIAIAR 535
Cdd:cd03295 79 YVIQQIGLFPhMTVEENIalvpkllKWPKE-----KIRERADELLA---LVGLDPA--EFADRYPHELSGGQQQRVGVAR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 25453402 536 ALVRNPKILLLDEATSALDTESEAVVQAALDKARE--GRTTIVIAHRL-STVRNADVIAGFDGGVIVEQGNHDELMR 609
Cdd:cd03295 149 ALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQelGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEILR 225
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1027-1245 |
5.92e-43 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 156.36 E-value: 5.92e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1027 VKFNGVMFNYPTRPN-IPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQL---LERfydPMAGTVFLDGKEIKQLN----V 1098
Cdd:COG1136 5 LELRNLTKSYGTGEGeVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNIlggLDR---PTSGEVLIDGQDISSLSerelA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1099 QWLRAHLGIVSQEPILFDC-SIAENIA----YGDNSRVVSHEEIVKAAKEANIHQFIDSLPekyntrvgdkgTQLSGGQK 1173
Cdd:COG1136 82 RLRRRHIGFVFQFFNLLPElTALENVAlpllLAGVSRKERRERARELLERVGLGDRLDHRP-----------SQLSGGQQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 25453402 1174 QRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLSTIQNADLIVVIQNGQVKE 1245
Cdd:COG1136 151 QRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRElnRELGTTIVMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
384-579 |
1.02e-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: 155.71 E-value: 1.02e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 384 LEFKNIHFSYPSRK-DVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRTINVRylreiI 462
Cdd:cd03293 1 LEVRNVSKTYGGGGgAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD-----R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 463 GVVSQEPVLFA-TTIAENIRYGRE--NVTMDEIEKAVKEANA----YDFIMKLPHkfdtlvgergaQLSGGQKQRIAIAR 535
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNVALGLElqGVPKAEARERAEELLElvglSGFENAYPH-----------QLSGGMRQRVALAR 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 25453402 536 ALVRNPKILLLDEATSALDTESEAVVQAALDK--AREGRTTIVIAH 579
Cdd:cd03293 145 ALAVDPDVLLLDEPFSALDALTREQLQEELLDiwRETGKTVLLVTH 190
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1036-1247 |
1.86e-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: 154.97 E-value: 1.86e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1036 YPTRPN-IPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIKQLNVQWL---RAHLGIVSQE 1111
Cdd:cd03257 11 FPTGGGsVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRkirRKEIQMVFQD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1112 PI-----LFdcSIAENIA-----YGDNSRvvsHEEIVKAAKEANIH-----QFIDSLPekyntrvgdkgTQLSGGQKQRI 1176
Cdd:cd03257 91 PMsslnpRM--TIGEQIAeplriHGKLSK---KEARKEAVLLLLVGvglpeEVLNRYP-----------HELSGGQRQRV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 25453402 1177 AIARALVRQPHILLLDEATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTIQN-ADLIVVIQNGQVKEHG 1247
Cdd:cd03257 155 AIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEelGLTLLFITHDLGVVAKiADRVAVMYAGKIVEEG 228
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
384-596 |
2.42e-42 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 152.73 E-value: 2.42e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 384 LEFKNIHFSYpsrKDVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRT--INVRYLREI 461
Cdd:cd03229 1 LELKNVSKRY---GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDleDELPPLRRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 462 IGVVSQEPVLFAT-TIAENIRYGrenvtmdeiekavkeanaydfimklphkfdtlvgergaqLSGGQKQRIAIARALVRN 540
Cdd:cd03229 78 IGMVFQDFALFPHlTVLENIALG---------------------------------------LSGGQQQRVALARALAMD 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 25453402 541 PKILLLDEATSALDTESEAVVQAALD--KAREGRTTIVIAHRLSTVRN-ADVIAGFDGG 596
Cdd:cd03229 119 PDVLLLDEPTSALDPITRREVRALLKslQAQLGITVVLVTHDLDEAARlADRVVVLRDG 177
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
1038-1247 |
2.69e-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: 154.21 E-value: 2.69e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1038 TRPNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIKQLNVQwlRAHLGIVSQEPILFD- 1116
Cdd:cd03259 9 TYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE--RRNIGMVFQDYALFPh 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1117 CSIAENIAYGDNSRVVSHEEIVKAAKEA----NIHQFIDSLPEkyntrvgdkgtQLSGGQKQRIAIARALVRQPHILLLD 1192
Cdd:cd03259 87 LTVAENIAFGLKLRGVPKAEIRARVRELlelvGLEGLLNRYPH-----------ELSGGQQQRVALARALAREPSLLLLD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 25453402 1193 EATSALDTESEKVVQEALDK--AREGRTCIVIAHRLS-TIQNADLIVVIQNGQVKEHG 1247
Cdd:cd03259 156 EPLSALDAKLREELREELKElqRELGITTIYVTHDQEeALALADRIAVMNEGRIVQVG 213
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
1045-1196 |
2.69e-42 |
|
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: 151.65 E-value: 2.69e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1045 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIKQLNVQWLRAHLGIVSQEPILF-DCSIAENI 1123
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFpRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 25453402 1124 AYGdnsrvVSHEEIVKAAKEANIHQFID--SLPEKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATS 1196
Cdd:pfam00005 81 RLG-----LLLKGLSKREKDARAEEALEklGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
108-624 |
3.01e-42 |
|
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: 169.74 E-value: 3.01e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 108 YYYTGIGAGVLIVAY-IQVSLWCLAAGRQIHkirQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFF 186
Cdd:TIGR00957 1011 YGALGILQGFAVFGYsMAVSIGGIQASRVLH---QDLLHNKLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPPVIKMFM 1087
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 187 QAMATFFGGFIIGFTRGWKLTLVILAISPVLGLSAGIWAKilSSFTDKELQAYAKAGAVAE--EVLAAIRTVIAFGGQKK 264
Cdd:TIGR00957 1088 GSLFNVIGALIVILLATPIAAVIIPPLGLLYFFVQRFYVA--SSRQLKRLESVSRSPVYSHfnETLLGVSVIRAFEEQER 1165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 265 ELERYNNNLEEAKR-----------LGIKKAITAN-ISMGAAFLLIYASYALAfwygTSLV-ISKEYTIgQVlTVFFSVL 331
Cdd:TIGR00957 1166 FIHQSDLKVDENQKayypsivanrwLAVRLECVGNcIVLFAALFAVISRHSLS----AGLVgLSVSYSL-QV-TFYLNWL 1239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 332 IGAFSvgQASPNIEAFANARgaayEVFSIIDNKPSI--DSFSKSGHKPdniQGNLEFKNIHFSYpsRKDVQ-ILKGLNLK 408
Cdd:TIGR00957 1240 VRMSS--EMETNIVAVERLK----EYSETEKEAPWQiqETAPPSGWPP---RGRVEFRNYCLRY--REDLDlVLRHINVT 1308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 409 VKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRTINVRYLREIIGVVSQEPVLFATTIAENI----RYGR 484
Cdd:TIGR00957 1309 IHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLdpfsQYSD 1388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 485 ENVTMdeiekAVKEANAYDFIMKLPHKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAA 564
Cdd:TIGR00957 1389 EEVWW-----ALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQST 1463
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 565 LDKAREGRTTIVIAHRLSTVRNADVIAGFDGGVIVEQGNHDELMREKGIYFKlvMTQTAG 624
Cdd:TIGR00957 1464 IRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRGIFYS--MAKDAG 1521
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
384-607 |
3.73e-42 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 155.19 E-value: 3.73e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 384 LEFKNIHFSYpsrKDVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYD--P---IEGEVSIDGQDI--RTINVR 456
Cdd:COG1117 12 IEVRNLNVYY---GDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDliPgarVEGEILLDGEDIydPDVDVV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 457 YLREIIGVVSQEPVLFATTIAENIRYG------RENVTMDEI-EKAVKEANAYDFImklphKfDTLvGERGAQLSGGQKQ 529
Cdd:COG1117 89 ELRRRVGMVFQKPNPFPKSIYDNVAYGlrlhgiKSKSELDEIvEESLRKAALWDEV-----K-DRL-KKSALGLSGGQQQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 530 RIAIARALVRNPKILLLDEATSALDTESEAVVQAALDKAREgRTTIVI-------AHRLStvrnaDVIAGFDGGVIVEQG 602
Cdd:COG1117 162 RLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKK-DYTIVIvthnmqqAARVS-----DYTAFFYLGELVEFG 235
|
....*
gi 25453402 603 NHDEL 607
Cdd:COG1117 236 PTEQI 240
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
384-609 |
4.68e-42 |
|
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: 154.20 E-value: 4.68e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 384 LEFKNIHFSYPSRkdvQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRTINVRYLREI-- 461
Cdd:cd03261 1 IELRGLTKSFGGR---TVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLrr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 462 -IGVVSQEPVLF-ATTIAENIRYG-RENVTMDE--IEKAVKeanaydfiMKLphkfdTLVGERG------AQLSGGQKQR 530
Cdd:cd03261 78 rMGMLFQSGALFdSLTVFENVAFPlREHTRLSEeeIREIVL--------EKL-----EAVGLRGaedlypAELSGGMKKR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 531 IAIARALVRNPKILLLDEATSALD-TESEAVVQAALD-KAREGRTTIVIAHRLSTVRN-ADVIAGFDGGVIVEQGNHDEL 607
Cdd:cd03261 145 VALARALALDPELLLYDEPTAGLDpIASGVIDDLIRSlKKELGLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPEEL 224
|
..
gi 25453402 608 MR 609
Cdd:cd03261 225 RA 226
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
384-610 |
6.20e-42 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 154.43 E-value: 6.20e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 384 LEFKNIHFSYPSRkdvQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRTINVRYLREIIG 463
Cdd:COG1120 2 LEAENLSVGYGGR---PVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 464 VVSQEPVL-FATTIAENIRYGR---------ENVTMDEI-EKAVKEANAYDFIMKLphkFDTlvgergaqLSGGQKQRIA 532
Cdd:COG1120 79 YVPQEPPApFGLTVRELVALGRyphlglfgrPSAEDREAvEEALERTGLEHLADRP---VDE--------LSGGERQRVL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 533 IARALVRNPKILLLDEATSALDTESEAVVQAALDK--AREGRTTIVIAHRLS-TVRNADVIAGFDGGVIVEQGNHDELMR 609
Cdd:COG1120 148 IARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRlaRERGRTVVMVLHDLNlAARYADRLVLLKDGRIVAQGPPEEVLT 227
|
.
gi 25453402 610 E 610
Cdd:COG1120 228 P 228
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
384-598 |
7.71e-42 |
|
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: 152.68 E-value: 7.71e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 384 LEFKNIHFSYpsrKDVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDI--RTINVRYLREI 461
Cdd:cd03262 1 IEIKNLHKSF---GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtdDKKNINELRQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 462 IGVVSQEPVLFA-TTIAENIRYGRENVT-MDEIEKavkEANAYDFIMK--LPHKFDtlvgERGAQLSGGQKQRIAIARAL 537
Cdd:cd03262 78 VGMVFQQFNLFPhLTVLENITLAPIKVKgMSKAEA---EERALELLEKvgLADKAD----AYPAQLSGGQQQRVAIARAL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 25453402 538 VRNPKILLLDEATSALDTE-SEAVVQAALDKAREGRTTIVIAHRLSTVRN-ADVIAGFDGGVI 598
Cdd:cd03262 151 AMNPKVMLFDEPTSALDPElVGEVLDVMKDLAEEGMTMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
385-596 |
1.76e-41 |
|
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: 149.70 E-value: 1.76e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 385 EFKNIHFSYPSRKdvqILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRTINVRYLREIIGV 464
Cdd:cd00267 1 EIENLSFRYGGRT---ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 465 VSQepvlfattiaenirygrenvtmdeiekavkeanaydfimklphkfdtlvgergaqLSGGQKQRIAIARALVRNPKIL 544
Cdd:cd00267 78 VPQ-------------------------------------------------------LSGGQRQRVALARALLLNPDLL 102
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 25453402 545 LLDEATSALDTESEAVVQAALDK-AREGRTTIVIAHRLSTVRNA-DVIAGFDGG 596
Cdd:cd00267 103 LLDEPTSGLDPASRERLLELLRElAEEGRTVIIVTHDPELAELAaDRVIVLKDG 156
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
401-1263 |
2.46e-41 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 166.49 E-value: 2.46e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 401 ILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVsidgqdirtinvrYLREIIGVVSQEPVLFATTIAENI 480
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV-------------WAERSIAYVPQQAWIMNATVRGNI 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 481 RYGRENVTMDeIEKAVK----EANaydfIMKLPHKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTE 556
Cdd:PTZ00243 742 LFFDEEDAAR-LADAVRvsqlEAD----LAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAH 816
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 557 -SEAVVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFDGGVIVEQGNHDELMREKgIYFKLVmTQTAGNEIELGNEACE 635
Cdd:PTZ00243 817 vGERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFMRTS-LYATLA-AELKENKDSKEGDADA 894
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 636 SKDGIDnvdmSSKDSGSSLIRRRSTRKSIRGPHD------QDGELST-KEALDDDVPpasfWrilklnSTEWPYFVvgvF 708
Cdd:PTZ00243 895 EVAEVD----AAPGGAVDHEPPVAKQEGNAEGGDgaaldaAAGRLMTrEEKASGSVP----W------STYVAYLR---F 957
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 709 CaiinGGLQPAFSIIFSKVVG-VFTKNDTPEIQRQNSNLFS----------LLFLILGIISFITFFLQGFTFGKAGeilT 777
Cdd:PTZ00243 958 C----GGLHAAGFVLATFAVTeLVTVSSGVWLSMWSTRSFKlsaatylyvyLGIVLLGTFSVPLRFFLSYEAMRRG---S 1030
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 778 KRLRYMVFKSMLRQDISWFDdpknTT--GALTTRLANDAaqvkGATGSRLAVITQNIANLGTGIIIS-LIYGWQLTLLLL 854
Cdd:PTZ00243 1031 RNMHRDLLRSVSRGTMSFFD----TTplGRILNRFSRDI----DILDNTLPMSYLYLLQCLFSICSSiLVTSASQPFVLV 1102
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 855 AIVP------------------IIAIAGVVEMKMLS--GQALKDKKELEGSGK---IATEAIEnfrtvvsltreqKFETM 911
Cdd:PTZ00243 1103 ALVPcgylyyrlmqfynsanreIRRIKSVAKSPVFTllEEALQGSATITAYGKahlVMQEALR------------RLDVV 1170
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 912 YAQSLqipYRNALKKAhvFGITFSFTQAMMYFSYAACFRFGAYLVArelmTFENVLLVFSAIVFGAMAVGQVSSFAPDYA 991
Cdd:PTZ00243 1171 YSCSY---LENVANRW--LGVRVEFLSNIVVTVIALIGVIGTMLRA----TSQEIGLVSLSLTMAMQTTATLNWLVRQVA 1241
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 992 KAKVSASHIIRII--------EKIPEID------------------SYSTEGLKP------NMLEGNVKFNGVMFNYptR 1039
Cdd:PTZ00243 1242 TVEADMNSVERLLyytdevphEDMPELDeevdalerrtgmaadvtgTVVIEPASPtsaaphPVQAGSLVFEGVQMRY--R 1319
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1040 PNIP-VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIKQLNVQWLRAHLGIVSQEPILFDCS 1118
Cdd:PTZ00243 1320 EGLPlVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDGT 1399
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1119 IAENIaygDNSRVVSHEEIVKAAKEANIHQFIDSLPEKYNTRVGDKGTQLSGGQKQRIAIARALV-RQPHILLLDEATSA 1197
Cdd:PTZ00243 1400 VRQNV---DPFLEASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLkKGSGFILMDEATAN 1476
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 25453402 1198 LDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIQNGQVKEHGTHQQL-LAQKGIYFSMV 1263
Cdd:PTZ00243 1477 IDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELvMNRQSIFHSMV 1543
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
384-602 |
3.54e-41 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 155.64 E-value: 3.54e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 384 LEFKNIHFSYpsrKDVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRTINVrYLREIiG 463
Cdd:COG3842 6 LELENVSKRY---GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPP-EKRNV-G 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 464 VVSQEPVLFA-TTIAENIRYG--RENVTMDEIEKAVKEANAydfIMKLPHKFDTLVgergAQLSGGQKQRIAIARALVRN 540
Cdd:COG3842 81 MVFQDYALFPhLTVAENVAFGlrMRGVPKAEIRARVAELLE---LVGLEGLADRYP----HQLSGGQQQRVALARALAPE 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 25453402 541 PKILLLDEATSALDTESEAVVQAALDK--AREGRTTIVIAHRLS---TVrnADVIAGFDGGVIVEQG 602
Cdd:COG3842 154 PRVLLLDEPLSALDAKLREEMREELRRlqRELGITFIYVTHDQEealAL--ADRIAVMNDGRIEQVG 218
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1043-1255 |
4.92e-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: 4.92e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1043 PVLQGLSLEVKKGQTLALVGSSGCGKSTV---VQLLERfydPMAGTVFLDGKEI--KQLNVQWLRAHLGIVSQEPILF-D 1116
Cdd:COG1126 15 EVLKGISLDVEKGEVVVIIGPSGSGKSTLlrcINLLEE---PDSGTITVDGEDLtdSKKDINKLRRKVGMVFQQFNLFpH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1117 CSIAENIAYGdnSRVV---SHEEIVKAAKEAnihqfidsLpekynTRVG--DKG----TQLSGGQKQRIAIARALVRQPH 1187
Cdd:COG1126 92 LTVLENVTLA--PIKVkkmSKAEAEERAMEL--------L-----ERVGlaDKAdaypAQLSGGQQQRVAIARALAMEPK 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 25453402 1188 ILLLDEATSALDTEsekVVQEALD--K--AREGRTCIVIAHRLSTIQN-ADLIVVIQNGQVKEHGTHQQLLAQ 1255
Cdd:COG1126 157 VMLFDEPTSALDPE---LVGEVLDvmRdlAKEGMTMVVVTHEMGFAREvADRVVFMDGGRIVEEGPPEEFFEN 226
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1036-1254 |
7.93e-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: 151.11 E-value: 7.93e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1036 YPTRP-NIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIKQLNVQWLRAHLGIVSQEPIL 1114
Cdd:COG1124 11 YGQGGrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRVQMVFQDPYA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1115 -------FDCSIAE--NIAYGDNSRvvshEEIVKAAKEANihqfidsLPEKYNTRVGDkgtQLSGGQKQRIAIARALVRQ 1185
Cdd:COG1124 91 slhprhtVDRILAEplRIHGLPDRE----ERIAELLEQVG-------LPPSFLDRYPH---QLSGGQRQRVAIARALILE 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 25453402 1186 PHILLLDEATSALDTesekVVQ-EALD-----KAREGRTCIVIAHRLSTIQN-ADLIVVIQNGQVKEHGTHQQLLA 1254
Cdd:COG1124 157 PELLLLDEPTSALDV----SVQaEILNllkdlREERGLTYLFVSHDLAVVAHlCDRVAVMQNGRIVEELTVADLLA 228
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1027-1255 |
8.35e-41 |
|
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: 150.42 E-value: 8.35e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1027 VKFNGVMFNYPTRPN-IPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQ---LLERfydPMAGTVFLDGKEIKQLN---VQ 1099
Cdd:cd03258 2 IELKNVSKVFGDTGGkVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRcinGLER---PTSGSVLVDGTDLTLLSgkeLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1100 WLRAHLGIVSQEPILFDC-SIAENIAYGdnsrvvshEEIVKAAKeANIHQFIDSLPEkyntRVG--DKG----TQLSGGQ 1172
Cdd:cd03258 79 KARRRIGMIFQHFNLLSSrTVFENVALP--------LEIAGVPK-AEIEERVLELLE----LVGleDKAdaypAQLSGGQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1173 KQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLSTIQN-ADLIVVIQNGQVKEHGTH 1249
Cdd:cd03258 146 KQRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDinRELGLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTV 225
|
....*.
gi 25453402 1250 QQLLAQ 1255
Cdd:cd03258 226 EEVFAN 231
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
384-612 |
2.48e-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: 149.62 E-value: 2.48e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 384 LEFKNIHFSYpsrKDVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRTINVRYLREIiG 463
Cdd:COG4555 2 IEVENLSKKY---GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQI-G 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 464 VVSQEPVLFAT-TIAENIRYGRE--NVTMDEIEKAVKEanaYDFIMKLPHKFDTLVGErgaqLSGGQKQRIAIARALVRN 540
Cdd:COG4555 78 VLPDERGLYDRlTVRENIRYFAElyGLFDEELKKRIEE---LIELLGLEEFLDRRVGE----LSTGMKKKVALARALVHD 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 25453402 541 PKILLLDEATSALDTES-EAVVQAALDKAREGRTTIVIAHRLSTVRN-ADVIAGFDGGVIVEQGNHDELMREKG 612
Cdd:COG4555 151 PKVLLLDEPTNGLDVMArRLLREILRALKKEGKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEIG 224
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
391-1264 |
2.62e-40 |
|
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: 163.16 E-value: 2.62e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 391 FSYPSRKDVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQdirtinvrylreiIGVVSQEPV 470
Cdd:TIGR01271 431 FSNFSLYVTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR-------------ISFSPQTSW 497
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 471 LFATTIAENIRYGrenVTMDEIE--KAVKEANAYDFIMKLPHKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDE 548
Cdd:TIGR01271 498 IMPGTIKDNIIFG---LSYDEYRytSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDS 574
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 549 ATSALD--TESEaVVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFDGGVIVEQGNHDELMREKGIYFKLVM------- 619
Cdd:TIGR01271 575 PFTHLDvvTEKE-IFESCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAKRPDFSSLLLgleafdn 653
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 620 ----------TQT-------------AGNEI------ELGNEACESK---------------------------DGIDNV 643
Cdd:TIGR01271 654 fsaerrnsilTETlrrvsidgdstvfSGPETikqsfkQPPPEFAEKRkqsiilnpiasarkfsfvqmgpqkaqaTTIEDA 733
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 644 DMSSKDSGSSLI------------------------------------------RRRSTRKSIRG--------------- 666
Cdd:TIGR01271 734 VREPSERKFSLVpedeqgeeslprgnqyhhglqhqaqrrqsvlqlmthsnrgenRREQLQTSFRKkssitqqnelaseld 813
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 667 ----PHDQDGELSTKEALDDD------------VPPASFWRI-LKLNSTEWPYFVVGVFCAIIngglqpaFSI-IFSKVV 728
Cdd:TIGR01271 814 iysrRLSKDSVYEISEEINEEdlkecfaderenVFETTTWNTyLRYITTNRNLVFVLIFCLVI-------FLAeVAASLL 886
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 729 GVFTKNDTPEIQRQ--------------------NSNLFSLLFLILGII-SFITF-FLQGFTFGKAGEILTKRLRYMVFK 786
Cdd:TIGR01271 887 GLWLITDNPSAPNYvdqqhanasspdvqkpviitPTSAYYIFYIYVGTAdSVLALgFFRGLPLVHTLLTVSKRLHEQMLH 966
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 787 SMLRQDISWFDDPKntTGALTTRLANDAAQVKGATGSRLAVITQ-NIANLGTGIIISLIYGWqltlLLLAIVPIIAIAGV 865
Cdd:TIGR01271 967 SVLQAPMAVLNTMK--AGRILNRFTKDMAIIDDMLPLTLFDFIQlTLIVLGAIFVVSVLQPY----IFIAAIPVAVIFIM 1040
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 866 VEMKML-SGQALKdKKELEGSGKIATEAIENFR---TVVSLTREQKFETMYAQSLQipyrnalkkahvfgitfsfTQAMM 941
Cdd:TIGR01271 1041 LRAYFLrTSQQLK-QLESEARSPIFSHLITSLKglwTIRAFGRQSYFETLFHKALN-------------------LHTAN 1100
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 942 YFSYAACFRfgaYLVARELMTFenvLLVFSAIVFGAMAVGQV----------------SSF------APDYAKAKVSASH 999
Cdd:TIGR01271 1101 WFLYLSTLR---WFQMRIDIIF---VFFFIAVTFIAIGTNQDgegevgiiltlamnilSTLqwavnsSIDVDGLMRSVSR 1174
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1000 IIRIIEkIPEIDSYSTEGLKPNML-----------------EGNVKFNGVMFNYpTRPNIPVLQGLSLEVKKGQTLALVG 1062
Cdd:TIGR01271 1175 VFKFID-LPQEEPRPSGGGGKYQLstvlvienphaqkcwpsGGQMDVQGLTAKY-TEAGRAVLQDLSFSVEGGQRVGLLG 1252
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1063 SSGCGKSTVVQLLERFYDpMAGTVFLDGKEIKQLNVQWLRAHLGIVSQEPILFDCSIAENIaygDNSRVVSHEEIVKAAK 1142
Cdd:TIGR01271 1253 RTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNL---DPYEQWSDEEIWKVAE 1328
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1143 EANIHQFIDSLPEKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKAREGRTCIVI 1222
Cdd:TIGR01271 1329 EVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILS 1408
|
1050 1060 1070 1080
....*....|....*....|....*....|....*....|..
gi 25453402 1223 AHRLSTIQNADLIVVIQNGQVKEHGTHQQLLAQKGIYFSMVS 1264
Cdd:TIGR01271 1409 EHRVEALLECQQFLVIEGSSVKQYDSIQKLLNETSLFKQAMS 1450
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1027-1255 |
3.15e-40 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 156.99 E-value: 3.15e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1027 VKFNGVMFNYPTRPNiPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDP---MAGTVFLDGKEIKQLNVQWLRA 1103
Cdd:COG1123 5 LEVRDLSVRYPGGDV-PAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHggrISGEVLLDGRDLLELSEALRGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1104 HLGIVSQEPI--LFDCSIAENIAYGDNSRVVSHEEIVKAAKEA----NIHQFIDSLPekyntrvgdkgTQLSGGQKQRIA 1177
Cdd:COG1123 84 RIGMVFQDPMtqLNPVTVGDQIAEALENLGLSRAEARARVLELleavGLERRLDRYP-----------HQLSGGQRQRVA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1178 IARALVRQPHILLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLSTI-QNADLIVVIQNGQVKEHGTHQQLLA 1254
Cdd:COG1123 153 IAMALALDPDLLIADEPTTALDVTTQAEILDLLRElqRERGTTVLLITHDLGVVaEIADRVVVMDDGRIVEDGPPEEILA 232
|
.
gi 25453402 1255 Q 1255
Cdd:COG1123 233 A 233
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
1027-1245 |
3.27e-40 |
|
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: 148.39 E-value: 3.27e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1027 VKFNGVMFNYPT-RPNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIKQLNvqwlrAHL 1105
Cdd:cd03293 1 LEVRNVSKTYGGgGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPG-----PDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1106 GIVSQEPILFD-CSIAENIAYGDNSRVVSHEEIVKAAKEAnIHQ-----FIDSLPEkyntrvgdkgtQLSGGQKQRIAIA 1179
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNVALGLELQGVPKAEARERAEEL-LELvglsgFENAYPH-----------QLSGGMRQRVALA 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 25453402 1180 RALVRQPHILLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLS-TIQNADLIVVIQN--GQVKE 1245
Cdd:cd03293 144 RALAVDPDVLLLDEPFSALDALTREQLQEELLDiwRETGKTVLLVTHDIDeAVFLADRVVVLSArpGRIVA 214
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1022-1248 |
3.85e-40 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 152.56 E-value: 3.85e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1022 MLEGNVKFNGVMFNYPTRPnipVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIKQLNVQwl 1101
Cdd:COG3842 1 MAMPALELENVSKRYGDVT---ALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPE-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1102 RAHLGIVSQEPILF-DCSIAENIAYGDNSRVVSHEEIVKAAKEA----NIHQFIDSLPekyntrvgdkgTQLSGGQKQRI 1176
Cdd:COG3842 76 KRNVGMVFQDYALFpHLTVAENVAFGLRMRGVPKAEIRARVAELlelvGLEGLADRYP-----------HQLSGGQQQRV 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 25453402 1177 AIARALVRQPHILLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLS---TIqnADLIVVIQNGQVKEHGT 1248
Cdd:COG3842 145 ALARALAPEPRVLLLDEPLSALDAKLREEMREELRRlqRELGITFIYVTHDQEealAL--ADRIAVMNDGRIEQVGT 219
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
106-638 |
4.19e-40 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 162.45 E-value: 4.19e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 106 YAYYYTGIGAGVLIVAYIQvSLW----CLAAGRQIHkirQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINEGIGDK 181
Cdd:PLN03232 952 YIVVYALLGFGQVAVTFTN-SFWlissSLHAAKRLH---DAMLNSILRAPMLFFHTNPTGRVINRFSKDIGDIDRNVANL 1027
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 182 IGMF----FQAMATFFggfIIGFTRgwklTLVILAISPVLGL--SAGIW-------AKILSSFTDKELqaYAKAGAvAEE 248
Cdd:PLN03232 1028 MNMFmnqlWQLLSTFA---LIGTVS----TISLWAIMPLLILfyAAYLYyqstsreVRRLDSVTRSPI--YAQFGE-ALN 1097
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 249 VLAAIRTVIAFGGQKKELERY--NN------NLEEAKRLGIKkaitaNISMGAAFLLIYASYAL----------AFWYGT 310
Cdd:PLN03232 1098 GLSSIRAYKAYDRMAKINGKSmdNNirftlaNTSSNRWLTIR-----LETLGGVMIWLTATFAVlrngnaenqaGFASTM 1172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 311 SLVISkeYTIgQVLTVFFSVLIGAFSVGQASPNIEAFANARGAAYEVFSIIDNKPSIDSFSKSGhkpdniqgNLEFKNIH 390
Cdd:PLN03232 1173 GLLLS--YTL-NITTLLSGVLRQASKAENSLNSVERVGNYIDLPSEATAIIENNRPVSGWPSRG--------SIKFEDVH 1241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 391 FSY-PSRKDVqiLKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRTINVRYLREIIGVVSQEP 469
Cdd:PLN03232 1242 LRYrPGLPPV--LHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSP 1319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 470 VLFATTIAENIRYGRENVTMDeIEKAVKEANAYDFIMKLPHKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEA 549
Cdd:PLN03232 1320 VLFSGTVRFNIDPFSEHNDAD-LWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEA 1398
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 550 TSALDTESEAVVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFDGGVIVEQGNHDELM-REKGIYFKLVMTQTAGNEIE 628
Cdd:PLN03232 1399 TASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLsRDTSAFFRMVHSTGPANAQY 1478
|
570
....*....|
gi 25453402 629 LGNEACESKD 638
Cdd:PLN03232 1479 LSNLVFERRE 1488
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
1041-1255 |
4.46e-40 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 148.67 E-value: 4.46e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1041 NIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIKQLNVQWlRAHLGIVSQEPILF-DCSI 1119
Cdd:COG1131 12 DKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEV-RRRIGYVPQEPALYpDLTV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1120 AENIAYGDNSRVVSHEEIVKAAKEAnIHQFidSLPEKYNTRVGdkgtQLSGGQKQRIAIARALVRQPHILLLDEATSALD 1199
Cdd:COG1131 91 RENLRFFARLYGLPRKEARERIDEL-LELF--GLTDAADRKVG----TLSGGMKQRLGLALALLHDPELLILDEPTSGLD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 25453402 1200 TESEKVVQEALDK-AREGRTCIVIAHRLSTIQN-ADLIVVIQNGQVKEHGTHQQLLAQ 1255
Cdd:COG1131 164 PEARRELWELLRElAAEGKTVLLSTHYLEEAERlCDRVAIIDKGRIVADGTPDELKAR 221
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
378-613 |
1.73e-39 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 148.22 E-value: 1.73e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 378 DNIQGNLEFKNIHFSYPSRKDvQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRTINVRY 457
Cdd:PRK13632 2 KNKSVMIKVENVSFSYPNSEN-NALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 458 LREIIGVVSQEP--VLFATTIAENIRYGREN--VTMDE----IEKAVKEANAYDFIMKLPHKfdtlvgergaqLSGGQKQ 529
Cdd:PRK13632 81 IRKKIGIIFQNPdnQFIGATVEDDIAFGLENkkVPPKKmkdiIDDLAKKVGMEDYLDKEPQN-----------LSGGQKQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 530 RIAIARALVRNPKILLLDEATSALDTESEAVVQAALDKAREGR--TTIVIAHRLSTVRNADVIAGFDGGVIVEQGNHDEL 607
Cdd:PRK13632 150 RVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRkkTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEI 229
|
....*.
gi 25453402 608 MREKGI 613
Cdd:PRK13632 230 LNNKEI 235
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1027-1258 |
2.11e-39 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 147.83 E-value: 2.11e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1027 VKFNGVMFNYPTRPNiPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIKQLNVQWLRAHLG 1106
Cdd:PRK13632 8 IKVENVSFSYPNSEN-NALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1107 IVSQEPilfD-----CSIAENIAYGDNSRVVSHEE----IVKAAKEANIHQFIDSLPEKyntrvgdkgtqLSGGQKQRIA 1177
Cdd:PRK13632 87 IIFQNP---DnqfigATVEDDIAFGLENKKVPPKKmkdiIDDLAKKVGMEDYLDKEPQN-----------LSGGQKQRVA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1178 IARALVRQPHILLLDEATSALDTESEKVVQEALDKAREGR--TCIVIAHRLSTIQNADLIVVIQNGQVKEHGTHQQLLAQ 1255
Cdd:PRK13632 153 IASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRkkTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEILNN 232
|
...
gi 25453402 1256 KGI 1258
Cdd:PRK13632 233 KEI 235
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1027-1253 |
4.58e-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: 4.58e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1027 VKFNGVMFNYPTRPnipVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIKQLNVQWLRAHLG 1106
Cdd:COG1120 2 LEAENLSVGYGGRP---VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1107 IVSQEPIL-FDCSIAENIAYG-----DNSRVVSHE--EIVKAA-KEANIHQFIDslpekynTRVgdkgTQLSGGQKQRIA 1177
Cdd:COG1120 79 YVPQEPPApFGLTVRELVALGryphlGLFGRPSAEdrEAVEEAlERTGLEHLAD-------RPV----DELSGGERQRVL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 25453402 1178 IARALVRQPHILLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLS-TIQNADLIVVIQNGQVKEHGTHQQLL 1253
Cdd:COG1120 148 IARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRlaRERGRTVVMVLHDLNlAARYADRLVLLKDGRIVAQGPPEEVL 226
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1027-1245 |
4.89e-39 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 146.39 E-value: 4.89e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1027 VKFNGVMFNYPTRPN-IPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIKQLnvqwlRAHL 1105
Cdd:COG1116 8 LELRGVSKRFPTGGGgVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGP-----GPDR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1106 GIVSQEPILFD-CSIAENIAYGDNSRVVSHEEIVKAAKEA----NIHQFIDSLPekyntrvgdkgTQLSGGQKQRIAIAR 1180
Cdd:COG1116 83 GVVFQEPALLPwLTVLDNVALGLELRGVPKAERRERARELlelvGLAGFEDAYP-----------HQLSGGMRQRVAIAR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 25453402 1181 ALVRQPHILLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAH------RLstiqnADLIVVIQN--GQVKE 1245
Cdd:COG1116 152 ALANDPEVLLMDEPFGALDALTRERLQDELLRlwQETGKTVLFVTHdvdeavFL-----ADRVVVLSArpGRIVE 221
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
703-1000 |
6.76e-39 |
|
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: 146.93 E-value: 6.76e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 703 FVVGVFCAIINGGLQPAFSIIFSKVVGVFTkndtPEIQRQNSNLFSLLFLILGIISFITFFLQGFTFGKAGEILTKRLRY 782
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLLIDDVI----PAGDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 783 MVFKSMLRQDISWFDdpKNTTGALTTRLANDAAQVKGATGSRLAVITQNIANLGTGIIISLIYGWQLTLLLLAIVPIIAI 862
Cdd:cd07346 77 DLFRHLQRLSLSFFD--RNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 863 AGVVEMKMLSGQALKDKKELEGSGKIATEAIENFRTVVSLTREQKFETMYAQSLQIPYRNALKKAHVFGITFSFTQAMMY 942
Cdd:cd07346 155 ILRYFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTA 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 25453402 943 FSYAACFRFGAYLVARELMTFENVLLVFSAIVFGAMAVGQVSSFAPDYAKAKVSASHI 1000
Cdd:cd07346 235 LGTALVLLYGGYLVLQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLERI 292
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
1027-1242 |
7.34e-39 |
|
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: 143.76 E-value: 7.34e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1027 VKFNGVMFNYPTRPNI--PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLL--ErfYDPMAGTVFLDGKeikqlnvqwlr 1102
Cdd:cd03250 1 ISVEDASFTWDSGEQEtsFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALlgE--LEKLSGSVSVPGS----------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1103 ahLGIVSQEPILFDCSIAENIAYG---DNSRVvshEEIVKAAKeanIHQFIDSLPEKYNTRVGDKGTQLSGGQKQRIAIA 1179
Cdd:cd03250 68 --IAYVSQEPWIQNGTIRENILFGkpfDEERY---EKVIKACA---LEPDLEILPDGDLTEIGEKGINLSGGQKQRISLA 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 25453402 1180 RALVRQPHILLLDEATSALDTES-----EKVVQEALdkaREGRTCIVIAHRLSTIQNADLIVVIQNGQ 1242
Cdd:cd03250 140 RAVYSDADIYLLDDPLSAVDAHVgrhifENCILGLL---LNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
1027-1243 |
7.78e-39 |
|
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: 144.17 E-value: 7.78e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1027 VKFNGVMFNYPTRPN-IPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIKQLNVQWL---- 1101
Cdd:cd03255 1 IELKNLSKTYGGGGEkVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1102 RAHLGIVSQE----PILfdcSIAENIAYGdnsrvVSHEEIVKAAKEANIHQFIDS--LPEKYNTRVGdkgtQLSGGQKQR 1175
Cdd:cd03255 81 RRHIGFVFQSfnllPDL---TALENVELP-----LLLAGVPKKERRERAEELLERvgLGDRLNHYPS----ELSGGQQQR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1176 IAIARALVRQPHILLLDEATSALDTESEKVVQEAL-DKAREGRTCIVIA-HRLSTIQNADLIVVIQNGQV 1243
Cdd:cd03255 149 VAIARALANDPKIILADEPTGNLDSETGKEVMELLrELNKEAGTTIVVVtHDPELAEYADRIIELRDGKI 218
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
385-602 |
1.19e-38 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 148.03 E-value: 1.19e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 385 EFKNIHFSYP-SRKDVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRTINVRYLREI-- 461
Cdd:PRK11153 3 ELKNISKVFPqGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKArr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 462 -IGVVSQEPVLFAT-TIAENIRYGRE--NVTMDEIEKAVKE----------ANAYdfimklPhkfdtlvgergAQLSGGQ 527
Cdd:PRK11153 83 qIGMIFQHFNLLSSrTVFDNVALPLElaGTPKAEIKARVTEllelvglsdkADRY------P-----------AQLSGGQ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 25453402 528 KQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDKA-REGRTTIV-IAHRLSTVRN-ADVIAGFDGGVIVEQG 602
Cdd:PRK11153 146 KQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDInRELGLTIVlITHEMDVVKRiCDRVAVIDAGRLVEQG 223
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1036-1248 |
1.45e-38 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 147.53 E-value: 1.45e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1036 YPTRPN-IPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQ---LLERfydPMAGTVFLDGKEIKQLNVQWLRA---HLGIV 1108
Cdd:COG1135 11 FPTKGGpVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRcinLLER---PTSGSVLVDGVDLTALSERELRAarrKIGMI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1109 SQEPILFD-CSIAENIAY-----GdnsrvVSHEEIVKAAKEanihqfidsLPEkyntRVG--DKG----TQLSGGQKQRI 1176
Cdd:COG1135 88 FQHFNLLSsRTVAENVALpleiaG-----VPKAEIRKRVAE---------LLE----LVGlsDKAdaypSQLSGGQKQRV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 25453402 1177 AIARALVRQPHILLLDEATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTIQN-ADLIVVIQNGQVKEHGT 1248
Cdd:COG1135 150 GIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRelGLTIVLITHEMDVVRRiCDRVAVLENGRIVEQGP 224
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
1027-1254 |
1.56e-38 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 144.37 E-value: 1.56e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1027 VKFNGVMFNYPTRPniPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIKQLNVQWLRAHLG 1106
Cdd:cd03295 1 IEFENVTKRYGGGK--KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1107 IVSQEPILF-DCSIAENIAYGDNSRVVSHEEIVKAAKEanIHQFIDSLPEKYNTRVGDkgtQLSGGQKQRIAIARALVRQ 1185
Cdd:cd03295 79 YVIQQIGLFpHMTVEENIALVPKLLKWPKEKIRERADE--LLALVGLDPAEFADRYPH---ELSGGQQQRVGVARALAAD 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 25453402 1186 PHILLLDEATSALDTESEKVVQEALDKARE--GRTCIVIAHRL-STIQNADLIVVIQNGQVKEHGTHQQLLA 1254
Cdd:cd03295 154 PPLLLMDEPFGALDPITRDQLQEEFKRLQQelGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEILR 225
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
384-600 |
2.21e-38 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 143.27 E-value: 2.21e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 384 LEFKNIHFSYPsrKDVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRTIN---VRYLRE 460
Cdd:COG2884 2 IRFENVSKRYP--GGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKrreIPYLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 461 IIGVVSQE-PVLFATTIAENIRY-----GRENvtmDEIEKAVKEAnaydfIMK--LPHKFDTLVgergAQLSGGQKQRIA 532
Cdd:COG2884 80 RIGVVFQDfRLLPDRTVYENVALplrvtGKSR---KEIRRRVREV-----LDLvgLSDKAKALP----HELSGGEQQRVA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 25453402 533 IARALVRNPKILLLDEATSALDTESEAVVQAALDKAREGRTTIVIA-HRLSTVRNAD--VIAgFDGGVIVE 600
Cdd:COG2884 148 IARALVNRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIAtHDLELVDRMPkrVLE-LEDGRLVR 217
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
1027-1256 |
2.98e-38 |
|
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: 144.50 E-value: 2.98e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1027 VKFNGVMFNYPtRPNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIK-QLNVQWLRAHL 1105
Cdd:TIGR04520 1 IEVENVSFSYP-ESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLdEENLWEIRKKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1106 GIVSQEPilfD----CSIAEN-IAYGDNSRVVSHEEIVK----AAKEANIHQFIDSLPEKyntrvgdkgtqLSGGQKQRI 1176
Cdd:TIGR04520 80 GMVFQNP---DnqfvGATVEDdVAFGLENLGVPREEMRKrvdeALKLVGMEDFRDREPHL-----------LSGGQKQRV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1177 AIARALVRQPHILLLDEATSALDTESEKVVQEALDKAR--EGRTCIVIAHRLSTIQNADLIVVIQNGQVKEHGTHQQLLA 1254
Cdd:TIGR04520 146 AIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNkeEGITVISITHDMEEAVLADRVIVMNKGKIVAEGTPREIFS 225
|
..
gi 25453402 1255 QK 1256
Cdd:TIGR04520 226 QV 227
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
108-341 |
3.01e-38 |
|
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: 145.35 E-value: 3.01e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 108 YYYTGIGAGVLIVA----YIQVSLWCLAAGRQIHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIG 183
Cdd:cd18573 41 KTFALALLGVFVVGaaanFGRVYLLRIAGERIVARLRKRLFKSILRQDAAFFDKNKTGELVSRLSSDTSVVGKSLTQNLS 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 184 MFFQAMATFFGGFIIGFTRGWKLTLVILAISPVLGLSAGIWAKILSSFTDKELQAYAKAGAVAEEVLAAIRTVIAFGGQK 263
Cdd:cd18573 121 DGLRSLVSGVGGIGMMLYISPKLTLVMLLVVPPIAVGAVFYGRYVRKLSKQVQDALADATKVAEERLSNIRTVRAFAAER 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 264 KELERYNNNLEEAKRLGIKKAITANISMGAAFLLIYASYALAFWYGTSLVISKEYTIGQvLTVF--FSVLIGAfSVGQAS 341
Cdd:cd18573 201 KEVERYAKKVDEVFDLAKKEALASGLFFGSTGFSGNLSLLSVLYYGGSLVASGELTVGD-LTSFlmYAVYVGS-SVSGLS 278
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
1038-1242 |
4.78e-38 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 140.40 E-value: 4.78e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1038 TRPNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIKQLN--VQWLRAHLGIVSQEPILF 1115
Cdd:cd03229 9 RYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEdeLPPLRRRIGMVFQDFALF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1116 -DCSIAENIAYGdnsrvvsheeivkaakeanihqfidslpekyntrvgdkgtqLSGGQKQRIAIARALVRQPHILLLDEA 1194
Cdd:cd03229 89 pHLTVLENIALG-----------------------------------------LSGGQQQRVALARALAMDPDVLLLDEP 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 25453402 1195 TSALDTESEKVVQEALD--KAREGRTCIVIAHRLSTIQN-ADLIVVIQNGQ 1242
Cdd:cd03229 128 TSALDPITRREVRALLKslQAQLGITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1022-1255 |
5.46e-38 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 144.00 E-value: 5.46e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1022 MLEGNVKFNGVMFNYPTRPNiPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIKQLNVQWL 1101
Cdd:PRK13635 1 MKEEIIRVEHISFRYPDAAT-YALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1102 RAHLGIVSQEPilfD-----CSIAENIAYGDNSRVVSHEEIVK----AAKEANIHQFIDSLPEKyntrvgdkgtqLSGGQ 1172
Cdd:PRK13635 80 RRQVGMVFQNP---DnqfvgATVQDDVAFGLENIGVPREEMVErvdqALRQVGMEDFLNREPHR-----------LSGGQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1173 KQRIAIARALVRQPHILLLDEATSALDTESEkvvQEALD-----KAREGRTCIVIAHRLSTIQNADLIVVIQNGQVKEHG 1247
Cdd:PRK13635 146 KQRVAIAGVLALQPDIIILDEATSMLDPRGR---REVLEtvrqlKEQKGITVLSITHDLDEAAQADRVIVMNKGEILEEG 222
|
....*...
gi 25453402 1248 THQQLLAQ 1255
Cdd:PRK13635 223 TPEEIFKS 230
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
384-554 |
8.84e-38 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 145.60 E-value: 8.84e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 384 LEFKNIHFSYpsrKDVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRTINVRYlREIiG 463
Cdd:COG3839 4 LELENVSKSY---GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKD-RNI-A 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 464 VVSQEPVLF-ATTIAENIRYG--RENVTMDEIEKAVKEANAydfIMKLPHkfdtLVGERGAQLSGGQKQRIAIARALVRN 540
Cdd:COG3839 79 MVFQSYALYpHMTVYENIAFPlkLRKVPKAEIDRRVREAAE---LLGLED----LLDRKPKQLSGGQRQRVALGRALVRE 151
|
170
....*....|....
gi 25453402 541 PKILLLDEATSALD 554
Cdd:COG3839 152 PKVFLLDEPLSNLD 165
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1043-1254 |
1.41e-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: 141.66 E-value: 1.41e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1043 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIKQLNV---QWLRAHLGIVSQEPILFDC-S 1118
Cdd:COG1127 19 VVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEkelYELRRRIGMLFQGGALFDSlT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1119 IAENIAYG-DNSRVVSHEEIVKAAKEA----NIHQFIDSLPEkyntrvgdkgtQLSGGQKQRIAIARALVRQPHILLLDE 1193
Cdd:COG1127 99 VFENVAFPlREHTDLSEAEIRELVLEKlelvGLPGAADKMPS-----------ELSGGMRKRVALARALALDPEILLYDE 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 25453402 1194 ATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTIQN-ADLIVVIQNGQVKEHGTHQQLLA 1254
Cdd:COG1127 168 PTAGLDPITSAVIDELIRELRDelGLTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPEELLA 231
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
706-998 |
1.95e-37 |
|
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: 142.70 E-value: 1.95e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 706 GVFCAIINGGLQPAFSIIFSKVVGVFTKNDtpeiQRQNSNLFSLLFLILGIISFITFFLQGFTFGKAGEILTKRLRYMVF 785
Cdd:cd18557 1 GLLFLLISSAAQLLLPYLIGRLIDTIIKGG----DLDVLNELALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 786 KSMLRQDISWFDdpKNTTGALTTRLANDAAQVKGATGSRLAVITQNIANLGTGIIISLIYGWQLTLLLLAIVPIIAIAGV 865
Cdd:cd18557 77 SSLLRQEIAFFD--KHKTGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 866 V---EMKMLSGQALkdkKELEGSGKIATEAIENFRTVVSLTREQKFETMYAQSLQIPYRNALKKAHVFGITFSFTQAMMY 942
Cdd:cd18557 155 IygrYIRKLSKEVQ---DALAKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQGITSLLIY 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 25453402 943 FSYAACFRFGAYLVAR------ELMTFenvlLVFSAIVfgAMAVGQVSSFAPDYAKAkVSAS 998
Cdd:cd18557 232 LSLLLVLWYGGYLVLSgqltvgELTSF----ILYTIMV--ASSVGGLSSLLADIMKA-LGAS 286
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1028-1242 |
4.45e-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: 136.99 E-value: 4.45e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1028 KFNGVMFNYPTRPnipVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIKQLNVQWLRAHLGI 1107
Cdd:cd00267 1 EIENLSFRYGGRT---ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1108 VSQepilfdcsiaeniaygdnsrvvsheeivkaakeanihqfidslpekyntrvgdkgtqLSGGQKQRIAIARALVRQPH 1187
Cdd:cd00267 78 VPQ---------------------------------------------------------LSGGQRQRVALARALLLNPD 100
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 25453402 1188 ILLLDEATSALDTESEKVVQEALDK-AREGRTCIVIAHRLSTIQNA-DLIVVIQNGQ 1242
Cdd:cd00267 101 LLLLDEPTSGLDPASRERLLELLRElAEEGRTVIIVTHDPELAELAaDRVIVLKDGK 157
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
384-598 |
5.73e-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: 137.14 E-value: 5.73e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 384 LEFKNIHFSYpsrKDVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRTiNVRYLREIIG 463
Cdd:cd03230 1 IEVRNLSKRY---GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 464 VVSQEPVLFAT-TIAENIRYgrenvtmdeiekavkeanaydfimklphkfdtlvgergaqlSGGQKQRIAIARALVRNPK 542
Cdd:cd03230 77 YLPEEPSLYENlTVRENLKL-----------------------------------------SGGMKQRLALAQALLHDPE 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 25453402 543 ILLLDEATSALDTESEAVVQAALDK-AREGRTTIVIAHRLSTVRN-ADVIAGFDGGVI 598
Cdd:cd03230 116 LLILDEPTSGLDPESRREFWELLRElKKEGKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
384-590 |
6.46e-37 |
|
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: 138.37 E-value: 6.46e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 384 LEFKNIHFSYPSRKDVQ--ILKGLNLKVKSGQTVALVGNSGCGKSTtvqLLQRL---YDPIEGEVSIDGQdirtinvryl 458
Cdd:cd03250 1 ISVEDASFTWDSGEQETsfTLKDINLEVPKGELVAIVGPVGSGKSS---LLSALlgeLEKLSGSVSVPGS---------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 459 reiIGVVSQEPVLFATTIAENIRYGREnvtMDEIE-KAVKEANA--YDFIMkLPHKFDTLVGERGAQLSGGQKQRIAIAR 535
Cdd:cd03250 68 ---IAYVSQEPWIQNGTIRENILFGKP---FDEERyEKVIKACAlePDLEI-LPDGDLTEIGEKGINLSGGQKQRISLAR 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 536 ALVRNPKILLLDEATSALDTESEA-----VVQAALdkaREGRTTIVIAHRLSTVRNADVI 590
Cdd:cd03250 141 AVYSDADIYLLDDPLSAVDAHVGRhifenCILGLL---LNNKTRILVTHQLQLLPHADQI 197
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
399-610 |
6.93e-37 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 142.18 E-value: 6.93e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 399 VQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRTINVRYLREI---IGVVSQEPvlFA-- 473
Cdd:COG4608 31 VKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELRPLrrrMQMVFQDP--YAsl 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 474 -------TTIAENIRYgRENVTMDEIEKAVKEA------NAyDFIMKLPHKFdtlvgergaqlSGGQKQRIAIARALVRN 540
Cdd:COG4608 109 nprmtvgDIIAEPLRI-HGLASKAERRERVAELlelvglRP-EHADRYPHEF-----------SGGQRQRIGIARALALN 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 25453402 541 PKILLLDEATSALDteseaV-VQAA-----LD-KAREGRTTIVIAHRLSTVRN-ADVIAGFDGGVIVEQGNHDELMRE 610
Cdd:COG4608 176 PKLIVCDEPVSALD-----VsIQAQvlnllEDlQDELGLTYLFISHDLSVVRHiSDRVAVMYLGKIVEIAPRDELYAR 248
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
1043-1263 |
8.48e-37 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 140.04 E-value: 8.48e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1043 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIKQLNVQWLRAHLGIVSQEPILFDCSIAEN 1122
Cdd:cd03288 35 PVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFN 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1123 IaygDNSRVVSHEEIVKAAKEANIHQFIDSLPEKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTES 1202
Cdd:cd03288 115 L---DPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMAT 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 25453402 1203 EKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIQNGQVKEHGTHQQLLAQK-GIYFSMV 1263
Cdd:cd03288 192 ENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEdGVFASLV 253
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
384-599 |
8.51e-37 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 139.42 E-value: 8.51e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 384 LEFKNIHFSYPSrkDVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRTINVRYLREI-- 461
Cdd:COG3638 3 LELRNLSKRYPG--GTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRLrr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 462 -IGVVSQEPVLFA-TTIAENI---RYGREN--------VTMDEIEKAvkeanaYDFIMK--LPHKFDtlvgERGAQLSGG 526
Cdd:COG3638 81 rIGMIFQQFNLVPrLSVLTNVlagRLGRTStwrsllglFPPEDRERA------LEALERvgLADKAY----QRADQLSGG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 25453402 527 QKQRIAIARALVRNPKILLLDEATSALDTE-SEAVVQAALDKARE-GRTTIVIAHRLSTVRN-ADVIAGFDGGVIV 599
Cdd:COG3638 151 QQQRVAIARALVQEPKLILADEPVASLDPKtARQVMDLLRRIAREdGITVVVNLHQVDLARRyADRIIGLRDGRVV 226
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
384-607 |
9.14e-37 |
|
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: 139.24 E-value: 9.14e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 384 LEFKNIHFSYPSrkDVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRTINVRYLREI-- 461
Cdd:cd03256 1 IEVENLSKTYPN--GKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLrr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 462 -IGVVSQEPVLFA-TTIAENIRYGR-----------ENVTMDEIEKAVKEANAYDFimklphkfDTLVGERGAQLSGGQK 528
Cdd:cd03256 79 qIGMIFQQFNLIErLSVLENVLSGRlgrrstwrslfGLFPKEEKQRALAALERVGL--------LDKAYQRADQLSGGQQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 529 QRIAIARALVRNPKILLLDEATSALDTE-SEAVVQAALDKARE-GRTTIVIAHRLSTVR-NADVIAGFDGGVIVEQGNHD 605
Cdd:cd03256 151 QRVAIARALMQQPKLILADEPVASLDPAsSRQVMDLLKRINREeGITVIVSLHQVDLAReYADRIVGLKDGRIVFDGPPA 230
|
..
gi 25453402 606 EL 607
Cdd:cd03256 231 EL 232
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
1027-1254 |
9.82e-37 |
|
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: 9.82e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1027 VKFNGVMFNYPTRPnipVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIKQLNV---QWLRA 1103
Cdd:cd03261 1 IELRGLTKSFGGRT---VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEaelYRLRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1104 HLGIVSQEPILFDC-SIAENIAYG--DNSRvVSHEEIVKAAKE----ANIHQFIDSLPEkyntrvgdkgtQLSGGQKQRI 1176
Cdd:cd03261 78 RMGMLFQSGALFDSlTVFENVAFPlrEHTR-LSEEEIREIVLEkleaVGLRGAEDLYPA-----------ELSGGMKKRV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1177 AIARALVRQPHILLLDEATSALD-TESEKVVQEALD-KAREGRTCIVIAHRLSTI-QNADLIVVIQNGQVKEHGTHQQLL 1253
Cdd:cd03261 146 ALARALALDPELLLYDEPTAGLDpIASGVIDDLIRSlKKELGLTSIMVTHDLDTAfAIADRIAVLYDGKIVAEGTPEELR 225
|
.
gi 25453402 1254 A 1254
Cdd:cd03261 226 A 226
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1041-1257 |
1.06e-36 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 139.22 E-value: 1.06e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1041 NIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIKQLNvQWLRAHLGIVSQEPILFD-CSI 1119
Cdd:COG4555 13 KVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEP-REARRQIGVLPDERGLYDrLTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1120 AENIAYGDNSRVVSHEEIVKAAKEAnIHQFIdsLPEKYNTRVGDkgtqLSGGQKQRIAIARALVRQPHILLLDEATSALD 1199
Cdd:COG4555 92 RENIRYFAELYGLFDEELKKRIEEL-IELLG--LEEFLDRRVGE----LSTGMKKKVALARALVHDPKVLLLDEPTNGLD 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1200 TESEKVVQEALDKAREGRTCIVIA-HRLSTIQN-ADLIVVIQNGQVKEHGTHQQLLAQKG 1257
Cdd:COG4555 165 VMARRLLREILRALKKEGKTVLFSsHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEIG 224
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1044-1252 |
3.32e-36 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 138.25 E-value: 3.32e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1044 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYD--P---MAGTVFLDGKEI--KQLNVQWLRAHLGIVSQEPILFD 1116
Cdd:COG1117 26 ALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDliPgarVEGEILLDGEDIydPDVDVVELRRRVGMVFQKPNPFP 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1117 CSIAENIAYG-----DNSRVVsHEEIVKAA-KEANihqfidsLPEKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILL 1190
Cdd:COG1117 106 KSIYDNVAYGlrlhgIKSKSE-LDEIVEESlRKAA-------LWDEVKDRLKKSALGLSGGQQQRLCIARALAVEPEVLL 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 25453402 1191 LDEATSALDTESEKVVQEALDKAREgRTCIVI-------AHRLStiqnaDLIVVIQNGQVKEHGTHQQL 1252
Cdd:COG1117 178 MDEPTSALDPISTAKIEELILELKK-DYTIVIvthnmqqAARVS-----DYTAFFYLGELVEFGPTEQI 240
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
384-610 |
3.97e-36 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 137.53 E-value: 3.97e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 384 LEFKNIHFSYPSRkdvQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRTINVRylreiIG 463
Cdd:COG1121 7 IELENLTVSYGGR---PVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRR-----IG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 464 VVSQEPVL---FATTIAENI---RYGRENVTM-------DEIEKAVKEANAYDFImklphkfDTLVGErgaqLSGGQKQR 530
Cdd:COG1121 79 YVPQRAEVdwdFPITVRDVVlmgRYGRRGLFRrpsradrEAVDEALERVGLEDLA-------DRPIGE----LSGGQQQR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 531 IAIARALVRNPKILLLDEATSALDTESEAVVQAALDK-AREGRTTIVIAHRLSTVR-NADVIAGFDGGVIVEqGNHDELM 608
Cdd:COG1121 148 VLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRElRREGKTILVVTHDLGAVReYFDRVLLLNRGLVAH-GPPEEVL 226
|
..
gi 25453402 609 RE 610
Cdd:COG1121 227 TP 228
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
50-354 |
9.59e-36 |
|
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: 138.00 E-value: 9.59e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 50 MLLGTLAaiihGIALPLMMlvfGDMTDSfANVGNNRSmsfynatdiyakledEMTTYAYYYTGIGAGVLIVAYIQVSLWC 129
Cdd:cd18576 5 LLLSSAI----GLVFPLLA---GQLIDA-ALGGGDTA---------------SLNQIALLLLGLFLLQAVFSFFRIYLFA 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 130 LAAGRQIHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFFQAMATFFGGFIIGFTRGWKLTLV 209
Cdd:cd18576 62 RVGERVVADLRKDLYRHLQRLPLSFFHERRVGELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWKLTLL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 210 ILAISPVLGLSAGIWAKILSSFTDKELQAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNNNLEEAKRLGIKKAITANI 289
Cdd:cd18576 142 MLATVPVVVLVAVLFGRRIRKLSKKVQDELAEANTIVEETLQGIRVVKAFTREDYEIERYRKALERVVKLALKRARIRAL 221
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 25453402 290 SMGAAFLLIYASYALAFWYGTSLVISKEYTIGQVLT-VFFSVLIGAfSVGQASPNIEAFANARGAA 354
Cdd:cd18576 222 FSSFIIFLLFGAIVAVLWYGGRLVLAGELTAGDLVAfLLYTLFIAG-SIGSLADLYGQLQKALGAS 286
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
1049-1255 |
1.65e-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: 136.62 E-value: 1.65e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1049 SLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIKQLNVQWLRA----HLGIVSQEPILF-DCSIAENI 1123
Cdd:cd03294 44 SLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRElrrkKISMVFQSFALLpHRTVLENV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1124 AYGDNSRVVSHEEIVKAAKEA----NIHQFIDSLPekyntrvgdkgTQLSGGQKQRIAIARALVRQPHILLLDEATSALD 1199
Cdd:cd03294 124 AFGLEVQGVPRAEREERAAEAlelvGLEGWEHKYP-----------DELSGGMQQRVGLARALAVDPDILLMDEAFSALD 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 25453402 1200 TESEKVVQEALDK--AREGRTCIVIAHRLS-TIQNADLIVVIQNGQVKEHGTHQQLLAQ 1255
Cdd:cd03294 193 PLIRREMQDELLRlqAELQKTIVFITHDLDeALRLGDRIAIMKDGRLVQVGTPEEILTN 251
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
406-610 |
1.91e-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: 136.23 E-value: 1.91e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 406 NLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRTINVRYLREI----IGVVSQEPVLFA-TTIAENI 480
Cdd:cd03294 44 SLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELrrkkISMVFQSFALLPhRTVLENV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 481 RYGRENVTMDEIEKAVKEANAY------DFIMKLPHkfdtlvgergaQLSGGQKQRIAIARALVRNPKILLLDEATSALD 554
Cdd:cd03294 124 AFGLEVQGVPRAEREERAAEALelvgleGWEHKYPD-----------ELSGGMQQRVGLARALAVDPDILLMDEAFSALD 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 25453402 555 TESEAVVQAALDK--AREGRTTIVIAHRLS-TVRNADVIAGFDGGVIVEQGNHDELMRE 610
Cdd:cd03294 193 PLIRREMQDELLRlqAELQKTIVFITHDLDeALRLGDRIAIMKDGRLVQVGTPEEILTN 251
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
384-608 |
3.82e-35 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 134.45 E-value: 3.82e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 384 LEFKNI--HFSypsrkDVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIR--TINVRYLR 459
Cdd:PRK09493 2 IEFKNVskHFG-----PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpKVDERLIR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 460 EIIGVVSQEPVLFATTIA-ENIRYGRENVtmdeieKAVKEANAYDFIMKLPHKfdtlVG--ERG----AQLSGGQKQRIA 532
Cdd:PRK09493 77 QEAGMVFQQFYLFPHLTAlENVMFGPLRV------RGASKEEAEKQARELLAK----VGlaERAhhypSELSGGQQQRVA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 25453402 533 IARALVRNPKILLLDEATSALDTE-SEAVVQAALDKAREGRTTIVIAHRLSTVRN-ADVIAGFDGGVIVEQGNHDELM 608
Cdd:PRK09493 147 IARALAVKPKLMLFDEPTSALDPElRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKvASRLIFIDKGRIAEDGDPQVLI 224
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
106-625 |
4.17e-35 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 146.42 E-value: 4.17e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 106 YAYYYTGIGAGVLIVAYIQvSLW----CLAAGRQIHkirQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINEGIGDK 181
Cdd:PLN03130 955 YNLIYALLSFGQVLVTLLN-SYWlimsSLYAAKRLH---DAMLGSILRAPMSFFHTNPLGRIINRFAKDLGDIDRNVAVF 1030
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 182 IGMF----FQAMATFFggfIIGFTRgwklTLVILAISPVLGLSAGIW---------AKILSSFTDKELqaYAKAGAvAEE 248
Cdd:PLN03130 1031 VNMFlgqiFQLLSTFV---LIGIVS----TISLWAIMPLLVLFYGAYlyyqstareVKRLDSITRSPV--YAQFGE-ALN 1100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 249 VLAAIRTVIAF------GGQKKEleryNN------NLEEAKRLGIKKAitaniSMGAAFLLIYASYAL----------AF 306
Cdd:PLN03130 1101 GLSTIRAYKAYdrmaeiNGRSMD----NNirftlvNMSSNRWLAIRLE-----TLGGLMIWLTASFAVmqngraenqaAF 1171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 307 WYGTSLVISKEYTIGQVLTvffSVLIGAfSVGQASPN-IEAFANARGAAYEVFSIIDNkpsidsfsksgHKPDN---IQG 382
Cdd:PLN03130 1172 ASTMGLLLSYALNITSLLT---AVLRLA-SLAENSLNaVERVGTYIDLPSEAPLVIEN-----------NRPPPgwpSSG 1236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 383 NLEFKNIHFSYpsRKDVQ-ILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRTINVRYLREI 461
Cdd:PLN03130 1237 SIKFEDVVLRY--RPELPpVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKV 1314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 462 IGVVSQEPVLFATTIAENIRYGRENVTMDEIEkAVKEANAYDFIMKLPHKFDTLVGERGAQLSGGQKQRIAIARALVRNP 541
Cdd:PLN03130 1315 LGIIPQAPVLFSGTVRFNLDPFNEHNDADLWE-SLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRS 1393
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 542 KILLLDEATSALDTESEAVVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFDGGVIVEQGNHDEL-MREKGIYFKLVMT 620
Cdd:PLN03130 1394 KILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLlSNEGSAFSKMVQS 1473
|
....*
gi 25453402 621 QTAGN 625
Cdd:PLN03130 1474 TGAAN 1478
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1027-1247 |
5.61e-35 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 133.25 E-value: 5.61e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1027 VKFNGVMFNYPtrPNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIKQLN---VQWLRA 1103
Cdd:COG2884 2 IRFENVSKRYP--GGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKrreIPYLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1104 HLGIVSQE-PILFDCSIAENIAY-----GdnsrvVSHEEIVKAAKEA----NIHQFIDSLPEkyntrvgdkgtQLSGGQK 1173
Cdd:COG2884 80 RIGVVFQDfRLLPDRTVYENVALplrvtG-----KSRKEIRRRVREVldlvGLSDKAKALPH-----------ELSGGEQ 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 25453402 1174 QRIAIARALVRQPHILLLDEATSALDTE-SEKVVqEALDKAREGRTCIVIA-HRLSTIQNADL-IVVIQNGQVKEHG 1247
Cdd:COG2884 144 QRVAIARALVNRPELLLADEPTGNLDPEtSWEIM-ELLEEINRRGTTVLIAtHDLELVDRMPKrVLELEDGRLVRDE 219
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
401-620 |
6.30e-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: 134.65 E-value: 6.30e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 401 ILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRTINVRYLREIIGVVSQEPVLFATTIAENI 480
Cdd:cd03288 36 VLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 481 RYGREnVTMDEIEKAVKEANAYDFIMKLPHKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAV 560
Cdd:cd03288 116 DPECK-CTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENI 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 25453402 561 VQAALDKAREGRTTIVIAHRLSTVRNADVIAGFDGGVIVEQGNHDELM-REKGIYFKLVMT 620
Cdd:cd03288 195 LQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLaQEDGVFASLVRT 255
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
387-579 |
8.72e-35 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 132.38 E-value: 8.72e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 387 KNIHFSYpsRKDVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIrtiNVRYLREIIGVVS 466
Cdd:cd03226 3 ENISFSY--KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPI---KAKERRKSIGYVM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 467 QEP--VLFATTIAENIRYGRENVTMD--EIEKAVKEANAYDFIMKLPHkfdtlvgergaQLSGGQKQRIAIARALVRNPK 542
Cdd:cd03226 78 QDVdyQLFTDSVREELLLGLKELDAGneQAETVLKDLDLYALKERHPL-----------SLSGGQKQRLAIAAALLSGKD 146
|
170 180 190
....*....|....*....|....*....|....*...
gi 25453402 543 ILLLDEATSALDTES-EAVVQAALDKAREGRTTIVIAH 579
Cdd:cd03226 147 LLIFDEPTSGLDYKNmERVGELIRELAAQGKAVIVITH 184
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
384-611 |
1.54e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 134.05 E-value: 1.54e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 384 LEFKNIHFSYPsrKDVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRTINVRYL--REI 461
Cdd:PRK13639 2 LETRDLKYSYP--DGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLevRKT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 462 IGVVSQEP--VLFATTIAENIRYGRENV--TMDEIEKAVKEA----NAYDFIMKLPHkfdtlvgergaQLSGGQKQRIAI 533
Cdd:PRK13639 80 VGIVFQNPddQLFAPTVEEDVAFGPLNLglSKEEVEKRVKEAlkavGMEGFENKPPH-----------HLSGGQKKRVAI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 534 ARALVRNPKILLLDEATSALDTE-SEAVVQAALDKAREGRTTIVIAHRLSTV-RNADVIAGFDGGVIVEQGNHDELMREK 611
Cdd:PRK13639 149 AGILAMKPEIIVLDEPTSGLDPMgASQIMKLLYDLNKEGITIIISTHDVDLVpVYADKVYVMSDGKIIKEGTPKEVFSDI 228
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
1027-1243 |
2.09e-34 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 132.49 E-value: 2.09e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1027 VKFNGVMFNYPTRPniPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIKQLN---VQWLRA 1103
Cdd:COG3638 3 LELRNLSKRYPGGT--PALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRgraLRRLRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1104 HLGIVSQEPILFD-CSIAENI---AYGDNS------RVVSHEEIVKAakeaniHQFIDS--LPEKYNTRVGdkgtQLSGG 1171
Cdd:COG3638 81 RIGMIFQQFNLVPrLSVLTNVlagRLGRTStwrsllGLFPPEDRERA------LEALERvgLADKAYQRAD----QLSGG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 25453402 1172 QKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEAL-DKARE-GRTCIVIAHRLSTIQN-ADLIVVIQNGQV 1243
Cdd:COG3638 151 QQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLrRIAREdGITVVVNLHQVDLARRyADRIIGLRDGRV 225
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
384-609 |
2.32e-34 |
|
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: 139.82 E-value: 2.32e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 384 LEFKNIHFSYPSRK--------DVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLyDPIEGEVSIDGQDIRTIN- 454
Cdd:COG4172 276 LEARDLKVWFPIKRglfrrtvgHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRL-IPSEGEIRFDGQDLDGLSr 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 455 --VRYLREIIGVVSQEPvlFAT-----TIAENIRYG----RENVTMDEIEKAVKEA-----------NAYdfimklPHKF 512
Cdd:COG4172 355 raLRPLRRRMQVVFQDP--FGSlsprmTVGQIIAEGlrvhGPGLSAAERRARVAEAleevgldpaarHRY------PHEF 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 513 dtlvgergaqlSGGQKQRIAIARALVRNPKILLLDEATSALDteseAVVQAA-LD-----KAREGRTTIVIAHRLSTVRN 586
Cdd:COG4172 427 -----------SGGQRQRIAIARALILEPKLLVLDEPTSALD----VSVQAQiLDllrdlQREHGLAYLFISHDLAVVRA 491
|
250 260
....*....|....*....|....
gi 25453402 587 -ADVIAGFDGGVIVEQGNHDELMR 609
Cdd:COG4172 492 lAHRVMVMKDGKVVEQGPTEQVFD 515
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
1044-1243 |
2.79e-34 |
|
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: 131.11 E-value: 2.79e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1044 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIKQLNVQW--LRAHLGIVSQEPILF-DCSIA 1120
Cdd:cd03262 15 VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNIneLRQKVGMVFQQFNLFpHLTVL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1121 ENIAYGdnSRVVSHEEIVKAAKEAnihqfidslpEKYNTRVG--DKGT----QLSGGQKQRIAIARALVRQPHILLLDEA 1194
Cdd:cd03262 95 ENITLA--PIKVKGMSKAEAEERA----------LELLEKVGlaDKADaypaQLSGGQQQRVAIARALAMNPKVMLFDEP 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 25453402 1195 TSALDTEsekVVQEALDK----AREGRTCIVIAHRLSTIQN-ADLIVVIQNGQV 1243
Cdd:cd03262 163 TSALDPE---LVGEVLDVmkdlAEEGMTMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
384-578 |
3.07e-34 |
|
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: 130.99 E-value: 3.07e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 384 LEFKNIHFSYPSrkDVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDI---RTINVRYLRE 460
Cdd:cd03292 1 IEFINVTKTYPN--GTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVsdlRGRAIPYLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 461 IIGVVSQEPVLFAT-TIAENIRYGRE--NVTMDEIEKAVKEANAydfIMKLPHKFDTLvgerGAQLSGGQKQRIAIARAL 537
Cdd:cd03292 79 KIGVVFQDFRLLPDrNVYENVAFALEvtGVPPREIRKRVPAALE---LVGLSHKHRAL----PAELSGGEQQRVAIARAI 151
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 25453402 538 VRNPKILLLDEATSALDTESEAVVQAALDKAREGRTTIVIA 578
Cdd:cd03292 152 VNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVA 192
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
1044-1253 |
4.54e-34 |
|
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: 131.30 E-value: 4.54e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1044 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIKQLNVQwlRAHLGIVSQEPILF-DCSIAEN 1122
Cdd:cd03299 14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE--KRDISYVPQNYALFpHMTVYKN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1123 IAYG----DNSRVVSHEEIVKAAKEANIHQFIDSLPEKyntrvgdkgtqLSGGQKQRIAIARALVRQPHILLLDEATSAL 1198
Cdd:cd03299 92 IAYGlkkrKVDKKEIERKVLEIAEMLGIDHLLNRKPET-----------LSGGEQQRVAIARALVVNPKILLLDEPFSAL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 25453402 1199 DTESEKVVQEALDKARE--GRTCIVIAHRLSTIQN-ADLIVVIQNGQVKEHGTHQQLL 1253
Cdd:cd03299 161 DVRTKEKLREELKKIRKefGVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEVF 218
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
385-602 |
4.98e-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: 129.09 E-value: 4.98e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 385 EFKNIHFSYPSRkdvQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRTINVRYLREIIGV 464
Cdd:cd03214 1 EVENLSVGYGGR---TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 465 VSQepvlfattiaenirygrenvtmdeiekAVKEANAYDFIMKLphkFDTlvgergaqLSGGQKQRIAIARALVRNPKIL 544
Cdd:cd03214 78 VPQ---------------------------ALELLGLAHLADRP---FNE--------LSGGERQRVLLARALAQEPPIL 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 25453402 545 LLDEATSALDTESE-AVVQAALDKARE-GRTTIVIAHRLS-TVRNADVIAGFDGGVIVEQG 602
Cdd:cd03214 120 LLDEPTSHLDIAHQiELLELLRRLARErGKTVVMVLHDLNlAARYADRVILLKDGRIVAQG 180
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1038-1255 |
7.69e-34 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 134.12 E-value: 7.69e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1038 TRPNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQL---LERfydPMAGTVFLDGKEIK-QLNVQwlRAHLGIVSQEPI 1113
Cdd:COG1118 11 RFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIiagLET---PDSGRIVLNGRDLFtNLPPR--ERRVGFVFQHYA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1114 LF-DCSIAENIAYGDNSRVVSHEEIVKAAKE----ANIHQFIDSLPekyntrvgdkgTQLSGGQKQRIAIARALVRQPHI 1188
Cdd:COG1118 86 LFpHMTVAENIAFGLRVRPPSKAEIRARVEEllelVQLEGLADRYP-----------SQLSGGQRQRVALARALAVEPEV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 25453402 1189 LLLDEATSALDT----ESEKVVQEALDkaREGRTCIVIAH------RLstiqnADLIVVIQNGQVKEHGTHQQLLAQ 1255
Cdd:COG1118 155 LLLDEPFGALDAkvrkELRRWLRRLHD--ELGGTTVFVTHdqeealEL-----ADRVVVMNQGRIEQVGTPDEVYDR 224
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
384-609 |
1.03e-33 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 131.68 E-value: 1.03e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 384 LEFKNIHFSYPSRKDvQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRTINVRYLREIIG 463
Cdd:PRK13635 6 IRVEHISFRYPDAAT-YALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 464 VVSQEP--VLFATTIAENIRYGREN--VTMDE----IEKAVKEANAYDFIMKLPHKfdtlvgergaqLSGGQKQRIAIAR 535
Cdd:PRK13635 85 MVFQNPdnQFVGATVQDDVAFGLENigVPREEmverVDQALRQVGMEDFLNREPHR-----------LSGGQKQRVAIAG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 25453402 536 ALVRNPKILLLDEATSALDTESEAVVQAALD--KAREGRTTIVIAHRLSTVRNADVIAGFDGGVIVEQGNHDELMR 609
Cdd:PRK13635 154 VLALQPDIIILDEATSMLDPRGRREVLETVRqlKEQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFK 229
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1027-1255 |
1.16e-33 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 130.21 E-value: 1.16e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1027 VKFNGVMFNYPTRPnipVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIKQLnvqwlRAHLG 1106
Cdd:COG1121 7 IELENLTVSYGGRP---VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA-----RRRIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1107 IVSQE-------PIlfdcSIAENIAYGDNSRV--------VSHEEIVKAAKEANIHQFIDslpekynTRVGdkgtQLSGG 1171
Cdd:COG1121 79 YVPQRaevdwdfPI----TVRDVVLMGRYGRRglfrrpsrADREAVDEALERVGLEDLAD-------RPIG----ELSGG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1172 QKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDK-AREGRTCIVIAHRLSTI-QNADLIVVIqNGQVKEHGTH 1249
Cdd:COG1121 144 QQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRElRREGKTILVVTHDLGAVrEYFDRVLLL-NRGLVAHGPP 222
|
....*.
gi 25453402 1250 QQLLAQ 1255
Cdd:COG1121 223 EEVLTP 228
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
385-598 |
1.47e-33 |
|
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: 128.81 E-value: 1.47e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 385 EFKNIHFSYPSRKdvqILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQdirtiNVRYLREIIGV 464
Cdd:cd03235 1 EVEDLTVSYGGHP---VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGK-----PLEKERKRIGY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 465 VSQEPVL---FATTIAENIRYGREN----------VTMDEIEKAVKEANAYDFImklphkfDTLVGErgaqLSGGQKQRI 531
Cdd:cd03235 73 VPQRRSIdrdFPISVRDVVLMGLYGhkglfrrlskADKAKVDEALERVGLSELA-------DRQIGE----LSGGQQQRV 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 25453402 532 AIARALVRNPKILLLDEATSALDTESEAVVQAALDK-AREGRTTIVIAHRLSTV-RNADVIAGFDGGVI 598
Cdd:cd03235 142 LLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRElRREGMTILVVTHDLGLVlEYFDRVLLLNRTVV 210
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
384-609 |
1.64e-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: 1.64e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 384 LEFKNIHFSYPSRkdvQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRT-INVRYLReiI 462
Cdd:COG1118 3 IEVRNISKRFGSF---TLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTnLPPRERR--V 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 463 GVVSQEPVLFA-TTIAENIRYG--RENVTMDEIEKAVKE----------ANAYdfimklPHkfdtlvgergaQLSGGQKQ 529
Cdd:COG1118 78 GFVFQHYALFPhMTVAENIAFGlrVRPPSKAEIRARVEEllelvqleglADRY------PS-----------QLSGGQRQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 530 RIAIARALVRNPKILLLDEATSALDT----ESEAVVQAALDkaREGRTTIVIAH-RLSTVRNADVIAGFDGGVIVEQGNH 604
Cdd:COG1118 141 RVALARALAVEPEVLLLDEPFGALDAkvrkELRRWLRRLHD--ELGGTTVFVTHdQEEALELADRVVVMNQGRIEQVGTP 218
|
....*
gi 25453402 605 DELMR 609
Cdd:COG1118 219 DEVYD 223
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
706-999 |
2.31e-33 |
|
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: 131.22 E-value: 2.31e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 706 GVFCAIINGGLQPAFSIIFSKVVGVFTKNDTPEIQRQNSNLFSLLFLILGIISF--ITFFLQGFTFGKAGEILTKRLRYM 783
Cdd:cd18780 1 GTIALLVSSGTNLALPYFFGQVIDAVTNHSGSGGEEALRALNQAVLILLGVVLIgsIATFLRSWLFTLAGERVVARLRKR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 784 VFKSMLRQDISWFDdpKNTTGALTTRLANDAAQVKGATGSRLAVITQNIANLGTGIIISLIYGWQLTLLLLAIVPIIAIA 863
Cdd:cd18780 81 LFSAIIAQEIAFFD--VTRTGELLNRLSSDTQVLQNAVTVNLSMLLRYLVQIIGGLVFMFTTSWKLTLVMLSVVPPLSIG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 864 GVVEMKMLSGQALKDKKELEGSGKIATEAIENFRTVVSLTREQKFETMYAQSLQIPYRNALKKAHVFGITFSFTQAMMYF 943
Cdd:cd18780 159 AVIYGKYVRKLSKKFQDALAAASTVAEESISNIRTVRSFAKETKEVSRYSEKINESYLLGKKLARASGGFNGFMGAAAQL 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 25453402 944 SYAACFRFGAYLV------ARELMTFenVLLVFSAivfgAMAVGQVSSFAPDYAKAkVSASH 999
Cdd:cd18780 239 AIVLVLWYGGRLVidgeltTGLLTSF--LLYTLTV----AMSFAFLSSLYGDFMQA-VGASV 293
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1027-1255 |
2.50e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 130.62 E-value: 2.50e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1027 VKFNGVMFNYPTRPNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIKQLNVQWLRAHLG 1106
Cdd:PRK13650 5 IEVKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1107 IVSQEP--ILFDCSIAENIAYGDNSRVVSHEEIVKAAKEA----NIHQFIDSLPEKyntrvgdkgtqLSGGQKQRIAIAR 1180
Cdd:PRK13650 85 MVFQNPdnQFVGATVEDDVAFGLENKGIPHEEMKERVNEAlelvGMQDFKEREPAR-----------LSGGQKQRVAIAG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 25453402 1181 ALVRQPHILLLDEATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTIQNADLIVVIQNGQVKEHGTHQQLLAQ 1255
Cdd:PRK13650 154 AVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDdyQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFSR 230
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
384-607 |
2.81e-33 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 129.51 E-value: 2.81e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 384 LEFKNIHFSYPSRKdvqILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYD-----PIEGEVSIDGQDI---RTINV 455
Cdd:PRK14239 6 LQVSDLSVYYNKKK---ALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnpevTITGSIVYNGHNIyspRTDTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 456 RyLREIIGVVSQEPVLFATTIAENIRYG------RENVTMDE-IEKAVKEANAYDFIMKLPHkfDTLVGergaqLSGGQK 528
Cdd:PRK14239 83 D-LRKEIGMVFQQPNPFPMSIYENVVYGlrlkgiKDKQVLDEaVEKSLKGASIWDEVKDRLH--DSALG-----LSGGQQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 529 QRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDKAREGRTTIVIAHRLSTV-RNADVIAGFDGGVIVEQGNHDEL 607
Cdd:PRK14239 155 QRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQAsRISDRTGFFLDGDLIEYNDTKQM 234
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
384-590 |
3.14e-33 |
|
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: 127.60 E-value: 3.14e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 384 LEFKNIHFSYPSRkdvQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRTINVRYlREIIG 463
Cdd:COG4133 3 LEAENLSCRRGER---LLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDY-RRRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 464 VVSQEPVLFAT-TIAENIR-----YGREnVTMDEIEKAVKEanaydfiMKLPHKFDTLVGergaQLSGGQKQRIAIARAL 537
Cdd:COG4133 79 YLGHADGLKPElTVRENLRfwaalYGLR-ADREAIDEALEA-------VGLAGLADLPVR----QLSAGQKRRVALARLL 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 25453402 538 VRNPKILLLDEATSALDTESEAVVQAALDKAREGRTTIVIA-HRLSTVRNADVI 590
Cdd:COG4133 147 LSPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTtHQPLELAAARVL 200
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
384-602 |
6.00e-33 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 129.00 E-value: 6.00e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 384 LEFKNIHFSYPSRKdvqILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDpIEGEVSIDG------QDI--RTINV 455
Cdd:PRK14258 8 IKVNNLSFYYDTQK---ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNE-LESEVRVEGrveffnQNIyeRRVNL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 456 RYLREIIGVVSQEPVLFATTIAENIRYG------RENVTMDEI-EKAVKEANAYDFIMKLPHKfdtlvgeRGAQLSGGQK 528
Cdd:PRK14258 84 NRLRRQVSMVHPKPNLFPMSVYDNVAYGvkivgwRPKLEIDDIvESALKDADLWDEIKHKIHK-------SALDLSGGQQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 529 QRIAIARALVRNPKILLLDEATSALDTESEAVVQAALD--KAREGRTTIVIAHRLSTV-RNADVIAGFDG-----GVIVE 600
Cdd:PRK14258 157 QRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQslRLRSELTMVIVSHNLHQVsRLSDFTAFFKGnenriGQLVE 236
|
..
gi 25453402 601 QG 602
Cdd:PRK14258 237 FG 238
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
719-987 |
6.01e-33 |
|
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: 129.94 E-value: 6.01e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 719 AFSIIFSKVVGVFTKNDT-PEIQRQNSNLFSLLFLILGIISFITFFLQGFTFGKAGEILTKRLRYMVFKSMLRQDISWFD 797
Cdd:cd18573 14 SVPFAIGKLIDVASKESGdIEIFGLSLKTFALALLGVFVVGAAANFGRVYLLRIAGERIVARLRKRLFKSILRQDAAFFD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 798 dpKNTTGALTTRLANDAAQVKGATGSRLAVITQNIANLGTGIIISLIYGWQLTLLLLAIVPIIAIAGVVEMKMLSGQALK 877
Cdd:cd18573 94 --KNKTGELVSRLSSDTSVVGKSLTQNLSDGLRSLVSGVGGIGMMLYISPKLTLVMLLVVPPIAVGAVFYGRYVRKLSKQ 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 878 DKKELEGSGKIATEAIENFRTVVSLTREQKFETMYAQSLQIPYRNALKKAHVFGITFSFTQAMMYFSYAACFRFGAYLVA 957
Cdd:cd18573 172 VQDALADATKVAEERLSNIRTVRAFAAERKEVERYAKKVDEVFDLAKKEALASGLFFGSTGFSGNLSLLSVLYYGGSLVA 251
|
250 260 270
....*....|....*....|....*....|
gi 25453402 958 RelmtfenvllvfsaivfGAMAVGQVSSFA 987
Cdd:cd18573 252 S-----------------GELTVGDLTSFL 264
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
384-610 |
8.19e-33 |
|
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: 127.17 E-value: 8.19e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 384 LEFKNIHFSYpsrKDVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRTINVRY-LREII 462
Cdd:cd03224 1 LEVENLNAGY---GKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHErARAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 463 GVVSQEPVLFAT-TIAENIRYGRENVTMDEIEKAVKEAnaYDFIMKLPHKFDTLVGergaQLSGGQKQRIAIARALVRNP 541
Cdd:cd03224 78 GYVPEGRRIFPElTVEENLLLGAYARRRAKRKARLERV--YELFPRLKERRKQLAG----TLSGGEQQMLAIARALMSRP 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 25453402 542 KILLLDEATSALdteSEAVVQ---AALDKAREGRTTIVI----AHRLSTVrnADVIAGFDGGVIVEQGNHDELMRE 610
Cdd:cd03224 152 KLLLLDEPSEGL---APKIVEeifEAIRELRDEGVTILLveqnARFALEI--ADRAYVLERGRVVLEGTAAELLAD 222
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
1043-1252 |
8.82e-33 |
|
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: 127.35 E-value: 8.82e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1043 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIkqLNVQWLRAHLGIVSQEPILF-DCSIAE 1121
Cdd:cd03300 14 VALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI--TNLPPHKRPVNTVFQNYALFpHLTVFE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1122 NIAYGDNSRVVSHEEIVKAAKEAnIHQF-IDSLPEKYNTrvgdkgtQLSGGQKQRIAIARALVRQPHILLLDEATSALDT 1200
Cdd:cd03300 92 NIAFGLRLKKLPKAEIKERVAEA-LDLVqLEGYANRKPS-------QLSGGQQQRVAIARALVNEPKVLLLDEPLGALDL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 25453402 1201 ESEKVVQEALDK--AREGRTCIVIAHRLS-TIQNADLIVVIQNGQVKEHGTHQQL 1252
Cdd:cd03300 164 KLRKDMQLELKRlqKELGITFVFVTHDQEeALTMSDRIAVMNKGKIQQIGTPEEI 218
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
1027-1243 |
1.17e-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: 124.82 E-value: 1.17e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1027 VKFNGVMFNYPTRPnipVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIKQLNVQwLRAHLG 1106
Cdd:cd03230 1 IEVRNLSKRYGKKT---ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEE-VKRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1107 IVSQEPILF-DCSIAENIaygdnsrvvsheeivkaakeanihqfidslpekyntrvgdkgtQLSGGQKQRIAIARALVRQ 1185
Cdd:cd03230 77 YLPEEPSLYeNLTVRENL-------------------------------------------KLSGGMKQRLALAQALLHD 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1186 PHILLLDEATSALDTESEKVVQEALDK-AREGRTCIVIAHRLSTIQN-ADLIVVIQNGQV 1243
Cdd:cd03230 114 PELLILDEPTSGLDPESRREFWELLRElKKEGKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1043-1248 |
1.35e-32 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 131.22 E-value: 1.35e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1043 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIKQLNVQwlRAHLGIVSQEPILF-DCSIAE 1121
Cdd:PRK09452 28 EVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE--NRHVNTVFQSYALFpHMTVFE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1122 NIAYGDNSRVVSHEEIVKAAKEA----NIHQFIDSLPekyntrvgdkgTQLSGGQKQRIAIARALVRQPHILLLDEATSA 1197
Cdd:PRK09452 106 NVAFGLRMQKTPAAEITPRVMEAlrmvQLEEFAQRKP-----------HQLSGGQQQRVAIARAVVNKPKVLLLDESLSA 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 25453402 1198 LDTESEKVVQEALdKA--RE-GRTCIVIAH-RLSTIQNADLIVVIQNGQVKEHGT 1248
Cdd:PRK09452 175 LDYKLRKQMQNEL-KAlqRKlGITFVFVTHdQEEALTMSDRIVVMRDGRIEQDGT 228
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
402-606 |
1.39e-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: 127.07 E-value: 1.39e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 402 LKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRTINVRylREIIGVVSQEPVLFA-TTIAENI 480
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE--KRDISYVPQNYALFPhMTVYKNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 481 RYGRENVTMD--EIEKAVKEANAydfIMKLPHkfdtLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESE 558
Cdd:cd03299 93 AYGLKKRKVDkkEIERKVLEIAE---MLGIDH----LLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTK 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 25453402 559 AVVQAALDKARE--GRTTIVIAHRLSTVRN-ADVIAGFDGGVIVEQGNHDE 606
Cdd:cd03299 166 EKLREELKKIRKefGVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPEE 216
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
1028-1243 |
2.11e-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: 126.53 E-value: 2.11e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1028 KFNGVMFNYPTrpNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIKQLNVQWL---RAH 1104
Cdd:cd03256 2 EVENLSKTYPN--GKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALrqlRRQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1105 LGIVSQEPILFD-CSIAENIAYGDNSRV---------VSHEEIVKAAkeANIHQFidSLPEKYNTRVGdkgtQLSGGQKQ 1174
Cdd:cd03256 80 IGMIFQQFNLIErLSVLENVLSGRLGRRstwrslfglFPKEEKQRAL--AALERV--GLLDKAYQRAD----QLSGGQQQ 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 25453402 1175 RIAIARALVRQPHILLLDEATSALDTESEKVVQEAL-DKARE-GRTCIVIAHRLSTI-QNADLIVVIQNGQV 1243
Cdd:cd03256 152 RVAIARALMQQPKLILADEPVASLDPASSRQVMDLLkRINREeGITVIVSLHQVDLArEYADRIVGLKDGRI 223
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1041-1252 |
2.88e-32 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 129.42 E-value: 2.88e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1041 NIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIKQLNVQwlRAHLGIVSQEPILFD-CSI 1119
Cdd:COG3839 15 GVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPK--DRNIAMVFQSYALYPhMTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1120 AENIAYGDNSRVVSHEEIVKAAKEA----NIHQFIDSLPekyntrvgdkgTQLSGGQKQRIAIARALVRQPHILLLDEAT 1195
Cdd:COG3839 93 YENIAFPLKLRKVPKAEIDRRVREAaellGLEDLLDRKP-----------KQLSGGQRQRVALGRALVREPKVFLLDEPL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 25453402 1196 SALD------TESE-KVVQEALdkareGRTCIVIAHRLS---TIqnADLIVVIQNGQVKEHGTHQQL 1252
Cdd:COG3839 162 SNLDaklrveMRAEiKRLHRRL-----GTTTIYVTHDQVeamTL--ADRIAVMNDGRIQQVGTPEEL 221
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
384-602 |
4.88e-32 |
|
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: 124.67 E-value: 4.88e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 384 LEFKNIHFSYPSRKdvqILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRtiNVRYLREIIG 463
Cdd:cd03301 1 VELENVTKRFGNVT---ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVT--DLPPKDRDIA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 464 VVSQEPVLFA-TTIAENIRYG--RENVTMDEIEKAVKEANAydfIMKLPHkfdtLVGERGAQLSGGQKQRIAIARALVRN 540
Cdd:cd03301 76 MVFQNYALYPhMTVYDNIAFGlkLRKVPKDEIDERVREVAE---LLQIEH----LLDRKPKQLSGGQRQRVALGRAIVRE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 25453402 541 PKILLLDEATSALDTESEAVVQAALDK--AREGRTTIVIAH-RLSTVRNADVIAGFDGGVIVEQG 602
Cdd:cd03301 149 PKVFLMDEPLSNLDAKLRVQMRAELKRlqQRLGTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
384-610 |
6.70e-32 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 125.04 E-value: 6.70e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 384 LEFKNIHFSYpsrKDVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIrtINVRYLREIIG 463
Cdd:cd03300 1 IELENVSKFY---GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI--TNLPPHKRPVN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 464 VVSQEPVLFA-TTIAENIRYG--RENVTMDEIEKAVKEAnaydfiMKLPhKFDTLVGERGAQLSGGQKQRIAIARALVRN 540
Cdd:cd03300 76 TVFQNYALFPhLTVFENIAFGlrLKKLPKAEIKERVAEA------LDLV-QLEGYANRKPSQLSGGQQQRVAIARALVNE 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 25453402 541 PKILLLDEATSALDTESEAVVQAALDK--AREGRTTIVIAHRLS---TVrnADVIAGFDGGVIVEQGNHDELMRE 610
Cdd:cd03300 149 PKVLLLDEPLGALDLKLRKDMQLELKRlqKELGITFVFVTHDQEealTM--SDRIAVMNKGKIQQIGTPEEIYEE 221
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
1028-1247 |
8.83e-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: 123.80 E-value: 8.83e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1028 KFNGVMFNYPTRPnipVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIKQLnvqwlRAHLGI 1107
Cdd:cd03235 1 EVEDLTVSYGGHP---VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE-----RKRIGY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1108 VSQEPIL---FDCSIAENIAYGDNSRVVSHEEIVKAAKEAnIHQFIDS--LPEKYNTRVGdkgtQLSGGQKQRIAIARAL 1182
Cdd:cd03235 73 VPQRRSIdrdFPISVRDVVLMGLYGHKGLFRRLSKADKAK-VDEALERvgLSELADRQIG----ELSGGQQQRVLLARAL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 25453402 1183 VRQPHILLLDEATSALDTESEKVVQEALDK-AREGRTCIVIAHRLSTIQN-ADLIVVIqNGQVKEHG 1247
Cdd:cd03235 148 VQDPDLLLLDEPFAGVDPKTQEDIYELLRElRREGMTILVVTHDLGLVLEyFDRVLLL-NRTVVASG 213
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1036-1255 |
8.89e-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: 127.09 E-value: 8.89e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1036 YPTRPN-IPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMA---GTVFLDGKEIKQLNVQWLRA----HLGI 1107
Cdd:COG0444 11 FPTRRGvVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPGitsGEILFDGEDLLKLSEKELRKirgrEIQM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1108 VSQEP---------ILFdcSIAENIAYgdnSRVVSHEEIVKAAKEA-------NIHQFIDSLPekyntrvgdkgTQLSGG 1171
Cdd:COG0444 91 IFQDPmtslnpvmtVGD--QIAEPLRI---HGGLSKAEARERAIELlervglpDPERRLDRYP-----------HELSGG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1172 QKQRIAIARALVRQPHILLLDEATSALDTesekVVQ-EALD-----KAREGRTCIVIAHRLSTI-QNADLIVVIQNGQVK 1244
Cdd:COG0444 155 MRQRVMIARALALEPKLLIADEPTTALDV----TIQaQILNllkdlQRELGLAILFITHDLGVVaEIADRVAVMYAGRIV 230
|
250
....*....|.
gi 25453402 1245 EHGTHQQLLAQ 1255
Cdd:COG0444 231 EEGPVEELFEN 241
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
378-611 |
1.49e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 125.23 E-value: 1.49e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 378 DNIqgnLEFKNIHFSYpsRKDVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRTINVRY 457
Cdd:PRK13647 2 DNI---IEVEDLHFRY--KDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKW 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 458 LREIIGVVSQEP--VLFATTIAENIRYGREN--VTMDEIEKAVKEA----NAYDFIMKLPHkfdtlvgergaQLSGGQKQ 529
Cdd:PRK13647 77 VRSKVGLVFQDPddQVFSSTVWDDVAFGPVNmgLDKDEVERRVEEAlkavRMWDFRDKPPY-----------HLSYGQKK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 530 RIAIARALVRNPKILLLDEATSALDTESEAVVQAALDK-AREGRTTIVIAHRLSTVRN-ADVIAGFDGGVIVEQGNHDEL 607
Cdd:PRK13647 146 RVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRlHNQGKTVIVATHDVDLAAEwADQVIVLKEGRVLAEGDKSLL 225
|
....
gi 25453402 608 MREK 611
Cdd:PRK13647 226 TDED 229
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
1030-1247 |
1.81e-31 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 121.77 E-value: 1.81e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1030 NGVMFNYPTRPnipVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIKQLNVQWLRAHLGIVS 1109
Cdd:cd03214 3 ENLSVGYGGRT---VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1110 QepilfdcsiaeniaygdnsrvvsheeivkAAKEANIHQFIDslpEKYNTrvgdkgtqLSGGQKQRIAIARALVRQPHIL 1189
Cdd:cd03214 80 Q-----------------------------ALELLGLAHLAD---RPFNE--------LSGGERQRVLLARALAQEPPIL 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 25453402 1190 LLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLS-TIQNADLIVVIQNGQVKEHG 1247
Cdd:cd03214 120 LLDEPTSHLDIAHQIELLELLRRlaRERGKTVVMVLHDLNlAARYADRVILLKDGRIVAQG 180
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
1027-1243 |
2.06e-31 |
|
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: 122.90 E-value: 2.06e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1027 VKFNGVMFNYPtrPNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIKQLN---VQWLRA 1103
Cdd:cd03292 1 IEFINVTKTYP--NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRgraIPYLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1104 HLGIVSQE-PILFDCSIAENIAYGDNSRVVSHEEIVKAAKEA----NIHQFIDSLPEkyntrvgdkgtQLSGGQKQRIAI 1178
Cdd:cd03292 79 KIGVVFQDfRLLPDRNVYENVAFALEVTGVPPREIRKRVPAAlelvGLSHKHRALPA-----------ELSGGEQQRVAI 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 25453402 1179 ARALVRQPHILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNA--DLIVVIQNGQV 1243
Cdd:cd03292 148 ARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTtrHRVIALERGKL 214
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
384-554 |
2.32e-31 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 127.37 E-value: 2.32e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 384 LEFKNIHFSYpsrKDVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDI-------RTINVr 456
Cdd:PRK09452 15 VELRGISKSF---DGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDIthvpaenRHVNT- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 457 ylreiigvVSQEPVLFA-TTIAENIRYG--RENVTMDEIEKAVKEAnaydfiMKLPHkFDTLVGERGAQLSGGQKQRIAI 533
Cdd:PRK09452 91 --------VFQSYALFPhMTVFENVAFGlrMQKTPAAEITPRVMEA------LRMVQ-LEEFAQRKPHQLSGGQQQRVAI 155
|
170 180
....*....|....*....|.
gi 25453402 534 ARALVRNPKILLLDEATSALD 554
Cdd:PRK09452 156 ARAVVNKPKVLLLDESLSALD 176
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1038-1237 |
2.49e-31 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 122.20 E-value: 2.49e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1038 TRPNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIKQLNVQWlRAHLGIVSQEPILF-D 1116
Cdd:COG4133 11 RRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDY-RRRLAYLGHADGLKpE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1117 CSIAENIA-----YGdnsRVVSHEEIVKAAKEANIHQFIDslpekynTRVGdkgtQLSGGQKQRIAIARALVRQPHILLL 1191
Cdd:COG4133 90 LTVRENLRfwaalYG---LRADREAIDEALEAVGLAGLAD-------LPVR----QLSAGQKRRVALARLLLSPAPLWLL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 25453402 1192 DEATSALDTESEKVVQEALDKAREGRTCIVIA-HRLSTIQNADLIVV 1237
Cdd:COG4133 156 DEPFTALDAAGVALLAELIAAHLARGGAVLLTtHQPLELAAARVLDL 202
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1040-1243 |
2.56e-31 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 129.75 E-value: 2.56e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1040 PNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIKQLNV-QWLRAHLGIVSQEPILF-DC 1117
Cdd:COG1129 15 GGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPrDAQAAGIAIIHQELNLVpNL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1118 SIAENIAYGD---NSRVVSHEEIVKAAKEA----NIHqfIDSlpekyNTRVGDkgtqLSGGQKQRIAIARALVRQPHILL 1190
Cdd:COG1129 95 SVAENIFLGReprRGGLIDWRAMRRRARELlarlGLD--IDP-----DTPVGD----LSVAQQQLVEIARALSRDARVLI 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 25453402 1191 LDEATSAL-DTESE---KVVQEaLdkAREGRTCIVIAHRLSTIQN-ADLIVVIQNGQV 1243
Cdd:COG1129 164 LDEPTASLtEREVErlfRIIRR-L--KAQGVAIIYISHRLDEVFEiADRVTVLRDGRL 218
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
384-588 |
2.62e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 124.84 E-value: 2.62e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 384 LEFKNIHFSYPSRKDVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRTINVRYLREIIG 463
Cdd:PRK13650 5 IEVKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 464 VVSQEP--VLFATTIAENIRYGREN--VTMDEIEKAVKEA----NAYDFIMKLPhkfdtlvgergAQLSGGQKQRIAIAR 535
Cdd:PRK13650 85 MVFQNPdnQFVGATVEDDVAFGLENkgIPHEEMKERVNEAlelvGMQDFKEREP-----------ARLSGGQKQRVAIAG 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 25453402 536 ALVRNPKILLLDEATSALDTESEAVVQAALDKARE--GRTTIVIAHRLSTVRNAD 588
Cdd:PRK13650 154 AVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDdyQMTVISITHDLDEVALSD 208
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
397-607 |
2.86e-31 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 123.71 E-value: 2.86e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 397 KDVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEG-----EVSIDGQdiRTIN-----VRYLREIIGVVS 466
Cdd:PRK11264 14 HGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGtirvgDITIDTA--RSLSqqkglIRQLRQHVGFVF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 467 QEPVLFA-TTIAENIRYGreNVTMDEIEKAVKEANAYDFIMKLphkfdTLVGERGA---QLSGGQKQRIAIARALVRNPK 542
Cdd:PRK11264 92 QNFNLFPhRTVLENIIEG--PVIVKGEPKEEATARARELLAKV-----GLAGKETSyprRLSGGQQQRVAIARALAMRPE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 25453402 543 ILLLDEATSALDTESEAVVQAALDK-AREGRTTIVIAHRLSTVRN-ADVIAGFDGGVIVEQGNHDEL 607
Cdd:PRK11264 165 VILFDEPTSALDPELVGEVLNTIRQlAQEKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKAL 231
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
1042-1254 |
3.29e-31 |
|
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: 122.54 E-value: 3.29e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1042 IPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIKQLNVQwLRAHLGI--VSQEPILF-DCS 1118
Cdd:cd03224 13 SQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPH-ERARAGIgyVPEGRRIFpELT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1119 IAENIAYGDNSRVvsheeivKAAKEANIHQFIDSLPEKYnTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSAL 1198
Cdd:cd03224 92 VEENLLLGAYARR-------RAKRKARLERVYELFPRLK-ERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 25453402 1199 dteSEKVVQE---ALDKAREGRTCIVIAHrlstiQNADLI-------VVIQNGQVKEHGTHQQLLA 1254
Cdd:cd03224 164 ---APKIVEEifeAIRELRDEGVTILLVE-----QNARFAleiadraYVLERGRVVLEGTAAELLA 221
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
400-601 |
3.72e-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: 123.76 E-value: 3.72e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 400 QILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRTIN---VRYLREIIGVVSQE---PVLFA 473
Cdd:TIGR02769 25 PVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDrkqRRAFRRDVQLVFQDspsAVNPR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 474 TTIAENIRYGRENVT-MDEIEKAVKEANAYDfIMKLPhkfDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSA 552
Cdd:TIGR02769 105 MTVRQIIGEPLRHLTsLDESEQKARIAELLD-MVGLR---SEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSN 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 25453402 553 LDTESEAVVQAALDK--AREGRTTIVIAHRLSTV-RNADVIAGFDGGVIVEQ 601
Cdd:TIGR02769 181 LDMVLQAVILELLRKlqQAFGTAYLFITHDLRLVqSFCQRVAVMDKGQIVEE 232
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1027-1248 |
4.17e-31 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 125.68 E-value: 4.17e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1027 VKFNGVMFNYPT-RPNIPVLQGLSLEVKKGQTLALVGSSGCGKST---VVQLLERfydPMAGTVFLDGKEIKQLNVQWLR 1102
Cdd:PRK11153 2 IELKNISKVFPQgGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTlirCINLLER---PTSGRVLVDGQDLTALSEKELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1103 A---HLGIVSQE-PILFDCSIAENIAYGdnsrvvshEEIVKAAKeANIHQFIDSLPEkyntRVG--DKG----TQLSGGQ 1172
Cdd:PRK11153 79 KarrQIGMIFQHfNLLSSRTVFDNVALP--------LELAGTPK-AEIKARVTELLE----LVGlsDKAdrypAQLSGGQ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 25453402 1173 KQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKA-RE-GRTCIVIAHRLSTI-QNADLIVVIQNGQVKEHGT 1248
Cdd:PRK11153 146 KQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDInRElGLTIVLITHEMDVVkRICDRVAVIDAGRLVEQGT 224
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1040-1252 |
4.98e-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: 4.98e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1040 PNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIKQLNVQwlRAHLGIVSQEPILF-DCS 1118
Cdd:cd03296 13 GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQ--ERNVGFVFQHYALFrHMT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1119 IAENIAYGDNSRVVShEEIVKAAKEANIHQFI-----DSLPEKYNTrvgdkgtQLSGGQKQRIAIARALVRQPHILLLDE 1193
Cdd:cd03296 91 VFDNVAFGLRVKPRS-ERPPEAEIRAKVHELLklvqlDWLADRYPA-------QLSGGQRQRVALARALAVEPKVLLLDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 25453402 1194 ATSALDTESEKVVQEALDKARE--GRTCIVIAHRLS-TIQNADLIVVIQNGQVKEHGTHQQL 1252
Cdd:cd03296 163 PFGALDAKVRKELRRWLRRLHDelHVTTVFVTHDQEeALEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
1039-1244 |
7.51e-31 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 120.82 E-value: 7.51e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1039 RPNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIKQlnvQWLRAHLGIVSQEP--ILFD 1116
Cdd:cd03226 10 KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKA---KERRKSIGYVMQDVdyQLFT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1117 CSIAENIAYGDNSRVVSHEEIVKAAKEANIHQFIDSLPekyntrvgdkgTQLSGGQKQRIAIARALVRQPHILLLDEATS 1196
Cdd:cd03226 87 DSVREELLLGLKELDAGNEQAETVLKDLDLYALKERHP-----------LSLSGGQKQRLAIAAALLSGKDLLIFDEPTS 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 25453402 1197 ALDTESEKVVQEALDK-AREGRTCIVIAHRLSTIQN-ADLIVVIQNGQVK 1244
Cdd:cd03226 156 GLDYKNMERVGELIRElAAQGKAVIVITHDYEFLAKvCDRVLLLANGAIV 205
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1038-1255 |
7.57e-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: 129.03 E-value: 7.57e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1038 TRPNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFyDPMAGTVFLDGKEIKQLN---VQWLRAHLGIVSQEPil 1114
Cdd:COG4172 295 TVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRL-IPSEGEIRFDGQDLDGLSrraLRPLRRRMQVVFQDP-- 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1115 FDC-----SIAENIAYGdnsRVVSHEEIVKAAKEANIhqfIDSLpekynTRVG-DKGT------QLSGGQKQRIAIARAL 1182
Cdd:COG4172 372 FGSlsprmTVGQIIAEG---LRVHGPGLSAAERRARV---AEAL-----EEVGlDPAArhryphEFSGGQRQRIAIARAL 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1183 VRQPHILLLDEATSALDteseKVVQ-EALD-----KAREGRTCIVIAHRLSTIQN-ADLIVVIQNGQVKEHGTHQQLLAQ 1255
Cdd:COG4172 441 ILEPKLLVLDEPTSALD----VSVQaQILDllrdlQREHGLAYLFISHDLAVVRAlAHRVMVMKDGKVVEQGPTEQVFDA 516
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1049-1255 |
1.01e-30 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 121.40 E-value: 1.01e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1049 SLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIKQLNVQwLRAhLGIVSQEPILFD-CSIAENIAYGD 1127
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPA-ERP-VSMLFQENNLFPhLTVAQNIGLGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1128 NSR----VVSHEEIVKAAKEANIHQFIDSLPEkyntrvgdkgtQLSGGQKQRIAIARALVRQPHILLLDEATSALD---- 1199
Cdd:COG3840 97 RPGlkltAEQRAQVEQALERVGLAGLLDRLPG-----------QLSGGQRQRVALARCLVRKRPILLLDEPFSALDpalr 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 25453402 1200 TESEKVVQEALDkaREGRTCIVIAHRLSTIQN-ADLIVVIQNGQVKEHGTHQQLLAQ 1255
Cdd:COG3840 166 QEMLDLVDELCR--ERGLTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAALLDG 220
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
384-607 |
1.02e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 122.89 E-value: 1.02e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 384 LEFKNIHFSYPSRKDVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRTINVRYLREIIG 463
Cdd:PRK13642 5 LEVENLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 464 VVSQEP--VLFATTIAENIRYGREN--VTMDEIEKAVKEA----NAYDFIMKLPhkfdtlvgergAQLSGGQKQRIAIAR 535
Cdd:PRK13642 85 MVFQNPdnQFVGATVEDDVAFGMENqgIPREEMIKRVDEAllavNMLDFKTREP-----------ARLSGGQKQRVAVAG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 25453402 536 ALVRNPKILLLDEATSALDTESEAVVQAALDKAREGR--TTIVIAHRLSTVRNADVIAGFDGGVIVEQGNHDEL 607
Cdd:PRK13642 154 IIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYqlTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSEL 227
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1045-1252 |
1.89e-30 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 123.69 E-value: 1.89e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1045 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIKQLN---VQWLRAHLGIVSQEPilFDC---- 1117
Cdd:COG4608 34 VDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSgreLRPLRRRMQMVFQDP--YASlnpr 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1118 -SIAENIAYG-DNSRVVSheeivKAAKEANIHQFIDslpekyntRVGDKGT-------QLSGGQKQRIAIARALVRQPHI 1188
Cdd:COG4608 112 mTVGDIIAEPlRIHGLAS-----KAERRERVAELLE--------LVGLRPEhadryphEFSGGQRQRIGIARALALNPKL 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 25453402 1189 LLLDEATSALDtesekV-VQ-------EALdKAREGRTCIVIAHRLSTIQN-ADLIVVIQNGQVKEHGTHQQL 1252
Cdd:COG4608 179 IVCDEPVSALD-----VsIQaqvlnllEDL-QDELGLTYLFISHDLSVVRHiSDRVAVMYLGKIVEIAPRDEL 245
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
1036-1252 |
2.22e-30 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 119.92 E-value: 2.22e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1036 YPTRPNiPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIKQlNVQWLRAHLGIVSQEPILF 1115
Cdd:cd03263 10 YKKGTK-PAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLGYCPQFDALF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1116 D-CSIAENIAYgdNSRVVSH-EEIVKAAKEANIHQFidSLPEKYNTRVGDkgtqLSGGQKQRIAIARALVRQPHILLLDE 1193
Cdd:cd03263 88 DeLTVREHLRF--YARLKGLpKSEIKEEVELLLRVL--GLTDKANKRART----LSGGMKRKLSLAIALIGGPSVLLLDE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1194 ATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVIQNGQVKEHGTHQQL 1252
Cdd:cd03263 160 PTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEAlCDRIAIMSDGKLRCIGSPQEL 219
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
1044-1248 |
2.63e-30 |
|
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: 120.23 E-value: 2.63e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1044 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIKQLNVQwLRAHLGIVS--QEPILF-DCSIA 1120
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPH-EIARLGIGRtfQIPRLFpELTVL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1121 ENI----------AYGDNSRVVSHEEIVKAAKEAnIHQFidSLPEKYNTRVGDkgtqLSGGQKQRIAIARALVRQPHILL 1190
Cdd:cd03219 94 ENVmvaaqartgsGLLLARARREEREARERAEEL-LERV--GLADLADRPAGE----LSYGQQRRLEIARALATDPKLLL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1191 LDEATSAL-DTESEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVIQNGQVKEHGT 1248
Cdd:cd03219 167 LDEPAAGLnPEETEELAELIRELRERGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGT 226
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
1045-1243 |
3.47e-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: 119.32 E-value: 3.47e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1045 LQGLSLEVK---KGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEI----KQLNVQWLRAHLGIVSQEPILF-D 1116
Cdd:cd03297 10 LPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLfdsrKKINLPPQQRKIGLVFQQYALFpH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1117 CSIAENIAYG-----DNSRVVSHEEIVKAAKeanihqfIDSLPEKYNTrvgdkgtQLSGGQKQRIAIARALVRQPHILLL 1191
Cdd:cd03297 90 LNVRENLAFGlkrkrNREDRISVDELLDLLG-------LDHLLNRYPA-------QLSGGEKQRVALARALAAQPELLLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 25453402 1192 DEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLSTIQN-ADLIVVIQNGQV 1243
Cdd:cd03297 156 DEPFSALDRALRLQLLPELKQikKNLNIPVIFVTHDLSEAEYlADRIVVMEDGRL 210
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
384-577 |
5.16e-30 |
|
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: 119.46 E-value: 5.16e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 384 LEFKNIHFSYPSR-KDVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRTIN----VRYL 458
Cdd:COG4181 9 IELRGLTKTVGTGaGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDedarARLR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 459 REIIGVVSQEPVLFATTIAEnirygrENVTM--------DEIEKAVKEANAYDfimklphkfdtlVGERG----AQLSGG 526
Cdd:COG4181 89 ARHVGFVFQSFQLLPTLTAL------ENVMLplelagrrDARARARALLERVG------------LGHRLdhypAQLSGG 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 25453402 527 QKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAAL-DKAREGRTTIVI 577
Cdd:COG4181 151 EQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLfELNRERGTTLVL 202
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
384-607 |
1.05e-29 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 124.75 E-value: 1.05e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 384 LEFKNIHFSYPSrkdVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRTINVRYLREI-I 462
Cdd:COG1129 5 LEMRGISKSFGG---VKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQAAgI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 463 GVVSQEPVLFAT-TIAENIRYGRENVT---MD--EIEKAVKEANAYdfiMKLPHKFDTLVGErgaqLSGGQKQRIAIARA 536
Cdd:COG1129 82 AIIHQELNLVPNlSVAENIFLGREPRRgglIDwrAMRRRARELLAR---LGLDIDPDTPVGD----LSVAQQQLVEIARA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 25453402 537 LVRNPKILLLDEATSAL-DTESEAVVQAALDKAREGRTTIVIAHRLSTVRN-ADVIAGFDGGVIVEQGNHDEL 607
Cdd:COG1129 155 LSRDARVLILDEPTASLtEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEiADRVTVLRDGRLVGTGPVAEL 227
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
400-600 |
1.21e-29 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 119.41 E-value: 1.21e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 400 QILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRTIN---VRYLREIIGVVSQEP---VLFA 473
Cdd:PRK10419 26 TVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNraqRKAFRRDIQMVFQDSisaVNPR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 474 TTIAENIRYG-RENVTMDEIEKAVKEANAYDfIMKLPhkfDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSA 552
Cdd:PRK10419 106 KTVREIIREPlRHLLSLDKAERLARASEMLR-AVDLD---DSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSN 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 25453402 553 LDTESEAVVQAALDKAREGRTT--IVIAHRLSTV-RNADVIAGFDGGVIVE 600
Cdd:PRK10419 182 LDLVLQAGVIRLLKKLQQQFGTacLFITHDLRLVeRFCQRVMVMDNGQIVE 232
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
402-610 |
1.29e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 120.15 E-value: 1.29e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 402 LKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDI--RTINVRYLREIIGVVSQEP--VLFATTIA 477
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdKKVKLSDIRKKVGLVFQYPeyQLFEETIE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 478 ENIRYGRENVTM--DEIEKAVKEANAydfIMKLPhkFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALD- 554
Cdd:PRK13637 103 KDIAFGPINLGLseEEIENRVKRAMN---IVGLD--YEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDp 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 25453402 555 -TESEAVVQAALDKAREGRTTIVIAHRLSTV-RNADVIAGFDGGVIVEQGNHDELMRE 610
Cdd:PRK13637 178 kGRDEILNKIKELHKEYNMTIILVSHSMEDVaKLADRIIVMNKGKCELQGTPREVFKE 235
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
384-603 |
1.32e-29 |
|
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: 116.88 E-value: 1.32e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 384 LEFKNIHF---SYPSRKDVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLL--QRLYDPIEGEVSIDGQDIRTINVRYl 458
Cdd:cd03213 4 LSFRNLTVtvkSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGRPLDKRSFRK- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 459 reIIGVVSQEPVLFAT-TIAENIrygrenvtmdeiekavkeanayDFIMKLphkfdtlvgeRGaqLSGGQKQRIAIARAL 537
Cdd:cd03213 83 --IIGYVPQDDILHPTlTVRETL----------------------MFAAKL----------RG--LSGGERKRVSIALEL 126
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 25453402 538 VRNPKILLLDEATSALDTESEAVVQAALDK-AREGRTTIVIAHRLSTvrnaDVIAGFDGGVIVEQGN 603
Cdd:cd03213 127 VSNPSLLFLDEPTSGLDSSSALQVMSLLRRlADTGRTIICSIHQPSS----EIFELFDKLLLLSQGR 189
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
749-965 |
1.35e-29 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen processing; This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350016 [Multi-domain] Cd Length: 289 Bit Score: 119.96 E-value: 1.35e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 749 LLFLILGIISFITFFLQGFTFGKAGEILTKRLRYMVFKSMLRQDISWFDdpKNTTGALTTRLANDAAQVKGATGSRLAVI 828
Cdd:cd18572 40 LLLLLLSVLSGLFSGLRGGCFSYAGTRLVRRLRRDLFRSLLRQDIAFFD--ATKTGELTSRLTSDCQKVSDPLSTNLNVF 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 829 TQNIANLGTGIIISLIYGWQLTLLLLAIVPIIAIAGVVE---MKMLSGQAlkdKKELEGSGKIATEAIENFRTVVSLTRE 905
Cdd:cd18572 118 LRNLVQLVGGLAFMFSLSWRLTLLAFITVPVIALITKVYgryYRKLSKEI---QDALAEANQVAEEALSNIRTVRSFATE 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 906 QKFETMYAQSLQIPYRNALKKAHVFGITFSFTQAMMYFSYAACFRFGAYLVARELMTFEN 965
Cdd:cd18572 195 EREARRYERALDKALKLSVRQALAYAGYVAVNTLLQNGTQVLVLFYGGHLVLSGRMSAGQ 254
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
384-611 |
1.52e-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: 118.65 E-value: 1.52e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 384 LEFKNIHFSYPSRKdvqILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEG-EVSIDGQDIRTINVRYLREII 462
Cdd:COG1119 4 LELRNVTVRRGGKT---ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGEDVWELRKRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 463 GVVS---------QEPVL-------FATTiaeniryGR-ENVTMDEIEKAVKEANAydfiMKLPHKFDTLVGergaQLSG 525
Cdd:COG1119 81 GLVSpalqlrfprDETVLdvvlsgfFDSI-------GLyREPTDEQRERARELLEL----LGLAHLADRPFG----TLSQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 526 GQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDK-AREGRTTIV-IAHRLStvrnaDVIAGFD------GGV 597
Cdd:COG1119 146 GEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKlAAEGAPTLVlVTHHVE-----EIPPGIThvlllkDGR 220
|
250
....*....|....
gi 25453402 598 IVEQGNHDELMREK 611
Cdd:COG1119 221 VVAAGPKEEVLTSE 234
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
384-599 |
1.57e-29 |
|
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: 115.60 E-value: 1.57e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 384 LEFKNIHFSYPSrkdVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRTINVRYLREI-I 462
Cdd:cd03216 1 LELRGITKRFGG---VKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARRAgI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 463 GVVSQepvlfattiaenirygrenvtmdeiekavkeanaydfimklphkfdtlvgergaqLSGGQKQRIAIARALVRNPK 542
Cdd:cd03216 78 AMVYQ-------------------------------------------------------LSVGERQMVEIARALARNAR 102
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 25453402 543 ILLLDEATSAL-DTESEAVVQAALDKAREGRTTIVIAHRLSTVRN-ADVIAGFDGGVIV 599
Cdd:cd03216 103 LLILDEPTAALtPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEiADRVTVLRDGRVV 161
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1027-1252 |
1.85e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 119.09 E-value: 1.85e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1027 VKFNGVMFNYPTRPNIpVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIKQLNVQWLRAHLG 1106
Cdd:PRK13648 8 IVFKNVSFQYQSDASF-TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1107 IVSQEPI-LFDCSIAE-NIAYGDNSRVVSHEEIV----KAAKEANIHQFIDSLPEkyntrvgdkgtQLSGGQKQRIAIAR 1180
Cdd:PRK13648 87 IVFQNPDnQFVGSIVKyDVAFGLENHAVPYDEMHrrvsEALKQVDMLERADYEPN-----------ALSGGQKQRVAIAG 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 25453402 1181 ALVRQPHILLLDEATSALDTESEKVVQEALDKAREGR--TCIVIAHRLSTIQNADLIVVIQNGQVKEHGTHQQL 1252
Cdd:PRK13648 156 VLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEI 229
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
384-579 |
4.16e-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: 116.45 E-value: 4.16e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 384 LEFKNIHFSYPSRKDVqILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRTiNVRYLREIIG 463
Cdd:cd03263 1 LQIRNLTKTYKKGTKP-AVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 464 VVSQEPVLFAT-TIAENIRY-----GRENVTMDEiekavkEANAYDFIMKLPHKFDTLVGergaQLSGGQKQRIAIARAL 537
Cdd:cd03263 79 YCPQFDALFDElTVREHLRFyarlkGLPKSEIKE------EVELLLRVLGLTDKANKRAR----TLSGGMKRKLSLAIAL 148
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 25453402 538 VRNPKILLLDEATSALDTESEAVVQAALDKAREGRTTIVIAH 579
Cdd:cd03263 149 IGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTH 190
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
377-611 |
4.79e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 118.41 E-value: 4.79e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 377 PDNIqgnLEFKNIHFSYPSrkDVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQ--DIRTIN 454
Cdd:PRK13636 2 EDYI---LKVEELNYNYSD--GTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpiDYSRKG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 455 VRYLREIIGVVSQEP--VLFATTIAENIRYGRENVTM--DEIEKAVKEANAYDFIMKLPHKfdtlvgeRGAQLSGGQKQR 530
Cdd:PRK13636 77 LMKLRESVGMVFQDPdnQLFSASVYQDVSFGAVNLKLpeDEVRKRVDNALKRTGIEHLKDK-------PTHCLSFGQKKR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 531 IAIARALVRNPKILLLDEATSALDTE--SEaVVQAALDKAREGRTTIVIA-HRLSTVR-NADVIAGFDGGVIVEQGNHDE 606
Cdd:PRK13636 150 VAIAGVLVMEPKVLVLDEPTAGLDPMgvSE-IMKLLVEMQKELGLTIIIAtHDIDIVPlYCDNVFVMKEGRVILQGNPKE 228
|
....*
gi 25453402 607 LMREK 611
Cdd:PRK13636 229 VFAEK 233
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
381-602 |
5.82e-29 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 116.94 E-value: 5.82e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 381 QGNLEFKNIHFSYpsrKDVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYD-----PIEGEVSIDGQDIRTINV 455
Cdd:PRK14247 1 MNKIEIRDLKVSF---GQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDIFKMDV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 456 RYLREIIGVVSQEPVLFAT-TIAENIRYG----RENVTMDEIEKAVKEANAYdfiMKLPHKFDTLVGERGAQLSGGQKQR 530
Cdd:PRK14247 78 IELRRRVQMVFQIPNPIPNlSIFENVALGlklnRLVKSKKELQERVRWALEK---AQLWDEVKDRLDAPAGKLSGGQQQR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 25453402 531 IAIARALVRNPKILLLDEATSALDTESEAVVQAALDKAREGRTTIVIAH-RLSTVRNADVIAGFDGGVIVEQG 602
Cdd:PRK14247 155 LCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHfPQQAARISDYVAFLYKGQIVEWG 227
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
383-609 |
6.39e-29 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 116.39 E-value: 6.39e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 383 NLEFKNIHFSYPsrkdVQILKgLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRTINVrYLREIi 462
Cdd:COG3840 1 MLRLDDLTYRYG----DFPLR-FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPP-AERPV- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 463 GVVSQEPVLFA-TTIAENI--------RYGRENVTmdEIEKAVKEANAYDFIMKLPhkfdtlvgergAQLSGGQKQRIAI 533
Cdd:COG3840 74 SMLFQENNLFPhLTVAQNIglglrpglKLTAEQRA--QVEQALERVGLAGLLDRLP-----------GQLSGGQRQRVAL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 534 ARALVRNPKILLLDEATSALD----TESEAVVQaalDKARE-GRTTIVIAHRLSTVRN-ADVIAGFDGGVIVEQGNHDEL 607
Cdd:COG3840 141 ARCLVRKRPILLLDEPFSALDpalrQEMLDLVD---ELCRErGLTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAAL 217
|
..
gi 25453402 608 MR 609
Cdd:COG3840 218 LD 219
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
1040-1247 |
7.25e-29 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 115.43 E-value: 7.25e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1040 PNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIKqlNVQWLRAHLGIVSQEPILF-DCS 1118
Cdd:cd03301 11 GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVT--DLPPKDRDIAMVFQNYALYpHMT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1119 IAENIAYGDNSRVVSHEEIVK----AAKEANIHQFIDSLPekyntrvgdkgTQLSGGQKQRIAIARALVRQPHILLLDEA 1194
Cdd:cd03301 89 VYDNIAFGLKLRKVPKDEIDErvreVAELLQIEHLLDRKP-----------KQLSGGQRQRVALGRAIVREPKVFLMDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 25453402 1195 TSALDTESEKVVQEALDK--AREGRTCIVIAH-RLSTIQNADLIVVIQNGQVKEHG 1247
Cdd:cd03301 158 LSNLDAKLRVQMRAELKRlqQRLGTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1040-1243 |
7.76e-29 |
|
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: 113.68 E-value: 7.76e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1040 PNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIKQLNVQwlRAH-LGIvsqepilfdcs 1118
Cdd:cd03216 11 GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPR--DARrAGI----------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1119 iaeniaygdnsrvvsheeivkaakeANIHQfidslpekyntrvgdkgtqLSGGQKQRIAIARALVRQPHILLLDEATSAL 1198
Cdd:cd03216 78 -------------------------AMVYQ-------------------LSVGERQMVEIARALARNARLLILDEPTAAL 113
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 25453402 1199 -DTESEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVIQNGQV 1243
Cdd:cd03216 114 tPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEiADRVTVLRDGRV 160
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1045-1264 |
9.17e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 117.14 E-value: 9.17e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1045 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIKQLNVQWLRAHLGIVSQEP--ILFDCSIAEN 1122
Cdd:PRK13647 21 LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLVFQDPddQVFSSTVWDD 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1123 IAYGDNSRVVSHEEIVKAAKEA----NIHQFIDSLPEkyntrvgdkgtQLSGGQKQRIAIARALVRQPHILLLDEATSAL 1198
Cdd:PRK13647 101 VAFGPVNMGLDKDEVERRVEEAlkavRMWDFRDKPPY-----------HLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYL 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 25453402 1199 DTESEKVVQEALDK-AREGRTCIVIAHRLS-TIQNADLIVVIQNGQVKEHG-----THQQLLAQKGIYFSMVS 1264
Cdd:PRK13647 170 DPRGQETLMEILDRlHNQGKTVIVATHDVDlAAEWADQVIVLKEGRVLAEGdksllTDEDIVEQAGLRLPLVA 242
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
378-629 |
1.77e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 116.44 E-value: 1.77e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 378 DNIqgnLEFKNIHFSYPSRKdVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDP---IEGEVSIDGQDIRTIN 454
Cdd:PRK13640 3 DNI---VEFKHVSFTYPDSK-KPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDGITLTAKT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 455 VRYLREIIGVVSQEP--VLFATTIAENIRYGREN--VTMDEIEKAVKEANA----YDFIMKLPhkfdtlvgergAQLSGG 526
Cdd:PRK13640 79 VWDIREKVGIVFQNPdnQFVGATVGDDVAFGLENraVPRPEMIKIVRDVLAdvgmLDYIDSEP-----------ANLSGG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 527 QKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDKARE--GRTTIVIAHRLSTVRNADVIAGFDGGVIVEQGNH 604
Cdd:PRK13640 148 QKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKknNLTVISITHDIDEANMADQVLVLDDGKLLAQGSP 227
|
250 260
....*....|....*....|....*
gi 25453402 605 DElmrekgIYFKLVMTQTAGNEIEL 629
Cdd:PRK13640 228 VE------IFSKVEMLKEIGLDIPF 246
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
383-605 |
1.89e-28 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 115.11 E-value: 1.89e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 383 NLEFKNIHFSYPSrkdVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDG------QDIRTINVR 456
Cdd:COG4161 2 SIQLKNINCFYGS---HQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGhqfdfsQKPSEKAIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 457 YLREIIGVVSQE----PVLfatTIAENIRYGRENVTMDEIEKAVKEANAYDFIMKLPHKFDTLvgerGAQLSGGQKQRIA 532
Cdd:COG4161 79 LLRQKVGMVFQQynlwPHL---TVMENLIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRF----PLHLSGGQQQRVA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 25453402 533 IARALVRNPKILLLDEATSALDTESEA-VVQAALDKAREGRTTIVIAHRLSTVRN-ADVIAGFDGGVIVEQGNHD 605
Cdd:COG4161 152 IARALMMEPQVLLFDEPTAALDPEITAqVVEIIRELSQTGITQVIVTHEVEFARKvASQVVYMEKGRIIEQGDAS 226
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
384-609 |
3.36e-28 |
|
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: 114.31 E-value: 3.36e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 384 LEFKNIHFSYPsrkDVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRTINV-RYLREII 462
Cdd:COG0410 4 LEVENLHAGYG---GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPhRIARLGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 463 GVVSQEPVLFAT-TIAENIRYGRENVTMDEIEKAVKEAnAYDFimklphkFDTLvGER----GAQLSGGQKQRIAIARAL 537
Cdd:COG0410 81 GYVPEGRRIFPSlTVEENLLLGAYARRDRAEVRADLER-VYEL-------FPRL-KERrrqrAGTLSGGEQQMLAIGRAL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 25453402 538 VRNPKILLLDEATSALdteSEAVVQ---AALDKAREGRTTIVI----AHRLSTVrnADVIAGFDGGVIVEQGNHDELMR 609
Cdd:COG0410 152 MSRPKLLLLDEPSLGL---APLIVEeifEIIRRLNREGVTILLveqnARFALEI--ADRAYVLERGRIVLEGTAAELLA 225
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
384-644 |
3.61e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 115.57 E-value: 3.61e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 384 LEFKNIHFSYPSRKDVQ---ILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRTI-NVRYLR 459
Cdd:PRK13633 5 IKCKNVSYKYESNEESTeklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEeNLWDIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 460 EIIGVVSQEP--VLFATTIAENIRYGREN--VTMDEIEKAVKEA----NAYDFIMKLPHkfdtlvgergaQLSGGQKQRI 531
Cdd:PRK13633 85 NKAGMVFQNPdnQIVATIVEEDVAFGPENlgIPPEEIRERVDESlkkvGMYEYRRHAPH-----------LLSGGQKQRV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 532 AIARALVRNPKILLLDEATSALDTESEAVVQAALDK--AREGRTTIVIAHRLSTVRNADVIAGFDGGVIVEQGNHDELMR 609
Cdd:PRK13633 154 AIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKElnKKYGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEIFK 233
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 25453402 610 E----KGIYFKL-VMTQTAgneIELGNEACESKDGIDNVD 644
Cdd:PRK13633 234 EvemmKKIGLDVpQVTELA---YELKKEGVDIPSDILTID 270
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
384-602 |
4.06e-28 |
|
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: 120.56 E-value: 4.06e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 384 LEFKNIHFSYPS-RKDVQILKGLNLKVKSGQTVALVGNSGCGKSTT----VQLLQRLYDPIEGEVSIDGQDIRTINVRYL 458
Cdd:COG4172 7 LSVEDLSVAFGQgGGTVEAVKGVSFDIAAGETLALVGESGSGKSVTalsiLRLLPDPAAHPSGSILFDGQDLLGLSEREL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 459 REI----IGVVSQEPV-----LFatTI----AENIRYGReNVTMDEIEKAVKE-------------ANAYdfimklPHkf 512
Cdd:COG4172 87 RRIrgnrIAMIFQEPMtslnpLH--TIgkqiAEVLRLHR-GLSGAAARARALEllervgipdperrLDAY------PH-- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 513 dtlvgergaQLSGGQKQRIAIARALVRNPKILLLDEATSALDteseAVVQAA-LD-----KAREGRTTIVIAHRLSTVRN 586
Cdd:COG4172 156 ---------QLSGGQRQRVMIAMALANEPDLLIADEPTTALD----VTVQAQiLDllkdlQRELGMALLLITHDLGVVRR 222
|
250
....*....|....*..
gi 25453402 587 -ADVIAGFDGGVIVEQG 602
Cdd:COG4172 223 fADRVAVMRQGEIVEQG 239
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
402-602 |
4.25e-28 |
|
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: 113.16 E-value: 4.25e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 402 LKGLNLKVK---SGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQ---DIR-TINVRYLREIIGVVSQEPVLFA- 473
Cdd:cd03297 10 LPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlfDSRkKINLPPQQRKIGLVFQQYALFPh 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 474 TTIAENIRYGRENVTMDEIEKAVKEANAYdfiMKLPHkfdtLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSAL 553
Cdd:cd03297 90 LNVRENLAFGLKRKRNREDRISVDELLDL---LGLDH----LLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSAL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 25453402 554 DTESEAVVQAALDK--AREGRTTIVIAHRLSTV-RNADVIAGFDGGVIVEQG 602
Cdd:cd03297 163 DRALRLQLLPELKQikKNLNIPVIFVTHDLSEAeYLADRIVVMEDGRLQYIG 214
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1038-1201 |
4.33e-28 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 112.96 E-value: 4.33e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1038 TRPNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDP---MAGTVFLDGKEIKQLNVQwlRAHLGIVSQEPIL 1114
Cdd:COG4136 10 TLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALPAE--QRRIGILFQDDLL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1115 FD-CSIAENIAYG---DNSRVVSHEEIVKAAKEANIHQFIDSLPEkyntrvgdkgtQLSGGQKQRIAIARALVRQPHILL 1190
Cdd:COG4136 88 FPhLSVGENLAFAlppTIGRAQRRARVEQALEEAGLAGFADRDPA-----------TLSGGQRARVALLRALLAEPRALL 156
|
170
....*....|.
gi 25453402 1191 LDEATSALDTE 1201
Cdd:COG4136 157 LDEPFSKLDAA 167
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
839-1259 |
6.24e-28 |
|
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: 123.13 E-value: 6.24e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 839 IIISLIYGWQ-LTLLLLA----IVPIIAIAGVVEMKMLSGQaLKDKKELEGSGKIATEAIENFRTVV----SLTREQKFE 909
Cdd:TIGR00957 445 VILALYFLWLnLGPSVLAgvavMVLMVPLNAVMAMKTKTYQ-VAHMKSKDNRIKLMNEILNGIKVLKlyawELAFLDKVE 523
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 910 TMYAQSLQIpyrnaLKKAHVFGITFSFTQAMMYFSYAAC-FRFGAYLVARELMTFENV---LLVFSAIVFGAMAVGQVSS 985
Cdd:TIGR00957 524 GIRQEELKV-----LKKSAYLHAVGTFTWVCTPFLVALItFAVYVTVDENNILDAEKAfvsLALFNILRFPLNILPMVIS 598
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 986 fapDYAKAKVSASHIiRIIEKIPEIDSYSTE--GLKPNmlEGN-VKFNGVMFNYpTRPNIPVLQGLSLEVKKGQTLALVG 1062
Cdd:TIGR00957 599 ---SIVQASVSLKRL-RIFLSHEELEPDSIErrTIKPG--EGNsITVHNATFTW-ARDLPPTLNGITFSIPEGALVAVVG 671
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1063 SSGCGKSTVVQLLERFYDPMAGTVFLDGKeikqlnvqwlrahLGIVSQEPILFDCSIAENIAYGDNSRVVSHEEIVKAAK 1142
Cdd:TIGR00957 672 QVGCGKSSLLSALLAEMDKVEGHVHMKGS-------------VAYVPQQAWIQNDSLRENILFGKALNEKYYQQVLEACA 738
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1143 eanIHQFIDSLPEKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEAL---DKAREGRTC 1219
Cdd:TIGR00957 739 ---LLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVigpEGVLKNKTR 815
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 25453402 1220 IVIAHRLSTIQNADLIVVIQNGQVKEHGTHQQLLAQKGIY 1259
Cdd:TIGR00957 816 ILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAF 855
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
384-554 |
6.86e-28 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 116.74 E-value: 6.86e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 384 LEFKNIHFSYpsrKDVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDI--RTINVRYlrei 461
Cdd:PRK11432 7 VVLKNITKRF---GSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVthRSIQQRD---- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 462 IGVVSQEPVLFA-TTIAENIRYG--RENVTMDEIEKAVKEANAydfIMKLPHKFDTLVGergaQLSGGQKQRIAIARALV 538
Cdd:PRK11432 80 ICMVFQSYALFPhMSLGENVGYGlkMLGVPKEERKQRVKEALE---LVDLAGFEDRYVD----QISGGQQQRVALARALI 152
|
170
....*....|....*.
gi 25453402 539 RNPKILLLDEATSALD 554
Cdd:PRK11432 153 LKPKVLLFDEPLSNLD 168
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
706-979 |
7.95e-28 |
|
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: 114.89 E-value: 7.95e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 706 GVFCAIINGGLQPAFSIIFSKVVG-VFTKNDTPEIQRqnsnLFSLLFLILGIISFITFFlQGFTFGKAGEILTKRLRYMV 784
Cdd:cd18576 1 GLILLLLSSAIGLVFPLLAGQLIDaALGGGDTASLNQ----IALLLLGLFLLQAVFSFF-RIYLFARVGERVVADLRKDL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 785 FKSMLRQDISWFDdpKNTTGALTTRLANDAAQVKGATGSRLAVITQNIANLGTGIIISLIYGWQLTLLLLAIVPIIAIAG 864
Cdd:cd18576 76 YRHLQRLPLSFFH--ERRVGELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWKLTLLMLATVPVVVLVA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 865 VV---EMKMLSGQALkdkKELEGSGKIATEAIENFRTVVSLTREQkFETM-YAQSLQIPYRNALKKAHVFGITFSFTQAM 940
Cdd:cd18576 154 VLfgrRIRKLSKKVQ---DELAEANTIVEETLQGIRVVKAFTRED-YEIErYRKALERVVKLALKRARIRALFSSFIIFL 229
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 25453402 941 MYFSYAACFRFGAYLVARELMTFENV--LLVFSAIVFGAMA 979
Cdd:cd18576 230 LFGAIVAVLWYGGRLVLAGELTAGDLvaFLLYTLFIAGSIG 270
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
402-609 |
1.09e-27 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 112.92 E-value: 1.09e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 402 LKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRTINVRylrEI----IGVVSQEPVLFAT-TI 476
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPH---EIarlgIGRTFQIPRLFPElTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 477 AENIRYG-----RENVTMDEIEKAVKEANAYDF----IMKLPHKFDTLVGErgaqLSGGQKQRIAIARALVRNPKILLLD 547
Cdd:cd03219 93 LENVMVAaqartGSGLLLARARREEREARERAEelleRVGLADLADRPAGE----LSYGQQRRLEIARALATDPKLLLLD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 25453402 548 EATSAL-DTESEAVVQAALDKAREGRTTIVIAHRLSTVRN-ADVIAGFDGGVIVEQGNHDELMR 609
Cdd:cd03219 169 EPAAGLnPEETEELAELIRELRERGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGTPDEVRN 232
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1044-1255 |
1.09e-27 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 115.97 E-value: 1.09e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1044 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIKQLNVQwlRAHLGIVSQEPILF-DCSIAEN 1122
Cdd:PRK11432 21 VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQ--QRDICMVFQSYALFpHMSLGEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1123 IAYGDNSRVVSHEEIVKAAKEAniHQFIDSlpEKYNTRVGDkgtQLSGGQKQRIAIARALVRQPHILLLDEATSALDTES 1202
Cdd:PRK11432 99 VGYGLKMLGVPKEERKQRVKEA--LELVDL--AGFEDRYVD---QISGGQQQRVALARALILKPKVLLFDEPLSNLDANL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 25453402 1203 EKVVQEaldKARE-----GRTCIVIAHRLS-TIQNADLIVVIQNGQVKEHGTHQQLLAQ 1255
Cdd:PRK11432 172 RRSMRE---KIRElqqqfNITSLYVTHDQSeAFAVSDTVIVMNKGKIMQIGSPQELYRQ 227
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
384-556 |
1.27e-27 |
|
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: 112.82 E-value: 1.27e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 384 LEFKNIHFSYPsrkDVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRTINVRylREIIG 463
Cdd:cd03296 3 IEVRNVSKRFG---DFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQ--ERNVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 464 VVSQEPVLFA-TTIAENIRYG------RENVTMDEIEKAVKEanaydfIMKLPHkFDTLVGERGAQLSGGQKQRIAIARA 536
Cdd:cd03296 78 FVFQHYALFRhMTVFDNVAFGlrvkprSERPPEAEIRAKVHE------LLKLVQ-LDWLADRYPAQLSGGQRQRVALARA 150
|
170 180
....*....|....*....|
gi 25453402 537 LVRNPKILLLDEATSALDTE 556
Cdd:cd03296 151 LAVEPKVLLLDEPFGALDAK 170
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
1043-1256 |
1.47e-27 |
|
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: 113.36 E-value: 1.47e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1043 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIKQLNVQWLRA---HLGIVSQepilfDC-- 1117
Cdd:TIGR02769 25 PVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQRRAfrrDVQLVFQ-----DSps 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1118 ------SIAENIAygdnsRVVSH-EEIVKAAKEANIHQFID--SLPEKYNTRVGdkgTQLSGGQKQRIAIARALVRQPHI 1188
Cdd:TIGR02769 100 avnprmTVRQIIG-----EPLRHlTSLDESEQKARIAELLDmvGLRSEDADKLP---RQLSGGQLQRINIARALAVKPKL 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 25453402 1189 LLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLSTIQN-ADLIVVIQNGQVKEHGTHQQLLAQK 1256
Cdd:TIGR02769 172 IVLDEAVSNLDMVLQAVILELLRKlqQAFGTAYLFITHDLRLVQSfCQRVAVMDKGQIVEECDVAQLLSFK 242
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1027-1254 |
1.50e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 113.65 E-value: 1.50e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1027 VKFNGVMFNYPTRPNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIKQLNVQWLRAHLG 1106
Cdd:PRK13642 5 LEVENLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1107 IVSQEP--ILFDCSIAENIAYGDNSRVVSHEEIVKAAKEANIHqfIDSLpeKYNTRvgdKGTQLSGGQKQRIAIARALVR 1184
Cdd:PRK13642 85 MVFQNPdnQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLA--VNML--DFKTR---EPARLSGGQKQRVAVAGIIAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 25453402 1185 QPHILLLDEATSALD----TESEKVVQEALDKARegRTCIVIAHRLSTIQNADLIVVIQNGQVKEHGTHQQLLA 1254
Cdd:PRK13642 158 RPEIIILDESTSMLDptgrQEIMRVIHEIKEKYQ--LTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFA 229
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
384-605 |
1.91e-27 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 112.41 E-value: 1.91e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 384 LEFKNIHFSYPSRkdvQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDG------QDIRTINVRY 457
Cdd:PRK11124 3 IQLNGINCFYGAH---QALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhfdfsKTPSDKAIRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 458 LREIIGVVSQEPVLFA-TTIAENIRYGRENVT-MDEiEKAVKEAnaydfiMKLphkFDTLVGERGA-----QLSGGQKQR 530
Cdd:PRK11124 80 LRRNVGMVFQQYNLWPhLTVQQNLIEAPCRVLgLSK-DQALARA------EKL---LERLRLKPYAdrfplHLSGGQQQR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 25453402 531 IAIARALVRNPKILLLDEATSALDTESEA-VVQAALDKAREGRTTIVIAHRLSTVRN-ADVIAGFDGGVIVEQGNHD 605
Cdd:PRK11124 150 VAIARALMMEPQVLLFDEPTAALDPEITAqIVSIIRELAETGITQVIVTHEVEVARKtASRVVYMENGHIVEQGDAS 226
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
384-607 |
2.87e-27 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 114.29 E-value: 2.87e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 384 LEFKNIHFSYPSRKD-------VQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRTIN-- 454
Cdd:PRK11308 6 LQAIDLKKHYPVKRGlfkperlVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADpe 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 455 -VRYLREIIGVVSQ-----------------EPVLFATTIAENIRygRENVtMDEIEKAVKEANAYDfimKLPHKFdtlv 516
Cdd:PRK11308 86 aQKLLRQKIQIVFQnpygslnprkkvgqileEPLLINTSLSAAER--REKA-LAMMAKVGLRPEHYD---RYPHMF---- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 517 gergaqlSGGQKQRIAIARALVRNPKILLLDEATSALDTESEA-VVQAALDKAREGRTTIV-IAHRLSTVRNA--DVIAG 592
Cdd:PRK11308 156 -------SGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAqVLNLMMDLQQELGLSYVfISHDLSVVEHIadEVMVM 228
|
250
....*....|....*
gi 25453402 593 FDGGViVEQGNHDEL 607
Cdd:PRK11308 229 YLGRC-VEKGTKEQI 242
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
1027-1241 |
3.21e-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: 110.88 E-value: 3.21e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1027 VKFNGVMFNYPtrPNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIKQLNVQWLRAH-- 1104
Cdd:cd03290 1 VQVTNGYFSWG--SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRnr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1105 --LGIVSQEPILFDCSIAENIAYGDNSRVVSHEEIVKAAkeaNIHQFIDSLPEKYNTRVGDKGTQLSGGQKQRIAIARAL 1182
Cdd:cd03290 79 ysVAYAAQKPWLLNATVEENITFGSPFNKQRYKAVTDAC---SLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 25453402 1183 VRQPHILLLDEATSALDTE-SEKVVQEALDK--AREGRTCIVIAHRLSTIQNADLIVVIQNG 1241
Cdd:cd03290 156 YQNTNIVFLDDPFSALDIHlSDHLMQEGILKflQDDKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
402-594 |
3.71e-27 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 112.18 E-value: 3.71e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 402 LKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPI-----EGEVSIDGQDI--RTINVRYLREIIGVVSQEPVLFAT 474
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLIpgfrvEGKVTFHGKNLyaPDVDPVEVRRRIGMVFQKPNPFPK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 475 TIAENIRYG-REN---VTMDE-IEKAVKEANAYDFIMklphkfDTLvGERGAQLSGGQKQRIAIARALVRNPKILLLDEA 549
Cdd:PRK14243 106 SIYDNIAYGaRINgykGDMDElVERSLRQAALWDEVK------DKL-KQSGLSLSGGQQQRLCIARAIAVQPEVILMDEP 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 25453402 550 TSALDTESEAVVQAALDKAREGRTTIVIAHRLSTV-RNADVIAGFD 594
Cdd:PRK14243 179 CSALDPISTLRIEELMHELKEQYTIIIVTHNMQQAaRVSDMTAFFN 224
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1027-1254 |
3.72e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 112.39 E-value: 3.72e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1027 VKFNGVMFNYPTrpNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIKQLN-VQWLRAHL 1105
Cdd:PRK13644 2 IRLENVSYSYPD--GTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSkLQGIRKLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1106 GIVSQEP--ILFDCSIAENIAYGDNSRVVSHEEIVKAAKEAnihqFIDSLPEKYNTRvgdKGTQLSGGQKQRIAIARALV 1183
Cdd:PRK13644 80 GIVFQNPetQFVGRTVEEDLAFGPENLCLPPIEIRKRVDRA----LAEIGLEKYRHR---SPKTLSGGQGQCVALAGILT 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 25453402 1184 RQPHILLLDEATSALDTESEKVVQEALDKA-REGRTCIVIAHRLSTIQNADLIVVIQNGQVKEHGTHQQLLA 1254
Cdd:PRK13644 153 MEPECLIFDEVTSMLDPDSGIAVLERIKKLhEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLS 224
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
396-602 |
3.77e-27 |
|
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: 110.82 E-value: 3.77e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 396 RKDVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLL-QRLYDP--IEGEVSIDGQDIRtinvRYL-REIIGVVSQEPVL 471
Cdd:cd03234 17 NKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAIsGRVEGGgtTSGQILFNGQPRK----PDQfQKCVAYVRQDDIL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 472 FAT-TIAENIRYGRENVTMDEIEKAVKEANAYDFIMKLPHkfDTLVG-ERGAQLSGGQKQRIAIARALVRNPKILLLDEA 549
Cdd:cd03234 93 LPGlTVRETLTYTAILRLPRKSSDAIRKKRVEDVLLRDLA--LTRIGgNLVKGISGGERRRVSIAVQLLWDPKVLILDEP 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 25453402 550 TSALDTESE-AVVQAALDKAREGRTTIVIAH--RLSTVRNADVIAGFDGGVIVEQG 602
Cdd:cd03234 171 TSGLDSFTAlNLVSTLSQLARRNRIVILTIHqpRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1043-1242 |
3.80e-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: 3.80e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1043 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFL-DGKEIkqlnvqwlrahLgIVSQEPILFDCSIAE 1121
Cdd:COG4178 377 PLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpAGARV-----------L-FLPQRPYLPLGTLRE 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1122 NIAYGDNSRVVSHEEIVKAAKEANIHQFIDSLPEkyntrVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTE 1201
Cdd:COG4178 445 ALLYPATAEAFSDAELREALEAVGLGHLAERLDE-----EADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEE 519
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 25453402 1202 SEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIQNGQ 1242
Cdd:COG4178 520 NEAALYQLLREELPGTTVISVGHRSTLAAFHDRVLELTGDG 560
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1045-1235 |
4.23e-27 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 111.79 E-value: 4.23e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1045 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYD-----PMAGTVFLDGKEI---KQLNVQwLRAHLGIVSQEPILFD 1116
Cdd:PRK14239 21 LNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnpevTITGSIVYNGHNIyspRTDTVD-LRKEIGMVFQQPNPFP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1117 CSIAENIAYGDNSRVVSHEEIVKAAKEANIHQfiDSLPEKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATS 1196
Cdd:PRK14239 100 MSIYENVVYGLRLKGIKDKQVLDEAVEKSLKG--ASIWDEVKDRLHDSALGLSGGQQQRVCIARVLATSPKIILLDEPTS 177
|
170 180 190
....*....|....*....|....*....|....*....
gi 25453402 1197 ALDTESEKVVQEALDKAREGRTCIVIAHrlsTIQNADLI 1235
Cdd:PRK14239 178 ALDPISAGKIEETLLGLKDDYTMLLVTR---SMQQASRI 213
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
1045-1226 |
5.59e-27 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 111.80 E-value: 5.59e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1045 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMA-----GTVFLDGKEI--KQLNVQWLRAHLGIVSQEPILFDC 1117
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLIPgfrveGKVTFHGKNLyaPDVDPVEVRRRIGMVFQKPNPFPK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1118 SIAENIAYGD--NSRVVSHEEIV-KAAKEAnihqfidSLPEKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEA 1194
Cdd:PRK14243 106 SIYDNIAYGAriNGYKGDMDELVeRSLRQA-------ALWDEVKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEP 178
|
170 180 190
....*....|....*....|....*....|..
gi 25453402 1195 TSALDTESEKVVQEALDKAREGRTCIVIAHRL 1226
Cdd:PRK14243 179 CSALDPISTLRIEELMHELKEQYTIIIVTHNM 210
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
384-626 |
5.77e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 111.77 E-value: 5.77e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 384 LEFKNIHFSYPSRKDVQiLKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRTINVRYLREIIG 463
Cdd:PRK13648 8 IVFKNVSFQYQSDASFT-LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 464 VVSQEP--VLFATTIAENIRYGREN--VTMDEIEKAVKEA----NAYDFIMKLPHkfdtlvgergaQLSGGQKQRIAIAR 535
Cdd:PRK13648 87 IVFQNPdnQFVGSIVKYDVAFGLENhaVPYDEMHRRVSEAlkqvDMLERADYEPN-----------ALSGGQKQRVAIAG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 536 ALVRNPKILLLDEATSALDTESEAVVQAALDKAREGR--TTIVIAHRLSTVRNADVIAGFDGGVIVEQG------NHDEL 607
Cdd:PRK13648 156 VLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEAMEADHVIVMNKGTVYKEGtpteifDHAEE 235
|
250 260
....*....|....*....|.
gi 25453402 608 MREKG--IYFKLVMTQTAGNE 626
Cdd:PRK13648 236 LTRIGldLPFPIKINQMLGHQ 256
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
384-604 |
8.34e-27 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 117.52 E-value: 8.34e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 384 LEFKNIHFSYPS-RKDVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRTIN----VRYL 458
Cdd:PRK10535 5 LELKDIRRSYPSgEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDadalAQLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 459 REIIGVVSQEPVLFATTIAEnirygrENVTMDEI----EKAVKEANAYDFIMKLphKFDTLVGERGAQLSGGQKQRIAIA 534
Cdd:PRK10535 85 REHFGFIFQRYHLLSHLTAA------QNVEVPAVyaglERKQRLLRAQELLQRL--GLEDRVEYQPSQLSGGQQQRVSIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 25453402 535 RALVRNPKILLLDEATSALDTESEAVVQAALDKARE-GRTTIVIAHRLSTVRNAD-VIAGFDGGVIVEQGNH 604
Cdd:PRK10535 157 RALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDrGHTVIIVTHDPQVAAQAErVIEIRDGEIVRNPPAQ 228
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1044-1245 |
1.20e-26 |
|
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: 109.83 E-value: 1.20e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1044 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQL---LERfydPMAGTVFLDGKEIKQLN----VQWLRAHLGIVSQE----P 1112
Cdd:COG4181 27 ILKGISLEVEAGESVAIVGASGSGKSTLLGLlagLDR---PTSGTVRLAGQDLFALDedarARLRARHVGFVFQSfqllP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1113 ILfdcSIAENIAygdnsrV----VSHEEIVKAAKEAnihqfidsLpekynTRVGDKG------TQLSGGQKQRIAIARAL 1182
Cdd:COG4181 104 TL---TALENVM------LplelAGRRDARARARAL--------L-----ERVGLGHrldhypAQLSGGEQQRVALARAF 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 25453402 1183 VRQPHILLLDEATSALDTESEKVVQEAL-DKARE-GRTCIVIAHRLSTIQNADLIVVIQNGQVKE 1245
Cdd:COG4181 162 ATEPAILFADEPTGNLDAATGEQIIDLLfELNRErGTTLVLVTHDPALAARCDRVLRLRAGRLVE 226
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1041-1254 |
1.34e-26 |
|
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: 109.69 E-value: 1.34e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1041 NIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIKQLNVqWLRAHLGI--VSQEPILF-DC 1117
Cdd:COG0410 15 GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPP-HRIARLGIgyVPEGRRIFpSL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1118 SIAENIAYGdnSRVVSHEEIVKAAKEAnIHQFIDSLPEKYNTRvgdkGTQLSGGQKQRIAIARALVRQPHILLLDEATSA 1197
Cdd:COG0410 94 TVEENLLLG--AYARRDRAEVRADLER-VYELFPRLKERRRQR----AGTLSGGEQQMLAIGRALMSRPKLLLLDEPSLG 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 25453402 1198 LdteSEKVVQEALDK----AREGRTCIVI---AHRLSTIqnADLIVVIQNGQVKEHGTHQQLLA 1254
Cdd:COG0410 167 L---APLIVEEIFEIirrlNREGVTILLVeqnARFALEI--ADRAYVLERGRIVLEGTAAELLA 225
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1027-1248 |
1.36e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 111.05 E-value: 1.36e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1027 VKFNGVMFNYPTRPNiPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMA---GTVFLDGKEIKQLNVQWLRA 1103
Cdd:PRK13640 6 VEFKHVSFTYPDSKK-PALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDnpnSKITVDGITLTAKTVWDIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1104 HLGIVSQEP--ILFDCSIAENIAYGDNSRVVSHEEIVK----AAKEANIHQFIDSLPEkyntrvgdkgtQLSGGQKQRIA 1177
Cdd:PRK13640 85 KVGIVFQNPdnQFVGATVGDDVAFGLENRAVPRPEMIKivrdVLADVGMLDYIDSEPA-----------NLSGGQKQRVA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 25453402 1178 IARALVRQPHILLLDEATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTIQNADLIVVIQNGQVKEHGT 1248
Cdd:PRK13640 154 IAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKknNLTVISITHDIDEANMADQVLVLDDGKLLAQGS 226
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
1027-1254 |
1.47e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 111.27 E-value: 1.47e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1027 VKFNGVMFNYptRPNIP----VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEI----KQLNV 1098
Cdd:PRK13634 3 ITFQKVEHRY--QYKTPferrALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVItagkKNKKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1099 QWLRAHLGIVSQ--EPILFDCSIAENIAYGDNSRVVSHEEIVKAAKEAnihqfID--SLPEKYNTRvgdKGTQLSGGQKQ 1174
Cdd:PRK13634 81 KPLRKKVGIVFQfpEHQLFEETVEKDICFGPMNFGVSEEDAKQKAREM-----IElvGLPEELLAR---SPFELSGGQMR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1175 RIAIARALVRQPHILLLDEATSALDTESEKVVQE---ALDKaREGRTCIVIAHRLSTIQN-ADLIVVIQNGQVKEHGTHQ 1250
Cdd:PRK13634 153 RVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEmfyKLHK-EKGLTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTPR 231
|
....
gi 25453402 1251 QLLA 1254
Cdd:PRK13634 232 EIFA 235
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
400-608 |
1.65e-26 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 110.06 E-value: 1.65e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 400 QILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRTI-------------NVRYLREIIGVVS 466
Cdd:PRK10619 19 EVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVrdkdgqlkvadknQLRLLRTRLTMVF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 467 QEPVLFA-TTIAENIRygRENVTMDEIEKAVKEANAYDFIMKLPHKfDTLVGERGAQLSGGQKQRIAIARALVRNPKILL 545
Cdd:PRK10619 99 QHFNLWShMTVLENVM--EAPIQVLGLSKQEARERAVKYLAKVGID-ERAQGKYPVHLSGGQQQRVSIARALAMEPEVLL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 25453402 546 LDEATSALDTESEAVVQAALDK-AREGRTTIVIAHRLSTVRNADVIAGF-DGGVIVEQGNHDELM 608
Cdd:PRK10619 176 FDEPTSALDPELVGEVLRIMQQlAEEGKTMVVVTHEMGFARHVSSHVIFlHQGKIEEEGAPEQLF 240
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
384-602 |
1.66e-26 |
|
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: 108.43 E-value: 1.66e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 384 LEFKNIHFSYPSRKdvqILKGLNLKVKSGQTvALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRtINVRYLREIIG 463
Cdd:cd03264 1 LQLENLTKRYGKKR---ALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVL-KQPQKLRRRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 464 VVSQEPVLFAT-TIAENIRY-----GRENVTMD-EIEKAVKEANAYDFimklphkfdtlVGERGAQLSGGQKQRIAIARA 536
Cdd:cd03264 76 YLPQEFGVYPNfTVREFLDYiawlkGIPSKEVKaRVDEVLELVNLGDR-----------AKKKIGSLSGGMRRRVGIAQA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 25453402 537 LVRNPKILLLDEATSALDTESEAVVQAALDKAREGRTTIVIAHRLSTVRN-ADVIAGFDGGVIVEQG 602
Cdd:cd03264 145 LVGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
1045-1241 |
2.62e-26 |
|
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: 108.71 E-value: 2.62e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1045 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIKQLNVQWLrahlgIVSQEPILFD-CSIAENI 1123
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM-----VVFQNYSLLPwLTVRENI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1124 AYGDNsRVVSHeeIVKAAKEANIHQFID--SLPEKYNTRVGdkgtQLSGGQKQRIAIARALVRQPHILLLDEATSALDTE 1201
Cdd:TIGR01184 76 ALAVD-RVLPD--LSKSERRAIVEEHIAlvGLTEAADKRPG----QLSGGMKQRVAIARALSIRPKVLLLDEPFGALDAL 148
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 25453402 1202 SEKVVQEALDKARE--GRTCIVIAHRL-STIQNADLIVVIQNG 1241
Cdd:TIGR01184 149 TRGNLQEELMQIWEehRVTVLMVTHDVdEALLLSDRVVMLTNG 191
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1044-1254 |
2.80e-26 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 109.07 E-value: 2.80e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1044 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEI--------KQLNVQWLRAHLGIVSQEPILF 1115
Cdd:PRK11264 18 VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIdtarslsqQKGLIRQLRQHVGFVFQNFNLF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1116 DC-SIAENIAYGdnsrvvshEEIVKA-AKEANIhqfidSLPEKYNTRVGDKGTQ------LSGGQKQRIAIARALVRQPH 1187
Cdd:PRK11264 98 PHrTVLENIIEG--------PVIVKGePKEEAT-----ARARELLAKVGLAGKEtsyprrLSGGQQQRVAIARALAMRPE 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 25453402 1188 ILLLDEATSALDTEsekVVQEALDK----AREGRTCIVIAHRLSTIQN-ADLIVVIQNGQVKEHGTHQQLLA 1254
Cdd:PRK11264 165 VILFDEPTSALDPE---LVGEVLNTirqlAQEKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKALFA 233
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1043-1253 |
2.90e-26 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 109.03 E-value: 2.90e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1043 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIK--QLNVQWLRAHLGIVSQEPILFDCSIA 1120
Cdd:PRK09493 15 QVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpKVDERLIRQEAGMVFQQFYLFPHLTA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1121 -ENIAYGD-NSRVVSHEEIVKAAKE--ANIhqfidSLPEkyntRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATS 1196
Cdd:PRK09493 95 lENVMFGPlRVRGASKEEAEKQAREllAKV-----GLAE----RAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTS 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 25453402 1197 ALDTE-SEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVIQNGQVKEHGTHQQLL 1253
Cdd:PRK09493 166 ALDPElRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKvASRLIFIDKGRIAEDGDPQVLI 224
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
384-611 |
3.19e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 110.25 E-value: 3.19e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 384 LEFKNIHFSY----PSRKdvQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDI----RTINV 455
Cdd:PRK13646 3 IRFDNVSYTYqkgtPYEH--QAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIthktKDKYI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 456 RYLREIIGVVSQ--EPVLFATTIAENIRYGRENVTMDeIEKAvkEANAYDFIMKLPHKFDTLvGERGAQLSGGQKQRIAI 533
Cdd:PRK13646 81 RPVRKRIGMVFQfpESQLFEDTVEREIIFGPKNFKMN-LDEV--KNYAHRLLMDLGFSRDVM-SQSPFQMSGGQMRKIAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 534 ARALVRNPKILLLDEATSALDTESEAVVQAALDKAR--EGRTTIVIAHRLSTV-RNADVIAGFDGGVIVEQGNHDELMRE 610
Cdd:PRK13646 157 VSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtdENKTIILVSHDMNEVaRYADEVIVMKEGSIVSQTSPKELFKD 236
|
.
gi 25453402 611 K 611
Cdd:PRK13646 237 K 237
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
1044-1264 |
4.01e-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: 4.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1044 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDpMAGTVFLDGKEIKQLNVQWLRAHLGIVSQEPILFDCSIAENI 1123
Cdd:cd03289 19 VLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKAFGVIPQKVFIFSGTFRKNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1124 -AYGDNSrvvsHEEIVKAAKEANIHQFIDSLPEKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTES 1202
Cdd:cd03289 98 dPYGKWS----DEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPIT 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 25453402 1203 EKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIQNGQVKEHGTHQQLLAQKGIYFSMVS 1264
Cdd:cd03289 174 YQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHFKQAIS 235
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
136-337 |
4.02e-26 |
|
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; The bacterial lipid flippase MsbA is found in Gram-negative bacteria and transports lipid A and lipopolysaccharide (LPS) from the cytoplasmic leaflet to the periplasmic leaflet of the inner membrane. MsbA is also a polyspecific transporter capable of transporting a broad spectrum of drug molecules. Additionally, MsbA exhibits significant sequence similarity to mammalian multidrug resistance (MDR) proteins such as human MDR protein 1 (MDR1) and LmrA from Lactococcus lactis. This subgroup also contains a putative transporter Brevibacillus brevis TycD; the location of the tycD gene within the Tyc (tyrocidine) biosynthesis operon suggests that TycD may play a role in the secretion of the cyclic decapeptide antibiotic tyrocidine. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349996 [Multi-domain] Cd Length: 292 Bit Score: 109.82 E-value: 4.02e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 136 IHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFFQAMATFFGGFIIGFTRGWKLTLVILAISP 215
Cdd:cd18552 71 VRDLRNDLFDKLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKLTLIALVVLP 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 216 VLGLSAGIWAKILSSFTDKELQAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNNNLEEAKRLGIKKAITANISMGAAF 295
Cdd:cd18552 151 LAALPIRRIGKRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIARARALSSPLME 230
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 25453402 296 LLIYASYALAFWYGTSLVISKEYTIGQvltvFFSVLIGAFSV 337
Cdd:cd18552 231 LLGAIAIALVLWYGGYQVISGELTPGE----FISFITALLLL 268
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
113-329 |
4.39e-26 |
|
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: 109.83 E-value: 4.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 113 IGAGVL--IVAYIQVSLWCLAAGRQIHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFFQAMA 190
Cdd:cd18542 46 LGVALLrgVFRYLQGYLAEKASQKVAYDLRNDLYDHLQRLSFSFHDKARTGDLMSRCTSDVDTIRRFLAFGLVELVRAVL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 191 TFFGGFIIGFTRGWKLTLVILAISPVLGLSAGIWAKILSSFTDKELQAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYN 270
Cdd:cd18542 126 LFIGALIIMFSINWKLTLISLAIIPFIALFSYVFFKKVRPAFEEIREQEGELNTVLQENLTGVRVVKAFAREDYEIEKFD 205
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 25453402 271 NNLEEAKRLGIKKAITANISMGAAFLLIYASYALAFWYGTSLVISKEYTIGQvLTVFFS 329
Cdd:cd18542 206 KENEEYRDLNIKLAKLLAKYWPLMDFLSGLQIVLVLWVGGYLVINGEITLGE-LVAFIS 263
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1045-1248 |
4.44e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 109.75 E-value: 4.44e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1045 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEI--KQLNVQWLRAHLGIVSQEP--ILFDCSIA 1120
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdKKVKLSDIRKKVGLVFQYPeyQLFEETIE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1121 ENIAYGDNSRVVSHEEIVKAAKEAnihqfIDSLPEKYNTrVGDKGT-QLSGGQKQRIAIARALVRQPHILLLDEATSALD 1199
Cdd:PRK13637 103 KDIAFGPINLGLSEEEIENRVKRA-----MNIVGLDYED-YKDKSPfELSGGQKRRVAIAGVVAMEPKILILDEPTAGLD 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 25453402 1200 TeseKVVQEALDKARE-----GRTCIVIAHRLSTIQN-ADLIVVIQNGQVKEHGT 1248
Cdd:PRK13637 177 P---KGRDEILNKIKElhkeyNMTIILVSHSMEDVAKlADRIIVMNKGKCELQGT 228
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
367-618 |
4.80e-26 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 116.80 E-value: 4.80e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 367 IDSFSKSGHKPDNIQ-GNLEFKNIHFSYpsRKDVQ-ILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVS 444
Cdd:PTZ00243 1291 IEPASPTSAAPHPVQaGSLVFEGVQMRY--REGLPlVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIR 1368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 445 IDGQDIRTINVRYLREIIGVVSQEPVLFATTIAENIRYGREnVTMDEIEKAVKEANAYDFIMKLPHKFDTLVGERGAQLS 524
Cdd:PTZ00243 1369 VNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQNVDPFLE-ASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYS 1447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 525 GGQKQRIAIARALV-RNPKILLLDEATSALDTESEAVVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFDGGVIVEQGN 603
Cdd:PTZ00243 1448 VGQRQLMCMARALLkKGSGFILMDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGS 1527
|
250
....*....|....*.
gi 25453402 604 HDEL-MREKGIYFKLV 618
Cdd:PTZ00243 1528 PRELvMNRQSIFHSMV 1543
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1043-1255 |
4.83e-26 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 114.40 E-value: 4.83e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1043 PVLQGLSLEVKKGQTLALVGSSGCGKS----TVVQLLERFYDPMAGTVFLDGKEIKQLNVQWLRA----HLGIVSQEPI- 1113
Cdd:COG4172 24 EAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERELRRirgnRIAMIFQEPMt 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1114 ----LFdcSIAENIA-----YGDNSRVVSHEEIVKAAKEANIHQfidslPEKyntRVGDKGTQLSGGQKQRIAIARALVR 1184
Cdd:COG4172 104 slnpLH--TIGKQIAevlrlHRGLSGAAARARALELLERVGIPD-----PER---RLDAYPHQLSGGQRQRVMIAMALAN 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 25453402 1185 QPHILLLDEATSALDTesekVVQ-EALD-----KAREGRTCIVIAHRLSTIQN-ADLIVVIQNGQVKEHGTHQQLLAQ 1255
Cdd:COG4172 174 EPDLLIADEPTTALDV----TVQaQILDllkdlQRELGMALLLITHDLGVVRRfADRVAVMRQGEIVEQGPTAELFAA 247
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
384-607 |
6.66e-26 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 110.18 E-value: 6.66e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 384 LEFKN--IHFSYPSRKDV-----QILK---GLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRTI 453
Cdd:PRK15079 9 LEVADlkVHFDIKDGKQWfwqppKTLKavdGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGM 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 454 NVRYLREI---IGVVSQEPV-------LFATTIAENIRYGRENVTMDEIEKAVKEANAY-----DFIMKLPHKFdtlvge 518
Cdd:PRK15079 89 KDDEWRAVrsdIQMIFQDPLaslnprmTIGEIIAEPLRTYHPKLSRQEVKDRVKAMMLKvgllpNLINRYPHEF------ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 519 rgaqlSGGQKQRIAIARALVRNPKILLLDEATSALDTESEA-VVQAALDKARE-GRTTIVIAHRLSTVRN-ADVIAGFDG 595
Cdd:PRK15079 163 -----SGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAqVVNLLQQLQREmGLSLIFIAHDLAVVKHiSDRVLVMYL 237
|
250
....*....|..
gi 25453402 596 GVIVEQGNHDEL 607
Cdd:PRK15079 238 GHAVELGTYDEV 249
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
398-607 |
8.43e-26 |
|
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: 106.69 E-value: 8.43e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 398 DVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRTiNVRYLREIIGVVSQEPvlfattIA 477
Cdd:cd03265 12 DFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREVRRRIGIVFQDL------SV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 478 ENIRYGRENVTM---------DEIEKAVKEANAYdfiMKLPHKFDTLVGergaQLSGGQKQRIAIARALVRNPKILLLDE 548
Cdd:cd03265 85 DDELTGWENLYIharlygvpgAERRERIDELLDF---VGLLEAADRLVK----TYSGGMRRRLEIARSLVHRPEVLFLDE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 25453402 549 ATSALDTESEAVVQAALDK--AREGRTTIVIAHRLSTVRN-ADVIAGFDGGVIVEQGNHDEL 607
Cdd:cd03265 158 PTIGLDPQTRAHVWEYIEKlkEEFGMTILLTTHYMEEAEQlCDRVAIIDHGRIIAEGTPEEL 219
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
383-607 |
9.54e-26 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 110.50 E-value: 9.54e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 383 NLEFKNIHFSYpsrKDVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQdiRTINVRYLREII 462
Cdd:PRK11000 3 SVTLRNVTKAY---GDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEK--RMNDVPPAERGV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 463 GVVSQEPVLFA-TTIAENIRYGRE--NVTMDEIEKAVKEANAydfIMKLPHkfdtLVGERGAQLSGGQKQRIAIARALVR 539
Cdd:PRK11000 78 GMVFQSYALYPhLSVAENMSFGLKlaGAKKEEINQRVNQVAE---VLQLAH----LLDRKPKALSGGQRQRVAIGRTLVA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 25453402 540 NPKILLLDEATSALDTESEavVQ-----AALDKaREGRTTIVIAH-RLSTVRNADVIAGFDGGVIVEQGNHDEL 607
Cdd:PRK11000 151 EPSVFLLDEPLSNLDAALR--VQmrieiSRLHK-RLGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
139-354 |
1.07e-25 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350019 [Multi-domain] Cd Length: 289 Bit Score: 108.73 E-value: 1.07e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 139 IRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFFQAMATFFGGFIIGFTRGWKLTLVILAISPVL- 217
Cdd:cd18575 71 LRKAVFAHLLRLSPSFFETTRTGEVLSRLTTDTTLIQTVVGSSLSIALRNLLLLIGGLVMLFITSPKLTLLVLLVIPLVv 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 218 --GLSAGIWAKILSSFTDKELqayAKAGAVAEEVLAAIRTVIAFGGQKKELERYNNNLEEA-----KRLGIKKAITAnis 290
Cdd:cd18575 151 lpIILFGRRVRRLSRASQDRL---ADLSAFAEETLSAIKTVQAFTREDAERQRFATAVEAAfaaalRRIRARALLTA--- 224
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 25453402 291 mgAAFLLIYASYALAFWYGTSLVISKEYTIGQvLTVF-FSVLIGAFSVGQASPNIEAFANARGAA 354
Cdd:cd18575 225 --LVIFLVFGAIVFVLWLGAHDVLAGRMSAGE-LSQFvFYAVLAAGSVGALSEVWGDLQRAAGAA 286
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1034-1256 |
1.11e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 108.24 E-value: 1.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1034 FNYPTrpNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIKQLNVQWL--RAHLGIVSQE 1111
Cdd:PRK13639 9 YSYPD--GTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLevRKTVGIVFQN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1112 P--ILFDCSIAENIAYGDNSRVVSHEEIVKAAKEAnihqfidslpekyNTRVGDKGTQ------LSGGQKQRIAIARALV 1183
Cdd:PRK13639 87 PddQLFAPTVEEDVAFGPLNLGLSKEEVEKRVKEA-------------LKAVGMEGFEnkpphhLSGGQKKRVAIAGILA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 25453402 1184 RQPHILLLDEATSALDTE-SEKVVQEALDKAREGRTCIVIAHRLSTIQ-NADLIVVIQNGQVKEHGTHQQLLAQK 1256
Cdd:PRK13639 154 MKPEIIVLDEPTSGLDPMgASQIMKLLYDLNKEGITIIISTHDVDLVPvYADKVYVMSDGKIIKEGTPKEVFSDI 228
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
384-610 |
1.29e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 108.15 E-value: 1.29e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 384 LEFKNIHFSYPSrkDVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRTIN-VRYLREII 462
Cdd:PRK13644 2 IRLENVSYSYPD--GTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSkLQGIRKLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 463 GVVSQEP--VLFATTIAENIRYGRENVTMD--EIEKAVKEANAYDFIMKLPHKfdtlvgeRGAQLSGGQKQRIAIARALV 538
Cdd:PRK13644 80 GIVFQNPetQFVGRTVEEDLAFGPENLCLPpiEIRKRVDRALAEIGLEKYRHR-------SPKTLSGGQGQCVALAGILT 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 25453402 539 RNPKILLLDEATSALDTES-EAVVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFDGGVIVEQGNHDELMRE 610
Cdd:PRK13644 153 MEPECLIFDEVTSMLDPDSgIAVLERIKKLHEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLSD 225
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
1027-1247 |
1.34e-25 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 106.04 E-value: 1.34e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1027 VKFNGVMFNYPTRPnipvlQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIKQLNVQwlRAHLG 1106
Cdd:cd03298 1 VRLDKIRFSYGEQP-----MHFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA--DRPVS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1107 IVSQEPILF-DCSIAENIAYGDNSRV----VSHEEIVKAAKEANIHQFIDSLPEkyntrvgdkgtQLSGGQKQRIAIARA 1181
Cdd:cd03298 74 MLFQENNLFaHLTVEQNVGLGLSPGLkltaEDRQAIEVALARVGLAGLEKRLPG-----------ELSGGERQRVALARV 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 25453402 1182 LVRQPHILLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLSTIQN-ADLIVVIQNGQVKEHG 1247
Cdd:cd03298 143 LVRDKPVLLLDEPFAALDPALRAEMLDLVLDlhAETKMTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1044-1243 |
1.43e-25 |
|
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: 107.43 E-value: 1.43e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1044 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIKQLNVqWLRAHLGIVS--QEPILF-DCSIA 1120
Cdd:COG0411 19 AVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPP-HRIARLGIARtfQNPRLFpELTVL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1121 ENIA----YGDNSRVVSH-----------EEIVKAAKEAnIHQFidSLPEKYNTRVGDkgtqLSGGQKQRIAIARALVRQ 1185
Cdd:COG0411 98 ENVLvaahARLGRGLLAAllrlprarreeREARERAEEL-LERV--GLADRADEPAGN----LSYGQQRRLEIARALATE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 25453402 1186 PHILLLDEATSAL-DTESEKVVqEALDKARE--GRTCIVIAHRLSTIQN-ADLIVVIQNGQV 1243
Cdd:COG0411 171 PKLLLLDEPAAGLnPEETEELA-ELIRRLRDerGITILLIEHDMDLVMGlADRIVVLDFGRV 231
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1043-1253 |
1.44e-25 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 107.16 E-value: 1.44e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1043 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIKQLNVQWLRAHLGIVSQEPIL-FDCSIAE 1121
Cdd:PRK13548 16 TLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQHSSLsFPFTVEE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1122 NIAYGdnsrVVSHEEIVKAAKEanihqfidsLPEKYNTRVGDKG------TQLSGGQKQRIAIARALVR------QPHIL 1189
Cdd:PRK13548 96 VVAMG----RAPHGLSRAEDDA---------LVAAALAQVDLAHlagrdyPQLSGGEQQRVQLARVLAQlwepdgPPRWL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 25453402 1190 LLDEATSALD-TESEKVVQEALDKARE-GRTCIVIAHRLS-TIQNADLIVVIQNGQVKEHGTHQQLL 1253
Cdd:PRK13548 163 LLDEPTSALDlAHQHHVLRLARQLAHErGLAVIVVLHDLNlAARYADRIVLLHQGRLVADGTPAEVL 229
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
98-357 |
1.50e-25 |
|
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: 108.17 E-value: 1.50e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 98 KLEDEMTTYAYYYTGIGAGVLIVAYIQVSLWCLAAGRQIHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINEG 177
Cdd:cd18784 30 KSQDKFSRAIIIMGLLAIASSVAAGIRGGLFTLAMARLNIRIRNLLFRSIVSQEIGFFDTVKTGDITSRLTSDTTTMSDT 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 178 IGDKIGMFFQAMATFFGGFIIGFTRGWKLTLVILAISPVLGLSA---GIWAKILSsftdKELQ-AYAKAGAVAEEVLAAI 253
Cdd:cd18784 110 VSLNLNIFLRSLVKAIGVIVFMFKLSWQLSLVTLIGLPLIAIVSkvyGDYYKKLS----KAVQdSLAKANEVAEETISSI 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 254 RTVIAFGGQKKELERYNNNLEEAKRLGIKKAITANISMGAAFLLIYASYALAFWYGTSLVISKEYTIGQvltvFFSVLIG 333
Cdd:cd18784 186 RTVRSFANEDGEANRYSEKLKDTYKLKIKEALAYGGYVWSNELTELALTVSTLYYGGHLVITGQISGGN----LISFILY 261
|
250 260
....*....|....*....|....*...
gi 25453402 334 AFSVGQASPNIEA----FANARGAAYEV 357
Cdd:cd18784 262 QLELGSCLESVGSvytgLMQAVGAAEKV 289
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
383-554 |
1.57e-25 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 109.55 E-value: 1.57e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 383 NLEFKNIHFSYPSrkDVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRTINVRyLREIi 462
Cdd:PRK11650 3 GLKLQAVRKSYDG--KTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPA-DRDI- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 463 GVVSQEPVLFA-TTIAENIRYGRENVTM--DEIEKAVKEANAydfIMKLphkfDTLVGERGAQLSGGQKQRIAIARALVR 539
Cdd:PRK11650 79 AMVFQNYALYPhMSVRENMAYGLKIRGMpkAEIEERVAEAAR---ILEL----EPLLDRKPRELSGGQRQRVAMGRAIVR 151
|
170
....*....|....*
gi 25453402 540 NPKILLLDEATSALD 554
Cdd:PRK11650 152 EPAVFLFDEPLSNLD 166
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
384-554 |
1.69e-25 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 106.34 E-value: 1.69e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 384 LEFKNIHFSYPSRKdvqILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRTINVRYLREIIG 463
Cdd:PRK10247 8 LQLQNVGYLAGDAK---ILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 464 VVSQEPVLFATTIAENIRYGRenvtmdEIEKAVKEANAY-DFIMK--LPhkfDTLVGERGAQLSGGQKQRIAIARALVRN 540
Cdd:PRK10247 85 YCAQTPTLFGDTVYDNLIFPW------QIRNQQPDPAIFlDDLERfaLP---DTILTKNIAELSGGEKQRISLIRNLQFM 155
|
170
....*....|....
gi 25453402 541 PKILLLDEATSALD 554
Cdd:PRK10247 156 PKVLLLDEITSALD 169
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1041-1255 |
2.15e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 107.48 E-value: 2.15e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1041 NIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIKQLNVQW-LRAHLGIVSQEPilfDCSI 1119
Cdd:PRK13633 22 EKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLWdIRNKAGMVFQNP---DNQI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1120 A-----ENIAYGDNSRVVSHEEIVK----AAKEANIHQFIDSLPEkyntrvgdkgtQLSGGQKQRIAIARALVRQPHILL 1190
Cdd:PRK13633 99 VativeEDVAFGPENLGIPPEEIRErvdeSLKKVGMYEYRRHAPH-----------LLSGGQKQRVAIAGILAMRPECII 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 25453402 1191 LDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLSTIQNADLIVVIQNGQVKEHGTHQQLLAQ 1255
Cdd:PRK13633 168 FDEPTAMLDPSGRREVVNTIKElnKKYGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEIFKE 234
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1043-1256 |
2.26e-25 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 106.64 E-value: 2.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1043 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIKQLNVQWLRAHLGIVSQEPIL-FDCSIAE 1121
Cdd:PRK11231 16 RILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHHLTpEGITVRE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1122 NIAYGdNSRVVSH--------EEIVKAAKEANihqFIDSLPEKyntRVgdkgTQLSGGQKQRIAIARALVRQPHILLLDE 1193
Cdd:PRK11231 96 LVAYG-RSPWLSLwgrlsaedNARVNQAMEQT---RINHLADR---RL----TDLSGGQRQRAFLAMVLAQDTPVVLLDE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 25453402 1194 ATSALD----TESEKVVQEAldkAREGRTCIVIAHRLS-TIQNADLIVVIQNGQVKEHGTHQQLLAQK 1256
Cdd:PRK11231 165 PTTYLDinhqVELMRLMREL---NTQGKTVVTVLHDLNqASRYCDHLVVLANGHVMAQGTPEEVMTPG 229
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1041-1247 |
2.54e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 106.54 E-value: 2.54e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1041 NIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYD-----PMAGTVFLDGKEIKQLNVQWLRAHLGIVSQEP-IL 1114
Cdd:PRK14247 15 QVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDIFKMDVIELRRRVQMVFQIPnPI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1115 FDCSIAENIAYGD--NSRVVSHEEIVKAAKEANIHQfidSLPEKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLD 1192
Cdd:PRK14247 95 PNLSIFENVALGLklNRLVKSKKELQERVRWALEKA---QLWDEVKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLAD 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 25453402 1193 EATSALDTESEKVVQEALDKAREGRTCIVIAH------RLStiqnaDLIVVIQNGQVKEHG 1247
Cdd:PRK14247 172 EPTANLDPENTAKIESLFLELKKDMTIVLVTHfpqqaaRIS-----DYVAFLYKGQIVEWG 227
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
400-556 |
3.15e-25 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 108.63 E-value: 3.15e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 400 QILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRTINVRYLReiIGVVSQEPVLFA-TTIAE 478
Cdd:PRK10851 16 QVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRK--VGFVFQHYALFRhMTVFD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 479 NIRYG------RENVTMDEIEKAVKEANAydfIMKLPHkfdtLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSA 552
Cdd:PRK10851 94 NIAFGltvlprRERPNAAAIKAKVTQLLE---MVQLAH----LADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGA 166
|
....
gi 25453402 553 LDTE 556
Cdd:PRK10851 167 LDAQ 170
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1027-1253 |
3.40e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 106.27 E-value: 3.40e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1027 VKFNGVMFNYPTRPnipVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDpMAGTVFLDGK-EI-------KQLNV 1098
Cdd:PRK14258 8 IKVNNLSFYYDTQK---ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNE-LESEVRVEGRvEFfnqniyeRRVNL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1099 QWLRAHLGIVSQEPILFDCSIAENIAYGDN----SRVVSHEEIVKAAKEANihqfidSLPEKYNTRVGDKGTQLSGGQKQ 1174
Cdd:PRK14258 84 NRLRRQVSMVHPKPNLFPMSVYDNVAYGVKivgwRPKLEIDDIVESALKDA------DLWDEIKHKIHKSALDLSGGQQQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1175 RIAIARALVRQPHILLLDEATSALDTESEKVVQEALD--KAREGRTCIVIAHRLSTIQN-ADLIVVIQN-----GQVKEH 1246
Cdd:PRK14258 158 RLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQslRLRSELTMVIVSHNLHQVSRlSDFTAFFKGnenriGQLVEF 237
|
....*..
gi 25453402 1247 GTHQQLL 1253
Cdd:PRK14258 238 GLTKKIF 244
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
327-580 |
3.56e-25 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 111.82 E-value: 3.56e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 327 FFSvliGAFSVG---QASpniEAFANARGAayevFS-IIDNKPSI----------DSFSKSGHKPDNIQ----------- 381
Cdd:COG4178 291 YFA---GEITLGglmQAA---SAFGQVQGA----LSwFVDNYQSLaewratvdrlAGFEEALEAADALPeaasrietsed 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 382 GNLEFKNIHFSYPSRKdvQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSI-DGQDIrtinvryLre 460
Cdd:COG4178 361 GALALEDLTLRTPDGR--PLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpAGARV-------L-- 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 461 iigVVSQEPVLFATTIAENIRY--GRENVTMDEIEKAVKEANaydfimkLPH---KFDTlVGERGAQLSGGQKQRIAIAR 535
Cdd:COG4178 430 ---FLPQRPYLPLGTLREALLYpaTAEAFSDAELREALEAVG-------LGHlaeRLDE-EADWDQVLSLGEQQRLAFAR 498
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 25453402 536 ALVRNPKILLLDEATSALDTESEAVVQAALDKAREGRTTIVIAHR 580
Cdd:COG4178 499 LLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHR 543
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
384-602 |
3.69e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 106.75 E-value: 3.69e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 384 LEFKNIHFSYPSRKDVQ--ILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRTI----NVRY 457
Cdd:PRK13649 3 INLQNVSYTYQAGTPFEgrALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTsknkDIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 458 LREIIGVVSQ--EPVLFATTIAENIRYGREN--VTMDEIEKAVKEANAYDFIMklphkfDTLVGERGAQLSGGQKQRIAI 533
Cdd:PRK13649 83 IRKKVGLVFQfpESQLFEETVLKDVAFGPQNfgVSQEEAEALAREKLALVGIS------ESLFEKNPFELSGGQMRRVAI 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 25453402 534 ARALVRNPKILLLDEATSALDTESEAVVQAALDKAREGRTTIV-IAHRLSTVRN-ADVIAGFDGGVIVEQG 602
Cdd:PRK13649 157 AGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVlVTHLMDDVANyADFVYVLEKGKLVLSG 227
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
384-602 |
5.57e-25 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 110.95 E-value: 5.57e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 384 LEFKNIHFSYPSRKDV--------QILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYdPIEGEVSIDGQDIRTINV 455
Cdd:PRK15134 276 LDVEQLQVAFPIRKGIlkrtvdhnVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLHNLNR 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 456 RYL---REIIGVVSQEP---------VLfaTTIAENIRYGRENVTMDEIEKAVKEAnaydfiMK-------LPHKFDtlv 516
Cdd:PRK15134 355 RQLlpvRHRIQVVFQDPnsslnprlnVL--QIIEEGLRVHQPTLSAAQREQQVIAV------MEevgldpeTRHRYP--- 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 517 gergAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDKAREGR--TTIVIAHRLSTVRNA--DVIAG 592
Cdd:PRK15134 424 ----AEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHqlAYLFISHDLHVVRALchQVIVL 499
|
250
....*....|
gi 25453402 593 FDGGViVEQG 602
Cdd:PRK15134 500 RQGEV-VEQG 508
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
388-595 |
5.95e-25 |
|
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: 104.34 E-value: 5.95e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 388 NIHFSYPSrkDVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEV----SIDGQDIRTINVRYLREIIG 463
Cdd:cd03290 5 NGYFSWGS--GLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsnKNESEPSFEATRSRNRYSVA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 464 VVSQEPVLFATTIAENIRYGreNVTMDEIEKAVKEANAYD-FIMKLPHKFDTLVGERGAQLSGGQKQRIAIARALVRNPK 542
Cdd:cd03290 83 YAAQKPWLLNATVEENITFG--SPFNKQRYKAVTDACSLQpDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTN 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 25453402 543 ILLLDEATSALDTE-SEAVVQAALDK--AREGRTTIVIAHRLSTVRNAD-VIAGFDG 595
Cdd:cd03290 161 IVFLDDPFSALDIHlSDHLMQEGILKflQDDKRTLVLVTHKLQYLPHADwIIAMKDG 217
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
1044-1247 |
6.08e-25 |
|
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: 103.90 E-value: 6.08e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1044 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIKQLNvqwlRAHLGIVSQEPILF-DCSIAEN 1122
Cdd:cd03269 15 ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA----RNRIGYLPEERGLYpKMKVIDQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1123 IAYGDNSRVVSHEEIVKAAKEAnIHQFidSLPEKYNTRVgdkgTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTES 1202
Cdd:cd03269 91 LVYLAQLKGLKKEEARRRIDEW-LERL--ELSEYANKRV----EELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVN 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 25453402 1203 EKVVQEAL-DKAREGRTCIVIAHRLSTIQN-ADLIVVIQNGQVKEHG 1247
Cdd:cd03269 164 VELLKDVIrELARAGKTVILSTHQMELVEElCDRVLLLNKGRAVLYG 210
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
384-602 |
6.26e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 105.31 E-value: 6.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 384 LEFKNIHFSYPSRkdvQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYD-----PIEGEVSIDGQDIRTINVR-- 456
Cdd:PRK14267 5 IETVNLRVYYGSN---HVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGRNIYSPDVDpi 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 457 YLREIIGVVSQEPVLFA-TTIAENIRYG-------RENVTMDE-IEKAVKEANAYDfimklphKFDTLVGERGAQLSGGQ 527
Cdd:PRK14267 82 EVRREVGMVFQYPNPFPhLTIYDNVAIGvklnglvKSKKELDErVEWALKKAALWD-------EVKDRLNDYPSNLSGGQ 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 25453402 528 KQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDKAREGRTTIVIAHR-LSTVRNADVIAGFDGGVIVEQG 602
Cdd:PRK14267 155 RQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSpAQAARVSDYVAFLYLGKLIEVG 230
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
1044-1247 |
7.23e-25 |
|
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: 103.81 E-value: 7.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1044 VLQGLSLEVKKGQTlALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIKQlNVQWLRAHLGIVSQEPILFDcsiaeni 1123
Cdd:cd03264 15 ALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLRRRIGYLPQEFGVYP------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1124 aygdNSRVVSHEEIVKAAKE---ANIHQFIDSLPEKYN--TRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSAL 1198
Cdd:cd03264 86 ----NFTVREFLDYIAWLKGipsKEVKARVDEVLELVNlgDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 25453402 1199 DTESEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVIQNGQVKEHG 1247
Cdd:cd03264 162 DPEERIRFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1044-1253 |
1.03e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 104.74 E-value: 1.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1044 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERF---YDP---MAGTVFLDGKEIKQLNVQWLRAHLGIVSQEPILF-D 1116
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLieiYDSkikVDGKVLYFGKDIFQIDAIKLRKEVGMVFQQPNPFpH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1117 CSIAENIAYGDNSRVVSHEEIVKAAKEANIHQFidSLPEKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATS 1196
Cdd:PRK14246 105 LSIYDNIAYPLKSHGIKEKREIKKIVEECLRKV--GLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTS 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 25453402 1197 ALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVIQNGQVKEHGTHQQLL 1253
Cdd:PRK14246 183 MIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARvADYVAFLYNGELVEWGSSNEIF 240
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1044-1255 |
1.08e-24 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 104.67 E-value: 1.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1044 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIK-------QLNV------QWLRAHLGIVSQ 1110
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgQLKVadknqlRLLRTRLTMVFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1111 EPILFdcsiaeniaygdnsrvvSHEEIVKAAKEANIHQFIDSLPE------KYNTRVG-DKGTQ------LSGGQKQRIA 1177
Cdd:PRK10619 100 HFNLW-----------------SHMTVLENVMEAPIQVLGLSKQEareravKYLAKVGiDERAQgkypvhLSGGQQQRVS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1178 IARALVRQPHILLLDEATSALDTESEKVVQEALDK-AREGRTCIVIAHRLSTIQN-ADLIVVIQNGQVKEHGTHQQLLAQ 1255
Cdd:PRK10619 163 IARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQlAEEGKTMVVVTHEMGFARHvSSHVIFLHQGKIEEEGAPEQLFGN 242
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
384-611 |
1.12e-24 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 104.85 E-value: 1.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 384 LEFKNIHFSYPSRkdvQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRTINVRYLREIIG 463
Cdd:PRK13548 3 LEARNLSVRLGGR---TLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 464 VVSQEPVL-FATTIAENIRYGRE--NVTMDEIEKAVKEANAydfIMKLPHkfdtLVGERGAQLSGGQKQRIAIARALVR- 539
Cdd:PRK13548 80 VLPQHSSLsFPFTVEEVVAMGRAphGLSRAEDDALVAAALA---QVDLAH----LAGRDYPQLSGGEQQRVQLARVLAQl 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 540 -----NPKILLLDEATSALD-TESEAVVQAALDKARE-GRTTIVIAHRLS-TVRNADVIAGFDGGVIVEQGNHDELMREK 611
Cdd:PRK13548 153 wepdgPPRWLLLDEPTSALDlAHQHHVLRLARQLAHErGLAVIVVLHDLNlAARYADRIVLLHQGRLVADGTPAEVLTPE 232
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
384-554 |
1.13e-24 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 104.94 E-value: 1.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 384 LEFKNIHFSYP-SRKDVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRTINVRylReii 462
Cdd:COG4525 4 LTVRHVSVRYPgGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGAD--R--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 463 GVVSQEPVLFA-TTIAENIRYGrenVTMDEIEKAVKEANAYDFImklphkfdTLVGERGA------QLSGGQKQRIAIAR 535
Cdd:COG4525 79 GVVFQKDALLPwLNVLDNVAFG---LRLRGVPKAERRARAEELL--------ALVGLADFarrriwQLSGGMRQRVGIAR 147
|
170
....*....|....*....
gi 25453402 536 ALVRNPKILLLDEATSALD 554
Cdd:COG4525 148 ALAADPRFLLMDEPFGALD 166
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1043-1247 |
1.34e-24 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 102.63 E-value: 1.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1043 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLL--ERFYDPMAGTVFLDGKEIKQlnvQWLRAHLGIVSQEPILFDC-SI 1119
Cdd:cd03213 23 QLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGRPLDK---RSFRKIIGYVPQDDILHPTlTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1120 AENIAYgdnsrvvsheeivkAAKeanihqfidsLpekyntrvgdKGtqLSGGQKQRIAIARALVRQPHILLLDEATSALD 1199
Cdd:cd03213 100 RETLMF--------------AAK----------L----------RG--LSGGERKRVSIALELVSNPSLLFLDEPTSGLD 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 25453402 1200 TESEKVVQEALDK-AREGRTCIVIAHRLST--IQNADLIVVIQNGQVKEHG 1247
Cdd:cd03213 144 SSSALQVMSLLRRlADTGRTIICSIHQPSSeiFELFDKLLLLSQGRVIYFG 194
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
384-607 |
1.42e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 104.88 E-value: 1.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 384 LEFKNIHFSYpsRKDVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRTINVRYLREIIG 463
Cdd:PRK13652 4 IETRDLCYSY--SGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 464 VVSQEP--VLFATTIAENIRYGRENVTMDE------IEKAVKEANAYDFIMKLPHkfdtlvgergaQLSGGQKQRIAIAR 535
Cdd:PRK13652 82 LVFQNPddQIFSPTVEQDIAFGPINLGLDEetvahrVSSALHMLGLEELRDRVPH-----------HLSGGEKKRVAIAG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 25453402 536 ALVRNPKILLLDEATSALDTESEAVVQAALDKARE--GRTTIVIAHRLSTVRN-ADVIAGFDGGVIVEQGNHDEL 607
Cdd:PRK13652 151 VIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPEtyGMTVIFSTHQLDLVPEmADYIYVMDKGRIVAYGTVEEI 225
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
1043-1248 |
1.87e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 104.83 E-value: 1.87e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1043 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEI----KQLNVQWLRAHLGIVSQ--EPILFD 1116
Cdd:PRK13649 21 RALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLItstsKNKDIKQIRKKVGLVFQfpESQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1117 CSIAENIAYGDNSRVVSHEEIVKAAKEA-NIHQFIDSLPEKyntrvgdKGTQLSGGQKQRIAIARALVRQPHILLLDEAT 1195
Cdd:PRK13649 101 ETVLKDVAFGPQNFGVSQEEAEALAREKlALVGISESLFEK-------NPFELSGGQMRRVAIAGILAMEPKILVLDEPT 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 25453402 1196 SALDTESEKVVQEALDKARE-GRTCIVIAHRLSTIQN-ADLIVVIQNGQVKEHGT 1248
Cdd:PRK13649 174 AGLDPKGRKELMTLFKKLHQsGMTIVLVTHLMDDVANyADFVYVLEKGKLVLSGK 228
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
384-602 |
1.94e-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: 102.83 E-value: 1.94e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 384 LEFKNIHFSY-PSRKDVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRTiNVRYLREII 462
Cdd:cd03266 2 ITADALTKRFrDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-EPAEARRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 463 GVVSQEPVLFA-TTIAENIRY--GRENVTMDEIEKAVKEanaydFIMKLphKFDTLVGERGAQLSGGQKQRIAIARALVR 539
Cdd:cd03266 81 GFVSDSTGLYDrLTARENLEYfaGLYGLKGDELTARLEE-----LADRL--GMEELLDRRVGGFSTGMRQKVAIARALVH 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 25453402 540 NPKILLLDEATSALDTESEAVVQAALDKAREGRTTIVIA-HRLSTV-RNADVIAGFDGGVIVEQG 602
Cdd:cd03266 154 DPPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFStHIMQEVeRLCDRVVVLHRGRVVYEG 218
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
384-602 |
2.08e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 104.91 E-value: 2.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 384 LEFKNIHFSYP--SRKDVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIR----TINVRY 457
Cdd:PRK13641 3 IKFENVDYIYSpgTPMEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgNKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 458 LREIIGVVSQ--EPVLFATTIAENIRYGRENVTMDEIEKAVKeanAYDFIMKLPHKfDTLVGERGAQLSGGQKQRIAIAR 535
Cdd:PRK13641 83 LRKKVSLVFQfpEAQLFENTVLKDVEFGPKNFGFSEDEAKEK---ALKWLKKVGLS-EDLISKSPFELSGGQMRRVAIAG 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 25453402 536 ALVRNPKILLLDEATSALDTES-EAVVQAALDKAREGRTTIVIAHrlstvrNADVIAGFDGGVIV-EQG 602
Cdd:PRK13641 159 VMAYEPEILCLDEPAAGLDPEGrKEMMQLFKDYQKAGHTVILVTH------NMDDVAEYADDVLVlEHG 221
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
384-611 |
2.60e-24 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 103.56 E-value: 2.60e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 384 LEFKNIHFSYPSRKdvqILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRTINVRYLREIIG 463
Cdd:PRK11231 3 LRTENLTVGYGTKR---ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 464 VVSQEPVL-FATTIAENIRYGRE------NVTMDEIEKAVKEAnaydfiMKLPHkFDTLVGERGAQLSGGQKQRIAIARA 536
Cdd:PRK11231 80 LLPQHHLTpEGITVRELVAYGRSpwlslwGRLSAEDNARVNQA------MEQTR-INHLADRRLTDLSGGQRQRAFLAMV 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 25453402 537 LVRNPKILLLDEATSALDTESEAVVQAALDKAR-EGRTTIVIAHRLSTV-RNADVIAGFDGGVIVEQGNHDELMREK 611
Cdd:PRK11231 153 LAQDTPVVLLDEPTTYLDINHQVELMRLMRELNtQGKTVVTVLHDLNQAsRYCDHLVVLANGHVMAQGTPEEVMTPG 229
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
1045-1255 |
2.81e-24 |
|
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: 105.95 E-value: 2.81e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1045 LQGLSLEVK-----KGQTlALVGSSGCGKSTVVQL---LERfydPMAGTVFLDGkEIKQ--LNVQWLRAH---LGIVSQE 1111
Cdd:COG4148 11 RGGFTLDVDftlpgRGVT-ALFGPSGSGKTTLLRAiagLER---PDSGRIRLGG-EVLQdsARGIFLPPHrrrIGYVFQE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1112 PILFD-CSIAENIAYG-----DNSRVVSHEEIVKAAkeaNIHQFIDSLPEkyntrvgdkgtQLSGGQKQRIAIARALVRQ 1185
Cdd:COG4148 86 ARLFPhLSVRGNLLYGrkrapRAERRISFDEVVELL---GIGHLLDRRPA-----------TLSGGERQRVAIGRALLSS 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 25453402 1186 PHILLLDEATSALDTESeKvvQEALDK----AREGRTCIV-IAHRLSTIQN-ADLIVVIQNGQVKEHGTHQQLLAQ 1255
Cdd:COG4148 152 PRLLLMDEPLAALDLAR-K--AEILPYlerlRDELDIPILyVSHSLDEVARlADHVVLLEQGRVVASGPLAEVLSR 224
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
134-354 |
2.98e-24 |
|
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: 104.44 E-value: 2.98e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 134 RQIHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFFQAMATFFGGFIIGFTRGWKLTLVILAI 213
Cdd:cd18551 66 RVVLDLRRRLWRRLLRLPVSFFDRRRSGDLVSRVTNDTTLLRELITSGLPQLVTGVLTVVGAVVLMFLLDWVLTLVTLAV 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 214 SPVLGLSAGIWAKILSSFTDKELQAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNNNLEEAKRLGIKKAITANISMGA 293
Cdd:cd18551 146 VPLAFLIILPLGRRIRKASKRAQDALGELSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAKIEALIGPL 225
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 25453402 294 AFLLIYASYALAFWYGTSLVISKEYTIGQVLTVFFSVLIGAFSVGQASPNIEAFANARGAA 354
Cdd:cd18551 226 MGLAVQLALLVVLGVGGARVASGALTVGTLVAFLLYLFQLITPLSQLSSFFTQLQKALGAL 286
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
397-602 |
3.37e-24 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 101.91 E-value: 3.37e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 397 KDVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDI-RTINVRylrEIIGVVSQEPVLFAT- 474
Cdd:cd03268 11 GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYqKNIEAL---RRIGALIEAPGFYPNl 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 475 TIAENIR-----YGRENVTMDEIEKAVKEANAydfimklPHKfdtlvgeRGAQLSGGQKQRIAIARALVRNPKILLLDEA 549
Cdd:cd03268 88 TARENLRllarlLGIRKKRIDEVLDVVGLKDS-------AKK-------KVKGFSLGMKQRLGIALALLGNPDLLILDEP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 25453402 550 TSALDTESEAVVQAAL-DKAREGRTTIVIAHRLSTVRN-ADVIAGFDGGVIVEQG 602
Cdd:cd03268 154 TNGLDPDGIKELRELIlSLRDQGITVLISSHLLSEIQKvADRIGIINKGKLIEEG 208
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
384-585 |
3.41e-24 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 108.19 E-value: 3.41e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 384 LEFKNIHFSYPSrkdVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRtinvrylreI-- 461
Cdd:COG3845 6 LELRGITKRFGG---VVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVR---------Irs 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 462 --------IGVVSQEPVLFAT-TIAENIRYGRENVT-----MDEIEKAVKE-ANAYDFIMKLphkfDTLVGergaQLSGG 526
Cdd:COG3845 74 prdaialgIGMVHQHFMLVPNlTVAENIVLGLEPTKggrldRKAARARIRElSERYGLDVDP----DAKVE----DLSVG 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 25453402 527 QKQRIAIARALVRNPKILLLDEATSALdTESEAV-VQAALDK-AREGRTTIVIAHRLSTVR 585
Cdd:COG3845 146 EQQRVEILKALYRGARILILDEPTAVL-TPQEADeLFEILRRlAAEGKSIIFITHKLREVM 205
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
384-611 |
3.52e-24 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 102.60 E-value: 3.52e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 384 LEFKNIHFSYpsrKDVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDI-RTINVRYLREII 462
Cdd:TIGR03410 1 LEVSNLNVYY---GQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDItKLPPHERARAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 463 GVVSQEPVLFAT-TIAENIRYGREnvTMDEIEKAVKeanayDFIMKL-PHKFDTLvGERGAQLSGGQKQRIAIARALVRN 540
Cdd:TIGR03410 78 AYVPQGREIFPRlTVEENLLTGLA--ALPRRSRKIP-----DEIYELfPVLKEML-GRRGGDLSGGQQQQLAIARALVTR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 25453402 541 PKILLLDEATSALDTESEAVVQAALDK--AREGRTTIVIAHRLSTVRN-ADVIAGFDGGVIVEQGNHDELMREK 611
Cdd:TIGR03410 150 PKLLLLDEPTEGIQPSIIKDIGRVIRRlrAEGGMAILLVEQYLDFARElADRYYVMERGRVVASGAGDELDEDK 223
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1042-1224 |
3.53e-24 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 106.07 E-value: 3.53e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1042 IPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIKQlnVQWLRAHLGIVSQEPILF-DCSIA 1120
Cdd:PRK11607 32 QHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSH--VPPYQRPINMMFQSYALFpHMTVE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1121 ENIAYGDNSRVVSHEEIVKAAKE--ANIHQfidslpEKYNTRvgdKGTQLSGGQKQRIAIARALVRQPHILLLDEATSAL 1198
Cdd:PRK11607 110 QNIAFGLKQDKLPKAEIASRVNEmlGLVHM------QEFAKR---KPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGAL 180
|
170 180
....*....|....*....|....*...
gi 25453402 1199 DTESEKVVQ-EALD-KAREGRTCIVIAH 1224
Cdd:PRK11607 181 DKKLRDRMQlEVVDiLERVGVTCVMVTH 208
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1045-1255 |
3.62e-24 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 105.05 E-value: 3.62e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1045 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIKQLN---VQWLRAHLGIVSQEPilfdcsiae 1121
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADpeaQKLLRQKIQIVFQNP--------- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1122 niaYGD-NSR----------VVSHEEIVKAAKEANIHQFIDSL---PEKYNtRVGDkgtQLSGGQKQRIAIARALVRQPH 1187
Cdd:PRK11308 102 ---YGSlNPRkkvgqileepLLINTSLSAAERREKALAMMAKVglrPEHYD-RYPH---MFSGGQRQRIAIARALMLDPD 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 25453402 1188 ILLLDEATSALDTESE-KVVQEALDKAREGRTCIV-IAHRLSTIQN-ADLIVVIQNGQVKEHGTHQQLLAQ 1255
Cdd:PRK11308 175 VVVADEPVSALDVSVQaQVLNLMMDLQQELGLSYVfISHDLSVVEHiADEVMVMYLGRCVEKGTKEQIFNN 245
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1027-1229 |
3.62e-24 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 102.86 E-value: 3.62e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1027 VKFNGVMFNYPTRPnipVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAG-TVFLDGKEIKQLNVQWLRAHL 1105
Cdd:COG1119 4 LELRNVTVRRGGKT---ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGEDVWELRKRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1106 GIVS---QEPILFDCSIAENIAYGDNS-----RVVSHEEIVKAakeaniHQFIDSLpekyntRVGDKG----TQLSGGQK 1173
Cdd:COG1119 81 GLVSpalQLRFPRDETVLDVVLSGFFDsiglyREPTDEQRERA------RELLELL------GLAHLAdrpfGTLSQGEQ 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 25453402 1174 QRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDK-AREGRTCIV-IAHRLSTI 1229
Cdd:COG1119 149 RRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKlAAEGAPTLVlVTHHVEEI 206
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
388-607 |
3.78e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 103.20 E-value: 3.78e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 388 NIHFSYPSRKDVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQ------DIRTINVRYLREI 461
Cdd:PRK14246 12 NISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkDIFQIDAIKLRKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 462 IGVVSQEPVLFA-TTIAENIRYGRENVTMD---EIEKAVKEANAYDFIMKLPHkfDTLvGERGAQLSGGQKQRIAIARAL 537
Cdd:PRK14246 92 VGMVFQQPNPFPhLSIYDNIAYPLKSHGIKekrEIKKIVEECLRKVGLWKEVY--DRL-NSPASQLSGGQQQRLTIARAL 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 25453402 538 VRNPKILLLDEATSALDTESEAVVQAALDKAREGRTTIVIAHRLSTV-RNADVIAGFDGGVIVEQGNHDEL 607
Cdd:PRK14246 169 ALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVaRVADYVAFLYNGELVEWGSSNEI 239
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1027-1256 |
3.95e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 104.14 E-value: 3.95e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1027 VKFNGVmfNYPTRPNIPV----LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIK----QLNV 1098
Cdd:PRK13641 3 IKFENV--DYIYSPGTPMekkgLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgNKNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1099 QWLRAHLGIVSQ--EPILFDCSIAENIAYGDNSRVVSHEEivkaAKEANIhqfidslpeKYNTRVG------DKGT-QLS 1169
Cdd:PRK13641 81 KKLRKKVSLVFQfpEAQLFENTVLKDVEFGPKNFGFSEDE----AKEKAL---------KWLKKVGlsedliSKSPfELS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1170 GGQKQRIAIARALVRQPHILLLDEATSALDTESEK-VVQEALDKAREGRTCIVIAHRLSTI-QNADLIVVIQNGQVKEHG 1247
Cdd:PRK13641 148 GGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKeMMQLFKDYQKAGHTVILVTHNMDDVaEYADDVLVLEHGKLIKHA 227
|
....*....
gi 25453402 1248 THQQLLAQK 1256
Cdd:PRK13641 228 SPKEIFSDK 236
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
1027-1247 |
4.49e-24 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 101.52 E-value: 4.49e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1027 VKFNGVMFNYPTRPnipVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIKQLNVQWlrAHLG 1106
Cdd:cd03268 1 LKTNDLTKTYGKKR---VLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEAL--RRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1107 IVSQEPILFD-CSIAENIAYGDNSRVVSHEEIVKAAKEANIHQfidslpekyntRVGDKGTQLSGGQKQRIAIARALVRQ 1185
Cdd:cd03268 76 ALIEAPGFYPnLTARENLRLLARLLGIRKKRIDEVLDVVGLKD-----------SAKKKVKGFSLGMKQRLGIALALLGN 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 25453402 1186 PHILLLDEATSALDTESEKVVQEAL-DKAREGRTCIVIAHRLSTIQN-ADLIVVIQNGQVKEHG 1247
Cdd:cd03268 145 PDLLILDEPTNGLDPDGIKELRELIlSLRDQGITVLISSHLLSEIQKvADRIGIINKGKLIEEG 208
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
703-1000 |
4.50e-24 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349986 [Multi-domain] Cd Length: 292 Bit Score: 104.05 E-value: 4.50e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 703 FVVGVFCAIINGglqpAFSIIFSKVVGVFTKNDTPEIQRQNSNLFSLLFLILGIISFITFFLQGFTFGKAGEILTKRLRY 782
Cdd:cd18542 1 YLLAILALLLAT----ALNLLIPLLIRRIIDSVIGGGLRELLWLLALLILGVALLRGVFRYLQGYLAEKASQKVAYDLRN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 783 MVFKSMLRQDISWFDdpKNTTGALTTRLANDAAQVKGATGSRLAVITQNIANLGTGIIISLIYGWQLTLLLLAIVPIIAI 862
Cdd:cd18542 77 DLYDHLQRLSFSFHD--KARTGDLMSRCTSDVDTIRRFLAFGLVELVRAVLLFIGALIIMFSINWKLTLISLAIIPFIAL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 863 AGVVEMKMLsGQALKDKKELEGS-GKIATEAIENFRTVVSLTRE----QKFETMYAQslqipYRNA-LKKAHVFGITFSF 936
Cdd:cd18542 155 FSYVFFKKV-RPAFEEIREQEGElNTVLQENLTGVRVVKAFAREdyeiEKFDKENEE-----YRDLnIKLAKLLAKYWPL 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 25453402 937 TQAMMYFSYAACFRFGAYLVARELMTFENvLLVFSAIVFG-AMAVGQVSSFAPDYAKAKVSASHI 1000
Cdd:cd18542 229 MDFLSGLQIVLVLWVGGYLVINGEITLGE-LVAFISYLWMlIWPVRQLGRLINDMSRASASAERI 292
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
386-611 |
5.20e-24 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 107.84 E-value: 5.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 386 FKNIHFSYPSRKdvqILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGqdirtiNVRylreiIGVV 465
Cdd:COG0488 1 LENLSKSFGGRP---LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK------GLR-----IGYL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 466 SQEPVLFAT-TIAENIRYGRENV--TMDEIEKAVKEANAYDFIM----KLPHKFDTLVG---ERGA-------------- 521
Cdd:COG0488 67 PQEPPLDDDlTVLDTVLDGDAELraLEAELEELEAKLAEPDEDLerlaELQEEFEALGGweaEARAeeilsglgfpeedl 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 522 -----QLSGGQKQRIAIARALVRNPKILLLDEATSALDTES----EAVVqaaldKAREGrTTIVIAH-R--LSTVrnADV 589
Cdd:COG0488 147 drpvsELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESiewlEEFL-----KNYPG-TVLVVSHdRyfLDRV--ATR 218
|
250 260
....*....|....*....|...
gi 25453402 590 IAGFDGGVIVE-QGNHDELMREK 611
Cdd:COG0488 219 ILELDRGKLTLyPGNYSAYLEQR 241
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
395-556 |
5.80e-24 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 101.40 E-value: 5.80e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 395 SRKDVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDP---IEGEVSIDGQDIRTINVrYLREIiGVVSQEPVL 471
Cdd:COG4136 10 TLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALPA-EQRRI-GILFQDDLL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 472 FA-TTIAENIRYG-RENVTM----DEIEKAVKEANaydfimkLPHKFDTLVgergAQLSGGQKQRIAIARALVRNPKILL 545
Cdd:COG4136 88 FPhLSVGENLAFAlPPTIGRaqrrARVEQALEEAG-------LAGFADRDP----ATLSGGQRARVALLRALLAEPRALL 156
|
170
....*....|.
gi 25453402 546 LDEATSALDTE 556
Cdd:COG4136 157 LDEPFSKLDAA 167
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
1048-1256 |
5.99e-24 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 105.19 E-value: 5.99e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1048 LSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEI----KQLNVQWLRAHLGIVSQEPILF-DCSIAEN 1122
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLfdsrKGIFLPPEKRRIGYVFQEARLFpHLSVRGN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1123 IAYG-----DNSRVVSHEEIVKAAkeaNIHQFIDSLPEKyntrvgdkgtqLSGGQKQRIAIARALVRQPHILLLDEATSA 1197
Cdd:TIGR02142 96 LRYGmkrarPSERRISFERVIELL---GIGHLLGRLPGR-----------LSGGEKQRVAIGRALLSSPRLLLMDEPLAA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 25453402 1198 LDTESEKVVQEALDKARE--GRTCIVIAHRLSTIQN-ADLIVVIQNGQVKEHGTHQQLLAQK 1256
Cdd:TIGR02142 162 LDDPRKYEILPYLERLHAefGIPILYVSHSLQEVLRlADRVVVLEDGRVAAAGPIAEVWASP 223
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
703-1000 |
6.35e-24 |
|
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: 103.28 E-value: 6.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 703 FVVGVFCAIINGGLQPAFSIIFSKVVGVFTKNdtpeiqrqNSNLFSLLFLI-LGIISFITFFLQGFTFGKAGEILTKRLR 781
Cdd:cd18551 1 LILALLLSLLGTAASLAQPLLVKNLIDALSAG--------GSSGGLLALLVaLFLLQAVLSALSSYLLGRTGERVVLDLR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 782 YMVFKSMLRQDISWFDdpKNTTGALTTRLANDAAQVKgatgsrlAVITQNIANLGTGII-------ISLIYGWQLTLLLL 854
Cdd:cd18551 73 RRLWRRLLRLPVSFFD--RRRSGDLVSRVTNDTTLLR-------ELITSGLPQLVTGVLtvvgavvLMFLLDWVLTLVTL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 855 AIVPIIAIAGVVEMKMLSGQALKDKKELEGSGKIATEAIENFRTVVSLTREQKFETMYAQSLQIPYRNALKKAHVFGITF 934
Cdd:cd18551 144 AVVPLAFLIILPLGRRIRKASKRAQDALGELSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAKIEALIG 223
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 25453402 935 SFTQAMMYFSYAACFRFGAYLVAR------ELMTFenVLLVFSAIvfgaMAVGQVSSFAPDYAKAKVSASHI 1000
Cdd:cd18551 224 PLMGLAVQLALLVVLGVGGARVASgaltvgTLVAF--LLYLFQLI----TPLSQLSSFFTQLQKALGALERI 289
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
405-602 |
7.19e-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: 101.03 E-value: 7.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 405 LNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRTINVRylREIIGVVSQEPVLFA-TTIAENIRYG 483
Cdd:cd03298 17 FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA--DRPVSMLFQENNLFAhLTVEQNVGLG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 484 R------ENVTMDEIEKAVKEANAYDFIMKLPhkfdtlvgergAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTES 557
Cdd:cd03298 95 LspglklTAEDRQAIEVALARVGLAGLEKRLP-----------GELSGGERQRVALARVLVRDKPVLLLDEPFAALDPAL 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 25453402 558 EAVVQAALDK--AREGRTTIVIAHRLSTVRN-ADVIAGFDGGVIVEQG 602
Cdd:cd03298 164 RAEMLDLVLDlhAETKMTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1027-1248 |
8.11e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 103.27 E-value: 8.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1027 VKFNGVmfNYPTRPNIP----VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEI----KQLNV 1098
Cdd:PRK13643 2 IKFEKV--NYTYQPNSPfasrALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVsstsKQKEI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1099 QWLRAHLGIVSQEP--ILFDCSIAENIAYGDNSRVVSHEEIVK-AAKEANIHQFIDSLPEKyntrvgdKGTQLSGGQKQR 1175
Cdd:PRK13643 80 KPVRKKVGVVFQFPesQLFEETVLKDVAFGPQNFGIPKEKAEKiAAEKLEMVGLADEFWEK-------SPFELSGGQMRR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 25453402 1176 IAIARALVRQPHILLLDEATSALDTESEKVVQEALDKARE-GRTCIVIAHRLSTIQN-ADLIVVIQNGQVKEHGT 1248
Cdd:PRK13643 153 VAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQsGQTVVLVTHLMDDVADyADYVYLLEKGHIISCGT 227
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
402-608 |
9.83e-24 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 105.12 E-value: 9.83e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 402 LKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRTINVRYLREI----IGVVSQEPVLFA-TTI 476
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVrrkkIAMVFQSFALMPhMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 477 AENIRYGREnvtMDEIEKAVKEANAYDFIMKLphKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTE 556
Cdd:PRK10070 124 LDNTAFGME---LAGINAEERREKALDALRQV--GLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPL 198
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 25453402 557 SEAVVQAALDK--AREGRTTIVIAHRL-STVRNADVIAGFDGGVIVEQGNHDELM 608
Cdd:PRK10070 199 IRTEMQDELVKlqAKHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
384-607 |
1.03e-23 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 104.92 E-value: 1.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 384 LEFKNIHFSYPSRKDVQilkGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRTINvRYLREIiG 463
Cdd:PRK11607 20 LEIRNLTKSFDGQHAVD---DVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVP-PYQRPI-N 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 464 VVSQEPVLFA-TTIAENIRYG--RENVTMDEIEKAVKE----ANAYDFIMKLPHkfdtlvgergaQLSGGQKQRIAIARA 536
Cdd:PRK11607 95 MMFQSYALFPhMTVEQNIAFGlkQDKLPKAEIASRVNEmlglVHMQEFAKRKPH-----------QLSGGQRQRVALARS 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 25453402 537 LVRNPKILLLDEATSALDTESEAVVQAALDK--AREGRTTIVIAH-RLSTVRNADVIAGFDGGVIVEQGNHDEL 607
Cdd:PRK11607 164 LAKRPKLLLLDEPMGALDKKLRDRMQLEVVDilERVGVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
700-1256 |
1.30e-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: 108.84 E-value: 1.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 700 WPYFVVGVFCAI--INGGLQPafsIIFSKVVGVFTKNDTPEiqRQNSNLFSLLFLILGIISFItfFLQGFTFG--KAGEI 775
Cdd:TIGR01271 80 WRFVFYGILLYFgeATKAVQP---LLLGRIIASYDPFNAPE--REIAYYLALGLCLLFIVRTL--LLHPAIFGlhHLGMQ 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 776 LTKRLRYMVFKSMLRQDISWFDdpKNTTGALTTRLANDAAQVKGATGSRLAVItqnIANLGTGIIISLIygWQLT----- 850
Cdd:TIGR01271 153 MRIALFSLIYKKTLKLSSRVLD--KISTGQLVSLLSNNLNKFDEGLALAHFVW---IAPLQVILLMGLI--WELLevngf 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 851 -----LLLLAIVPiiAIAGVVEMKMLSGQALKDKKELegsgKIATEAIENFRTVVSLTREQKFETMYAQSLQIPYRNALK 925
Cdd:TIGR01271 226 cglgfLILLALFQ--ACLGQKMMPYRDKRAGKISERL----AITSEIIENIQSVKAYCWEEAMEKIIKNIRQDELKLTRK 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 926 KAHVfgitfsftqamMYFSYAACFRFGAYLVARELMTF---ENVLL--VFSAIVFGAMAVGQVSSFAPDYAKAKVSASHI 1000
Cdd:TIGR01271 300 IAYL-----------RYFYSSAFFFSGFFVVFLSVVPYaliKGIILrrIFTTISYCIVLRMTVTRQFPGAIQTWYDSLGA 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1001 IRIIEKIPEIDSYST---------------------------EGLKPN-----MLEGNvkfNGVMFNYPTRPNIPVLQGL 1048
Cdd:TIGR01271 369 ITKIQDFLCKEEYKTleynltttevemvnvtaswdegigelfEKIKQNnkarkQPNGD---DGLFFSNFSLYVTPVLKNI 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1049 SLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKeikqlnvqwlrahLGIVSQEPILFDCSIAENIAYGDN 1128
Cdd:TIGR01271 446 SFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR-------------ISFSPQTSWIMPGTIKDNIIFGLS 512
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1129 SRVVSHEEIVKAAKeanIHQFIDSLPEKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQE 1208
Cdd:TIGR01271 513 YDEYRYTSVIKACQ---LEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIFE 589
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 25453402 1209 A-LDKAREGRTCIVIAHRLSTIQNADLIVVIQNGQVKEHGTHQQLLAQK 1256
Cdd:TIGR01271 590 ScLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAKR 638
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1028-1224 |
1.53e-23 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 101.48 E-value: 1.53e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1028 KFNGVMFNYP-TRPNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIKQLNvqwlrAHLG 1106
Cdd:COG4525 5 TVRHVSVRYPgGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPG-----ADRG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1107 IVSQEPILFD-CSIAENIAYGDNSRVVSheeivKAAKEANIHQFIdslpekynTRVGDKGT------QLSGGQKQRIAIA 1179
Cdd:COG4525 80 VVFQKDALLPwLNVLDNVAFGLRLRGVP-----KAERRARAEELL--------ALVGLADFarrriwQLSGGMRQRVGIA 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 25453402 1180 RALVRQPHILLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAH 1224
Cdd:COG4525 147 RALAADPRFLLMDEPFGALDALTREQMQELLLDvwQRTGKGVFLITH 193
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1027-1256 |
1.92e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 101.85 E-value: 1.92e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1027 VKFNGVMFNYPTrpNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEI--KQLNVQWLRAH 1104
Cdd:PRK13636 6 LKVEELNYNYSD--GTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIdySRKGLMKLRES 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1105 LGIVSQEP--ILFDCSIAENIAYGDNSRVVSHEEIVKAAKEANIHQFIDSLPekyntrvgDKGTQ-LSGGQKQRIAIARA 1181
Cdd:PRK13636 84 VGMVFQDPdnQLFSASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLK--------DKPTHcLSFGQKKRVAIAGV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1182 LVRQPHILLLDEATSALD----TESEKVVQEALDKAreGRTCIVIAHRLSTIQ-NADLIVVIQNGQVKEHGTHQQLLAQK 1256
Cdd:PRK13636 156 LVMEPKVLVLDEPTAGLDpmgvSEIMKLLVEMQKEL--GLTIIIATHDIDIVPlYCDNVFVMKEGRVILQGNPKEVFAEK 233
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1038-1245 |
1.97e-23 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 101.30 E-value: 1.97e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1038 TRPNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIKQLN----------VQWL------ 1101
Cdd:PRK10419 21 KHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNraqrkafrrdIQMVfqdsis 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1102 ----RAHLGIVSQEPI--LFDCSIAENIAygdnsRVVSHEEIVKAAKEanihqFIDSLPEkyntrvgdkgtQLSGGQKQR 1175
Cdd:PRK10419 101 avnpRKTVREIIREPLrhLLSLDKAERLA-----RASEMLRAVDLDDS-----VLDKRPP-----------QLSGGQLQR 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 25453402 1176 IAIARALVRQPHILLLDEATSALDteseKVVQ-EALD-----KAREGRTCIVIAHRLSTIQN-ADLIVVIQNGQVKE 1245
Cdd:PRK10419 160 VCLARALAVEPKLLILDEAVSNLD----LVLQaGVIRllkklQQQFGTACLFITHDLRLVERfCQRVMVMDNGQIVE 232
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
377-614 |
2.20e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 102.62 E-value: 2.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 377 PDNIQGN--LEFKNIHFSYPSRKDVQI--LKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSID----GQ 448
Cdd:PRK13631 13 PNPLSDDiiLRVKNLYCVFDEKQENELvaLNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGdiyiGD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 449 DIRTI------------NVRYLREIIGVVSQEP--VLFATTIAENIRYGRENVTMDEIEkAVKEANAYDFIMKLPHKFDt 514
Cdd:PRK13631 93 KKNNHelitnpyskkikNFKELRRRVSMVFQFPeyQLFKDTIEKDIMFGPVALGVKKSE-AKKLAKFYLNKMGLDDSYL- 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 515 lvgERGA-QLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEA-VVQAALDKAREGRTTIVIAHRLSTVRN-ADVIA 591
Cdd:PRK13631 171 ---ERSPfGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHeMMQLILDAKANNKTVFVITHTMEHVLEvADEVI 247
|
250 260
....*....|....*....|...
gi 25453402 592 GFDGGVIVEQGNHDELMREKGIY 614
Cdd:PRK13631 248 VMDKGKILKTGTPYEIFTDQHII 270
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
1030-1256 |
2.30e-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: 101.47 E-value: 2.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1030 NGVMFNYPTRPNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKeikqlnvqwlrahLGIVS 1109
Cdd:cd03291 38 NNLFFSNLCLVGAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-------------ISFSS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1110 QEPILFDCSIAENIAYGDNSRVVSHEEIVKAAKeanIHQFIDSLPEKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHIL 1189
Cdd:cd03291 105 QFSWIMPGTIKENIIFGVSYDEYRYKSVVKACQ---LEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLY 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 25453402 1190 LLDEATSALDTESEKVVQEA-LDKAREGRTCIVIAHRLSTIQNADLIVVIQNGQVKEHGTHQQLLAQK 1256
Cdd:cd03291 182 LLDSPFGYLDVFTEKEIFEScVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSLR 249
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
384-611 |
2.54e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 101.64 E-value: 2.54e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 384 LEFKNIHFSYPSRKDVQ--ILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDI----RTINVRY 457
Cdd:PRK13634 3 ITFQKVEHRYQYKTPFErrALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVItagkKNKKLKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 458 LREIIGVVSQ--EPVLFATTIAENIRYGRENVTMDEiEKAVKEANAYDFIMKLPHK------FDtlvgergaqLSGGQKQ 529
Cdd:PRK13634 83 LRKKVGIVFQfpEHQLFEETVEKDICFGPMNFGVSE-EDAKQKAREMIELVGLPEEllarspFE---------LSGGQMR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 530 RIAIARALVRNPKILLLDEATSALDTESEAVVQ---AALDKaREGRTTIVIAHRLSTVRN-ADVIAGFDGGVIVEQGNHD 605
Cdd:PRK13634 153 RVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMemfYKLHK-EKGLTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTPR 231
|
....*.
gi 25453402 606 ELMREK 611
Cdd:PRK13634 232 EIFADP 237
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
357-581 |
2.71e-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: 107.69 E-value: 2.71e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 357 VFSIIDnKPSIDSFSKSGHKPDNIQGNLEFKNIHFS--YPS--RKDVQ------------ILKGLNLKVKSGQTVALVGN 420
Cdd:TIGR01271 1175 VFKFID-LPQEEPRPSGGGGKYQLSTVLVIENPHAQkcWPSggQMDVQgltakyteagraVLQDLSFSVEGGQRVGLLGR 1253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 421 SGCGKSTTVQLLQRLYDpIEGEVSIDGQDIRTINVRYLREIIGVVSQEPVLFATTIAENIRyGRENVTMDEIEKAVKEAN 500
Cdd:TIGR01271 1254 TGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNLD-PYEQWSDEEIWKVAEEVG 1331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 501 AYDFIMKLPHKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDKAREGRTTIVIAHR 580
Cdd:TIGR01271 1332 LKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHR 1411
|
.
gi 25453402 581 L 581
Cdd:TIGR01271 1412 V 1412
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
405-611 |
2.73e-23 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 102.88 E-value: 2.73e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 405 LNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDG---QDIRT-INVRYLREIIGVVSQEPVLFA-TTIAEN 479
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGrtlFDSRKgIFLPPEKRRIGYVFQEARLFPhLSVRGN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 480 IRYGRENVTMDEieKAVKEANAYDfIMKLPHkfdtLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEA 559
Cdd:TIGR02142 96 LRYGMKRARPSE--RRISFERVIE-LLGIGH----LLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKY 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 25453402 560 VVQAALDK-AREGRTTIV-IAHRLSTV-RNADVIAGFDGGVIVEQGNHDELMREK 611
Cdd:TIGR02142 169 EILPYLERlHAEFGIPILyVSHSLQEVlRLADRVVVLEDGRVAAAGPIAEVWASP 223
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1034-1259 |
3.00e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 102.24 E-value: 3.00e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1034 FNYPTRPNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQ-------------LLERFY-----DPMAGTVFLDGKEIKq 1095
Cdd:PRK13631 31 FDEKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVThfnglikskygtiQVGDIYigdkkNNHELITNPYSKKIK- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1096 lNVQWLRAHLGIVSQEP--ILFDCSIAENIAYGDNSRVVSHEEivkAAKEANIHQFIDSLPEKYNTRvgdKGTQLSGGQK 1173
Cdd:PRK13631 110 -NFKELRRRVSMVFQFPeyQLFKDTIEKDIMFGPVALGVKKSE---AKKLAKFYLNKMGLDDSYLER---SPFGLSGGQK 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1174 QRIAIARALVRQPHILLLDEATSALDTESEK-VVQEALDKAREGRTCIVIAHRLSTI-QNADLIVVIQNGQVKEHGTHQQ 1251
Cdd:PRK13631 183 RRVAIAGILAIQPEILIFDEPTAGLDPKGEHeMMQLILDAKANNKTVFVITHTMEHVlEVADEVIVMDKGKILKTGTPYE 262
|
....*...
gi 25453402 1252 LLAQKGIY 1259
Cdd:PRK13631 263 IFTDQHII 270
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
416-557 |
3.10e-23 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 102.87 E-value: 3.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 416 ALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDG---QDIRT-INV-RYLREIiGVVSQEPVLFAT-TIAENIRYGRenvtm 489
Cdd:COG4148 29 ALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGevlQDSARgIFLpPHRRRI-GYVFQEARLFPHlSVRGNLLYGR----- 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 25453402 490 deieKAVKEANAYDfimklphKFDTLVG--------ERG-AQLSGGQKQRIAIARALVRNPKILLLDEATSALDTES 557
Cdd:COG4148 103 ----KRAPRAERRI-------SFDEVVEllgighllDRRpATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLAR 168
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
382-581 |
3.49e-23 |
|
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: 101.08 E-value: 3.49e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 382 GNLEFKNIHFSYPSRKDVqILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDpIEGEVSIDGQDIRTINVRYLREI 461
Cdd:cd03289 1 GQMTVKDLTAKYTEGGNA-VLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 462 IGVVSQEPVLFATTIAENIR-YGRENvtMDEIEKAVKEANAYDFIMKLPHKFDTLVGERGAQLSGGQKQRIAIARALVRN 540
Cdd:cd03289 79 FGVIPQKVFIFSGTFRKNLDpYGKWS--DEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSK 156
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 25453402 541 PKILLLDEATSALDTESEAVVQAALDKAREGRTTIVIAHRL 581
Cdd:cd03289 157 AKILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRI 197
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1044-1252 |
3.87e-23 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 102.47 E-value: 3.87e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1044 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIKQLNVQwlRAHLGIVSQEPILF-DCSIAEN 1122
Cdd:PRK10851 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHAR--DRKVGFVFQHYALFrHMTVFDN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1123 IAYGdnSRVV-SHEEIVKAAKEANIHQFID-----SLPEKYNTrvgdkgtQLSGGQKQRIAIARALVRQPHILLLDEATS 1196
Cdd:PRK10851 95 IAFG--LTVLpRRERPNAAAIKAKVTQLLEmvqlaHLADRYPA-------QLSGGQKQRVALARALAVEPQILLLDEPFG 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 25453402 1197 ALDTESEKVVQEALDKARE--GRTCIVIAH-RLSTIQNADLIVVIQNGQVKEHGTHQQL 1252
Cdd:PRK10851 166 ALDAQVRKELRRWLRQLHEelKFTSVFVTHdQEEAMEVADRVVVMSQGNIEQAGTPDQV 224
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
384-608 |
3.91e-23 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 100.30 E-value: 3.91e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 384 LEFKNIHFSY------PSRKDVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRTINVRY 457
Cdd:COG4167 5 LEVRNLSKTFkyrtglFRRQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDYKY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 458 LREIIGVVSQEPvlfATTIAENIRYG-------RENVTMDEIEKAVKeanaydfImklphkFDTL--VGERGAQ------ 522
Cdd:COG4167 85 RCKHIRMIFQDP---NTSLNPRLNIGqileeplRLNTDLTAEEREER-------I------FATLrlVGLLPEHanfyph 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 523 -LSGGQKQRIAIARALVRNPKILLLDEATSALDTESEA-VVQAALD-KAREGRTTIVIAHRLSTVRN-ADVIAGFDGGVI 598
Cdd:COG4167 149 mLSSGQKQRVALARALILQPKIIIADEALAALDMSVRSqIINLMLElQEKLGISYIYVSQHLGIVKHiSDKVLVMHQGEV 228
|
250
....*....|
gi 25453402 599 VEQGNHDELM 608
Cdd:COG4167 229 VEYGKTAEVF 238
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
384-610 |
5.29e-23 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 99.37 E-value: 5.29e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 384 LEFKNIHFSypsRKDVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLL--QRLYDPIEGEVSIDGQDI--RTINVR--- 456
Cdd:COG0396 1 LEIKNLHVS---VEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLmgHPKYEVTSGSILLDGEDIleLSPDERara 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 457 -------YLREIIGV-VSQepvlFATTIAENIRygRENVTMDEIEKAVKEANAydfIMKLPHKFdtlvGERG--AQLSGG 526
Cdd:COG0396 78 giflafqYPVEIPGVsVSN----FLRTALNARR--GEELSAREFLKLLKEKMK---ELGLDEDF----LDRYvnEGFSGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 527 QKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDKAR-EGRTTIVIAH--RLSTVRNADVIAGFDGGVIVEQGN 603
Cdd:COG0396 145 EKKRNEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRsPDRGILIITHyqRILDYIKPDFVHVLVDGRIVKSGG 224
|
....*..
gi 25453402 604 HdELMRE 610
Cdd:COG0396 225 K-ELALE 230
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
397-579 |
5.48e-23 |
|
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: 99.05 E-value: 5.48e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 397 KDVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQ----DI-----RTI-NVRylREIIGVVS 466
Cdd:COG4778 22 KRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDggwvDLaqaspREIlALR--RRTIGYVS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 467 QepvlFATTIAeniRYGRENVTMDE-IEKAVKEANAYDFIMKLPHKFDtlVGERGAQL-----SGGQKQRIAIARALVRN 540
Cdd:COG4778 100 Q----FLRVIP---RVSALDVVAEPlLERGVDREEARARARELLARLN--LPERLWDLppatfSGGEQQRVNIARGFIAD 170
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 25453402 541 PKILLLDEATSALDTESEAVVQAALDKAREGRTTIV-IAH 579
Cdd:COG4778 171 PPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIgIFH 210
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1049-1256 |
5.92e-23 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 98.89 E-value: 5.92e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1049 SLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEikQLNVQWLRAHLGIVSQEPILFD-CSIAENIAYGD 1127
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQD--HTTTPPSRRPVSMLFQENNLFShLTVAQNIGLGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1128 NS----RVVSHEEIVKAAKEANIHQFIDSLPekyntrvgdkgTQLSGGQKQRIAIARALVRQPHILLLDEATSALD---- 1199
Cdd:PRK10771 97 NPglklNAAQREKLHAIARQMGIEDLLARLP-----------GQLSGGQRQRVALARCLVREQPILLLDEPFSALDpalr 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 25453402 1200 TESEKVVQEALDkaREGRTCIVIAHRLS-TIQNADLIVVIQNGQVKEHGTHQQLLAQK 1256
Cdd:PRK10771 166 QEMLTLVSQVCQ--ERQLTLLMVSHSLEdAARIAPRSLVVADGRIAWDGPTDELLSGK 221
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
1044-1243 |
6.24e-23 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 98.88 E-value: 6.24e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1044 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMA---GTVFLDGKEIKQlnVQWLRaHLGIVSQEPILFDC-SI 1119
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFNGQPRKP--DQFQK-CVAYVRQDDILLPGlTV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1120 AENIAYGDNSRvvSHEEIVKAAKEANIHQFidSLPEKYNTRVGDKG-TQLSGGQKQRIAIARALVRQPHILLLDEATSAL 1198
Cdd:cd03234 99 RETLTYTAILR--LPRKSSDAIRKKRVEDV--LLRDLALTRIGGNLvKGISGGERRRVSIAVQLLWDPKVLILDEPTSGL 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 25453402 1199 DTESE-KVVQEALDKAREGRTCIVIAH--RLSTIQNADLIVVIQNGQV 1243
Cdd:cd03234 175 DSFTAlNLVSTLSQLARRNRIVILTIHqpRSDLFRLFDRILLLSSGEI 222
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1043-1239 |
6.78e-23 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 98.63 E-value: 6.78e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1043 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIKQLNVQWLRAHLGIVSQEPILFDCSIAEN 1122
Cdd:PRK10247 21 KILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTLFGDTVYDN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1123 IAYGDNSRvvsHEEIVKAAKEANIHQFidSLPEKyntrVGDKG-TQLSGGQKQRIAIARALVRQPHILLLDEATSALDTE 1201
Cdd:PRK10247 101 LIFPWQIR---NQQPDPAIFLDDLERF--ALPDT----ILTKNiAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDES 171
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 25453402 1202 SEKVVQEALDK-AREGRTCIV-IAHRLSTIQNADLIVVIQ 1239
Cdd:PRK10247 172 NKHNVNEIIHRyVREQNIAVLwVTHDKDEINHADKVITLQ 211
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1037-1247 |
9.05e-23 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 98.21 E-value: 9.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1037 PTRPNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIKQlNVQWLRAHLGIVSQEPILFD 1116
Cdd:cd03266 13 DVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-EPAEARRRLGFVSDSTGLYD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1117 -CSIAENIAY-GDnsrvvsheeiVKAAKEANIHQFIDSLPEKY------NTRVGDkgtqLSGGQKQRIAIARALVRQPHI 1188
Cdd:cd03266 92 rLTARENLEYfAG----------LYGLKGDELTARLEELADRLgmeellDRRVGG----FSTGMRQKVAIARALVHDPPV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 25453402 1189 LLLDEATSALDTESEKVVQEALDKAREGRTCIVIA-HRLSTIQN-ADLIVVIQNGQVKEHG 1247
Cdd:cd03266 158 LLLDEPTTGLDVMATRALREFIRQLRALGKCILFStHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
402-579 |
9.30e-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: 98.31 E-value: 9.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 402 LKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRTINVRYLreiigVVSQEPVLFA-TTIAENI 480
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM-----VVFQNYSLLPwLTVRENI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 481 RYGRENVTMD----EIEKAVKEANAYDFIMKLPHKfdtlvgeRGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTE 556
Cdd:TIGR01184 76 ALAVDRVLPDlsksERRAIVEEHIALVGLTEAADK-------RPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDAL 148
|
170 180
....*....|....*....|....*
gi 25453402 557 SEAVVQAALDKARE--GRTTIVIAH 579
Cdd:TIGR01184 149 TRGNLQEELMQIWEehRVTVLMVTH 173
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1040-1246 |
1.01e-22 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 99.00 E-value: 1.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1040 PNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIKQLNvqwlrAHLGIVSQ-EPILFDCS 1118
Cdd:PRK11248 12 GGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPG-----AERGVVFQnEGLLPWRN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1119 IAENIAYGDNSRVVSHEEIVKAAKEANIhqfidslpekyntRVGDKGT------QLSGGQKQRIAIARALVRQPHILLLD 1192
Cdd:PRK11248 87 VQDNVAFGLQLAGVEKMQRLEIAHQMLK-------------KVGLEGAekryiwQLSGGQRQRVGIARALAANPQLLLLD 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 25453402 1193 EATSALDTESEKVVQEALDK--AREGRTCIVIAHrlsTIQNA-----DLIVVIQN-GQVKEH 1246
Cdd:PRK11248 154 EPFGALDAFTREQMQTLLLKlwQETGKQVLLITH---DIEEAvfmatELVLLSPGpGRVVER 212
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1045-1243 |
1.44e-22 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 103.18 E-value: 1.44e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1045 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIKQLN-VQWLRAHLGIVSQEPILFDC-SIAEN 1122
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSpRDAIALGIGMVHQHFMLVPNlTVAEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1123 IAYGDNSRVVSHEEIVKAAKEanihqfIDSLPEKY------NTRVGDkgtqLSGGQKQRIAIARALVRQPHILLLDEATS 1196
Cdd:COG3845 101 IVLGLEPTKGGRLDRKAARAR------IRELSERYgldvdpDAKVED----LSVGEQQRVEILKALYRGARILILDEPTA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 25453402 1197 AL-DTESEKVVqEALDK-AREGRTCIVIAHRLSTI-QNADLIVVIQNGQV 1243
Cdd:COG3845 171 VLtPQEADELF-EILRRlAAEGKSIIFITHKLREVmAIADRVTVLRRGKV 219
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1044-1247 |
1.64e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 98.38 E-value: 1.64e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1044 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYD-----PMAGTVFLDGKEIKQLNVQWL--RAHLGIVSQEPILF- 1115
Cdd:PRK14267 19 VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGRNIYSPDVDPIevRREVGMVFQYPNPFp 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1116 DCSIAENIAYGD--NSRVVSHEEIVK----AAKEAnihqfidSLPEKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHIL 1189
Cdd:PRK14267 99 HLTIYDNVAIGVklNGLVKSKKELDErvewALKKA-------ALWDEVKDRLNDYPSNLSGGQRQRLVIARALAMKPKIL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 25453402 1190 LLDEATSALDTESEKVVQEALDKAREGRTCIVIAHrlSTIQNA---DLIVVIQNGQVKEHG 1247
Cdd:PRK14267 172 LMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTH--SPAQAArvsDYVAFLYLGKLIEVG 230
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
384-601 |
1.82e-22 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 102.77 E-value: 1.82e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 384 LEFKNIHFSYPSrkdVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRTINVRYLREI-I 462
Cdd:PRK10762 5 LQLKGIDKAFPG---VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQEAgI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 463 GVVSQEPVLFAT-TIAENIRYGRENVT-MDEIE--KAVKEANAYDFIMKLPHKFDTLVGErgaqLSGGQKQRIAIARALV 538
Cdd:PRK10762 82 GIIHQELNLIPQlTIAENIFLGREFVNrFGRIDwkKMYAEADKLLARLNLRFSSDKLVGE----LSIGEQQMVEIAKVLS 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 25453402 539 RNPKILLLDEATSAL-DTESEAVVQAALDKAREGRTTIVIAHRLSTVRNA--DVIAGFDGGVIVEQ 601
Cdd:PRK10762 158 FESKVIIMDEPTDALtDTETESLFRVIRELKSQGRGIVYISHRLKEIFEIcdDVTVFRDGQFIAER 223
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
1044-1248 |
1.90e-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: 97.60 E-value: 1.90e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1044 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIKQLNVQWlRAHLGI--VSQEPILF-DCSIA 1120
Cdd:TIGR03410 15 ILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHE-RARAGIayVPQGREIFpRLTVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1121 ENIAYGDNSRVVSHEEIVkaakeANIHQFIDSLPEKYNTRVGDkgtqLSGGQKQRIAIARALVRQPHILLLDEATSALDT 1200
Cdd:TIGR03410 94 ENLLTGLAALPRRSRKIP-----DEIYELFPVLKEMLGRRGGD----LSGGQQQQLAIARALVTRPKLLLLDEPTEGIQP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 25453402 1201 ESEKVVQEALDK--AREGRTCIVIAHRLS-TIQNADLIVVIQNGQVKEHGT 1248
Cdd:TIGR03410 165 SIIKDIGRVIRRlrAEGGMAILLVEQYLDfARELADRYYVMERGRVVASGA 215
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1042-1242 |
2.79e-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: 96.73 E-value: 2.79e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1042 IPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEikqlnvQW-------------LRAH-LGI 1107
Cdd:COG4778 24 LPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDG------GWvdlaqaspreilaLRRRtIGY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1108 VSQ---------------EPILfdcsiaeniaygdnSRVVSHEEIVKAAKEAnIHQFidSLPEKY-----NTrvgdkgtq 1167
Cdd:COG4778 98 VSQflrviprvsaldvvaEPLL--------------ERGVDREEARARAREL-LARL--NLPERLwdlppAT-------- 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 25453402 1168 LSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKAREGRTCIV-IAHRLSTIQN-ADLIVVIQNGQ 1242
Cdd:COG4778 153 FSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIgIFHDEEVREAvADRVVDVTPFS 229
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
1043-1254 |
3.83e-22 |
|
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: 96.46 E-value: 3.83e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1043 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIKQLNVqWLRAHLGI--VSQEPILF-DCSI 1119
Cdd:cd03218 14 KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPM-HKRARLGIgyLPQEASIFrKLTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1120 AENIAYGDNSRVVSHEEIVKAAkEANIHQF-IDSLPEKyntrvgdKGTQLSGGQKQRIAIARALVRQPHILLLDEATSAL 1198
Cdd:cd03218 93 EENILAVLEIRGLSKKEREEKL-EELLEEFhITHLRKS-------KASSLSGGERRRVEIARALATNPKFLLLDEPFAGV 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 25453402 1199 DTESEKVVQEALDKAREGRTCIVIA-HRLS-TIQNADLIVVIQNGQVKEHGTHQQLLA 1254
Cdd:cd03218 165 DPIAVQDIQKIIKILKDRGIGVLITdHNVReTLSITDRAYIIYEGKVLAEGTPEEIAA 222
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
384-581 |
3.95e-22 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 97.46 E-value: 3.95e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 384 LEFKNIH--FSYPSRKDVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRTINVrYLR-E 460
Cdd:COG1101 2 LELKNLSktFNPGTVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPE-YKRaK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 461 IIGVVSQEPVL---FATTIAEN------------IRYGRENVTMDEIEKAVKEANaydfiMKLPHKFDTLVGergaQLSG 525
Cdd:COG1101 81 YIGRVFQDPMMgtaPSMTIEENlalayrrgkrrgLRRGLTKKRRELFRELLATLG-----LGLENRLDTKVG----LLSG 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 25453402 526 GQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDK--AREGRTTIVIAHRL 581
Cdd:COG1101 152 GQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKivEENNLTTLMVTHNM 209
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
385-614 |
4.65e-22 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 97.08 E-value: 4.65e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 385 EFKNIHFSYpsrKDVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRTINVRYLREIIGV 464
Cdd:COG4604 3 EIKNVSKRY---GGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 465 VSQEPVlFAT--TIAENIRYGR-----ENVTmDEIEKAVKEANAYDFIMKLPHKF-DtlvgergaQLSGGQKQRIAIARA 536
Cdd:COG4604 80 LRQENH-INSrlTVRELVAFGRfpyskGRLT-AEDREIIDEAIAYLDLEDLADRYlD--------ELSGGQRQRAFIAMV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 537 LVRNPKILLLDEATSALDTESEAVVQAALDK-ARE-GRTTIVIAHRLstvrN-----ADVIAGFDGGVIVEQGNHDELMR 609
Cdd:COG4604 150 LAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRlADElGKTVVIVLHDI----NfascyADHIVAMKDGRVVAQGTPEEIIT 225
|
....*...
gi 25453402 610 E---KGIY 614
Cdd:COG4604 226 PevlSDIY 233
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1026-1199 |
4.80e-22 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 99.53 E-value: 4.80e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1026 NVKFNGVMFNYPTrpNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQL---LERFydpMAGTVFLDGKEIKQLnvqwlr 1102
Cdd:PRK11650 3 GLKLQAVRKSYDG--KTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMvagLERI---TSGEIWIGGRVVNEL------ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1103 ahlgivsqEPILFDC-------------SIAENIAYGDNSRVVSHEEI----VKAAKEANIHQFIDSLPEkyntrvgdkg 1165
Cdd:PRK11650 72 --------EPADRDIamvfqnyalyphmSVRENMAYGLKIRGMPKAEIeervAEAARILELEPLLDRKPR---------- 133
|
170 180 190
....*....|....*....|....*....|....
gi 25453402 1166 tQLSGGQKQRIAIARALVRQPHILLLDEATSALD 1199
Cdd:PRK11650 134 -ELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLD 166
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1044-1250 |
5.56e-22 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 96.62 E-value: 5.56e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1044 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDP------MAGTVFLDGKEIKQLNVQWLRAHLGIVSQE----PI 1113
Cdd:PRK11124 17 ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPrsgtlnIAGNHFDFSKTPSDKAIRELRRNVGMVFQQynlwPH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1114 LfdcSIAENIAYGDnSRV--VSHEEIVKAAKEA----NIHQFIDSLPekyntrvgdkgTQLSGGQKQRIAIARALVRQPH 1187
Cdd:PRK11124 97 L---TVQQNLIEAP-CRVlgLSKDQALARAEKLlerlRLKPYADRFP-----------LHLSGGQQQRVAIARALMMEPQ 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 25453402 1188 ILLLDEATSALDTE-SEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVIQNGQVKEHGTHQ 1250
Cdd:PRK11124 162 VLLFDEPTAALDPEiTAQIVSIIRELAETGITQVIVTHEVEVARKtASRVVYMENGHIVEQGDAS 226
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
384-590 |
5.65e-22 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 101.16 E-value: 5.65e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 384 LEFKNIHFSYPsrkDVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYdP---IEGEVSIDGQDIRTINVRYLRE 460
Cdd:PRK13549 6 LEMKNITKTFG---GVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PhgtYEGEIIFEGEELQASNIRDTER 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 461 I-IGVVSQEPVLFAT-TIAENIRYGRENVTMDEIEKAVKEANAYDFIMKLphKFDTLVGERGAQLSGGQKQRIAIARALV 538
Cdd:PRK13549 82 AgIAIIHQELALVKElSVLENIFLGNEITPGGIMDYDAMYLRAQKLLAQL--KLDINPATPVGNLGLGQQQLVEIAKALN 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 25453402 539 RNPKILLLDEATSALdTESEAVVQAAL--DKAREGRTTIVIAHRLSTVRN-ADVI 590
Cdd:PRK13549 160 KQARLLILDEPTASL-TESETAVLLDIirDLKAHGIACIYISHKLNEVKAiSDTI 213
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
1043-1248 |
5.90e-22 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 96.29 E-value: 5.90e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1043 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLL---ERfYDPMAGTVFLDGKEIKQLNVQwLRAHLGI-VS-QEPI---- 1113
Cdd:COG0396 14 EILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLmghPK-YEVTSGSILLDGEDILELSPD-ERARAGIfLAfQYPVeipg 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1114 ------LfdcSIAENIAYGDNSRVV-SHEEIVKAAKEANihqfidsLPEKYNTR---VGdkgtqLSGGQKQRIAIARALV 1183
Cdd:COG0396 92 vsvsnfL---RTALNARRGEELSAReFLKLLKEKMKELG-------LDEDFLDRyvnEG-----FSGGEKKRNEILQMLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 25453402 1184 RQPHILLLDEATSALDTESEKVVQEALDKAR-EGRTCIVIAH--RLSTIQNADLIVVIQNGQVKEHGT 1248
Cdd:COG0396 157 LEPKLAILDETDSGLDIDALRIVAEGVNKLRsPDRGILIITHyqRILDYIKPDFVHVLVDGRIVKSGG 224
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
399-609 |
6.97e-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: 96.65 E-value: 6.97e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 399 VQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRTINVRylrEII--GVVS--QEPVLFAT 474
Cdd:COG0411 17 LVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPH---RIArlGIARtfQNPRLFPE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 475 -TIAENIRYGRENVTMDEIEKAV--------KEANAYDFIM------KLPHKFDTLVGErgaqLSGGQKQRIAIARALVR 539
Cdd:COG0411 94 lTVLENVLVAAHARLGRGLLAALlrlprarrEEREARERAEellervGLADRADEPAGN----LSYGQQRRLEIARALAT 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 25453402 540 NPKILLLDEATSAL-DTESEAVVQAALD-KAREGRTTIVIAHRLSTVRN-ADVIAGFDGGVIVEQGNHDELMR 609
Cdd:COG0411 170 EPKLLLLDEPAAGLnPEETEELAELIRRlRDERGITILLIEHDMDLVMGlADRIVVLDFGRVIAEGTPAEVRA 242
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
384-608 |
7.41e-22 |
|
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: 95.69 E-value: 7.41e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 384 LEFKNIHFSYPSRKdvqILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRTINV-RYLREII 462
Cdd:cd03218 1 LRAENLSKRYGKRK---VVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMhKRARLGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 463 GVVSQEPVLFAT-TIAENIRYGRE--NVTMDEIEKAVKEANAYDFIMKLPHKFdtlvgerGAQLSGGQKQRIAIARALVR 539
Cdd:cd03218 78 GYLPQEASIFRKlTVEENILAVLEirGLSKKEREEKLEELLEEFHITHLRKSK-------ASSLSGGERRRVEIARALAT 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 25453402 540 NPKILLLDEATSALDTESEAVVQAALDKAREGRTTIVIA-HR----LSTVRNADVIagFDGGVIVEqGNHDELM 608
Cdd:cd03218 151 NPKFLLLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITdHNvretLSITDRAYII--YEGKVLAE-GTPEEIA 221
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
1049-1253 |
7.85e-22 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 99.72 E-value: 7.85e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1049 SLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIKQLNVQWL----RAHLGIVSQE-PILFDCSIAENI 1123
Cdd:PRK10070 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELrevrRKKIAMVFQSfALMPHMTVLDNT 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1124 AYGDNSRVVSHEE----IVKAAKEANIHQFIDSLPEkyntrvgdkgtQLSGGQKQRIAIARALVRQPHILLLDEATSALD 1199
Cdd:PRK10070 128 AFGMELAGINAEErrekALDALRQVGLENYAHSYPD-----------ELSGGMRQRVGLARALAINPDILLMDEAFSALD 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 25453402 1200 TESEKVVQEALDK--AREGRTCIVIAHRL-STIQNADLIVVIQNGQVKEHGTHQQLL 1253
Cdd:PRK10070 197 PLIRTEMQDELVKlqAKHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1042-1245 |
1.04e-21 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 95.23 E-value: 1.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1042 IPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIKQLNVQW---LRA-HLGIVSQEPILFDC 1117
Cdd:PRK10584 23 LSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEArakLRAkHVGFVFQSFMLIPT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1118 SIA-ENIAY-----GDNSRvVSHEEIVKAAKEANIHQFIDSLPekyntrvgdkgTQLSGGQKQRIAIARALVRQPHILLL 1191
Cdd:PRK10584 103 LNAlENVELpallrGESSR-QSRNGAKALLEQLGLGKRLDHLP-----------AQLSGGEQQRVALARAFNGRPDVLFA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 25453402 1192 DEATSALDTES-EKVVQEALDKARE-GRTCIVIAHRLSTIQNADLIVVIQNGQVKE 1245
Cdd:PRK10584 171 DEPTGNLDRQTgDKIADLLFSLNREhGTTLILVTHDLQLAARCDRRLRLVNGQLQE 226
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
51-329 |
1.13e-21 |
|
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: 96.71 E-value: 1.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 51 LLGTLAAIIHGIALPLMMLVFGDMTDSFANVGNNRSmsfynatdiyakledEMTTYAYYYTGIGAGVLIVAYIQVSLWcL 130
Cdd:cd18541 2 LLGILFLILVDLLQLLIPRIIGRAIDALTAGTLTAS---------------QLLRYALLILLLALLIGIFRFLWRYLI-F 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 131 AAGRQI-HKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFFQAMATFFGGFIIGFTRGWKLTLV 209
Cdd:cd18541 66 GASRRIeYDLRNDLFAHLLTLSPSFYQKNRTGDLMARATNDLNAVRMALGPGILYLVDALFLGVLVLVMMFTISPKLTLI 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 210 ILAISPVLGLSAGIWAKILSSFTDKELQAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNNNLEEAKRLGIKKAITANI 289
Cdd:cd18541 146 ALLPLPLLALLVYRLGKKIHKRFRKVQEAFSDLSDRVQESFSGIRVIKAFVQEEAEIERFDKLNEEYVEKNLRLARVDAL 225
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 25453402 290 SMGAAFLLIYASYALAFWYGTSLVISKEYTIGQvLTVFFS 329
Cdd:cd18541 226 FFPLIGLLIGLSFLIVLWYGGRLVIRGTITLGD-LVAFNS 264
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
1026-1249 |
1.50e-21 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 95.08 E-value: 1.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1026 NVKFNGVMFNYPTRPnipVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDG------KEIKQLNVQ 1099
Cdd:COG4161 2 SIQLKNINCFYGSHQ---ALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGhqfdfsQKPSEKAIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1100 WLRAHLGIVSQE----PILfdcSIAENIAYG-----DNSRVVSHEEIVKAAKEANIHQFIDSLPekyntrvgdkgTQLSG 1170
Cdd:COG4161 79 LLRQKVGMVFQQynlwPHL---TVMENLIEApckvlGLSKEQAREKAMKLLARLRLTDKADRFP-----------LHLSG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1171 GQKQRIAIARALVRQPHILLLDEATSALDTE-SEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVIQNGQVKEHGT 1248
Cdd:COG4161 145 GQQQRVAIARALMMEPQVLLFDEPTAALDPEiTAQVVEIIRELSQTGITQVIVTHEVEFARKvASQVVYMEKGRIIEQGD 224
|
.
gi 25453402 1249 H 1249
Cdd:COG4161 225 A 225
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1038-1253 |
1.61e-21 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 98.76 E-value: 1.61e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1038 TRPNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIKQLNVQWLRAHLGIVSQEPIL-FD 1116
Cdd:PRK09536 12 EFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLsFE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1117 CSIAENIAYGDN---SRVVSHEEIVKAAKE-----ANIHQFIDSlpekyntrvgdKGTQLSGGQKQRIAIARALVRQPHI 1188
Cdd:PRK09536 92 FDVRQVVEMGRTphrSRFDTWTETDRAAVEramerTGVAQFADR-----------PVTSLSGGERQRVLLARALAQATPV 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1189 LLLDEATSALDTESE----KVVQEALDkarEGRTCIVIAHRLS-TIQNADLIVVIQNGQVKEHGTHQQLL 1253
Cdd:PRK09536 161 LLLDEPTASLDINHQvrtlELVRRLVD---DGKTAVAAIHDLDlAARYCDELVLLADGRVRAAGPPADVL 227
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
392-588 |
2.06e-21 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 93.45 E-value: 2.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 392 SYPSRkdvQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGqdirTINVRYLREIIGVVSQEPVl 471
Cdd:NF040873 1 GYGGR---PVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG----GARVAYVPQRSEVPDSLPL- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 472 fatTIAENIRYGR-------ENVTMDEiEKAVKEAnaydfIMKLphKFDTLVGERGAQLSGGQKQRIAIARALVRNPKIL 544
Cdd:NF040873 73 ---TVRDLVAMGRwarrglwRRLTRDD-RAAVDDA-----LERV--GLADLAGRQLGELSGGQRQRALLAQGLAQEADLL 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 25453402 545 LLDEATSALDTESEAVVQAAL-DKAREGRTTIVIAHRLSTVRNAD 588
Cdd:NF040873 142 LLDEPTTGLDAESRERIIALLaEEHARGATVVVVTHDLELVRRAD 186
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
1034-1252 |
2.69e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 95.92 E-value: 2.69e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1034 FNYPTRPNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTV---FLDGKEIKQL-------------- 1096
Cdd:PRK13651 12 FNKKLPTELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewiFKDEKNKKKTkekekvleklviqk 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1097 -------NVQWLRAHLGIVSQ--EPILFDCSIAENIAYGDNSRVVSHEEIVKAAKEanihqFID--SLPEKYNTRvgdKG 1165
Cdd:PRK13651 92 trfkkikKIKEIRRRVGVVFQfaEYQLFEQTIEKDIIFGPVSMGVSKEEAKKRAAK-----YIElvGLDESYLQR---SP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1166 TQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKA-REGRTCIVIAHRL-STIQNADLIVVIQNGQ- 1242
Cdd:PRK13651 164 FELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLnKQGKTIILVTHDLdNVLEWTKRTIFFKDGKi 243
|
250
....*....|
gi 25453402 1243 VKEHGTHQQL 1252
Cdd:PRK13651 244 IKDGDTYDIL 253
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
756-1268 |
3.91e-21 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 100.82 E-value: 3.91e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 756 IISFITFFlqGFTFGKAGEI--------LTKRLRYMVFKSMLRQDISWFDDPKNT--TGALTTRLANDAaqvkgatgSRL 825
Cdd:PLN03232 342 VYAFLIFF--GVTFGVLCESqyfqnvgrVGFRLRSTLVAAIFHKSLRLTHEARKNfaSGKVTNMITTDA--------NAL 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 826 AVITQNIANLGTG---IIISLIYGWQL--------TLLLLAIVPIIAIAgVVEMKMLSGQALK--DKKElegsgKIATEA 892
Cdd:PLN03232 412 QQIAEQLHGLWSApfrIIVSMVLLYQQlgvaslfgSLILFLLIPLQTLI-VRKMRKLTKEGLQwtDKRV-----GIINEI 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 893 IENFRTVVSLTREQKFETMyAQSLQIPYRNALKKAHVFgitFSFTQAMMYFS--YAACFRFGAYLVARELMTfenvllvf 970
Cdd:PLN03232 486 LASMDTVKCYAWEKSFESR-IQGIRNEELSWFRKAQLL---SAFNSFILNSIpvVVTLVSFGVFVLLGGDLT-------- 553
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 971 SAIVFGAMAVGQVSSFA----PDYAKAKVSASHIIRIIEKI---PEIDSYSTEGLKPNMLEGNVKfNGvMFNYPTRPNIP 1043
Cdd:PLN03232 554 PARAFTSLSLFAVLRSPlnmlPNLLSQVVNANVSLQRIEELllsEERILAQNPPLQPGAPAISIK-NG-YFSWDSKTSKP 631
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1044 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLdgkeikqlnvqwLRAHLGIVSQEPILFDCSIAENI 1123
Cdd:PLN03232 632 TLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSSVV------------IRGSVAYVPQVSWIFNATVRENI 699
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1124 AYGDNsrvVSHEEIVKAAKEANIHQFIDSLPEKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTE-S 1202
Cdd:PLN03232 700 LFGSD---FESERYWRAIDVTALQHDLDLLPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHvA 776
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 25453402 1203 EKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIQNGQVKEHGTHQQlLAQKGIYFSMVSVQAG 1268
Cdd:PLN03232 777 HQVFDSCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAE-LSKSGSLFKKLMENAG 841
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1044-1254 |
4.13e-21 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 99.01 E-value: 4.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1044 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYdPMAGTVFLDGKEIKQLNVQWL---RAHLGIVSQEP---ILFDC 1117
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLHNLNRRQLlpvRHRIQVVFQDPnssLNPRL 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1118 SIAENIAYGDNsrvVSHEEIVKAAKEAnihQFIDSLPEkyntrVG-DKGT------QLSGGQKQRIAIARALVRQPHILL 1190
Cdd:PRK15134 380 NVLQIIEEGLR---VHQPTLSAAQREQ---QVIAVMEE-----VGlDPETrhrypaEFSGGQRQRIAIARALILKPSLII 448
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 25453402 1191 LDEATSALDteseKVVQE---ALDKAREGR---TCIVIAHRLSTIQN-ADLIVVIQNGQVKEHGTHQQLLA 1254
Cdd:PRK15134 449 LDEPTSSLD----KTVQAqilALLKSLQQKhqlAYLFISHDLHVVRAlCHQVIVLRQGEVVEQGDCERVFA 515
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
384-610 |
4.28e-21 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 95.18 E-value: 4.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 384 LEFKNIHFSYpsrKDVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRTINVR---YLRE 460
Cdd:COG4152 2 LELKGLTKRF---GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRRrigYLPE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 461 iigvvsqEPVLFAT-TIAENIRY-GR-ENVTMDEIEKAVKEanaydfIMKlphKFDtlVGERGA----QLSGGQKQRIAI 533
Cdd:COG4152 79 -------ERGLYPKmKVGEQLVYlARlKGLSKAEAKRRADE------WLE---RLG--LGDRANkkveELSKGNQQKVQL 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 25453402 534 ARALVRNPKILLLDEATSALDTES-EAVVQAALDKAREGRTTIVIAHRLSTV-RNADVIAGFDGGVIVEQGNHDELMRE 610
Cdd:COG4152 141 IAALLHDPELLILDEPFSGLDPVNvELLKDVIRELAAKGTTVIFSSHQMELVeELCDRIVIINKGRKVLSGSVDEIRRQ 219
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
1036-1238 |
5.88e-21 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 91.91 E-value: 5.88e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1036 YPTRPnipVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIKQLNVQwlrahlgiVSQEPILF 1115
Cdd:NF040873 2 YGGRP---VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQ--------RSEVPDSL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1116 DCSIAENIAYGDNSRVVSHEEIVKAAKEAnihqFIDSLpekynTRVGDKG------TQLSGGQKQRIAIARALVRQPHIL 1189
Cdd:NF040873 71 PLTVRDLVAMGRWARRGLWRRLTRDDRAA----VDDAL-----ERVGLADlagrqlGELSGGQRQRALLAQGLAQEADLL 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 25453402 1190 LLDEATSALDTESEKVVQEAL-DKAREGRTCIVIAHRLSTIQNADLIVVI 1238
Cdd:NF040873 142 LLDEPTTGLDAESRERIIALLaEEHARGATVVVVTHDLELVRRADPCVLL 191
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1040-1242 |
5.88e-21 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 98.08 E-value: 5.88e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1040 PNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYdPMA---GTVFLDGKEIKQLNVQWL-RAHLGIVSQEPILF 1115
Cdd:PRK13549 16 GGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHGtyeGEIIFEGEELQASNIRDTeRAGIAIIHQELALV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1116 -DCSIAENIAYGD---NSRVVSHEEIVKAAKE--ANIHQFIDSlpekyNTRVGDkgtqLSGGQKQRIAIARALVRQPHIL 1189
Cdd:PRK13549 95 kELSVLENIFLGNeitPGGIMDYDAMYLRAQKllAQLKLDINP-----ATPVGN----LGLGQQQLVEIAKALNKQARLL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 25453402 1190 LLDEATSALdTESEKVVQEAL--DKAREGRTCIVIAHRLSTIQN-ADLIVVIQNGQ 1242
Cdd:PRK13549 166 ILDEPTASL-TESETAVLLDIirDLKAHGIACIYISHKLNEVKAiSDTICVIRDGR 220
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1036-1255 |
5.94e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 94.48 E-value: 5.94e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1036 YPTRPNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIKQLNVQWLRAHLGIVSQEP--I 1113
Cdd:PRK13652 11 YSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQNPddQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1114 LFDCSIAENIAYGD-----NSRVVSHeEIVKAAKEANIHQFIDSLPEkyntrvgdkgtQLSGGQKQRIAIARALVRQPHI 1188
Cdd:PRK13652 91 IFSPTVEQDIAFGPinlglDEETVAH-RVSSALHMLGLEELRDRVPH-----------HLSGGEKKRVAIAGVIAMEPQV 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1189 LLLDEATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTI-QNADLIVVIQNGQVKEHGTHQQLLAQ 1255
Cdd:PRK13652 159 LVLDEPTAGLDPQGVKELIDFLNDLPEtyGMTVIFSTHQLDLVpEMADYIYVMDKGRIVAYGTVEEIFLQ 228
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
703-973 |
7.51e-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: 94.41 E-value: 7.51e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 703 FVVGVFCAIINGGLQPAFSIIFSKVV-GVFTKNDTPEIqrqnsNLFSLLFLILGIISFITFFLQGFTFGKAGEILTKRLR 781
Cdd:cd18552 1 LALAILGMILVAATTAALAWLLKPLLdDIFVEKDLEAL-----LLVPLAIIGLFLLRGLASYLQTYLMAYVGQRVVRDLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 782 YMVFKSMLRQDISWFDdpKNTTGALTTRLANDAAQVKGATGSRLAVITQNIANLGTGIIISLIYGWQLTLLLLAIVPIIA 861
Cdd:cd18552 76 NDLFDKLLRLPLSFFD--RNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKLTLIALVVLPLAA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 862 IAGVV---EMKMLSgqalkdKKELEGSGKIAT---EAIENFRTVVSLTREQKFETMYAQSLQIPYRNALKKAHVFGITFS 935
Cdd:cd18552 154 LPIRRigkRLRKIS------RRSQESMGDLTSvlqETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIARARALSSP 227
|
250 260 270
....*....|....*....|....*....|....*...
gi 25453402 936 FTQAMMYFSYAACFRFGAYLVARELMTFENVLLVFSAI 973
Cdd:cd18552 228 LMELLGAIAIALVLWYGGYQVISGELTPGEFISFITAL 265
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1034-1243 |
7.83e-21 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 93.61 E-value: 7.83e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1034 FNYPTRPNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIKQLNVqWLRA-HLGIVSQEP 1112
Cdd:COG1101 11 FNPGTVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPE-YKRAkYIGRVFQDP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1113 ILFDC---SIAEN--IAYGDNSRvvshEEIVKAAKEANIHQFIDS-------LPEKYNTRVGdkgtQLSGGQKQRIAIAR 1180
Cdd:COG1101 90 MMGTApsmTIEENlaLAYRRGKR----RGLRRGLTKKRRELFRELlatlglgLENRLDTKVG----LLSGGQRQALSLLM 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 25453402 1181 ALVRQPHILLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLS-TIQNADLIVVIQNGQV 1243
Cdd:COG1101 162 ATLTKPKLLLLDEHTAALDPKTAALVLELTEKivEENNLTTLMVTHNMEqALDYGNRLIMMHEGRI 227
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
384-602 |
8.10e-21 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 91.96 E-value: 8.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 384 LEFKNIHFSYpsrKDVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRTINvrylREIIG 463
Cdd:cd03269 1 LEVENVTKRF---GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA----RNRIG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 464 VVSQEPVLF-ATTIAENIRYGRENVTMdEIEKAVKEANAYDFIMKLPHKFDtlvgERGAQLSGGQKQRIAIARALVRNPK 542
Cdd:cd03269 74 YLPEERGLYpKMKVIDQLVYLAQLKGL-KKEEARRRIDEWLERLELSEYAN----KRVEELSKGNQQKVQFIAAVIHDPE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 25453402 543 ILLLDEATSALDTES-EAVVQAALDKAREGRTTIVIAHRLSTV-RNADVIAGFDGGVIVEQG 602
Cdd:cd03269 149 LLILDEPFSGLDPVNvELLKDVIRELARAGKTVILSTHQMELVeELCDRVLLLNKGRAVLYG 210
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
399-579 |
9.35e-21 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 92.53 E-value: 9.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 399 VQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRTINVR---YLR-EIIGVVSQEPVLFAT 474
Cdd:PRK10584 23 LSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEaraKLRaKHVGFVFQSFMLIPT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 475 TIAenirygRENVTMDEIEKAVKEANAYDFIMKLPHKFDtlVGER----GAQLSGGQKQRIAIARALVRNPKILLLDEAT 550
Cdd:PRK10584 103 LNA------LENVELPALLRGESSRQSRNGAKALLEQLG--LGKRldhlPAQLSGGEQQRVALARAFNGRPDVLFADEPT 174
|
170 180 190
....*....|....*....|....*....|.
gi 25453402 551 SALDTES-EAVVQAALDKAREGRTT-IVIAH 579
Cdd:PRK10584 175 GNLDRQTgDKIADLLFSLNREHGTTlILVTH 205
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1043-1254 |
9.66e-21 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 93.53 E-value: 9.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1043 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEI--KQLNVQWLRAHLGIVSQEP--ILFDCS 1118
Cdd:PRK13638 15 PVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLdySKRGLLALRQQVATVFQDPeqQIFYTD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1119 IAENIAYGDNSRVVSHEEIVKAAKEAniHQFIDSlpekynTRVGDKGTQ-LSGGQKQRIAIARALVRQPHILLLDEATSA 1197
Cdd:PRK13638 95 IDSDIAFSLRNLGVPEAEITRRVDEA--LTLVDA------QHFRHQPIQcLSHGQKKRVAIAGALVLQARYLLLDEPTAG 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 25453402 1198 LDTESEKVVQEALDK-AREGRTCIVIAHRLSTI-QNADLIVVIQNGQVKEHGTHQQLLA 1254
Cdd:PRK13638 167 LDPAGRTQMIAIIRRiVAQGNHVIISSHDIDLIyEISDAVYVLRQGQILTHGAPGEVFA 225
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
391-613 |
1.14e-20 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 93.53 E-value: 1.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 391 FSYpsrKDVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQ--DIRTINVRYLREIIGVVSQE 468
Cdd:PRK13638 9 FRY---QDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKplDYSKRGLLALRQQVATVFQD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 469 P--VLFATTIAENIRYGREN--VTMDEIEKAVKEANaydfimklphkfdTLVGERGAQ------LSGGQKQRIAIARALV 538
Cdd:PRK13638 86 PeqQIFYTDIDSDIAFSLRNlgVPEAEITRRVDEAL-------------TLVDAQHFRhqpiqcLSHGQKKRVAIAGALV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 539 RNPKILLLDEATSALDTESEAVVQAALDK-AREGRTTIVIAHRLSTV----------RNADVIAGFDGGVIVEQGnhdEL 607
Cdd:PRK13638 153 LQARYLLLDEPTAGLDPAGRTQMIAIIRRiVAQGNHVIISSHDIDLIyeisdavyvlRQGQILTHGAPGEVFACT---EA 229
|
....*.
gi 25453402 608 MREKGI 613
Cdd:PRK13638 230 MEQAGL 235
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
384-610 |
1.18e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 93.64 E-value: 1.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 384 LEFKNIHFSYPSRKDV--QILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRTIN----VRY 457
Cdd:PRK13643 2 IKFEKVNYTYQPNSPFasRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSkqkeIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 458 LREIIGVVSQEP--VLFATTIAENIRYGREN--VTMDEIEKAVKE-----ANAYDFIMKLPHkfdtlvgergaQLSGGQK 528
Cdd:PRK13643 82 VRKKVGVVFQFPesQLFEETVLKDVAFGPQNfgIPKEKAEKIAAEklemvGLADEFWEKSPF-----------ELSGGQM 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 529 QRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDKARE-GRTTIVIAHRLSTVRN-ADVIAGFDGGVIVEQGNHDE 606
Cdd:PRK13643 151 RRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQsGQTVVLVTHLMDDVADyADYVYLLEKGHIISCGTPSD 230
|
....
gi 25453402 607 LMRE 610
Cdd:PRK13643 231 VFQE 234
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
138-327 |
1.82e-20 |
|
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: 93.17 E-value: 1.82e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 138 KIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFFQAMATFFGGFIIGFTRGWKLTLVILAISPVL 217
Cdd:cd18590 70 RLRHQLFSSLVQQDIGFFEKTKTGDLTSRLSTDTTLMSRSVALNANVLLRSLVKTLGMLGFMLSLSWQLTLLTLIEMPLT 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 218 GLSAGIWAKILSSFTDKELQAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNNNLEEAKRLGIKKAITANISMGAAFLL 297
Cdd:cd18590 150 AIAQKVYNTYHQKLSQAVQDSIAKAGELAREAVSSIRTVRSFKAEEEEACRYSEALERTYNLKDRRDTVRAVYLLVRRVL 229
|
170 180 190
....*....|....*....|....*....|
gi 25453402 298 IYASYALAFWYGTSLVISKEYTIGQVLTVF 327
Cdd:cd18590 230 QLGVQVLMLYCGRQLIQSGHLTTGSLVSFI 259
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
1036-1270 |
2.08e-20 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 98.31 E-value: 2.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1036 YPTRPNIpVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVfldgkeikqlnvqWLRAHLGIVSQEPILF 1115
Cdd:PTZ00243 668 FELEPKV-LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV-------------WAERSIAYVPQQAWIM 733
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1116 DCSIAENIAYGDNSRVVSHEEIVKAAK-EANIHQfidsLPEKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEA 1194
Cdd:PTZ00243 734 NATVRGNILFFDEEDAARLADAVRVSQlEADLAQ----LGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDP 809
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 25453402 1195 TSALDTE-SEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIQNGQVKEHGTHQQlLAQKGIYFSMVSVQAGAK 1270
Cdd:PTZ00243 810 LSALDAHvGERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSAD-FMRTSLYATLAAELKENK 885
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
384-580 |
2.11e-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: 89.52 E-value: 2.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 384 LEFKNIHFSYPSRKdvQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDirtiNVRYLreiig 463
Cdd:cd03223 1 IELENLSLATPDGR--VLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGE----DLLFL----- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 464 vvSQEPVLFATTIAENIRYGRENVtmdeiekavkeanaydfimklphkfdtlvgergaqLSGGQKQRIAIARALVRNPKI 543
Cdd:cd03223 70 --PQRPYLPLGTLREQLIYPWDDV-----------------------------------LSGGEQQRLAFARLLLHKPKF 112
|
170 180 190
....*....|....*....|....*....|....*...
gi 25453402 544 LLLDEATSALDTESEAvvqAALDKAREGRTTIV-IAHR 580
Cdd:cd03223 113 VFLDEATSALDEESED---RLYQLLKELGITVIsVGHR 147
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1043-1246 |
3.28e-20 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 95.90 E-value: 3.28e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1043 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLdGKEIKqlnvqwlrahLGIVSQEPILFDcsiaen 1122
Cdd:COG0488 329 TLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVK----------IGYFDQHQEELD------ 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1123 iaygDNSRVVSH-EEIVKAAKEANIHQFIDSL---PEKYNTRVGDkgtqLSGGQKQRIAIARALVRQPHILLLDEATSAL 1198
Cdd:COG0488 392 ----PDKTVLDElRDGAPGGTEQEVRGYLGRFlfsGDDAFKPVGV----LSGGEKARLALAKLLLSPPNVLLLDEPTNHL 463
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 25453402 1199 DTESEKVVQEALDkAREGrTCIVIAH-R--LSTIqnADLIVVIQNGQVKEH 1246
Cdd:COG0488 464 DIETLEALEEALD-DFPG-TVLLVSHdRyfLDRV--ATRILEFEDGGVREY 510
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1043-1193 |
3.38e-20 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 91.24 E-value: 3.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1043 PVLQGLSLEVKKGQTLALVGSSGCGKSTVvqllerFY------DPMAGTVFLDGKEIKQLNVqWLRAHLGI--VSQEPIL 1114
Cdd:COG1137 17 TVVKDVSLEVNQGEIVGLLGPNGAGKTTT------FYmivglvKPDSGRIFLDGEDITHLPM-HKRARLGIgyLPQEASI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1115 F-DCSIAENIaygdnsRVVSheEIVKAAKEAnIHQFIDSLPEKYN-TRVGD-KGTQLSGGQKQRIAIARALVRQPHILLL 1191
Cdd:COG1137 90 FrKLTVEDNI------LAVL--ELRKLSKKE-REERLEELLEEFGiTHLRKsKAYSLSGGERRRVEIARALATNPKFILL 160
|
..
gi 25453402 1192 DE 1193
Cdd:COG1137 161 DE 162
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
1027-1256 |
3.42e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 92.54 E-value: 3.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1027 VKFNGVMFNYP--TRPNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEI----KQLNVQW 1100
Cdd:PRK13646 3 IRFDNVSYTYQkgTPYEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIthktKDKYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1101 LRAHLGIVSQ--EPILFDCSIAENIAYGDNSRVVSHEEIVKAAkeaniHQFIDSLPEKYNTrVGDKGTQLSGGQKQRIAI 1178
Cdd:PRK13646 83 VRKRIGMVFQfpESQLFEDTVEREIIFGPKNFKMNLDEVKNYA-----HRLLMDLGFSRDV-MSQSPFQMSGGQMRKIAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1179 ARALVRQPHILLLDEATSALDTESEKVVQEALDKAR--EGRTCIVIAHRLSTI-QNADLIVVIQNGQVKEHGTHQQLLAQ 1255
Cdd:PRK13646 157 VSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtdENKTIILVSHDMNEVaRYADEVIVMKEGSIVSQTSPKELFKD 236
|
.
gi 25453402 1256 K 1256
Cdd:PRK13646 237 K 237
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
384-610 |
3.53e-20 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 95.75 E-value: 3.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 384 LEFKNIHFSYPSrkdVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRTINVR-YLREII 462
Cdd:PRK11288 5 LSFDGIGKTFPG---VKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTaALAAGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 463 GVVSQE----PVLfatTIAENIRYGRenvtmdeiekavkeanaydfimkLPHKF-----DTLVGERGAQL---------- 523
Cdd:PRK11288 82 AIIYQElhlvPEM---TVAENLYLGQ-----------------------LPHKGgivnrRLLNYEAREQLehlgvdidpd 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 524 ------SGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDKAR-EGRTTIVIAHRLSTV-RNADVIAGF-D 594
Cdd:PRK11288 136 tplkylSIGQRQMVEIAKALARNARVIAFDEPTSSLSAREIEQLFRVIRELRaEGRVILYVSHRMEEIfALCDAITVFkD 215
|
250 260
....*....|....*....|.
gi 25453402 595 GGVI-----VEQGNHDELMRE 610
Cdd:PRK11288 216 GRYVatfddMAQVDRDQLVQA 236
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
376-609 |
4.05e-20 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 91.77 E-value: 4.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 376 KPDNIQGNLEFKNIHFSYPSRKdvqILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRTINV 455
Cdd:PRK10575 4 YTNHSDTTFALRNVSFRVPGRT---LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 456 R-YLREIIGVVSQEPVLFATTIAENI------------RYGRENvtmdeiEKAVKEANAYDFIMKLPHKfdtLVGergaQ 522
Cdd:PRK10575 81 KaFARKVAYLPQQLPAAEGMTVRELVaigrypwhgalgRFGAAD------REKVEEAISLVGLKPLAHR---LVD----S 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 523 LSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDK-ARE-GRTTIVIAHRLS-TVRNADVIAGFDGGVIV 599
Cdd:PRK10575 148 LSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRlSQErGLTVIAVLHDINmAARYCDYLVALRGGEMI 227
|
250
....*....|
gi 25453402 600 EQGNHDELMR 609
Cdd:PRK10575 228 AQGTPAELMR 237
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1044-1248 |
4.14e-20 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 90.65 E-value: 4.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1044 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIKQLNVQW---LRAH-LGIVSQ-EPILFDCS 1118
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAkaeLRNQkLGFIYQfHHLLPDFT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1119 IAENIAY----GDNSRVVSHEEIVKAAKEANIHQfidslpekyntRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEA 1194
Cdd:PRK11629 104 ALENVAMplliGKKKPAEINSRALEMLAAVGLEH-----------RANHRPSELSGGERQRVAIARALVNNPRLVLADEP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 25453402 1195 TSALDTESEKVVQEALDK--AREGRTCIVIAHRLSTIQNADLIVVIQNGQVKEHGT 1248
Cdd:PRK11629 173 TGNLDARNADSIFQLLGElnRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRLTAELS 228
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1030-1243 |
5.08e-20 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 95.95 E-value: 5.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1030 NGVMFNYPT-RPNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIKQLNVQWL----RAH 1104
Cdd:PRK10535 8 KDIRRSYPSgEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALaqlrREH 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1105 LGIVSQE-PILFDCSIAENI----AYGDNSRvvsheeivkAAKEANIHQFIDSLpeKYNTRVGDKGTQLSGGQKQRIAIA 1179
Cdd:PRK10535 88 FGFIFQRyHLLSHLTAAQNVevpaVYAGLER---------KQRLLRAQELLQRL--GLEDRVEYQPSQLSGGQQQRVSIA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 25453402 1180 RALVRQPHILLLDEATSALDTESEKVVQEALDKARE-GRTCIVIAHRLSTIQNADLIVVIQNGQV 1243
Cdd:PRK10535 157 RALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDrGHTVIIVTHDPQVAAQAERVIEIRDGEI 221
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
388-590 |
5.45e-20 |
|
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: 91.84 E-value: 5.45e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 388 NIHFSYPSRKDVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQdirtinvrylreiIGVVSQ 467
Cdd:cd03291 39 NLFFSNLCLVGAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-------------ISFSSQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 468 EPVLFATTIAENIRYGrenVTMDEI--EKAVKEANAYDFIMKLPHKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILL 545
Cdd:cd03291 106 FSWIMPGTIKENIIFG---VSYDEYryKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYL 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 25453402 546 LDEATSALD--TESEaVVQAALDKAREGRTTIVIAHRLSTVRNADVI 590
Cdd:cd03291 183 LDSPFGYLDvfTEKE-IFESCVCKLMANKTRILVTSKMEHLKKADKI 228
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
384-554 |
5.59e-20 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 90.89 E-value: 5.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 384 LEFKNIHFSYPSRkdvQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRTInvrylREIIG 463
Cdd:PRK11247 13 LLLNAVSKRYGER---TVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEA-----REDTR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 464 VVSQEPVLFA-TTIAENIRYGRENVTMDEIEKAVKEANAYDfimklphkfdtLVGERGAQLSGGQKQRIAIARALVRNPK 542
Cdd:PRK11247 85 LMFQDARLLPwKKVIDNVGLGLKGQWRDAALQALAAVGLAD-----------RANEWPAALSGGQKQRVALARALIHRPG 153
|
170
....*....|..
gi 25453402 543 ILLLDEATSALD 554
Cdd:PRK11247 154 LLLLDEPLGALD 165
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1044-1255 |
9.04e-20 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 91.32 E-value: 9.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1044 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIKQLNvqwlRAHLGIVSQEPILF-DCSIAEN 1122
Cdd:COG4152 16 AVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPED----RRRIGYLPEERGLYpKMKVGEQ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1123 IAY-----GdnsrvVSHEEIVKAAKEanihqFID--SLPEKYNTRVGDkgtqLSGGQKQRIAIARALVRQPHILLLDEAT 1195
Cdd:COG4152 92 LVYlarlkG-----LSKAEAKRRADE-----WLErlGLGDRANKKVEE----LSKGNQQKVQLIAALLHDPELLILDEPF 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 25453402 1196 SALDTES-EKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVIQNGQVKEHGTHQQLLAQ 1255
Cdd:COG4152 158 SGLDPVNvELLKDVIRELAAKGTTVIFSSHQMELVEElCDRIVIINKGRKVLSGSVDEIRRQ 219
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1045-1242 |
1.05e-19 |
|
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: 94.12 E-value: 1.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1045 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFY--DPMAGTVFLDGKEIKQLNVQWL-RAHLGIVSQEPILF-DCSIA 1120
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYphGTWDGEIYWSGSPLKASNIRDTeRAGIVIIHQELTLVpELSVA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1121 ENIAYGD----NSRVVSHEEIVKAAKEANIHQFIDSLPekyNTR-VGDKGtqlsGGQKQRIAIARALVRQPHILLLDEAT 1195
Cdd:TIGR02633 97 ENIFLGNeitlPGGRMAYNAMYLRAKNLLRELQLDADN---VTRpVGDYG----GGQQQLVEIAKALNKQARLLILDEPS 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 25453402 1196 SAL-DTESEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVIQNGQ 1242
Cdd:TIGR02633 170 SSLtEKETEILLDIIRDLKAHGVACVYISHKLNEVKAvCDTICVIRDGQ 218
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
384-602 |
1.08e-19 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 94.92 E-value: 1.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 384 LEFKNIHFSYPSR--------KDVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRTIN- 454
Cdd:PRK10261 314 LQVRNLVTRFPLRsgllnrvtREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSp 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 455 --VRYLREIIGVVSQEPvlFAT---------TIAENIRY--------GRENVTMDEIEKAVKEANAYDFimklPHKFdtl 515
Cdd:PRK10261 394 gkLQALRRDIQFIFQDP--YASldprqtvgdSIMEPLRVhgllpgkaAAARVAWLLERVGLLPEHAWRY----PHEF--- 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 516 vgergaqlSGGQKQRIAIARALVRNPKILLLDEATSALDTESEA-VVQAALDKARE-GRTTIVIAHRLSTV-RNADVIAG 592
Cdd:PRK10261 465 --------SGGQRQRICIARALALNPKVIIADEAVSALDVSIRGqIINLLLDLQRDfGIAYLFISHDMAVVeRISHRVAV 536
|
250
....*....|
gi 25453402 593 FDGGVIVEQG 602
Cdd:PRK10261 537 MYLGQIVEIG 546
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
395-602 |
1.39e-19 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 92.60 E-value: 1.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 395 SRKDVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRTINVRYLREIIGVVSQEPVL-FA 473
Cdd:PRK09536 12 EFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLsFE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 474 TTIAENIRYGREN-----VTMDE-----IEKAVKEANAYDFIMKlphKFDTlvgergaqLSGGQKQRIAIARALVRNPKI 543
Cdd:PRK09536 92 FDVRQVVEMGRTPhrsrfDTWTEtdraaVERAMERTGVAQFADR---PVTS--------LSGGERQRVLLARALAQATPV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 25453402 544 LLLDEATSALDTESEA-VVQAALDKAREGRTTIVIAHRLS-TVRNADVIAGFDGGVIVEQG 602
Cdd:PRK09536 161 LLLDEPTASLDINHQVrTLELVRRLVDDGKTAVAAIHDLDlAARYCDELVLLADGRVRAAG 221
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
384-606 |
1.64e-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: 1.64e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 384 LEFKNIHFSYPSRKdvqILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIdGQdirtiNVRylreiIG 463
Cdd:COG0488 316 LELEGLSKSYGDKT---LLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GE-----TVK-----IG 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 464 VVSQEPVLFAT--TIAENIRYGRENVTmdeiekavkEANAYDFIMKL---PHKFDTLVGErgaqLSGGQKQRIAIARALV 538
Cdd:COG0488 382 YFDQHQEELDPdkTVLDELRDGAPGGT---------EQEVRGYLGRFlfsGDDAFKPVGV----LSGGEKARLALAKLLL 448
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 25453402 539 RNPKILLLDEATSALDTESEAVVQAALDkAREGrTTIVIAH-R--LSTVrnADVIAGFDGGVIVE-QGNHDE 606
Cdd:COG0488 449 SPPNVLLLDEPTNHLDIETLEALEEALD-DFPG-TVLLVSHdRyfLDRV--ATRILEFEDGGVREyPGGYDD 516
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
384-548 |
1.67e-19 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 89.32 E-value: 1.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 384 LEFKNIHFSYPSRkdvQILKGLNLKVKSGQTVALVGNSGCGKSTT----VQLLQrlydPIEGEVSIDGQDIRTINVrYLR 459
Cdd:COG1137 4 LEAENLVKSYGKR---TVVKDVSLEVNQGEIVGLLGPNGAGKTTTfymiVGLVK----PDSGRIFLDGEDITHLPM-HKR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 460 EI--IGVVSQEPVLFAT-TIAENIRYGRENVTMDEIEKAvkeanaydfimklpHKFDTLVGE---------RGAQLSGGQ 527
Cdd:COG1137 76 ARlgIGYLPQEASIFRKlTVEDNILAVLELRKLSKKERE--------------ERLEELLEEfgithlrksKAYSLSGGE 141
|
170 180
....*....|....*....|.
gi 25453402 528 KQRIAIARALVRNPKILLLDE 548
Cdd:COG1137 142 RRRVEIARALATNPKFILLDE 162
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
384-611 |
2.07e-19 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 91.05 E-value: 2.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 384 LEFKNIHFSYpsrKDVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRTiNVRYLREIIG 463
Cdd:PRK13536 42 IDLAGVSKSY---GDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA-RARLARARIG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 464 VVSQEPVL-FATTIAEN-IRYGRE-NVTMDEIEKAVkeANAYDFiMKLPHKFDTLVgergAQLSGGQKQRIAIARALVRN 540
Cdd:PRK13536 118 VVPQFDNLdLEFTVRENlLVFGRYfGMSTREIEAVI--PSLLEF-ARLESKADARV----SDLSGGMKRRLTLARALIND 190
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 25453402 541 PKILLLDEATSALDTESEAVVQAALDK--AReGRTTIVIAHRLSTV-RNADVIAGFDGGVIVEQGNHDELMREK 611
Cdd:PRK13536 191 PQLLILDEPTTGLDPHARHLIWERLRSllAR-GKTILLTTHFMEEAeRLCDRLCVLEAGRKIAEGRPHALIDEH 263
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
703-963 |
2.08e-19 |
|
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: 90.14 E-value: 2.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 703 FVVGVFCAIINGGLQPAFSIIFSKVVGVFTKNDTPEIQrqNSNLFSLLFLILGIISFITFFLQGFTFGKAGEILTKRLRY 782
Cdd:cd18544 1 FILALLLLLLATALELLGPLLIKRAIDDYIVPGQGDLQ--GLLLLALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 783 MVFKSMLRQDISWFDdpKNTTGALTTRLANDAAQVKGATGSRLAVITQNIANLgTGIIISLIY-GWQLTLLLLAIVPIIA 861
Cdd:cd18544 79 DLFSHIQRLPLSFFD--RTPVGRLVTRVTNDTEALNELFTSGLVTLIGDLLLL-IGILIAMFLlNWRLALISLLVLPLLL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 862 IAGVVeMKMLSGQALKDKKEL--EGSGKIAtEAIENFRTVVSLTREQKFETMYAQsLQIPYRNALKKA-HVFGITFSFTQ 938
Cdd:cd18544 156 LATYL-FRKKSRKAYREVREKlsRLNAFLQ-ESISGMSVIQLFNREKREFEEFDE-INQEYRKANLKSiKLFALFRPLVE 232
|
250 260
....*....|....*....|....*
gi 25453402 939 AMMYFSYAACFRFGAYLVARELMTF 963
Cdd:cd18544 233 LLSSLALALVLWYGGGQVLSGAVTL 257
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1045-1249 |
2.16e-19 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 88.39 E-value: 2.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1045 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIKQLN---VQWLRAHLGIVSQEP-ILFDCSIA 1120
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKnreVPFLRRQIGMIFQDHhLLMDRTVY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1121 ENIAYgdnsrvvshEEIVKAAKEANIHQFIDSLPEKyntrVG--DKG----TQLSGGQKQRIAIARALVRQPHILLLDEA 1194
Cdd:PRK10908 98 DNVAI---------PLIIAGASGDDIRRRVSAALDK----VGllDKAknfpIQLSGGEQQRVGIARAVVNKPAVLLADEP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 25453402 1195 TSALDTE-SEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIQNgQVKEHGTH 1249
Cdd:PRK10908 165 TGNLDDAlSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLS-DGHLHGGV 219
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1050-1247 |
2.54e-19 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 91.24 E-value: 2.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1050 LEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIKqlNVQWLRAHLGIVSQEPILF-DCSIAENIAYGDN 1128
Cdd:PRK11000 24 LDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMN--DVPPAERGVGMVFQSYALYpHLSVAENMSFGLK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1129 SRVVSHEEIVKAAKE-ANIHQfIDSLPEKyntrvgdKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEkvVQ 1207
Cdd:PRK11000 102 LAGAKKEEINQRVNQvAEVLQ-LAHLLDR-------KPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALR--VQ 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 25453402 1208 EALDKA----REGRTCIVIAH-RLSTIQNADLIVVIQNGQVKEHG 1247
Cdd:PRK11000 172 MRIEISrlhkRLGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVG 216
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
406-554 |
2.70e-19 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 88.49 E-value: 2.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 406 NLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRTINVRylREIIGVVSQEPVLFA-TTIAENIRYG- 483
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS--RRPVSMLFQENNLFShLTVAQNIGLGl 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 25453402 484 RENVTMDEIEKAVKEANAY-----DFIMKLPhkfdtlvgergAQLSGGQKQRIAIARALVRNPKILLLDEATSALD 554
Cdd:PRK10771 97 NPGLKLNAAQREKLHAIARqmgieDLLARLP-----------GQLSGGQRQRVALARCLVREQPILLLDEPFSALD 161
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1029-1255 |
2.89e-19 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 92.67 E-value: 2.89e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1029 FNGVMFNYPtrpNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIKQLNVQ-WLRAHLGI 1107
Cdd:PRK11288 7 FDGIGKTFP---GVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTaALAAGVAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1108 VSQEPILF-DCSIAENIAYGD--NSR-VVSHEEIVKAAKEANIHQFIDSLPekyNTRVGDkgtqLSGGQKQRIAIARALV 1183
Cdd:PRK11288 84 IYQELHLVpEMTVAENLYLGQlpHKGgIVNRRLLNYEAREQLEHLGVDIDP---DTPLKY----LSIGQRQMVEIAKALA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1184 RQPHILLLDEATSALDT-ESE---KVVQEALDkarEGRTCIVIAHRLSTI-QNADLIVVIQNGQ-VKEHG-----THQQL 1252
Cdd:PRK11288 157 RNARVIAFDEPTSSLSArEIEqlfRVIRELRA---EGRVILYVSHRMEEIfALCDAITVFKDGRyVATFDdmaqvDRDQL 233
|
...
gi 25453402 1253 LAQ 1255
Cdd:PRK11288 234 VQA 236
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
1048-1255 |
2.91e-19 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 89.13 E-value: 2.91e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1048 LSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIKQLNVQWLRAHLGIVSQEPilfdcsiaeNIAYgd 1127
Cdd:COG4167 32 VSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDYKYRCKHIRMIFQDP---------NTSL-- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1128 NSRVvsheeivkaakeaNIHQFIDsLPEKYNT----------------RVG-------DKGTQLSGGQKQRIAIARALVR 1184
Cdd:COG4167 101 NPRL-------------NIGQILE-EPLRLNTdltaeereerifatlrLVGllpehanFYPHMLSSGQKQRVALARALIL 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 25453402 1185 QPHILLLDEATSALD--TESEKV-----VQEaldkaREGRTCIVIAHRLSTIQN-ADLIVVIQNGQVKEHGTHQQLLAQ 1255
Cdd:COG4167 167 QPKIIIADEALAALDmsVRSQIInlmleLQE-----KLGISYIYVSQHLGIVKHiSDKVLVMHQGEVVEYGKTAEVFAN 240
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1029-1224 |
2.98e-19 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 92.82 E-value: 2.98e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1029 FNGVMFNYPTRPnipVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGkeikqlnvqwlRAHLGIV 1108
Cdd:COG0488 1 LENLSKSFGGRP---LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK-----------GLRIGYL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1109 SQEPILFD-CSIAENIAYGDNSRV--------------VSHEEIVKAAK-------------EANIHQFIDSL---PEKY 1157
Cdd:COG0488 67 PQEPPLDDdLTVLDTVLDGDAELRaleaeleeleaklaEPDEDLERLAElqeefealggweaEARAEEILSGLgfpEEDL 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 25453402 1158 NTRVGDkgtqLSGGQKQRIAIARALVRQPHILLLDEATSALDTESekvVQ--EALDKAREGrTCIVIAH 1224
Cdd:COG0488 147 DRPVSE----LSGGWRRRVALARALLSEPDLLLLDEPTNHLDLES---IEwlEEFLKNYPG-TVLVVSH 207
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
396-578 |
3.55e-19 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 87.24 E-value: 3.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 396 RKDVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRTINVR----YLREIIGVvsqEPVL 471
Cdd:PRK13539 12 RGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAeachYLGHRNAM---KPAL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 472 fatTIAENIRYGRE--NVTMDEIEKAVKeanaydfIMKLPHKFDTlvgeRGAQLSGGQKQRIAIARALVRNPKILLLDEA 549
Cdd:PRK13539 89 ---TVAENLEFWAAflGGEELDIAAALE-------AVGLAPLAHL----PFGYLSAGQKRRVALARLLVSNRPIWILDEP 154
|
170 180
....*....|....*....|....*....
gi 25453402 550 TSALDTESEAVVqAALDKAREGRTTIVIA 578
Cdd:PRK13539 155 TAALDAAAVALF-AELIRAHLAQGGIVIA 182
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1043-1255 |
3.69e-19 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 92.85 E-value: 3.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1043 PVLQGLSLEVKKGQTLALVGSSGCGKS-TVVQLLERFYDP----MAGTVFLDGKEIKQLNVQWLRAHLG----IVSQEPI 1113
Cdd:PRK15134 23 TVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFHGESLLHASEQTLRGVRGnkiaMIFQEPM 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1114 L-------FDCSIAENIA-YGDNSRVVSHEEIVKAAKEANIHQfidslpekYNTRVGDKGTQLSGGQKQRIAIARALVRQ 1185
Cdd:PRK15134 103 VslnplhtLEKQLYEVLSlHRGMRREAARGEILNCLDRVGIRQ--------AAKRLTDYPHQLSGGERQRVMIAMALLTR 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 25453402 1186 PHILLLDEATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTI-QNADLIVVIQNGQVKEHGTHQQLLAQ 1255
Cdd:PRK15134 175 PELLIADEPTTALDVSVQAQILQLLRELQQelNMGLLFITHNLSIVrKLADRVAVMQNGRCVEQNRAATLFSA 247
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
384-610 |
4.08e-19 |
|
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: 86.81 E-value: 4.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 384 LEFKNIHFSypsRKDVQILKGLNLKVKSGQTVALVGNSGCGKSTtvqLLQRL-----YDPIEGEVSIDGQDIR--TINVR 456
Cdd:cd03217 1 LEIKDLHVS---VGGKEILKGVNLTIKKGEVHALMGPNGSGKST---LAKTImghpkYEVTEGEILFKGEDITdlPPEER 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 457 yLREIIGVVSQEPVLFA-TTIAENIRYGRENvtmdeiekavkeanaydfimklphkfdtlvgergaqLSGGQKQRIAIAR 535
Cdd:cd03217 75 -ARLGIFLAFQYPPEIPgVKNADFLRYVNEG------------------------------------FSGGEKKRNEILQ 117
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 25453402 536 ALVRNPKILLLDEATSALDTESEAVVQAALDKAR-EGRTTIVIAH--RLSTVRNADVIAGFDGGVIVEQGNhDELMRE 610
Cdd:cd03217 118 LLLLEPDLAILDEPDSGLDIDALRLVAEVINKLReEGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVKSGD-KELALE 194
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
384-579 |
5.03e-19 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 88.22 E-value: 5.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 384 LEFKNIHFSYPSRKdvqILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRTINVRYlreiiG 463
Cdd:PRK11248 2 LQISHLYADYGGKP---ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER-----G 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 464 VVSQ-EPVLFATTIAENIRYGREnvtMDEIEKAVKEANAYDFIMKlphkfdtlVGERGA------QLSGGQKQRIAIARA 536
Cdd:PRK11248 74 VVFQnEGLLPWRNVQDNVAFGLQ---LAGVEKMQRLEIAHQMLKK--------VGLEGAekryiwQLSGGQRQRVGIARA 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 25453402 537 LVRNPKILLLDEATSALDTESEAVVQAALDK--AREGRTTIVIAH 579
Cdd:PRK11248 143 LAANPQLLLLDEPFGALDAFTREQMQTLLLKlwQETGKQVLLITH 187
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
1030-1243 |
5.63e-19 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 88.20 E-value: 5.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1030 NGVMFNYPTRPnipVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDP-----MAGTVFL-DGKEIKQLNVQWLRa 1103
Cdd:PRK11247 16 NAVSKRYGERT---VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPsagelLAGTAPLaEAREDTRLMFQDAR- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1104 hlgivsqepILFDCSIAENIAYGdnsrvvsheeiVKAAKEANIHQFIDS--LPEkyntRVGDKGTQLSGGQKQRIAIARA 1181
Cdd:PRK11247 92 ---------LLPWKKVIDNVGLG-----------LKGQWRDAALQALAAvgLAD----RANEWPAALSGGQKQRVALARA 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 25453402 1182 LVRQPHILLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLS-TIQNADLIVVIQNGQV 1243
Cdd:PRK11247 148 LIHRPGLLLLDEPLGALDALTRIEMQDLIESlwQQHGFTVLLVTHDVSeAVAMADRVLLIEEGKI 212
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
390-577 |
5.82e-19 |
|
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: 87.39 E-value: 5.82e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 390 HFSYPSRKDVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRTINVRYLREiIGVV--SQ 467
Cdd:cd03267 25 SLFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRR-IGVVfgQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 468 EPVLFATTIAENIRYGRE--NVTMDEIEKAVKEANAydfIMKLPHKFDTLVgergAQLSGGQKQRIAIARALVRNPKILL 545
Cdd:cd03267 104 TQLWWDLPVIDSFYLLAAiyDLPPARFKKRLDELSE---LLDLEELLDTPV----RQLSLGQRMRAEIAAALLHEPEILF 176
|
170 180 190
....*....|....*....|....*....|...
gi 25453402 546 LDEATSALDTESEAVVQAALDKA-REGRTTIVI 577
Cdd:cd03267 177 LDEPTIGLDVVAQENIRNFLKEYnRERGTTVLL 209
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
1044-1254 |
6.04e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 88.61 E-value: 6.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1044 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAG-----TVFLDGKEI-KQLNVQWLRAHLGIVSQEPILFDC 1117
Cdd:PRK14271 36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIfNYRDVLEFRRRVGMLFQRPNPFPM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1118 SIAENIAYGDNSRVVSHEEIVKAAKEANIHQFidSLPEKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSA 1197
Cdd:PRK14271 116 SIMDNVLAGVRAHKLVPRKEFRGVAQARLTEV--GLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSA 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 25453402 1198 LDTESEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVIQNGQVKEHGTHQQLLA 1254
Cdd:PRK14271 194 LDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARiSDRAALFFDGRLVEEGPTEQLFS 251
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
401-582 |
8.39e-19 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 86.79 E-value: 8.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 401 ILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRTINVRYLREI----IGVVSQEPVLFATTI 476
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELrnqkLGFIYQFHHLLPDFT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 477 AenirygRENVTMDEI--EKAVKEANAYDFIMKLPHKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALD 554
Cdd:PRK11629 104 A------LENVAMPLLigKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLD 177
|
170 180 190
....*....|....*....|....*....|
gi 25453402 555 TESEAVVQAALDK--AREGRTTIVIAHRLS 582
Cdd:PRK11629 178 ARNADSIFQLLGElnRLQGTAFLVVTHDLQ 207
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1044-1243 |
8.64e-19 |
|
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: 85.56 E-value: 8.64e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1044 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIKQLNV-QWLRAHLGIVSQEP----ILFDCS 1118
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPrDAIRAGIAYVPEDRkregLVLDLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1119 IAENIAYGDnsrvvsheeivkaakeanihqfidslpekyntrvgdkgtQLSGGQKQRIAIARALVRQPHILLLDEATSAL 1198
Cdd:cd03215 95 VAENIALSS---------------------------------------LLSGGNQQKVVLARWLARDPRVLILDEPTRGV 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 25453402 1199 DTES-EKVVQEALDKAREGRTCIVIahrlST-----IQNADLIVVIQNGQV 1243
Cdd:cd03215 136 DVGAkAEIYRLIRELADAGKAVLLI----SSeldelLGLCDRILVMYEGRI 182
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
384-579 |
9.50e-19 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 84.04 E-value: 9.50e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 384 LEFKNIHFSYPSRKdvqILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDgqdiRTINVRYLreiig 463
Cdd:cd03221 1 IELENLSKTYGGKL---LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWG----STVKIGYF----- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 464 vvsqepvlfattiaenirygrenvtmdeiekavkeanaydfimklphkfdtlvgergAQLSGGQKQRIAIARALVRNPKI 543
Cdd:cd03221 69 ---------------------------------------------------------EQLSGGEKMRLALAKLLLENPNL 91
|
170 180 190
....*....|....*....|....*....|....*.
gi 25453402 544 LLLDEATSALDTESEAVVQAALdKAREGrTTIVIAH 579
Cdd:cd03221 92 LLLDEPTNHLDLESIEALEEAL-KEYPG-TVILVSH 125
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
384-610 |
1.07e-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: 91.40 E-value: 1.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 384 LEFKNIHFSYPS--RKDVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVS-------IDGQDIRTIN 454
Cdd:TIGR03269 280 IKVRNVSKRYISvdRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNvrvgdewVDMTKPGPDG 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 455 VRYLREIIGVVSQEPVLFA-TTIAENIRygrENVTM---DEI--EKAV--------KEANAYDFIMKLPHkfdtlvgerg 520
Cdd:TIGR03269 360 RGRAKRYIGILHQEYDLYPhRTVLDNLT---EAIGLelpDELarMKAVitlkmvgfDEEKAEEILDKYPD---------- 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 521 aQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDKARE--GRTTIVIAHRLSTVRN-ADVIAGFDGGV 597
Cdd:TIGR03269 427 -ELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREemEQTFIIVSHDMDFVLDvCDRAALMRDGK 505
|
250
....*....|...
gi 25453402 598 IVEQGNHDELMRE 610
Cdd:TIGR03269 506 IVKIGDPEEIVEE 518
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
103-329 |
1.24e-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: 87.83 E-value: 1.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 103 MTTYAYYYTGIGAGVLIVAYIQVSLWCLAAGRQIHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKI 182
Cdd:cd18544 40 LLLLALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRDLFSHIQRLPLSFFDRTPVGRLVTRVTNDTEALNELFTSGL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 183 GMFFQAMATFFGGFIIGFTRGWKLTLVILAISPVLGLSAGIWAKILSSFTDKELQAYAKAGAVAEEVLAAIRTVIAFGGQ 262
Cdd:cd18544 120 VTLIGDLLLLIGILIAMFLLNWRLALISLLVLPLLLLATYLFRKKSRKAYREVREKLSRLNAFLQESISGMSVIQLFNRE 199
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 25453402 263 KKELERYNNNLEEAKRLGIKKAITANISMGAAFLLIYASYALAFWYGTSLVISKEYTIGqVLTVFFS 329
Cdd:cd18544 200 KREFEEFDEINQEYRKANLKSIKLFALFRPLVELLSSLALALVLWYGGGQVLSGAVTLG-VLYAFIQ 265
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1022-1254 |
1.28e-18 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 88.32 E-value: 1.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1022 MLEGNVKFNGVMFNYPTRPnipVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIKQlNVQWL 1101
Cdd:PRK13537 3 MSVAPIDFRNVEKRYGDKL---VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPS-RARHA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1102 RAHLGIVSQ----EPilfDCSIAENIaygdnsRVVSHEEIVKAAK-EANIHQFID--SLPEKYNTRVGDkgtqLSGGQKQ 1174
Cdd:PRK13537 79 RQRVGVVPQfdnlDP---DFTVRENL------LVFGRYFGLSAAAaRALVPPLLEfaKLENKADAKVGE----LSGGMKR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1175 RIAIARALVRQPHILLLDEATSALDTESEKVVQEALDK--AReGRTCIVIAHRLSTIQN-ADLIVVIQNGQVKEHGTHQQ 1251
Cdd:PRK13537 146 RLTLARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSllAR-GKTILLTTHFMEEAERlCDRLCVIEEGRKIAEGAPHA 224
|
...
gi 25453402 1252 LLA 1254
Cdd:PRK13537 225 LIE 227
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
112-336 |
1.31e-18 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350008 [Multi-domain] Cd Length: 307 Bit Score: 87.95 E-value: 1.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 112 GIGAGVLIVAYIQVSLWCLAAGRQIHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFFQAMAT 191
Cdd:cd18564 62 GIALLRGLASYAGTYLTALVGQRVVLDLRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGAIQDLLVSGVLPLLTNLLT 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 192 FFGGFIIGFTRGWKLTLVILAISPVLGLSAGIWAKILSSFTDKELQAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNN 271
Cdd:cd18564 142 LVGMLGVMFWLDWQLALIALAVAPLLLLAARRFSRRIKEASREQRRREGALASVAQESLSAIRVVQAFGREEHEERRFAR 221
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 25453402 272 NLEEAKRLGIK-KAITANISMGAAfLLIYASYALAFWYGTSLVISKEYTIGQvLTVFFSVLIGAFS 336
Cdd:cd18564 222 ENRKSLRAGLRaARLQALLSPVVD-VLVAVGTALVLWFGAWLVLAGRLTPGD-LLVFLAYLKNLYK 285
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1027-1256 |
1.47e-18 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 88.73 E-value: 1.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1027 VKFNGVMFNYPTRPnipVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIKQlNVQWLRAHLG 1106
Cdd:PRK13536 42 IDLAGVSKSYGDKA---VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA-RARLARARIG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1107 IVSQepilFD-----CSIAEN-IAYGDNSRVvSHEEIvkaakEANIHQFID--SLPEKYNTRVGDkgtqLSGGQKQRIAI 1178
Cdd:PRK13536 118 VVPQ----FDnldleFTVRENlLVFGRYFGM-STREI-----EAVIPSLLEfaRLESKADARVSD----LSGGMKRRLTL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1179 ARALVRQPHILLLDEATSALDTESEKVVQEALDK--AReGRTCIVIAHRLSTIQN-ADLIVVIQNGQVKEHGTHQQLLAQ 1255
Cdd:PRK13536 184 ARALINDPQLLILDEPTTGLDPHARHLIWERLRSllAR-GKTILLTTHFMEEAERlCDRLCVLEAGRKIAEGRPHALIDE 262
|
.
gi 25453402 1256 K 1256
Cdd:PRK13536 263 H 263
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1044-1248 |
1.48e-18 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 86.67 E-value: 1.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1044 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKeikqlnVQWLrahLGI-VSQEPILfdcSIAEN 1122
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGR------VSAL---LELgAGFHPEL---TGREN 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1123 I-----AYGdnsrvVSHEEIVKAAKE----ANIHQFIDsLPEKYntrvgdkgtqLSGGQKQRIAIARALVRQPHILLLDE 1193
Cdd:COG1134 109 IylngrLLG-----LSRKEIDEKFDEivefAELGDFID-QPVKT----------YSSGMRARLAFAVATAVDPDILLVDE 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 25453402 1194 ATSALDTE-SEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVIQNGQVKEHGT 1248
Cdd:COG1134 173 VLAVGDAAfQKKCLARIRELRESGRTVIFVSHSMGAVRRlCDRAIWLEKGRLVMDGD 229
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
384-602 |
1.54e-18 |
|
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: 84.99 E-value: 1.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 384 LEFKNIHFSYPS-RKDVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLL-QRLYD-PIEGEVSIDGQDIRtinvRYLRE 460
Cdd:cd03232 4 LTWKNLNYTVPVkGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLaGRKTAgVITGEILINGRPLD----KNFQR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 461 IIGVVSQEPVLFAT-TIAENIRygrenvtmdeiekavkeanaydFIMKLphkfdtlvgeRGaqLSGGQKQRIAIARALVR 539
Cdd:cd03232 80 STGYVEQQDVHSPNlTVREALR----------------------FSALL----------RG--LSVEQRKRLTIGVELAA 125
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 25453402 540 NPKILLLDEATSALDTESEAVVQAALDK-AREGRTTIVIAHRLStvrnADVIAGFDGGVIVEQG 602
Cdd:cd03232 126 KPSILFLDEPTSGLDSQAAYNIVRFLKKlADSGQAILCTIHQPS----ASIFEKFDRLLLLKRG 185
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
384-608 |
2.14e-18 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 87.55 E-value: 2.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 384 LEFKNIHFSYpsrKDVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRTiNVRYLREIIG 463
Cdd:PRK13537 8 IDFRNVEKRY---GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPS-RARHARQRVG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 464 VVSQ----EPVLfatTIAENIR-YGRE-NVTMDEIEKAVkeANAYDFiMKLPHKFDTLVGErgaqLSGGQKQRIAIARAL 537
Cdd:PRK13537 84 VVPQfdnlDPDF---TVRENLLvFGRYfGLSAAAARALV--PPLLEF-AKLENKADAKVGE----LSGGMKRRLTLARAL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 25453402 538 VRNPKILLLDEATSALDTESEAVVQAALDK--AReGRTTIVIAHRLSTV-RNADVIAGFDGGVIVEQGNHDELM 608
Cdd:PRK13537 154 VNDPDVLVLDEPTTGLDPQARHLMWERLRSllAR-GKTILLTTHFMEEAeRLCDRLCVIEEGRKIAEGAPHALI 226
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
384-611 |
2.17e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 87.45 E-value: 2.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 384 LEFKNIHFSYPSRK--DVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRTI-------- 453
Cdd:PRK13651 3 IKVKNIVKIFNKKLptELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKkktkekek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 454 ----------------NVRYLREIIGVVSQ--EPVLFATTIAENIRYGRENVTMDEiEKAVKEANAYDFIMKLPHKFDtl 515
Cdd:PRK13651 83 vleklviqktrfkkikKIKEIRRRVGVVFQfaEYQLFEQTIEKDIIFGPVSMGVSK-EEAKKRAAKYIELVGLDESYL-- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 516 vgERGA-QLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDKA-REGRTTIVIAHRLSTV--RNADVIA 591
Cdd:PRK13651 160 --QRSPfELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLnKQGKTIILVTHDLDNVleWTKRTIF 237
|
250 260
....*....|....*....|
gi 25453402 592 GFDGGVIVEQGNHDELMREK 611
Cdd:PRK13651 238 FKDGKIIKDGDTYDILSDNK 257
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
405-602 |
2.39e-18 |
|
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: 91.61 E-value: 2.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 405 LNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRTiNVRYLREIIGVVSQEPVLFA-TTIAENIRYg 483
Cdd:TIGR01257 949 LNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET-NLDAVRQSLGMCPQHNILFHhLTVAEHILF- 1026
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 484 RENVTMDEIEKAVKEANAYDFIMKLPHKFDtlvgERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQA 563
Cdd:TIGR01257 1027 YAQLKGRSWEEAQLEMEAMLEDTGLHHKRN----EEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWD 1102
|
170 180 190
....*....|....*....|....*....|....*....
gi 25453402 564 ALDKAREGRTTIVIAHRLStvrNADVIAgfDGGVIVEQG 602
Cdd:TIGR01257 1103 LLLKYRSGRTIIMSTHHMD---EADLLG--DRIAIISQG 1136
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1045-1270 |
2.57e-18 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 86.22 E-value: 2.57e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1045 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLL----------ERFYDPMAGTVFLDGKEIKqlNVQWLRAHLGIVSQEPIL 1114
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLsglitgdksaGSHIELLGRTVQREGRLAR--DIRKSRANTGYIFQQFNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1115 FD-CSIAENIAYGDNSRVVSHEEIVKAAKEANIHQFIDSLpekynTRVG------DKGTQLSGGQKQRIAIARALVRQPH 1187
Cdd:PRK09984 98 VNrLSVLENVLIGALGSTPFWRTCFSWFTREQKQRALQAL-----TRVGmvhfahQRVSTLSGGQQQRVAIARALMQQAK 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1188 ILLLDEATSALDTESEKVVQEALD--KAREGRTCIVIAHRLS-TIQNADLIVVIQNGQVKEHGTHQQLLAQK--GIYFSM 1262
Cdd:PRK09984 173 VILADEPIASLDPESARIVMDTLRdiNQNDGITVVVTLHQVDyALRYCERIVALRQGHVFYDGSSQQFDNERfdHLYRSI 252
|
....*...
gi 25453402 1263 VSVQAGAK 1270
Cdd:PRK09984 253 NRVEENAK 260
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
749-1193 |
3.26e-18 |
|
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: 89.86 E-value: 3.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 749 LLFLILGIISFITFFLQGFTFGKAGEILTKRLRYMVFKSMLRQDISWFDdpKNTTGALTTRLANDAAQVKGATgSRLAVI 828
Cdd:COG4615 52 LLFAGLLVLLLLSRLASQLLLTRLGQHAVARLRLRLSRRILAAPLERLE--RIGAARLLAALTEDVRTISQAF-VRLPEL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 829 TQNIANlgtgIIISLIY-GWQLTLLLLAIVPIIAIAGVVEMKMLSgqalKDKKELEGSGKIATEAIENFRTVVSLTREQK 907
Cdd:COG4615 129 LQSVAL----VLGCLAYlAWLSPPLFLLTLVLLGLGVAGYRLLVR----RARRHLRRAREAEDRLFKHFRALLEGFKELK 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 908 F-----ETMYAQSLQIP---YRNALKKAHV-FGITFSFTQAMMYFSYAACFrfgaYLVARELMTFENVLLVFS-AIVFGA 977
Cdd:COG4615 201 LnrrrrRAFFDEDLQPTaerYRDLRIRADTiFALANNWGNLLFFALIGLIL----FLLPALGWADPAVLSGFVlVLLFLR 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 978 MAVGQVSSFAPDYAKAKVSASHIIRIIEKIPEIDSYSTEGLKPNMLEG--NVKFNGVMFNYPTRPNIP--VLQGLSLEVK 1053
Cdd:COG4615 277 GPLSQLVGALPTLSRANVALRKIEELELALAAAEPAAADAAAPPAPADfqTLELRGVTYRYPGEDGDEgfTLGPIDLTIR 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1054 KGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIKQLNVQWLRAHLGIVSQEPILFDcsiaenIAYGdnsrvvs 1133
Cdd:COG4615 357 RGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQLFSAVFSDFHLFD------RLLG------- 423
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 25453402 1134 heeIVKAAKEANIHQFIDSLPEKYNTRVGDKG---TQLSGGQKQRIAIARALVRQPHILLLDE 1193
Cdd:COG4615 424 ---LDGEADPARARELLERLELDHKVSVEDGRfstTDLSQGQRKRLALLVALLEDRPILVFDE 483
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
1027-1225 |
3.67e-18 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 82.97 E-value: 3.67e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1027 VKFNGVMFNYPTrpNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEikqlnvqwlraHLG 1106
Cdd:cd03223 1 IELENLSLATPD--GRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGE-----------DLL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1107 IVSQEPILFDCSIAENIAYgdnsrvvsheeivkaakeanihqfidslPEkyntrvgdkGTQLSGGQKQRIAIARALVRQP 1186
Cdd:cd03223 68 FLPQRPYLPLGTLREQLIY----------------------------PW---------DDVLSGGEQQRLAFARLLLHKP 110
|
170 180 190
....*....|....*....|....*....|....*....
gi 25453402 1187 HILLLDEATSALDTESEKVVQEALDKarEGRTCIVIAHR 1225
Cdd:cd03223 111 KFVFLDEATSALDEESEDRLYQLLKE--LGITVISVGHR 147
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
746-986 |
3.71e-18 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350019 [Multi-domain] Cd Length: 289 Bit Score: 86.38 E-value: 3.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 746 LFSLLFLILGIISFITFFLqgftFGKAGEILTKRLRYMVFKSMLRQDISWFDdpKNTTGALTTRLANDAAQVKGATGSRL 825
Cdd:cd18575 41 LLLAVALVLALASALRFYL----VSWLGERVVADLRKAVFAHLLRLSPSFFE--TTRTGEVLSRLTTDTTLIQTVVGSSL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 826 AVITQNIANLGTGIIISLIYGWQLTLLLLAIVPIIAIAGVV---EMKMLSGQAlKDKkeLEGSGKIATEAIENFRTVVSL 902
Cdd:cd18575 115 SIALRNLLLLIGGLVMLFITSPKLTLLVLLVIPLVVLPIILfgrRVRRLSRAS-QDR--LADLSAFAEETLSAIKTVQAF 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 903 TREQKFETMYAQSLQIPYRNALKKAHvfgitfsftqammyfsyaacfrfgaylvARELMTFENVLLVFSAIVF------- 975
Cdd:cd18575 192 TREDAERQRFATAVEAAFAAALRRIR----------------------------ARALLTALVIFLVFGAIVFvlwlgah 243
|
250
....*....|....*
gi 25453402 976 ----GAMAVGQVSSF 986
Cdd:cd18575 244 dvlaGRMSAGELSQF 258
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
117-329 |
4.25e-18 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350007 [Multi-domain] Cd Length: 296 Bit Score: 86.41 E-value: 4.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 117 VLIVAYIQVSLWCLAAGRQ----------IHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFF 186
Cdd:cd18563 46 VLGLAGAYVLSALLGILRGrllarlgeriTADLRRDLYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDFLSDGLPDFL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 187 QAMATFFGGFIIGFTRGWKLTLVILAISPVLG-LSAGIWAKILSSFTdKELQAYAKAGAVAEEVLAAIRTVIAFGGQKKE 265
Cdd:cd18563 126 TNILMIIGIGVVLFSLNWKLALLVLIPVPLVVwGSYFFWKKIRRLFH-RQWRRWSRLNSVLNDTLPGIRVVKAFGQEKRE 204
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 25453402 266 LERYNNNLEEAKRLGIKKAITANISMGAAFLLIYASYALAFWYGTSLVISKEYTIGqVLTVFFS 329
Cdd:cd18563 205 IKRFDEANQELLDANIRAEKLWATFFPLLTFLTSLGTLIVWYFGGRQVLSGTMTLG-TLVAFLS 267
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
1025-1255 |
5.27e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 85.83 E-value: 5.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1025 GNVKFNGVMFNYPTRP--NIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDG-------KEIKQ 1095
Cdd:PRK13645 5 KDIILDNVSYTYAKKTpfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDyaipanlKKIKE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1096 lnVQWLRAHLGIVSQEP--ILFDCSIAENIAYGDNSRVVSHEEIVKaakeaNIHQFID--SLPEKYNTRvgdKGTQLSGG 1171
Cdd:PRK13645 85 --VKRLRKEIGLVFQFPeyQLFQETIEKDIAFGPVNLGENKQEAYK-----KVPELLKlvQLPEDYVKR---SPFELSGG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1172 QKQRIAIARALVRQPHILLLDEATSALDTESEK---VVQEALDKaREGRTCIVIAHRLSTI-QNADLIVVIQNGQVKEHG 1247
Cdd:PRK13645 155 QKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEdfiNLFERLNK-EYKKRIIMVTHNMDQVlRIADEVIVMHEGKVISIG 233
|
250
....*....|....
gi 25453402 1248 ------THQQLLAQ 1255
Cdd:PRK13645 234 spfeifSNQELLTK 247
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
52-322 |
5.41e-18 |
|
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: 86.06 E-value: 5.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 52 LGTLAAIIHGIALPLMMlvfGDMTDSFANVGNNRSMSFYNATDIYA-KLedeMTTYAyyytgiGAGVLIVAYIqvSLWCL 130
Cdd:cd18574 3 LSALAAALVNIQIPLLL---GDLVNVISRSLKETNGDFIEDLKKPAlKL---LGLYL------LQSLLTFAYI--SLLSV 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 131 AAGRQIHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSK--------INEGIgdkigmffQAMATFFGGFIIGFTR 202
Cdd:cd18574 69 VGERVAARLRNDLFSSLLRQDIAFFDTHRTGELVNRLTADVQEfkssfkqcVSQGL--------RSVTQTVGCVVSLYLI 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 203 GWKLTLVILAISPVLGLSAGIWAKILSSFTDKELQAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNNNLEEAKRL--- 279
Cdd:cd18574 141 SPKLTLLLLVIVPVVVLVGTLYGSFLRKLSRRAQAQVAKATGVADEALGNIRTVRAFAMEDRELELYEEEVEKAAKLnek 220
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 25453402 280 -----GIKKAITaNISMGAAFLLIYasyalafWYGTSLVISKEYTIGQ 322
Cdd:cd18574 221 lglgiGIFQGLS-NLALNGIVLGVL-------YYGGSLVSRGELTAGD 260
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
50-329 |
5.60e-18 |
|
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: 85.92 E-value: 5.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 50 MLLGTLAAIIHGIALPLMMLVFGDMTDS-FANVGNNRSMSFynatdiyakleDEMTTYAYYYTGIGAGVLIVAYIQVslW 128
Cdd:cd18547 1 LILVIILAIISTLLSVLGPYLLGKAIDLiIEGLGGGGGVDF-----------SGLLRILLLLLGLYLLSALFSYLQN--R 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 129 CLA--AGRQIHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFFQAMATFFGGFIIGFTRGWKL 206
Cdd:cd18547 68 LMArvSQRTVYDLRKDLFEKLQRLPLSYFDTHSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPLL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 207 TLVILAISPVLGLSAGIWAKILSSFTDKELQAYAKAGAVAEEVLAAIRTVIAFGGQKKELER---YNNNLEEAkrlGIKK 283
Cdd:cd18547 148 TLIVLVTVPLSLLVTKFIAKRSQKYFRKQQKALGELNGYIEEMISGQKVVKAFNREEEAIEEfdeINEELYKA---SFKA 224
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 25453402 284 AITANISMGAAFLLIYASYALAFWYGTSLVISKEYTIGqVLTVFFS 329
Cdd:cd18547 225 QFYSGLLMPIMNFINNLGYVLVAVVGGLLVINGALTVG-VIQAFLQ 269
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
703-986 |
7.84e-18 |
|
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: 85.53 E-value: 7.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 703 FVVGVFCAIINGGLQPAFSIIFSKVVGVFTKNDTPEIQRQNSNLFSLLFLILGI--ISFITFFLQGFTFGKAGEILTKRL 780
Cdd:cd18547 1 LILVIILAIISTLLSVLGPYLLGKAIDLIIEGLGGGGGVDFSGLLRILLLLLGLylLSALFSYLQNRLMARVSQRTVYDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 781 RYMVFKSMLRQDISWFDdpKNTTGALTTRLANDAAQVKGATGSRLAVITQNIANLGTGIIISLIYGWQLTLLLLAIVPII 860
Cdd:cd18547 81 RKDLFEKLQRLPLSYFD--THSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPLLTLIVLVTVPLS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 861 AIAgvveMKMLSGQALKD-KKELEGSGKI---ATEAIENFRTVVSLTRE----QKFETMYAQslqipYRNALKKAHVF-G 931
Cdd:cd18547 159 LLV----TKFIAKRSQKYfRKQQKALGELngyIEEMISGQKVVKAFNREeeaiEEFDEINEE-----LYKASFKAQFYsG 229
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 25453402 932 ITFSFTQAMMYFSYAACFRFGAYLVarelmtfenvllvfsaiVFGAMAVGQVSSF 986
Cdd:cd18547 230 LLMPIMNFINNLGYVLVAVVGGLLV-----------------INGALTVGVIQAF 267
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
379-598 |
8.57e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 85.44 E-value: 8.57e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 379 NIQGNLEFKNIHFSYPSRK--DVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLY-----DPIEGEVSIDGQDIR 451
Cdd:PRK13645 2 DFSKDIILDNVSYTYAKKTpfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIisetgQTIVGDYAIPANLKK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 452 TINVRYLREIIGVVSQEP--VLFATTIAENIRYGRENVTMDEiEKAVKEANAYDFIMKLPHKFdtlVGERGAQLSGGQKQ 529
Cdd:PRK13645 82 IKEVKRLRKEIGLVFQFPeyQLFQETIEKDIAFGPVNLGENK-QEAYKKVPELLKLVQLPEDY---VKRSPFELSGGQKR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 25453402 530 RIAIARALVRNPKILLLDEATSALDTESEAVVQAALDK--AREGRTTIVIAHRLSTV-RNAD-VIAGFDGGVI 598
Cdd:PRK13645 158 RVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERlnKEYKKRIIMVTHNMDQVlRIADeVIVMHEGKVI 230
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
1045-1252 |
8.95e-18 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 83.57 E-value: 8.95e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1045 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIKQlNVQWLRAHLGIVSQEPILFDCSIA-ENI 1123
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREVRRRIGIVFQDLSVDDELTGwENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1124 A-----YGdnsrvVSHEEIVKAAKEAniHQFIDsLPEKYNTRVGdkgtQLSGGQKQRIAIARALVRQPHILLLDEATSAL 1198
Cdd:cd03265 95 YiharlYG-----VPGAERRERIDEL--LDFVG-LLEAADRLVK----TYSGGMRRRLEIARSLVHRPEVLFLDEPTIGL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 25453402 1199 DTESEKVVQEALDK--AREGRTCIVIAHRLSTI-QNADLIVVIQNGQVKEHGTHQQL 1252
Cdd:cd03265 163 DPQTRAHVWEYIEKlkEEFGMTILLTTHYMEEAeQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1043-1248 |
9.23e-18 |
|
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: 89.69 E-value: 9.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1043 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIkQLNVQWLRAHLGIVSQEPILFD-CSIAE 1121
Cdd:TIGR01257 944 PAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-ETNLDAVRQSLGMCPQHNILFHhLTVAE 1022
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1122 NIAYGDNSRVVSHEEiVKAAKEANIHQfiDSLPEKYNTRVGDkgtqLSGGQKQRIAIARALVRQPHILLLDEATSALDTE 1201
Cdd:TIGR01257 1023 HILFYAQLKGRSWEE-AQLEMEAMLED--TGLHHKRNEEAQD----LSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPY 1095
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 25453402 1202 SEKVVQEALDKAREGRTCIVIAHRLStiqNADL----IVVIQNGQVKEHGT 1248
Cdd:TIGR01257 1096 SRRSIWDLLLKYRSGRTIIMSTHHMD---EADLlgdrIAIISQGRLYCSGT 1143
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
1047-1252 |
1.31e-17 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 85.53 E-value: 1.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1047 GLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEI-KQLNVQWL--RAHLGIVSQEPILF---DCSIA 1120
Cdd:PRK15079 39 GVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLlGMKDDEWRavRSDIQMIFQDPLASlnpRMTIG 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1121 ENIA------YGDNSRVVSHEEiVKA--AKEANIHQFIDSLPEKYntrvgdkgtqlSGGQKQRIAIARALVRQPHILLLD 1192
Cdd:PRK15079 119 EIIAeplrtyHPKLSRQEVKDR-VKAmmLKVGLLPNLINRYPHEF-----------SGGQCQRIGIARALILEPKLIICD 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 25453402 1193 EATSALDTESE-KVVQEALDKARE-GRTCIVIAHRLSTIQN-ADLIVVIQNGQVKEHGTHQQL 1252
Cdd:PRK15079 187 EPVSALDVSIQaQVVNLLQQLQREmGLSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEV 249
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1043-1243 |
1.38e-17 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 87.38 E-value: 1.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1043 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIKQLNV-QWLRAHLGIVS----QEPILFDC 1117
Cdd:COG1129 266 GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPrDAIRAGIAYVPedrkGEGLVLDL 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1118 SIAENI---AYGDNSR--VVSHEEIVKAAKEanihqFIDSLpekyNTRVGDKGT---QLSGGQKQRIAIARALVRQPHIL 1189
Cdd:COG1129 346 SIRENItlaSLDRLSRggLLDRRRERALAEE-----YIKRL----RIKTPSPEQpvgNLSGGNQQKVVLAKWLATDPKVL 416
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 25453402 1190 LLDEATSALD--TESE--KVVQEAldkAREGRTCIVIahrlST-----IQNADLIVVIQNGQV 1243
Cdd:COG1129 417 ILDEPTRGIDvgAKAEiyRLIREL---AAEGKAVIVI----SSelpelLGLSDRILVMREGRI 472
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
397-638 |
1.47e-17 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 87.55 E-value: 1.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 397 KDVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRL--YDPIEGEV----------------SIDGQ---------- 448
Cdd:TIGR03269 11 DGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIiyhvalcekcgyverpSKVGEpcpvcggtle 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 449 ----DIRTINVRYLREIIGVVSqepVLFATTIAeniRYGRENV------TMDEIEKAVKEA--NAYDFI--MKLPHKFDT 514
Cdd:TIGR03269 91 peevDFWNLSDKLRRRIRKRIA---IMLQRTFA---LYGDDTVldnvleALEEIGYEGKEAvgRAVDLIemVQLSHRITH 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 515 LVGErgaqLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDKA--REGRTTIVIAHRLSTVRN-ADVIA 591
Cdd:TIGR03269 165 IARD----LSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAvkASGISMVLTSHWPEVIEDlSDKAI 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 25453402 592 GFDGGVIVEQGNHDELMrekGIYFKLVMTQTAGNEIELGNEACESKD 638
Cdd:TIGR03269 241 WLENGEIKEEGTPDEVV---AVFMEGVSEVEKECEVEVGEPIIKVRN 284
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
747-965 |
1.79e-17 |
|
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: 84.28 E-value: 1.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 747 FSLLFLILGIISFITFFLQG-----FTFGKAGeiLTKRLRYMVFKSMLRQDISWFDdpKNTTGALTTRLANDAAQVKGAT 821
Cdd:cd18784 35 FSRAIIIMGLLAIASSVAAGirgglFTLAMAR--LNIRIRNLLFRSIVSQEIGFFD--TVKTGDITSRLTSDTTTMSDTV 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 822 GSRLAVITQNIANLGTGIIISLIYGWQLTLLLLAIVPIIAIAGVVEMKMLSGQALKDKKELEGSGKIATEAIENFRTVVS 901
Cdd:cd18784 111 SLNLNIFLRSLVKAIGVIVFMFKLSWQLSLVTLIGLPLIAIVSKVYGDYYKKLSKAVQDSLAKANEVAEETISSIRTVRS 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 25453402 902 LTREQKFETMYAQSLQIPYRNALKKAHVFGiTFSFTQAMMYFS-YAACFRFGAYLVARELMTFEN 965
Cdd:cd18784 191 FANEDGEANRYSEKLKDTYKLKIKEALAYG-GYVWSNELTELAlTVSTLYYGGHLVITGQISGGN 254
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
1034-1247 |
2.32e-17 |
|
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: 82.58 E-value: 2.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1034 FNYPTRPNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKeikqlnVQW-LRAHLGIVSQ-- 1110
Cdd:cd03220 27 GRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGR------VSSlLGLGGGFNPElt 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1111 --EPILFDCSIaeniaYGdnsrvVSHEEIvkAAKEANIHQFIDsLPEKYNTRVGdkgtQLSGGQKQRIAIARALVRQPHI 1188
Cdd:cd03220 101 grENIYLNGRL-----LG-----LSRKEI--DEKIDEIIEFSE-LGDFIDLPVK----TYSSGMKARLAFAIATALEPDI 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 25453402 1189 LLLDEATSALDTE-SEKVVQEALDKAREGRTCIVIAHRLSTI-QNADLIVVIQNGQVKEHG 1247
Cdd:cd03220 164 LLIDEVLAVGDAAfQEKCQRRLRELLKQGKTVILVSHDPSSIkRLCDRALVLEKGKIRFDG 224
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
384-607 |
2.37e-17 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 87.03 E-value: 2.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 384 LEFKNIHFSYPSrkdVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRTINVRYLREI-I 462
Cdd:PRK15439 12 LCARSISKQYSG---VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLgI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 463 GVVSQEPVLFAT-TIAENIRYG--RENVTMDEIEKAVKEANAYdfiMKLPHKFDTL-VGERgaqlsggqkQRIAIARALV 538
Cdd:PRK15439 89 YLVPQEPLLFPNlSVKENILFGlpKRQASMQKMKQLLAALGCQ---LDLDSSAGSLeVADR---------QIVEILRGLM 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 25453402 539 RNPKILLLDEATSALD-TESEAV---VQAALDKareGRTTIVIAHRLSTVRN-ADVIAGFDGGVIVEQGNHDEL 607
Cdd:PRK15439 157 RDSRILILDEPTASLTpAETERLfsrIRELLAQ---GVGIVFISHKLPEIRQlADRISVMRDGTIALSGKTADL 227
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
1038-1245 |
2.80e-17 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 86.77 E-value: 2.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1038 TRPNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYdP---MAGTVFLDGKE-----IKQlnvqwlRAHLGIV- 1108
Cdd:NF040905 10 TFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PhgsYEGEILFDGEVcrfkdIRD------SEALGIVi 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1109 -SQE----PILfdcSIAENIAYGdNSR----VVSHEEIVKAAKE--ANIhqfidSLPEKYNTRVGDKGTqlsgGQKQRIA 1177
Cdd:NF040905 83 iHQElaliPYL---SIAENIFLG-NERakrgVIDWNETNRRAREllAKV-----GLDESPDTLVTDIGV----GKQQLVE 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1178 IARALVRQPHILLLDEATSAL-DTESEKVVQEALDKAREGRTCIVIAHRLSTI-QNADLIVVIQNGQVKE 1245
Cdd:NF040905 150 IAKALSKDVKLLILDEPTAALnEEDSAALLDLLLELKAQGITSIIISHKLNEIrRVADSITVLRDGRTIE 219
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
1044-1247 |
2.87e-17 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 81.42 E-value: 2.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1044 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERF--YDPMAGTVFLDGKEIKQLNVQwLRAHLGI--VSQEPIlfdcsi 1119
Cdd:cd03217 15 ILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPE-ERARLGIflAFQYPP------ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1120 aeniaygdnsrvvsheEI--VKAAKeanihqFIDSLPEKyntrvgdkgtqLSGGQKQRIAIARALVRQPHILLLDEATSA 1197
Cdd:cd03217 88 ----------------EIpgVKNAD------FLRYVNEG-----------FSGGEKKRNEILQLLLLEPDLAILDEPDSG 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 25453402 1198 LDTESEKVVQEALDKAR-EGRTCIVIAH--RLSTIQNADLIVVIQNGQVKEHG 1247
Cdd:cd03217 135 LDIDALRLVAEVINKLReEGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVKSG 187
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
395-578 |
3.46e-17 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 81.25 E-value: 3.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 395 SRKDVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRTINVRYLREIIGVVSQEPVLFAT 474
Cdd:TIGR01189 9 SRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLPGLKPEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 475 TIAENIRYGRE--NVTMDEIEKAVKEANaydfimkLPHKFDTLVgergAQLSGGQKQRIAIARALVRNPKILLLDEATSA 552
Cdd:TIGR01189 89 SALENLHFWAAihGGAQRTIEDALAAVG-------LTGFEDLPA----AQLSAGQQRRLALARLWLSRRPLWILDEPTTA 157
|
170 180
....*....|....*....|....*.
gi 25453402 553 LDTESEAVVQAALDkAREGRTTIVIA 578
Cdd:TIGR01189 158 LDKAGVALLAGLLR-AHLARGGIVLL 182
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
400-607 |
3.66e-17 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 86.30 E-value: 3.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 400 QILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLY--DPIE---GEVSIDGQDIRTINVRYLREI----IGVVSQEPV 470
Cdd:PRK15134 23 TVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLpsPPVVypsGDIRFHGESLLHASEQTLRGVrgnkIAMIFQEPM 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 471 LFAT---TIAENI-------RYGRENVTMDE---------IEKAVKEANAYdfimklPHkfdtlvgergaQLSGGQKQRI 531
Cdd:PRK15134 103 VSLNplhTLEKQLyevlslhRGMRREAARGEilncldrvgIRQAAKRLTDY------PH-----------QLSGGERQRV 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 25453402 532 AIARALVRNPKILLLDEATSALDTESEAVVQAALDKARE--GRTTIVIAHRLSTVRN-ADVIAGFDGGVIVEQGNHDEL 607
Cdd:PRK15134 166 MIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQelNMGLLFITHNLSIVRKlADRVAVMQNGRCVEQNRAATL 244
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1047-1252 |
4.44e-17 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 82.35 E-value: 4.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1047 GLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIKQLNVQWLrAHLGIVS--QEPILF-DCSIAENI 1123
Cdd:PRK11300 23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQI-ARMGVVRtfQHVRLFrEMTVIENL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1124 AygdnsrVVSHEEI--------------VKAAKEA--NIHQFID--SLPEKYNTRVGDkgtqLSGGQKQRIAIARALVRQ 1185
Cdd:PRK11300 102 L------VAQHQQLktglfsgllktpafRRAESEAldRAATWLErvGLLEHANRQAGN----LAYGQQRRLEIARCMVTQ 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1186 PHILLLDEATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTIQN-ADLIVVIQNGQVKEHGTHQQL 1252
Cdd:PRK11300 172 PEILMLDEPAAGLNPKETKELDELIAELRNehNVTVLLIEHDMKLVMGiSDRIYVVNQGTPLANGTPEEI 241
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
1044-1253 |
5.37e-17 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 82.34 E-value: 5.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1044 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIKQLNVQWLRAHLGIVSQEPIL-FDCSIAEN 1122
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTpGDITVQEL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1123 IAYG--------DNSRVVSHEEIVKAAKEANIHQFIDslpEKYNTrvgdkgtqLSGGQKQRIAIARALVRQPHILLLDEA 1194
Cdd:PRK10253 102 VARGryphqplfTRWRKEDEEAVTKAMQATGITHLAD---QSVDT--------LSGGQRQRAWIAMVLAQETAIMLLDEP 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 25453402 1195 TSALDTESEKVVQEALDK--AREGRTCIVIAHRLS-TIQNADLIVVIQNGQVKEHGTHQQLL 1253
Cdd:PRK10253 171 TTWLDISHQIDLLELLSElnREKGYTLAAVLHDLNqACRYASHLIALREGKIVAQGAPKEIV 232
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
395-559 |
6.22e-17 |
|
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: 80.61 E-value: 6.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 395 SRKDVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRTINVRYLREIIGVVSQEPVLFAT 474
Cdd:cd03231 9 ERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 475 TIAENIRYGRENVTMDEIEKAVKEANAYDFimklphkFDTLVgergAQLSGGQKQRIAIARALVRNPKILLLDEATSALD 554
Cdd:cd03231 89 SVLENLRFWHADHSDEQVEEALARVGLNGF-------EDRPV----AQLSAGQQRRVALARLLLSGRPLWILDEPTTALD 157
|
....*
gi 25453402 555 TESEA 559
Cdd:cd03231 158 KAGVA 162
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
371-602 |
6.50e-17 |
|
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: 81.04 E-value: 6.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 371 SKSGHKPDNIQGNLEFKNIHFSYPSRKDVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQdi 450
Cdd:cd03220 7 SKSYPTYKGGSSSLKKLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGR-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 451 rtinvrylreiigvVSqePVLFATTIAENIRYGRENVTM---------DEIEKavKEANAYDFiMKLPHKFDTLVGErga 521
Cdd:cd03220 85 --------------VS--SLLGLGGGFNPELTGRENIYLngrllglsrKEIDE--KIDEIIEF-SELGDFIDLPVKT--- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 522 qLSGGQKQRIAIARALVRNPKILLLDEATSALDtesEAVVQAALDKARE----GRTTIVIAHRLSTVRN-ADVIAGFDGG 596
Cdd:cd03220 143 -YSSGMKARLAFAIATALEPDILLIDEVLAVGD---AAFQEKCQRRLREllkqGKTVILVSHDPSSIKRlCDRALVLEKG 218
|
....*.
gi 25453402 597 VIVEQG 602
Cdd:cd03220 219 KIRFDG 224
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1039-1255 |
7.78e-17 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 85.24 E-value: 7.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1039 RPNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTV-------FLDGKEIKQLNVQWLRAHLGIVSQE 1111
Cdd:TIGR03269 294 RGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnvrvgdeWVDMTKPGPDGRGRAKRYIGILHQE 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1112 PILF-DCSIAENIaygdnSRVVSHEEIVKAAKEANIHQF-IDSLPEKYNTRVGDKGT-QLSGGQKQRIAIARALVRQPHI 1188
Cdd:TIGR03269 374 YDLYpHRTVLDNL-----TEAIGLELPDELARMKAVITLkMVGFDEEKAEEILDKYPdELSEGERHRVALAQVLIKEPRI 448
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1189 LLLDEATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTIQN-ADLIVVIQNGQVKEHGTHQQLLAQ 1255
Cdd:TIGR03269 449 VILDEPTGTMDPITKVDVTHSILKAREemEQTFIIVSHDMDFVLDvCDRAALMRDGKIVKIGDPEEIVEE 518
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
107-548 |
8.33e-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: 85.23 E-value: 8.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 107 AYYYTGIGAGVLIVAYIQvslwclaagRQIHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINEGIGDkIGMFF 186
Cdd:COG4615 60 LLLLSRLASQLLLTRLGQ---------HAVARLRLRLSRRILAAPLERLERIGAARLLAALTEDVRTISQAFVR-LPELL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 187 QAMATFFGGFIIGFTRGWKLTLVILAIspvlgLSAGIWAKILssFTDKELQAYAKAGAVAEEVLAAIRTVIafGGQKkEL 266
Cdd:COG4615 130 QSVALVLGCLAYLAWLSPPLFLLTLVL-----LGLGVAGYRL--LVRRARRHLRRAREAEDRLFKHFRALL--EGFK-EL 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 267 ------------ERYNNNLEEAKRLGIKKAITANISMGAAFLLIYASYALAFWYGTSLV-ISKEYTIGQVLTVFF----- 328
Cdd:COG4615 200 klnrrrrraffdEDLQPTAERYRDLRIRADTIFALANNWGNLLFFALIGLILFLLPALGwADPAVLSGFVLVLLFlrgpl 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 329 SVLIGAF-SVGQAS---PNIEAFANARGAAYEVFSIIDNKPSIDSFSKsghkpdniqgnLEFKNIHFSYPSRKDVQ--IL 402
Cdd:COG4615 280 SQLVGALpTLSRANvalRKIEELELALAAAEPAAADAAAPPAPADFQT-----------LELRGVTYRYPGEDGDEgfTL 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 403 KGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRTINVRYLREIIGVVSQEPVLFATTiaenirY 482
Cdd:COG4615 349 GPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQLFSAVFSDFHLFDRL------L 422
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 25453402 483 GRENVTMDEiekavkEANAYDFIMKLPHK-------FDTLvgergaQLSGGQKQRIAIARALVRNPKILLLDE 548
Cdd:COG4615 423 GLDGEADPA------RARELLERLELDHKvsvedgrFSTT------DLSQGQRKRLALLVALLEDRPILVFDE 483
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
1039-1253 |
8.39e-17 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 85.48 E-value: 8.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1039 RPNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLErFYDP----MAGTVFLDGKEIkqlNVQWLRAHLGIVSQEPIL 1114
Cdd:TIGR00955 35 RPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALA-FRSPkgvkGSGSVLLNGMPI---DAKEMRAISAYVQQDDLF 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1115 FDCSIA-ENIAYgdNSRVVSHEEIVKAAKEANIHQFID--SLPEKYNTRVGDKGTQ--LSGGQKQRIAIARALVRQPHIL 1189
Cdd:TIGR00955 111 IPTLTVrEHLMF--QAHLRMPRRVTKKEKRERVDEVLQalGLRKCANTRIGVPGRVkgLSGGERKRLAFASELLTDPPLL 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 25453402 1190 LLDEATSALDTES-EKVVQEALDKAREGRTCIVIAHRLST--IQNADLIVVIQNGQVKEHGTHQQLL 1253
Cdd:TIGR00955 189 FCDEPTSGLDSFMaYSVVQVLKGLAQKGKTIICTIHQPSSelFELFDKIILMAEGRVAYLGSPDQAV 255
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
384-627 |
8.79e-17 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 84.88 E-value: 8.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 384 LEFKNIHFSYpsrKDVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLY--DPIEGEVSIDGQDIRTINVRYL-RE 460
Cdd:TIGR02633 2 LEMKGIVKTF---GGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYphGTWDGEIYWSGSPLKASNIRDTeRA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 461 IIGVVSQEPVLFAT-TIAENIRYGRE----NVTMDEIEkAVKEANAYDFIMKLPHKFDTL-VGERGaqlsGGQKQRIAIA 534
Cdd:TIGR02633 79 GIVIIHQELTLVPElSVAENIFLGNEitlpGGRMAYNA-MYLRAKNLLRELQLDADNVTRpVGDYG----GGQQQLVEIA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 535 RALVRNPKILLLDEATSAL-DTESEAVVQAALDKAREGRTTIVIAHRLSTVRnadviAGFDGGVIVEQGNHDELMREKGI 613
Cdd:TIGR02633 154 KALNKQARLLILDEPSSSLtEKETEILLDIIRDLKAHGVACVYISHKLNEVK-----AVCDTICVIRDGQHVATKDMSTM 228
|
250
....*....|....
gi 25453402 614 YFKLVMTQTAGNEI 627
Cdd:TIGR02633 229 SEDDIITMMVGREI 242
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
401-608 |
9.26e-17 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 81.96 E-value: 9.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 401 ILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRTINVRYLREIIGVVSQEPVLFA-TTIAEN 479
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTPGdITVQEL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 480 IRYGRE------NVTMDEIEKAVKEANAYDFIMKLP-HKFDTlvgergaqLSGGQKQRIAIARALVRNPKILLLDEATSA 552
Cdd:PRK10253 102 VARGRYphqplfTRWRKEDEEAVTKAMQATGITHLAdQSVDT--------LSGGQRQRAWIAMVLAQETAIMLLDEPTTW 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 25453402 553 LDTESEA-VVQAALDKARE-GRTTIVIAHRLS-TVRNADVIAGFDGGVIVEQGNHDELM 608
Cdd:PRK10253 174 LDISHQIdLLELLSELNREkGYTLAAVLHDLNqACRYASHLIALREGKIVAQGAPKEIV 232
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
384-585 |
9.39e-17 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 84.84 E-value: 9.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 384 LEFKNIHFSYPSrkdVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRTINVRYLREI-I 462
Cdd:PRK09700 6 ISMAGIGKSFGP---VHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLgI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 463 GVVSQE-PVLFATTIAENIRYGRE------NVTMDEIEKAVKEANAYDFIMKLPHKFDTLVGErgaqLSGGQKQRIAIAR 535
Cdd:PRK09700 83 GIIYQElSVIDELTVLENLYIGRHltkkvcGVNIIDWREMRVRAAMMLLRVGLKVDLDEKVAN----LSISHKQMLEIAK 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 25453402 536 ALVRNPKILLLDEATSALDTESEAVVQAALDKAR-EGRTTIVIAHRLSTVR 585
Cdd:PRK09700 159 TLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRkEGTAIVYISHKLAEIR 209
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
384-608 |
1.03e-16 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 81.76 E-value: 1.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 384 LEFKNIH--FSYPS----RKDVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDG---------- 447
Cdd:PRK15112 5 LEVRNLSktFRYRTgwfrRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDhplhfgdysy 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 448 --QDIRTI-----NVRYLREIIGVVSQEPVLFATTIAENIRYGRENVTMDEIEKAVKEANAYdfimklPHkfdtlvgerg 520
Cdd:PRK15112 85 rsQRIRMIfqdpsTSLNPRQRISQILDFPLRLNTDLEPEQREKQIIETLRQVGLLPDHASYY------PH---------- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 521 aQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEA-VVQAALD-KAREGRTTIVIAHRLSTVRN-ADVIAGFDGGV 597
Cdd:PRK15112 149 -MLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSqLINLMLElQEKQGISYIYVTQHLGMMKHiSDQVLVMHQGE 227
|
250
....*....|.
gi 25453402 598 IVEQGNHDELM 608
Cdd:PRK15112 228 VVERGSTADVL 238
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1042-1243 |
1.31e-16 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 84.72 E-value: 1.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1042 IPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKeiKQLNVQWLRAH-LGI--VSQEPILF-DC 1117
Cdd:PRK15439 24 VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGN--PCARLTPAKAHqLGIylVPQEPLLFpNL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1118 SIAENIAYGDNSRVVSHEEIVKAAKEANIHQFIDSlpekyntrvgdKGTQLSGGQKQRIAIARALVRQPHILLLDEATSA 1197
Cdd:PRK15439 102 SVKENILFGLPKRQASMQKMKQLLAALGCQLDLDS-----------SAGSLEVADRQIVEILRGLMRDSRILILDEPTAS 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 25453402 1198 LD-TESEKV---VQEALDKareGRTCIVIAHRLSTI-QNADLIVVIQNGQV 1243
Cdd:PRK15439 171 LTpAETERLfsrIRELLAQ---GVGIVFISHKLPEIrQLADRISVMRDGTI 218
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
384-599 |
1.36e-16 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 82.46 E-value: 1.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 384 LEFKNIH--FSYPSrKDVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDP---IEGEVSIDGQDIRTINVRYL 458
Cdd:PRK09473 13 LDVKDLRvtFSTPD-GDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAngrIGGSATFNGREILNLPEKEL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 459 REI----IGVVSQEPVlfaTTIAENIRYG-------------------RENVTMDEiekAVKEANAYDFIMKLPHKFdtl 515
Cdd:PRK09473 92 NKLraeqISMIFQDPM---TSLNPYMRVGeqlmevlmlhkgmskaeafEESVRMLD---AVKMPEARKRMKMYPHEF--- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 516 vgergaqlSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDK-AREGRTTIV-IAHRLStvrnadVIAGF 593
Cdd:PRK09473 163 --------SGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNElKREFNTAIImITHDLG------VVAGI 228
|
....*.
gi 25453402 594 DGGVIV 599
Cdd:PRK09473 229 CDKVLV 234
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
384-590 |
1.42e-16 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 84.46 E-value: 1.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 384 LEFKNIHFSYPSrkdVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYdPI---EGEVSIDGQ-----DIRTinv 455
Cdd:NF040905 2 LEMRGITKTFPG---VKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PHgsyEGEILFDGEvcrfkDIRD--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 456 rylREIIGVV--SQE----PVLfatTIAENIRYGRENVTMDEI--EKAVKEANAYDFIMKLPHKFDTLVGERGAqlsgGQ 527
Cdd:NF040905 75 ---SEALGIViiHQElaliPYL---SIAENIFLGNERAKRGVIdwNETNRRARELLAKVGLDESPDTLVTDIGV----GK 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 25453402 528 KQRIAIARALVRNPKILLLDEATSAL-DTESEAVVQAALDKAREGRTTIVIAHRLSTVRN-ADVI 590
Cdd:NF040905 145 QQLVEIAKALSKDVKLLILDEPTAALnEEDSAALLDLLLELKAQGITSIIISHKLNEIRRvADSI 209
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1039-1252 |
1.51e-16 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 84.91 E-value: 1.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1039 RPNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDG-------------KEIKQLNVQWLR-AH 1104
Cdd:PRK10261 26 QQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllrrrsrqvielSEQSAAQMRHVRgAD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1105 LGIVSQEPI-----LFDC--SIAENIAYGDNsrvVSHEEIVKAAKeanihQFIDS--LPEKyNTRVGDKGTQLSGGQKQR 1175
Cdd:PRK10261 106 MAMIFQEPMtslnpVFTVgeQIAESIRLHQG---ASREEAMVEAK-----RMLDQvrIPEA-QTILSRYPHQLSGGMRQR 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1176 IAIARALVRQPHILLLDEATSALDTESE-------KVVQEALDKAregrtCIVIAHRLSTIQN-ADLIVVIQNGQVKEHG 1247
Cdd:PRK10261 177 VMIAMALSCRPAVLIADEPTTALDVTIQaqilqliKVLQKEMSMG-----VIFITHDMGVVAEiADRVLVMYQGEAVETG 251
|
....*
gi 25453402 1248 THQQL 1252
Cdd:PRK10261 252 SVEQI 256
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
400-595 |
1.53e-16 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 79.92 E-value: 1.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 400 QILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDI---RTINVRYLREIIGVVSQE-------- 468
Cdd:PRK10908 16 QALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDItrlKNREVPFLRRQIGMIFQDhhllmdrt 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 469 -------PVLFATTIAENIRYgRENVTMDEIEKAVKEANaydfimkLPhkfdtlvgergAQLSGGQKQRIAIARALVRNP 541
Cdd:PRK10908 96 vydnvaiPLIIAGASGDDIRR-RVSAALDKVGLLDKAKN-------FP-----------IQLSGGEQQRVGIARAVVNKP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 25453402 542 KILLLDEATSALDTE-SEAVVQAALDKAREGRTTIVIAHRLSTV--RNADVIAGFDG 595
Cdd:PRK10908 157 AVLLADEPTGNLDDAlSEGILRLFEEFNRVGVTVLMATHDIGLIsrRSYRMLTLSDG 213
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
1009-1255 |
1.69e-16 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 84.25 E-value: 1.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1009 EIDSYSTEGLKPNMLEG--NVKFNGVMFNYPTrPNIPVlQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTV 1086
Cdd:PRK10522 303 ALAPYKAEFPRPQAFPDwqTLELRNVTFAYQD-NGFSV-GPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEI 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1087 FLDGKEIKQLNVQWLRAHLGIVSQEPILFDcsiaeniaygdnsRVVSHEEivKAAKEANIHQFIDSLPEKYNTRVGD--- 1163
Cdd:PRK10522 381 LLDGKPVTAEQPEDYRKLFSAVFTDFHLFD-------------QLLGPEG--KPANPALVEKWLERLKMAHKLELEDgri 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1164 KGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVV-QEALDKARE-GRTCIVIAHRLSTIQNADLIVVIQNG 1241
Cdd:PRK10522 446 SNLKLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRREFyQVLLPLLQEmGKTIFAISHDDHYFIHADRLLEMRNG 525
|
250
....*....|....*
gi 25453402 1242 QVKE-HGTHQQLLAQ 1255
Cdd:PRK10522 526 QLSElTGEERDAASR 540
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
1043-1223 |
2.28e-16 |
|
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: 78.94 E-value: 2.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1043 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIKQLNVQWLRAHLGIVSQEPILFDCSIAEN 1122
Cdd:TIGR01189 14 MLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLPGLKPELSALEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1123 IAYgdnsrvvsheeivkaakEANIHQFIDSLPEKYNTRVGDKG------TQLSGGQKQRIAIARALVRQPHILLLDEATS 1196
Cdd:TIGR01189 94 LHF-----------------WAAIHGGAQRTIEDALAAVGLTGfedlpaAQLSAGQQRRLALARLWLSRRPLWILDEPTT 156
|
170 180
....*....|....*....|....*..
gi 25453402 1197 ALDTESEKVVQEALDkAREGRTCIVIA 1223
Cdd:TIGR01189 157 ALDKAGVALLAGLLR-AHLARGGIVLL 182
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
388-609 |
2.43e-16 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 84.14 E-value: 2.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 388 NIHFSYPSRKdVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRTIN--VRYLREI---- 461
Cdd:PRK10261 19 NIAFMQEQQK-IAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRSrqVIELSEQsaaq 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 462 --------IGVVSQEPV-----LFAT--TIAENIR----YGREnvtmdeieKAVKEANAYDFIMKLPHKfDTLVGERGAQ 522
Cdd:PRK10261 98 mrhvrgadMAMIFQEPMtslnpVFTVgeQIAESIRlhqgASRE--------EAMVEAKRMLDQVRIPEA-QTILSRYPHQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 523 LSGGQKQRIAIARALVRNPKILLLDEATSALDTESEA-------VVQAALDKAregrtTIVIAHRLSTVRN-ADVIAGFD 594
Cdd:PRK10261 169 LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAqilqlikVLQKEMSMG-----VIFITHDMGVVAEiADRVLVMY 243
|
250
....*....|....*
gi 25453402 595 GGVIVEQGNHDELMR 609
Cdd:PRK10261 244 QGEAVETGSVEQIFH 258
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
1027-1242 |
3.15e-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: 76.72 E-value: 3.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1027 VKFNGVMFNYPTRPnipVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLerfydpmagtvfldgkeikqlnvqwlrahlg 1106
Cdd:cd03221 1 IELENLSKTYGGKL---LLKDISLTINPGDRIGLVGRNGAGKSTLLKLI------------------------------- 46
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1107 ivsqepilfdcsiaeniaygdNSRVVSHEEIVKAAKEANIHQFidslpekyntrvgdkgTQLSGGQKQRIAIARALVRQP 1186
Cdd:cd03221 47 ---------------------AGELEPDEGIVTWGSTVKIGYF----------------EQLSGGEKMRLALAKLLLENP 89
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 25453402 1187 HILLLDEATSALDTESEKVVQEALdKAREGrTCIVIAHRLSTIQN-ADLIVVIQNGQ 1242
Cdd:cd03221 90 NLLLLDEPTNHLDLESIEALEEAL-KEYPG-TVILVSHDRYFLDQvATKIIELEDGK 144
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1043-1248 |
3.23e-16 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 79.74 E-value: 3.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1043 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIKQLNVQWLRAHLGIVSQEPILfdcsiaen 1122
Cdd:COG4604 15 VVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAILRQENHI-------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1123 iaygdNSRV-----VS-----H---------EEIVKAAkeanIHQF-IDSLPEKYNTrvgdkgtQLSGGQKQRIAIARAL 1182
Cdd:COG4604 87 -----NSRLtvrelVAfgrfpYskgrltaedREIIDEA----IAYLdLEDLADRYLD-------ELSGGQRQRAFIAMVL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 25453402 1183 VRQPHILLLDEATSALD----TESEKVVQEAldkARE-GRTCIVIAHRLstiqN-----ADLIVVIQNGQVKEHGT 1248
Cdd:COG4604 151 AQDTDYVLLDEPLNNLDmkhsVQMMKLLRRL---ADElGKTVVIVLHDI----NfascyADHIVAMKDGRVVAQGT 219
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1038-1223 |
3.26e-16 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 78.76 E-value: 3.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1038 TRPNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIKQLNVQWLRAHLGIVSQ-EPILfd 1116
Cdd:PRK13539 11 VRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHYLGHRNAmKPAL-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1117 cSIAENIA-----YGDnsrvvsHEEIVKAAKEANIHQFIDSLPEKYntrvgdkgtqLSGGQKQRIAIARALVRQPHILLL 1191
Cdd:PRK13539 89 -TVAENLEfwaafLGG------EELDIAAALEAVGLAPLAHLPFGY----------LSAGQKRRVALARLLVSNRPIWIL 151
|
170 180 190
....*....|....*....|....*....|..
gi 25453402 1192 DEATSALDTESEKVVQEALdKAREGRTCIVIA 1223
Cdd:PRK13539 152 DEPTAALDAAAVALFAELI-RAHLAQGGIVIA 182
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1040-1242 |
3.61e-16 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 83.13 E-value: 3.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1040 PNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIK-------QlnvqwlRAHLGIVSQEP 1112
Cdd:PRK10762 15 PGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfngpkssQ------EAGIGIIHQEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1113 ILFD-CSIAENIAYGdnsrvvshEEIVKAAKEAN---IHQFIDSLPEKYN------TRVGDkgtqLSGGQKQRIAIARAL 1182
Cdd:PRK10762 89 NLIPqLTIAENIFLG--------REFVNRFGRIDwkkMYAEADKLLARLNlrfssdKLVGE----LSIGEQQMVEIAKVL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 25453402 1183 VRQPHILLLDEATSAL-DTESE---KVVQEALDkarEGRTCIVIAHRLSTI-QNADLIVVIQNGQ 1242
Cdd:PRK10762 157 SFESKVIIMDEPTDALtDTETEslfRVIRELKS---QGRGIVYISHRLKEIfEICDDVTVFRDGQ 218
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
400-607 |
3.87e-16 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 83.56 E-value: 3.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 400 QILKGLNLKVKSGQTVALVGNSGCGKSTtvqLLQRL--YDP----IEGEVSIDGqdiRTINVRYLREIIGVVSQEPVLFA 473
Cdd:TIGR00955 39 HLLKNVSGVAKPGELLAVMGSSGAGKTT---LMNALafRSPkgvkGSGSVLLNG---MPIDAKEMRAISAYVQQDDLFIP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 474 T-TIAENI------RYGReNVTMDEIEKAVKEanaydFI--MKLPHKFDTLVGERGAQ--LSGGQKQRIAIARALVRNPK 542
Cdd:TIGR00955 113 TlTVREHLmfqahlRMPR-RVTKKEKRERVDE-----VLqaLGLRKCANTRIGVPGRVkgLSGGERKRLAFASELLTDPP 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 25453402 543 ILLLDEATSALDTESEA-VVQAALDKAREGRTTIVIAHRLST--VRNADVIAGFDGGVIVEQGNHDEL 607
Cdd:TIGR00955 187 LLFCDEPTSGLDSFMAYsVVQVLKGLAQKGKTIICTIHQPSSelFELFDKIILMAEGRVAYLGSPDQA 254
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
401-607 |
6.14e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 79.75 E-value: 6.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 401 ILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEG-----EVSIDGQDIRTI-NVRYLREIIGVVSQEPVLFAT 474
Cdd:PRK14271 36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFNYrDVLEFRRRVGMLFQRPNPFPM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 475 TIAENIRYG-RENVTMDEIE-KAVKEANAYDfiMKLPHKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSA 552
Cdd:PRK14271 116 SIMDNVLAGvRAHKLVPRKEfRGVAQARLTE--VGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSA 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 25453402 553 LDTESEAVVQAALDKAREGRTTIVIAHRLS-TVRNADVIAGFDGGVIVEQGNHDEL 607
Cdd:PRK14271 194 LDPTTTEKIEEFIRSLADRLTVIIVTHNLAqAARISDRAALFFDGRLVEEGPTEQL 249
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
1044-1210 |
7.53e-16 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 77.53 E-value: 7.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1044 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIKQLNVQWLRAHLGIVSQEPILFDCSIAENI 1123
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSVLENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1124 AY--GDNSRvvshEEIVKAAKEANIHQFIDsLPekyntrvgdkGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTE 1201
Cdd:cd03231 95 RFwhADHSD----EQVEEALARVGLNGFED-RP----------VAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKA 159
|
....*....
gi 25453402 1202 SEKVVQEAL 1210
Cdd:cd03231 160 GVARFAEAM 168
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1033-1247 |
7.71e-16 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 82.60 E-value: 7.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1033 MFNYPTRpNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIKQLN---VQWLRAHLGIVS 1109
Cdd:PRK10261 329 LLNRVTR-EVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSpgkLQALRRDIQFIF 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1110 QEPILfDCSIAENIAYGDNSRVVSHEEIVKAAKEANIHQFIDslpekyntRVGDKGT-------QLSGGQKQRIAIARAL 1182
Cdd:PRK10261 408 QDPYA-SLDPRQTVGDSIMEPLRVHGLLPGKAAAARVAWLLE--------RVGLLPEhawryphEFSGGQRQRICIARAL 478
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 25453402 1183 VRQPHILLLDEATSALDTE-SEKVVQEALDKARE-GRTCIVIAHRLSTIQN-ADLIVVIQNGQVKEHG 1247
Cdd:PRK10261 479 ALNPKVIIADEAVSALDVSiRGQIINLLLDLQRDfGIAYLFISHDMAVVERiSHRVAVMYLGQIVEIG 546
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1022-1258 |
8.28e-16 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 78.38 E-value: 8.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1022 MLEGNVKFNGVMFNYPtrpNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLerFYDPMA--GTVFLDGKEIKQL-NV 1098
Cdd:PRK11614 1 MEKVMLSFDKVSAHYG---KIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTL--CGDPRAtsGRIVFDGKDITDWqTA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1099 QWLRAHLGIVSQEPILFD-CSIAENIAYGdnSRVVSHEEIvkaakEANIHQFIDSLPEKYNTRVGDKGTqLSGGQKQRIA 1177
Cdd:PRK11614 76 KIMREAVAIVPEGRRVFSrMTVEENLAMG--GFFAERDQF-----QERIKWVYELFPRLHERRIQRAGT-MSGGEQQMLA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1178 IARALVRQPHILLLDEATSALdteSEKVVQEALDKAR----EGRTCIVIAHRLS-TIQNADLIVVIQNGQVKEHGTHQQL 1252
Cdd:PRK11614 148 IGRALMSQPRLLLLDEPSLGL---APIIIQQIFDTIEqlreQGMTIFLVEQNANqALKLADRGYVLENGHVVLEDTGDAL 224
|
....*.
gi 25453402 1253 LAQKGI 1258
Cdd:PRK11614 225 LANEAV 230
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
384-603 |
8.36e-16 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 78.40 E-value: 8.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 384 LEFKNIHFSYPSRKdvqILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRTINVR-YLREII 462
Cdd:PRK10895 4 LTAKNLAKAYKGRR---VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHaRARRGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 463 GVVSQEPVLFAT-TIAENIrygrenVTMDEIEKAVKEANAYDFIMKLPHKFDT--LVGERGAQLSGGQKQRIAIARALVR 539
Cdd:PRK10895 81 GYLPQEASIFRRlSVYDNL------MAVLQIRDDLSAEQREDRANELMEEFHIehLRDSMGQSLSGGERRRVEIARALAA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 25453402 540 NPKILLLDEATSALDTESEAVVQAALDKAREGRTTIVIAHRlsTVRnaDVIAGFDGGVIVEQGN 603
Cdd:PRK10895 155 NPKFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDH--NVR--ETLAVCERAYIVSQGH 214
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1027-1252 |
1.02e-15 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 78.65 E-value: 1.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1027 VKFNGVMFnypTRPNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIKQLNVQWL---RA 1103
Cdd:PRK11831 8 VDMRGVSF---TRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLytvRK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1104 HLGIVSQEPILF-DCSIAENIAYGDNSRVVSHEEIVKAAKEANIHQfidslpekyntrVGDKG------TQLSGGQKQRI 1176
Cdd:PRK11831 85 RMSMLFQSGALFtDMNVFDNVAYPLREHTQLPAPLLHSTVMMKLEA------------VGLRGaaklmpSELSGGMARRA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 25453402 1177 AIARALVRQPHILLLDEATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTIQN-ADLIVVIQNGQVKEHGTHQQL 1252
Cdd:PRK11831 153 ALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSalGVTCVVVSHDVPEVLSiADHAYIVADKKIVAHGSAQAL 231
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
366-610 |
1.17e-15 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 78.20 E-value: 1.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 366 SIDSFSKSGHKPDNIQGNLEFKNIHFSYPSRKDVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSI 445
Cdd:COG1134 6 EVENVSKSYRLYHEPSRSLKELLLRRRRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 446 DGqdirtiNVRYLREIIGVVSQEpvlfaTTIAENIR-----YGrenVTMDEIEKAVKEANAY----DFImklphkfDTLV 516
Cdd:COG1134 86 NG------RVSALLELGAGFHPE-----LTGRENIYlngrlLG---LSRKEIDEKFDEIVEFaelgDFI-------DQPV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 517 GergaQLSGGQKQRIAIARALVRNPKILLLDEATSALDTE----SEAVVQaalDKAREGRTTIVIAHRLSTVRN-ADVIA 591
Cdd:COG1134 145 K----TYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAfqkkCLARIR---ELRESGRTVIFVSHSMGAVRRlCDRAI 217
|
250
....*....|....*....
gi 25453402 592 GFDGGVIVEQGNHDELMRE 610
Cdd:COG1134 218 WLEKGRLVMDGDPEEVIAA 236
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
405-610 |
1.30e-15 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 78.05 E-value: 1.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 405 LNLKVKSGQTVALVGNSGCGKSTtvqLLQRLYD--PIEGEVSIDGQDIRTINVRYLREIIGVVSQE-PVLFATTIAENI- 480
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKST---LLARMAGllPGSGSIQFAGQPLEAWSAAELARHRAYLSQQqTPPFAMPVFQYLt 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 481 RYGRENVTMDEIEKAVKE-ANAYDFIMKLPhkfdTLVGergaQLSGGQKQRIAIARALVR-----NP--KILLLDEATSA 552
Cdd:PRK03695 92 LHQPDKTRTEAVASALNEvAEALGLDDKLG----RSVN----QLSGGEWQRVRLAAVVLQvwpdiNPagQLLLLDEPMNS 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 25453402 553 LDTESeavvQAALDK-----AREGRTTIVIAHRLS-TVRNADVIAGFDGGVIVEQGNHDELMRE 610
Cdd:PRK03695 164 LDVAQ----QAALDRllselCQQGIAVVMSSHDLNhTLRHADRVWLLKQGKLLASGRRDEVLTP 223
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
139-335 |
2.18e-15 |
|
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: 78.21 E-value: 2.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 139 IRQKFFHAIMNqeigwFDVHDVGE-----LNTRLTDDVSKINEGIGDKIGMFFQAMATFFGGFIIGFTRGWKLTLVILAI 213
Cdd:cd18548 74 LRKDLFEKIQS-----FSFAEIDKfgtssLITRLTNDVTQVQNFVMMLLRMLVRAPIMLIGAIIMAFRINPKLALILLVA 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 214 SPVLGLSAGIWAKILSSFTDKELQAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNNNLEEAKRLGIKKAITANISMGA 293
Cdd:cd18548 149 IPILALVVFLIMKKAIPLFKKVQKKLDRLNRVVRENLTGIRVIRAFNREDYEEERFDKANDDLTDTSLKAGRLMALLNPL 228
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 25453402 294 AFLLIYASYALAFWYGTSLVISKEYTIGQV-------LTVFFSVLIGAF 335
Cdd:cd18548 229 MMLIMNLAIVAILWFGGHLINAGSLQVGDLvafinylMQILMSLMMLSM 277
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
138-335 |
2.30e-15 |
|
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette transporters; This group includes the 6-TMD of the peptidase-containing ATP-binding cassette transporters (PCATs) such as Clostridium thermocellum PCAT1, a polypeptide processing and secretion transporter, and LagD, a bacteriocin ABC transporter from Lactococcus lactis. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs. The transporters involved in protein secretion often contain additional peptidase domains essential for substrate processing. These peptidase domains belong to the cysteine protease superfamily, classified as family C39, bacteriocin-processing peptidase. LagD is highly similar to the peptidase-containing ATP-binding cassette transporters (PCATs). In Gram-positive bacteria, the PCATs are responsible for exporting quorum-sensing or antimicrobial peptides called bacteriocins.
Pssm-ID: 350014 [Multi-domain] Cd Length: 294 Bit Score: 78.26 E-value: 2.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 138 KIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDdVSKINEGIGDKIGMFFQAMATFFGGFIIGFTRGWKLTLVILAISPVL 217
Cdd:cd18570 76 RLILGYFKHLLKLPLSFFETRKTGEIISRFND-ANKIREAISSTTISLFLDLLMVIISGIILFFYNWKLFLITLLIIPLY 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 218 GLSAGIWAKILSSFTDKELQAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNNNLEEAKRLGIKKAITANISMGAAFLL 297
Cdd:cd18570 155 ILIILLFNKPFKKKNREVMESNAELNSYLIESLKGIETIKSLNAEEQFLKKIEKKFSKLLKKSFKLGKLSNLQSSIKGLI 234
|
170 180 190
....*....|....*....|....*....|....*...
gi 25453402 298 IYASYALAFWYGTSLVISKEYTIGQVLTvfFSVLIGAF 335
Cdd:cd18570 235 SLIGSLLILWIGSYLVIKGQLSLGQLIA--FNALLGYF 270
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1044-1254 |
2.87e-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: 80.23 E-value: 2.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1044 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERF--YDPMAGTVFLDGKEIKQLNVQWLRAHLG---------IVSQEP 1112
Cdd:TIGR03269 15 VLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIYHVALCEKCGYVERPSKVGepcpvcggtLEPEEV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1113 ILFDCS------IAENIA---------YGDNSRVV----SHEEIVKAAKEAnIHQFIDSLPE-KYNTRVGDKGTQLSGGQ 1172
Cdd:TIGR03269 95 DFWNLSdklrrrIRKRIAimlqrtfalYGDDTVLDnvleALEEIGYEGKEA-VGRAVDLIEMvQLSHRITHIARDLSGGE 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1173 KQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKA--REGRTCIVIAHRLSTIQN-ADLIVVIQNGQVKEHGTH 1249
Cdd:TIGR03269 174 KQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAvkASGISMVLTSHWPEVIEDlSDKAIWLENGEIKEEGTP 253
|
....*
gi 25453402 1250 QQLLA 1254
Cdd:TIGR03269 254 DEVVA 258
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
395-609 |
3.18e-15 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 77.56 E-value: 3.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 395 SRKDVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQ-RLYDP-------IEGEVSIDGQDIRTINVRYLREIIGVVS 466
Cdd:PRK13547 10 ARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAgDLTGGgaprgarVTGDVTLNGEPLAAIDAPRLARLRAVLP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 467 Q--EPVlFATTIAENIRYGR----------ENVTMDEIEKAVKEANAydfimklphkfDTLVGERGAQLSGGQKQRIAIA 534
Cdd:PRK13547 90 QaaQPA-FAFSAREIVLLGRypharragalTHRDGEIAWQALALAGA-----------TALVGRDVTTLSGGELARVQFA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 535 RAL---------VRNPKILLLDEATSALDTESE----AVVQAALDKAREGRTTIVIAHRLSTvRNADVIAGFDGGVIVEQ 601
Cdd:PRK13547 158 RVLaqlwpphdaAQPPRYLLLDEPTAALDLAHQhrllDTVRRLARDWNLGVLAIVHDPNLAA-RHADRIAMLADGAIVAH 236
|
....*...
gi 25453402 602 GNHDELMR 609
Cdd:PRK13547 237 GAPADVLT 244
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
759-963 |
4.25e-15 |
|
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: 77.59 E-value: 4.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 759 FITFFLQG-FTF------GKAGEILTKRLRYMVFKSMLRQDISWFDdpKNTTGALTTRLANDAAQVKGATGSrlaVITQN 831
Cdd:cd18574 49 LGLYLLQSlLTFayisllSVVGERVAARLRNDLFSSLLRQDIAFFD--THRTGELVNRLTADVQEFKSSFKQ---CVSQG 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 832 IANLG--TGIIISLIY-GWQLTLLLLAIVPIIAIAGVV---EMKMLSGQAlkdKKELEGSGKIATEAIENFRTVVSLTRE 905
Cdd:cd18574 124 LRSVTqtVGCVVSLYLiSPKLTLLLLVIVPVVVLVGTLygsFLRKLSRRA---QAQVAKATGVADEALGNIRTVRAFAME 200
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 25453402 906 QKFETMYAQSLQipyrNALKKAHVFGITFSFTQAMMYFS---------YaacfrFGAYLVAR------ELMTF 963
Cdd:cd18574 201 DRELELYEEEVE----KAAKLNEKLGLGIGIFQGLSNLAlngivlgvlY-----YGGSLVSRgeltagDLMSF 264
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
385-594 |
4.47e-15 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 80.92 E-value: 4.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 385 EFKNIHFSYPSRKDV-QILKGLNLKVKSGQTVALVGNSGCGKSTtvqLLQRLYDPIEGEVSIDGqdIRTINVRYLRE--- 460
Cdd:TIGR00956 761 HWRNLTYEVKIKKEKrVILNNVDGWVKPGTLTALMGASGAGKTT---LLNVLAERVTTGVITGG--DRLVNGRPLDSsfq 835
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 461 -IIGVVSQEPVLFAT-TIAENIRYGRENVTMDEIEKavKEANAY-DFIMKL---PHKFDTLVGERGAQLSGGQKQRIAIA 534
Cdd:TIGR00956 836 rSIGYVQQQDLHLPTsTVRESLRFSAYLRQPKSVSK--SEKMEYvEEVIKLlemESYADAVVGVPGEGLNVEQRKRLTIG 913
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 25453402 535 RALVRNPKILL-LDEATSALDTESEAVVQAALDK-AREGRTTIVIAHRLStvrnADVIAGFD 594
Cdd:TIGR00956 914 VELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKlADHGQAILCTIHQPS----AILFEEFD 971
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
384-553 |
4.72e-15 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 76.07 E-value: 4.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 384 LEFKNIHFSYpsrKDVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRTI-NVRYLREII 462
Cdd:PRK11614 6 LSFDKVSAHY---GKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWqTAKIMREAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 463 GVVSQEPVLFA-TTIAENIRYGRENVTMDEIEKAVKEAnaYDFIMKLPHKfdtlVGERGAQLSGGQKQRIAIARALVRNP 541
Cdd:PRK11614 83 AIVPEGRRVFSrMTVEENLAMGGFFAERDQFQERIKWV--YELFPRLHER----RIQRAGTMSGGEQQMLAIGRALMSQP 156
|
170
....*....|..
gi 25453402 542 KILLLDEATSAL 553
Cdd:PRK11614 157 RLLLLDEPSLGL 168
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
384-604 |
5.62e-15 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 75.98 E-value: 5.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 384 LEFKNIHFSYpsrKDVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLL--QRLYDPIEGEVSIDGQDIRTIN------- 454
Cdd:PRK09580 2 LSIKDLHVSV---EDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLagREDYEVTGGTVEFKGKDLLELSpedrage 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 455 -----VRYLREIIGVVSQepvLFATTIAENIRYGRENVTMDEIEKAvkeanayDFI------MKLPHkfDTLVGERGAQL 523
Cdd:PRK09580 79 gifmaFQYPVEIPGVSNQ---FFLQTALNAVRSYRGQEPLDRFDFQ-------DLMeekialLKMPE--DLLTRSVNVGF 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 524 SGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDKAREG-RTTIVIAH--RLSTVRNADVIAGFDGGVIVE 600
Cdd:PRK09580 147 SGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGkRSFIIVTHyqRILDYIKPDYVHVLYQGRIVK 226
|
....
gi 25453402 601 QGNH 604
Cdd:PRK09580 227 SGDF 230
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1045-1241 |
6.26e-15 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 79.06 E-value: 6.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1045 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIKQLNVQwLRAHLG--IVSQEPILFD-CSIAE 1121
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHK-LAAQLGigIIYQELSVIDeLTVLE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1122 NIAYGDN-SRVVSHEEIV---KAAKEANIHQFIDSLPEKYNTRVGDkgtqLSGGQKQRIAIARALVRQPHILLLDEATSA 1197
Cdd:PRK09700 100 NLYIGRHlTKKVCGVNIIdwrEMRVRAAMMLLRVGLKVDLDEKVAN----LSISHKQMLEIAKTLMLDAKVIIMDEPTSS 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 25453402 1198 L-DTESEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVIQNG 1241
Cdd:PRK09700 176 LtNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRiCDRYTVMKDG 221
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
127-325 |
6.42e-15 |
|
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: 76.74 E-value: 6.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 127 LWCLAAGRQIHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFFQAMATFFGGFIIGFTRGWKL 206
Cdd:cd18589 59 IYNITMSRIHSRLQGLVFAAVLRQEIAFFDSNQTGDIVSRVTTDTEDMSESLSENLSLLMWYLARGLFLFIFMLWLSPKL 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 207 TLVILAISPVLGLSAGIWAKILSSFTDKELQAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNNNLEEAKRLGIKKAIT 286
Cdd:cd18589 139 ALLTALGLPLLLLVPKFVGKFQQSLAVQVQKSLARANQVAVETFSAMKTVRSFANEEGEAQRYRQRLQKTYRLNKKEAAA 218
|
170 180 190
....*....|....*....|....*....|....*....
gi 25453402 287 ANISMGAAFLLIYASYALAFWYGTSLVISKEYTIGQVLT 325
Cdd:cd18589 219 YAVSMWTSSFSGLALKVGILYYGGQLVTAGTVSSGDLVT 257
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
402-596 |
6.79e-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: 74.01 E-value: 6.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 402 LKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRTINVRYLREI-IGVVSQEPV---LFAT-TI 476
Cdd:cd03215 16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAgIAYVPEDRKregLVLDlSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 477 AENIrygrenvtmdeiekavkeanaydfimklphkfdTLvgerGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTE 556
Cdd:cd03215 96 AENI---------------------------------AL----SSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVG 138
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 25453402 557 SEAVVQAALDK-AREGRTTIVIAHRLSTV-RNADVIAGFDGG 596
Cdd:cd03215 139 AKAEIYRLIRElADAGKAVLLISSELDELlGLCDRILVMYEG 180
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1034-1254 |
6.99e-15 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 76.37 E-value: 6.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1034 FNYPT----RPNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIKQLNVQWLRAHLGIVS 1109
Cdd:PRK15112 14 FRYRTgwfrRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIRMIF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1110 QEPilfdcSIAEN----IAYGDNSRVVSHEEIVKAAKEANIHQFIDS---LPEKYNTRvgdkGTQLSGGQKQRIAIARAL 1182
Cdd:PRK15112 94 QDP-----STSLNprqrISQILDFPLRLNTDLEPEQREKQIIETLRQvglLPDHASYY----PHMLAPGQKQRLGLARAL 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 25453402 1183 VRQPHILLLDEATSALD-TESEKVVQEALD-KAREGRTCIVIAHRLSTIQN-ADLIVVIQNGQVKEHGTHQQLLA 1254
Cdd:PRK15112 165 ILRPKVIIADEALASLDmSMRSQLINLMLElQEKQGISYIYVTQHLGMMKHiSDQVLVMHQGEVVERGSTADVLA 239
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1045-1253 |
7.10e-15 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 76.12 E-value: 7.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1045 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIKQLNVQWL----RAHL-----GIVSQEP--- 1112
Cdd:PRK11701 22 CRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALseaeRRRLlrtewGFVHQHPrdg 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1113 ILFDCSIAENI-----AYGDNSrvvsHEEIVKAAKEANIHQFIDSlpekynTRVGDKGTQLSGGQKQRIAIARALVRQPH 1187
Cdd:PRK11701 102 LRMQVSAGGNIgerlmAVGARH----YGDIRATAGDWLERVEIDA------ARIDDLPTTFSGGMQQRLQIARNLVTHPR 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 25453402 1188 ILLLDEATSALDTEsekvVQ-EALDKARE-----GRTCIVIAHRLSTIQN-ADLIVVIQNGQVKEHGTHQQLL 1253
Cdd:PRK11701 172 LVFMDEPTGGLDVS----VQaRLLDLLRGlvrelGLAVVIVTHDLAVARLlAHRLLVMKQGRVVESGLTDQVL 240
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1041-1243 |
8.82e-15 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 78.53 E-value: 8.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1041 NIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLL--ERfyDPMAGTVFLDGKEIKQLNVQWLRAH-LGIVSQEP----- 1112
Cdd:COG3845 270 GVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALagLR--PPASGSIRLDGEDITGLSPRERRRLgVAYIPEDRlgrgl 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1113 ILfDCSIAENIA--YGDNSRVVSHEEIVKAAkeanIHQFIDSLPEKYNTRVGDKGT---QLSGGQKQRIAIARALVRQPH 1187
Cdd:COG3845 348 VP-DMSVAENLIlgRYRRPPFSRGGFLDRKA----IRAFAEELIEEFDVRTPGPDTparSLSGGNQQKVILARELSRDPK 422
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 25453402 1188 ILLLDEATSALDTESEKVVQEALDKAR-EGRTCIVIAHRLSTIQN-ADLIVVIQNGQV 1243
Cdd:COG3845 423 LLIAAQPTRGLDVGAIEFIHQRLLELRdAGAAVLLISEDLDEILAlSDRIAVMYEGRI 480
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
400-554 |
9.02e-15 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 77.22 E-value: 9.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 400 QILKGLNLKVK-----SGQTvALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQ---DI-RTINVRYLREIIGVVSQEPV 470
Cdd:PRK11144 8 QQLGDLCLTVNltlpaQGIT-AIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRvlfDAeKGICLPPEKRRIGYVFQDAR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 471 LFA-TTIAENIRYGrenvtMDEIEKAvkeanaydfimklphKFDTLVGERG---------AQLSGGQKQRIAIARALVRN 540
Cdd:PRK11144 87 LFPhYKVRGNLRYG-----MAKSMVA---------------QFDKIVALLGieplldrypGSLSGGEKQRVAIGRALLTA 146
|
170
....*....|....
gi 25453402 541 PKILLLDEATSALD 554
Cdd:PRK11144 147 PELLLMDEPLASLD 160
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
703-962 |
1.09e-14 |
|
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349985 [Multi-domain] Cd Length: 293 Bit Score: 76.30 E-value: 1.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 703 FVVGVFCAIINGGLQpafsIIFSKVVGVFTknDTpeIQRQNSNL-----FSLLFLILGIISFITFFLQGFTFGKAGEILT 777
Cdd:cd18541 1 YLLGILFLILVDLLQ----LLIPRIIGRAI--DA--LTAGTLTAsqllrYALLILLLALLIGIFRFLWRYLIFGASRRIE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 778 KRLRYMVFKSMLRQDISWFDdpKNTTGALTTRLANDAAQVKGATGSRLAVITQNIANLGTGIIISLIYGWQLTLLLLAIV 857
Cdd:cd18541 73 YDLRNDLFAHLLTLSPSFYQ--KNRTGDLMARATNDLNAVRMALGPGILYLVDALFLGVLVLVMMFTISPKLTLIALLPL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 858 PIIAIAGVVEMKMLSGQALKDKKELegsGKIATEAIENF---RTVVSLTREQKFETMYAQSLQIPYRNALKKAHVFGITF 934
Cdd:cd18541 151 PLLALLVYRLGKKIHKRFRKVQEAF---SDLSDRVQESFsgiRVIKAFVQEEAEIERFDKLNEEYVEKNLRLARVDALFF 227
|
250 260
....*....|....*....|....*...
gi 25453402 935 SFTQAMMYFSYAACFRFGAYLVARELMT 962
Cdd:cd18541 228 PLIGLLIGLSFLIVLWYGGRLVIRGTIT 255
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
1007-1227 |
1.86e-14 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 78.25 E-value: 1.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1007 IPEIDSYSTEGLKPNMLEGN----VKFNGVMF-NYP--TRPNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFY 1079
Cdd:TIGR00954 423 VEEIESGREGGRNSNLVPGRgiveYQDNGIKFeNIPlvTPNGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELW 502
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1080 DPMAGTVFLDGKeikqlnvqwlrAHLGIVSQEPILFDCSIAENIAYGDNS-----RVVSHEEIVKAAKEANIHQFIDSlp 1154
Cdd:TIGR00954 503 PVYGGRLTKPAK-----------GKLFYVPQRPYMTLGTLRDQIIYPDSSedmkrRGLSDKDLEQILDNVQLTHILER-- 569
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 25453402 1155 EKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKAreGRTCIVIAHRLS 1227
Cdd:TIGR00954 570 EGGWSAVQDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCREF--GITLFSVSHRKS 640
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
740-967 |
2.33e-14 |
|
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: 75.07 E-value: 2.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 740 QRQNSNLFSLLFLILGIISFITFFLQG-----FTFgkAGEILTKRLRYMVFKSMLRQDISWFDdpKNTTGALTTRLANDA 814
Cdd:cd18590 28 GEYQHNAFTSAIGLMCLFSLGSSLSAGlrgglFMC--TLSRLNLRLRHQLFSSLVQQDIGFFE--KTKTGDLTSRLSTDT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 815 AQVKGATGSRLAVITQN-IANLGT-GIIISLiyGWQLTLLLLAIVPIIAIAgvveMKMLSGQALKDKKELEGS----GKI 888
Cdd:cd18590 104 TLMSRSVALNANVLLRSlVKTLGMlGFMLSL--SWQLTLLTLIEMPLTAIA----QKVYNTYHQKLSQAVQDSiakaGEL 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 25453402 889 ATEAIENFRTVVSLTREQKFETMYAQSLQIPYRNALKKAHVFGITFSFTQAMMYFSYAACFRFGAYLVARELMTFENVL 967
Cdd:cd18590 178 AREAVSSIRTVRSFKAEEEEACRYSEALERTYNLKDRRDTVRAVYLLVRRVLQLGVQVLMLYCGRQLIQSGHLTTGSLV 256
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
110-327 |
2.71e-14 |
|
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: 74.81 E-value: 2.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 110 YTGIGAGVLIVAYIQVSLWCLAAGRQ----------IHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINEGIG 179
Cdd:cd18545 36 LSGLLIIALLFLALNLVNWVASRLRIylmakvgqriLYDLRQDLFSHLQKLSFSFFDSRPVGKILSRVINDVNSLSDLLS 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 180 DKIGMFFQAMATFFGGFIIGFTRGWKLTLVILAISPVLGLSAGIWAKILSSFTDKELQAYAKAGAVAEEVLAAIRTVIAF 259
Cdd:cd18545 116 NGLINLIPDLLTLVGIVIIMFSLNVRLALVTLAVLPLLVLVVFLLRRRARKAWQRVRKKISNLNAYLHESISGIRVIQSF 195
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 25453402 260 GGQKKELERY---NNNLEEAKRlgikKAITANISMGAAFLLIYA-SYALAFWYGTSLVISKEYTIGqVLTVF 327
Cdd:cd18545 196 AREDENEEIFdelNRENRKANM----RAVRLNALFWPLVELISAlGTALVYWYGGKLVLGGAITVG-VLVAF 262
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1038-1243 |
2.97e-14 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 77.08 E-value: 2.97e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1038 TRPNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIKQLN-----------VQWLRAHLG 1106
Cdd:PRK10982 257 TSLRQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNaneainhgfalVTEERRSTG 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1107 IVSQEPILFDCSIAENIAYGDNSRVVSHEEIvkaakEANIHQFIDSLPEK---YNTRVGdkgtQLSGGQKQRIAIARALV 1183
Cdd:PRK10982 337 IYAYLDIGFNSLISNIRNYKNKVGLLDNSRM-----KSDTQWVIDSMRVKtpgHRTQIG----SLSGGNQQKVIIGRWLL 407
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 25453402 1184 RQPHILLLDEATSALDTESE-KVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVIQNGQV 1243
Cdd:PRK10982 408 TQPEILMLDEPTRGIDVGAKfEIYQLIAELAKKDKGIIIISSEMPELLGiTDRILVMSNGLV 469
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
386-578 |
3.17e-14 |
|
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: 72.68 E-value: 3.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 386 FKNIHFSYPSRKD-VQILKGLNLKVKSGQTVALVGNSGCGKSTtvqLLQRL------YDPIEGEVSIDGQDIRTINVRYL 458
Cdd:cd03233 6 WRNISFTTGKGRSkIPILKDFSGVVKPGEMVLVLGRPGSGCST---LLKALanrtegNVSVEGDIHYNGIPYKEFAEKYP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 459 REIIgVVSQEPVLFAT-TIAEnirygrenvTMDeiekAVKEANAYDFImklphkfdtlvgeRGaqLSGGQKQRIAIARAL 537
Cdd:cd03233 83 GEII-YVSEEDVHFPTlTVRE---------TLD----FALRCKGNEFV-------------RG--ISGGERKRVSIAEAL 133
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 25453402 538 VRNPKILLLDEATSALDTESeavvqaALD-------KAREGRTTIVIA 578
Cdd:cd03233 134 VSRASVLCWDNSTRGLDSST------ALEilkcirtMADVLKTTTFVS 175
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
390-580 |
4.05e-14 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 73.07 E-value: 4.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 390 HFSYPSRKDVQ-ILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLY--DPIEGEVSIDGQDIrtinvrylreiigvvS 466
Cdd:COG2401 33 AFGVELRVVERyVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPDNQF---------------G 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 467 QEpvlfaTTIAENIryGRENVTMDEIE--KAVKEANAYDFIMKLPHkfdtlvgergaqLSGGQKQRIAIARALVRNPKIL 544
Cdd:COG2401 98 RE-----ASLIDAI--GRKGDFKDAVEllNAVGLSDAVLWLRRFKE------------LSTGQKFRFRLALLLAERPKLL 158
|
170 180 190
....*....|....*....|....*....|....*...
gi 25453402 545 LLDEATSALDTESEAVVQAALDK-AREGRTTIVIA-HR 580
Cdd:COG2401 159 VIDEFCSHLDRQTAKRVARNLQKlARRAGITLVVAtHH 196
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
384-611 |
5.52e-14 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 76.22 E-value: 5.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 384 LEFKNIhfSYPSRKDVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRTINVRYLREI-I 462
Cdd:COG3845 258 LEVENL--SVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLgV 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 463 GVVSQEPVLFAT----TIAENI---RYGRENVT------MDEIEKAVKEanaydfIMKlphKFD-------TLVGergaQ 522
Cdd:COG3845 336 AYIPEDRLGRGLvpdmSVAENLilgRYRRPPFSrggfldRKAIRAFAEE------LIE---EFDvrtpgpdTPAR----S 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 523 LSGGQKQRIAIARALVRNPKILLLDEATSALDTES-EAVVQAALDKAREGRTTIVIAHRLSTVRN-ADVIAGFDGGVIVE 600
Cdd:COG3845 403 LSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAiEFIHQRLLELRDAGAAVLLISEDLDEILAlSDRIAVMYEGRIVG 482
|
250
....*....|.
gi 25453402 601 QGNHDELMREK 611
Cdd:COG3845 483 EVPAAEATREE 493
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
374-607 |
5.57e-14 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 73.65 E-value: 5.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 374 GHKPDNIqgnLEFKNIHFSypsRKDVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRTI 453
Cdd:PRK11831 1 EQSVANL---VDMRGVSFT---RGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAM 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 454 NVRYL---REIIGVVSQEPVLFA-TTIAENIRYG-RENVTMDE--IEKAVkeanaydfIMKLphkfdTLVGERGA----- 521
Cdd:PRK11831 75 SRSRLytvRKRMSMLFQSGALFTdMNVFDNVAYPlREHTQLPAplLHSTV--------MMKL-----EAVGLRGAaklmp 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 522 -QLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDKARE--GRTTIVIAHR----LSTVRNADVIAGFD 594
Cdd:PRK11831 142 sELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSalGVTCVVVSHDvpevLSIADHAYIVADKK 221
|
250
....*....|...
gi 25453402 595 ggvIVEQGNHDEL 607
Cdd:PRK11831 222 ---IVAHGSAQAL 231
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
398-609 |
6.43e-14 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 73.20 E-value: 6.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 398 DVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDP----IEGEVSIDGQDIRTINVRylREIIGVVSQEP---- 469
Cdd:PRK10418 15 AQPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGKPVAPCALR--GRKIATIMQNPrsaf 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 470 ---VLFATTIAENIR-YGRE--NVTMDEIEKAVKEANAyDFIMKLpHKFdtlvgergaQLSGGQKQRIAIARALVRNPKI 543
Cdd:PRK10418 93 nplHTMHTHARETCLaLGKPadDATLTAALEAVGLENA-ARVLKL-YPF---------EMSGGMLQRMMIALALLCEAPF 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 25453402 544 LLLDEATSALDteseAVVQA-ALD-----KAREGRTTIVIAHRLSTV-RNADVIAGFDGGVIVEQGNHDELMR 609
Cdd:PRK10418 162 IIADEPTTDLD----VVAQArILDllesiVQKRALGMLLVTHDMGVVaRLADDVAVMSHGRIVEQGDVETLFN 230
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1037-1254 |
9.97e-14 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 75.35 E-value: 9.97e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1037 PTRPNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPM-AGTVFLDGKEIKQLN-VQWLRAHLGIVSQEP-- 1112
Cdd:PRK13549 270 PVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPGRwEGEIFIDGKPVKIRNpQQAIAQGIAMVPEDRkr 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1113 --ILFDCSIAENIAYGDNSRVVSHEEIVKAAKEANIHQFIDSLPEKYNT---RVGdkgtQLSGGQKQRIAIARALVRQPH 1187
Cdd:PRK13549 350 dgIVPVMGVGKNITLAALDRFTGGSRIDDAAELKTILESIQRLKVKTASpelAIA----RLSGGNQQKAVLAKCLLLNPK 425
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 25453402 1188 ILLLDEATSALDT----ESEKVVQEAldkAREGRTCIVIAHRLSTIQN-ADLIVVIQNGQVK-----EHGTHQQLLA 1254
Cdd:PRK13549 426 ILILDEPTRGIDVgakyEIYKLINQL---VQQGVAIIVISSELPEVLGlSDRVLVMHEGKLKgdlinHNLTQEQVME 499
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
1030-1253 |
1.06e-13 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 72.90 E-value: 1.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1030 NGVMFNYPTRPnipVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIKQLNVQWLRAHLGIVS 1109
Cdd:PRK10575 15 RNVSFRVPGRT---LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1110 QE-PILFDCSIAENIA------------YGDNSRVVSHEEIVKAAKEANIHQFIDSlpekyntrvgdkgtqLSGGQKQRI 1176
Cdd:PRK10575 92 QQlPAAEGMTVRELVAigrypwhgalgrFGAADREKVEEAISLVGLKPLAHRLVDS---------------LSGGERQRA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1177 AIARALVRQPHILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAhRLSTIQNA----DLIVVIQNGQVKEHGTHQQL 1252
Cdd:PRK10575 157 WIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIA-VLHDINMAarycDYLVALRGGEMIAQGTPAEL 235
|
.
gi 25453402 1253 L 1253
Cdd:PRK10575 236 M 236
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
402-584 |
1.37e-13 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 72.61 E-value: 1.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 402 LKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRtinvRYLRE-IIGVVSQE-------PVLFA 473
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTR----QALQKnLVAYVPQSeevdwsfPVLVE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 474 TTIAENiRYGreNVTMDEIEKA-----VKEANAYDFIMKLPHKfdtLVGErgaqLSGGQKQRIAIARALVRNPKILLLDE 548
Cdd:PRK15056 99 DVVMMG-RYG--HMGWLRRAKKrdrqiVTAALARVDMVEFRHR---QIGE----LSGGQKKRVFLARAIAQQGQVILLDE 168
|
170 180 190
....*....|....*....|....*....|....*..
gi 25453402 549 ATSALDTESEAVVQAALDKAR-EGRTTIVIAHRLSTV 584
Cdd:PRK15056 169 PFTGVDVKTEARIISLLRELRdEGKTMLVSTHNLGSV 205
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
404-579 |
1.52e-13 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 70.99 E-value: 1.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 404 GLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRTINVRYLREII------GVvsqEPVLfatTIA 477
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDLLylghqpGI---KTEL---TAL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 478 ENIRY---GRENVTMDEIEKAVKEANAYDFiMKLPhkfdtlvgerGAQLSGGQKQRIAIARALVRNPKILLLDEATSALD 554
Cdd:PRK13538 93 ENLRFyqrLHGPGDDEALWEALAQVGLAGF-EDVP----------VRQLSAGQQRRVALARLWLTRAPLWILDEPFTAID 161
|
170 180
....*....|....*....|....*.
gi 25453402 555 TESEAVVQAALDK-AREGRTTIVIAH 579
Cdd:PRK13538 162 KQGVARLEALLAQhAEQGGMVILTTH 187
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
1042-1243 |
1.55e-13 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 71.59 E-value: 1.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1042 IPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGkeikqlNVQW-----LRAHLGIV--SQEPIL 1114
Cdd:cd03267 34 VEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAG------LVPWkrrkkFLRRIGVVfgQKTQLW 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1115 FDCSIAENIAYgdNSRVVsheEIVKAAKEANIHQFIDSLPEkynTRVGDKGT-QLSGGQKQRIAIARALVRQPHILLLDE 1193
Cdd:cd03267 108 WDLPVIDSFYL--LAAIY---DLPPARFKKRLDELSELLDL---EELLDTPVrQLSLGQRMRAEIAAALLHEPEILFLDE 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 25453402 1194 ATSALDTESEKVVQEALDKAREGR--TCIVIAHRLSTIQN-ADLIVVIQNGQV 1243
Cdd:cd03267 180 PTIGLDVVAQENIRNFLKEYNRERgtTVLLTSHYMKDIEAlARRVLVIDKGRL 232
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1041-1248 |
1.92e-13 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 71.60 E-value: 1.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1041 NIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERF--YDPMAGTVFLDGKEIKQLNVQwLRAHLGI----------- 1107
Cdd:CHL00131 19 ENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHpaYKILEGDILFKGESILDLEPE-ERAHLGIflafqypieip 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1108 -VSQEPILfdcsiaeNIAYgdNSRVVSHEEivkaaKEANIHQFIDSLPEKYNTrVGDKGTQL--------SGGQKQRIAI 1178
Cdd:CHL00131 98 gVSNADFL-------RLAY--NSKRKFQGL-----PELDPLEFLEIINEKLKL-VGMDPSFLsrnvnegfSGGEKKRNEI 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 25453402 1179 ARALVRQPHILLLDEATSALDTESEKVVQEALDKAREGRTCIV-IAH--RLSTIQNADLIVVIQNGQVKEHGT 1248
Cdd:CHL00131 163 LQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIIlITHyqRLLDYIKPDYVHVMQNGKIIKTGD 235
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
400-596 |
2.80e-13 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 71.58 E-value: 2.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 400 QILKGLNLKVKSGQTVALVGNSGCGKSTtvqLLQRLYDPIEGE------VSIDGQDIR-----TINVRYLREIIGVVSQE 468
Cdd:PRK09984 18 QALHAVDLNIHHGEMVALLGPSGSGKST---LLRHLSGLITGDksagshIELLGRTVQregrlARDIRKSRANTGYIFQQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 469 PVLF-ATTIAENIRYGRENVT------MDEIEKAVKEaNAYDFIMK--LPHkfdtLVGERGAQLSGGQKQRIAIARALVR 539
Cdd:PRK09984 95 FNLVnRLSVLENVLIGALGSTpfwrtcFSWFTREQKQ-RALQALTRvgMVH----FAHQRVSTLSGGQQQRVAIARALMQ 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 25453402 540 NPKILLLDEATSALDTESEAVVQAALD--KAREGRTTIVIAH----------RLSTVRNADVIagFDGG 596
Cdd:PRK09984 170 QAKVILADEPIASLDPESARIVMDTLRdiNQNDGITVVVTLHqvdyalryceRIVALRQGHVF--YDGS 236
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1044-1258 |
3.16e-13 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 70.69 E-value: 3.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1044 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIKQLNVQwLRAHLGI--VSQEPILFD-CSIA 1120
Cdd:PRK10895 18 VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLH-ARARRGIgyLPQEASIFRrLSVY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1121 ENIA-----YGDNSRVVSHEEIVKAAKEANIHQFIDSLpekyntrvgdkGTQLSGGQKQRIAIARALVRQPHILLLDEAT 1195
Cdd:PRK10895 97 DNLMavlqiRDDLSAEQREDRANELMEEFHIEHLRDSM-----------GQSLSGGERRRVEIARALAANPKFILLDEPF 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 25453402 1196 SALDTESEKVVQEALDKARE-GRTCIVIAHRL-STIQNADLIVVIQNGQVKEHGTHQQLLAQKGI 1258
Cdd:PRK10895 166 AGVDPISVIDIKRIIEHLRDsGLGVLITDHNVrETLAVCERAYIVSQGHLIAHGTPTEILQDEHV 230
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
411-603 |
3.30e-13 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 68.55 E-value: 3.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 411 SGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEV-SIDGQDIRTINVRYLREIIgvvsqepvlfattiaenirygrenvtm 489
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGViYIDGEDILEEVLDQLLLII--------------------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 490 deiekavkeanaydfimklphkfdtlVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALD--- 566
Cdd:smart00382 54 --------------------------VGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElrl 107
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 25453402 567 ----KAREGRTTIVIAHRLSTVRNADVIAGFDGGVIVEQGN 603
Cdd:smart00382 108 llllKSEKNLTVILTTNDEKDLGPALLRRRFDRRIVLLLIL 148
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
732-1000 |
4.02e-13 |
|
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: 71.28 E-value: 4.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 732 TKNDTPEIQRQnsnlfSLLFLILGIISFITFFLQGFTFGKAGEILTKRLRYMVFKSMLRQDISWFDdpKNTTGALTTRLA 811
Cdd:cd18548 31 ANGDLSYILRT-----GLLMLLLALLGLIAGILAGYFAAKASQGFGRDLRKDLFEKIQSFSFAEID--KFGTSSLITRLT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 812 NDAAQVKGA--TGSRLAVITqnIANLGTGIIISLIYGWQLTLLLLAIVPIIAIAGVVEMKMLSGQALKDKKELEGSGKIA 889
Cdd:cd18548 104 NDVTQVQNFvmMLLRMLVRA--PIMLIGAIIMAFRINPKLALILLVAIPILALVVFLIMKKAIPLFKKVQKKLDRLNRVV 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 890 TEAIENFRTVVSLTRE----QKFETMyAQSLqipYRNALKKAHVFGITFSFTQAMMYFSYAACFRFGAYLVARELMTFEN 965
Cdd:cd18548 182 RENLTGIRVIRAFNREdyeeERFDKA-NDDL---TDTSLKAGRLMALLNPLMMLIMNLAIVAILWFGGHLINAGSLQVGD 257
|
250 260 270
....*....|....*....|....*....|....*....
gi 25453402 966 vLLVFSA----IVFGAMAVGQVSSFAPdyaKAKVSASHI 1000
Cdd:cd18548 258 -LVAFINylmqILMSLMMLSMVFVMLP---RASASAKRI 292
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
384-588 |
4.97e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 69.21 E-value: 4.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 384 LEFKNIHFSYpsrKDVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRTINVRYLREIIG 463
Cdd:PRK13540 2 LDVIELDFDY---HDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 464 VVSQEPVLFATTIAEN----IRYGRENVTMDEIEKavkeanaydfIMKLPHKFDTLVGergaQLSGGQKQRIAIARALVR 539
Cdd:PRK13540 79 VGHRSGINPYLTLRENclydIHFSPGAVGITELCR----------LFSLEHLIDYPCG----LLSSGQKRQVALLRLWMS 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 25453402 540 NPKILLLDEATSALDTESEAVVQAALDKAR-EGRTTIVIAHRLSTVRNAD 588
Cdd:PRK13540 145 KAKLWLLDEPLVALDELSLLTIITKIQEHRaKGGAVLLTSHQDLPLNKAD 194
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
136-333 |
6.95e-13 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349994 [Multi-domain] Cd Length: 294 Bit Score: 70.59 E-value: 6.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 136 IHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFFQAMATFFGGFIIGFTRGWKLTLVILAISP 215
Cdd:cd18550 71 MYDLRVQLYAHLQRMSLAFFTRTRTGEIQSRLNNDVGGAQSVVTGTLTSVVSNVVTLVATLVAMLALDWRLALLSLVLLP 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 216 VLGLSAGIWAKILSSFTDKELQAYAKAGAVAEEVLAA--IRTVIAFGGQKKELERYNNNLEEAKRLGIKKAITANISMGA 293
Cdd:cd18550 151 LFVLPTRRVGRRRRKLTREQQEKLAELNSIMQETLSVsgALLVKLFGREDDEAARFARRSRELRDLGVRQALAGRWFFAA 230
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 25453402 294 AFLLIYASYALAFWYGTSLVISKEYTIGQVltVFFSVLIG 333
Cdd:cd18550 231 LGLFTAIGPALVYWVGGLLVIGGGLTIGTL--VAFTALLG 268
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
412-602 |
8.54e-13 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 69.95 E-value: 8.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 412 GQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRTINV---------RYLREIIGVVSQEP-------VLFATT 475
Cdd:PRK11701 32 GEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLyalseaerrRLLRTEWGFVHQHPrdglrmqVSAGGN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 476 IAENI------RYGRENVT----MDEIEKAVkeanayDFIMKLPHKFdtlvgergaqlSGGQKQRIAIARALVRNPKILL 545
Cdd:PRK11701 112 IGERLmavgarHYGDIRATagdwLERVEIDA------ARIDDLPTTF-----------SGGMQQRLQIARNLVTHPRLVF 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 25453402 546 LDEATSALDTEseavVQAA-LDKARE-----GRTTIVIAHRLSTVRN-ADVIAGFDGGVIVEQG 602
Cdd:PRK11701 175 MDEPTGGLDVS----VQARlLDLLRGlvrelGLAVVIVTHDLAVARLlAHRLLVMKQGRVVESG 234
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
384-600 |
9.98e-13 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 72.31 E-value: 9.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 384 LEFKNIHFSYPSRKDVqiLKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRTINVRYLREIIG 463
Cdd:PRK10522 323 LELRNVTFAYQDNGFS--VGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFS 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 464 VVSQEPVLFATTIaeniryGRENvtmdeieKAVKEANAYDFI--MKLPHKFdTLVGERGA--QLSGGQKQRIAIARALVR 539
Cdd:PRK10522 401 AVFTDFHLFDQLL------GPEG-------KPANPALVEKWLerLKMAHKL-ELEDGRISnlKLSKGQKKRLALLLALAE 466
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 25453402 540 NPKILLLDEATSALDTESEAVV-QAALDKARE-GRTTIVIAHRLSTVRNADVIAGFDGGVIVE 600
Cdd:PRK10522 467 ERDILLLDEWAADQDPHFRREFyQVLLPLLQEmGKTIFAISHDDHYFIHADRLLEMRNGQLSE 529
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
408-610 |
1.51e-12 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 70.16 E-value: 1.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 408 KVKSGQTVALVGNSGCGKSTTVQLLQRLYDpIEGEVS-----IDGQDIRTINVRYLREIIG----VVSQEPVlfaTTIae 478
Cdd:PRK11022 29 SVKQGEVVGIVGESGSGKSVSSLAIMGLID-YPGRVMaekleFNGQDLQRISEKERRNLVGaevaMIFQDPM---TSL-- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 479 NIRYGRENVTMDEIE------KAVKEANAYDFImklphkfdTLVG-----ER----GAQLSGGQKQRIAIARALVRNPKI 543
Cdd:PRK11022 103 NPCYTVGFQIMEAIKvhqggnKKTRRQRAIDLL--------NQVGipdpaSRldvyPHQLSGGMSQRVMIAMAIACRPKL 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 544 LLLDEATSALDTESEA-VVQAALD-KAREGRTTIVIAHRLSTV-RNADVIAGFDGGVIVEQGNHDELMRE 610
Cdd:PRK11022 175 LIADEPTTALDVTIQAqIIELLLElQQKENMALVLITHDLALVaEAAHKIIVMYAGQVVETGKAHDIFRA 244
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
1043-1225 |
1.90e-12 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 68.06 E-value: 1.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1043 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFY--DPMAGTVFLDGKEIKQlnvqwlrahlgivsqepilfDCSIA 1120
Cdd:COG2401 44 YVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPDNQFGR--------------------EASLI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1121 ENIAYGDNsrvvsheeiVKAAKEAnIHQFIDSLPEKYNTRVgdkgTQLSGGQKQRIAIARALVRQPHILLLDEATSALDT 1200
Cdd:COG2401 104 DAIGRKGD---------FKDAVEL-LNAVGLSDAVLWLRRF----KELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDR 169
|
170 180
....*....|....*....|....*..
gi 25453402 1201 ESEKVVQEALDKA--REGRTCIVIAHR 1225
Cdd:COG2401 170 QTAKRVARNLQKLarRAGITLVVATHH 196
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
387-584 |
2.03e-12 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 68.60 E-value: 2.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 387 KNIHFSYPSRKdvqILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQdirtinvryLReiIGVVS 466
Cdd:PRK09544 8 ENVSVSFGQRR---VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGK---------LR--IGYVP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 467 QEPVLFAT---TIAENIRYgRENVTMDEIEKAVKEANAYDFIMKLPHKfdtlvgergaqLSGGQKQRIAIARALVRNPKI 543
Cdd:PRK09544 74 QKLYLDTTlplTVNRFLRL-RPGTKKEDILPALKRVQAGHLIDAPMQK-----------LSGGETQRVLLARALLNRPQL 141
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 25453402 544 LLLDEATSALDTESEAVVQAALDKARE--GRTTIVIAHRLSTV 584
Cdd:PRK09544 142 LVLDEPTQGVDVNGQVALYDLIDQLRRelDCAVLMVSHDLHLV 184
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
392-579 |
2.61e-12 |
|
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: 71.12 E-value: 2.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 392 SYPSRKdvQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDgqdiRTINVRYLreiigvvSQEPVL 471
Cdd:TIGR03719 13 VVPPKK--EILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQ----PGIKVGYL-------PQEPQL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 472 FAT-TIAENI-------------------RYGRENVTMD-------EIEKAVKEANAYDFIMKLPHKFDTLVGERG---- 520
Cdd:TIGR03719 80 DPTkTVRENVeegvaeikdaldrfneisaKYAEPDADFDklaaeqaELQEIIDAADAWDLDSQLEIAMDALRCPPWdadv 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 25453402 521 AQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALdKAREGrTTIVIAH 579
Cdd:TIGR03719 160 TKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHL-QEYPG-TVVAVTH 216
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1037-1254 |
3.63e-12 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 70.24 E-value: 3.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1037 PTRPNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYD-PMAGTVFLDGKEIKQLN-VQWLRAHLGIVSQEP-- 1112
Cdd:TIGR02633 268 VINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPgKFEGNVFINGKPVDIRNpAQAIRAGIAMVPEDRkr 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1113 --ILFDCSIAENIAYGDNSRVVSHEEIVKAAKEANIHQFIDSLpeKYNTRVGDKG-TQLSGGQKQRIAIARALVRQPHIL 1189
Cdd:TIGR02633 348 hgIVPILGVGKNITLSVLKSFCFKMRIDAAAELQIIGSAIQRL--KVKTASPFLPiGRLSGGNQQKAVLAKMLLTNPRVL 425
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 25453402 1190 LLDEATSALDTESEKVVQEALDK-AREGRTCIVIAHRLSTIQN-ADLIVVIQNGQVK----EHG-THQQLLA 1254
Cdd:TIGR02633 426 ILDEPTRGVDVGAKYEIYKLINQlAQEGVAIIVVSSELAEVLGlSDRVLVIGEGKLKgdfvNHAlTQEQVLA 497
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
394-576 |
3.82e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 68.96 E-value: 3.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 394 PSRKDVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRTINVRYLREIiGVV----SQ-- 467
Cdd:COG4586 30 REYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFKRRKEFARRI-GVVfgqrSQlw 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 468 --EPVLfattiaENIRYGRE--NVTMDEIEKAVKEanaYDFIMKLPHKFDTLVgeRgaQLSGGQKQRIAIARALVRNPKI 543
Cdd:COG4586 109 wdLPAI------DSFRLLKAiyRIPDAEYKKRLDE---LVELLDLGELLDTPV--R--QLSLGQRMRCELAAALLHRPKI 175
|
170 180 190
....*....|....*....|....*....|....
gi 25453402 544 LLLDEATSALDTESEAVVQAALDKA-REGRTTIV 576
Cdd:COG4586 176 LFLDEPTIGLDVVSKEAIREFLKEYnRERGTTIL 209
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
1048-1247 |
4.20e-12 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 69.13 E-value: 4.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1048 LSLEVK-----KGQTlALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEI----KQLNVQWLRAHLGIVSQEPILF-DC 1117
Cdd:PRK11144 13 LCLTVNltlpaQGIT-AIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLfdaeKGICLPPEKRRIGYVFQDARLFpHY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1118 SIAENIAYG-DNSRVVSHEEIVKAAKeanihqfIDSLPEKYNTRvgdkgtqLSGGQKQRIAIARALVRQPHILLLDEATS 1196
Cdd:PRK11144 92 KVRGNLRYGmAKSMVAQFDKIVALLG-------IEPLLDRYPGS-------LSGGEKQRVAIGRALLTAPELLLMDEPLA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 25453402 1197 ALDTESEKVVQEALDK-AREGRTCIV-IAHRLSTI-QNADLIVVIQNGQVKEHG 1247
Cdd:PRK11144 158 SLDLPRKRELLPYLERlAREINIPILyVSHSLDEIlRLADRVVVLEQGKVKAFG 211
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
384-603 |
5.77e-12 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 67.36 E-value: 5.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 384 LEFKNIHFSYpsrKDVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLL--QRLYDPIEGEVSIDGQDIRTIN------- 454
Cdd:CHL00131 8 LEIKNLHASV---NENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIagHPAYKILEGDILFKGESILDLEpeerahl 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 455 -----VRYLREIIGVVSQEpvlFATTIAENIRYGRENVTMDEIEkavkeanAYDFIM-KLPhkfdtLVGERGAQL----- 523
Cdd:CHL00131 85 giflaFQYPIEIPGVSNAD---FLRLAYNSKRKFQGLPELDPLE-------FLEIINeKLK-----LVGMDPSFLsrnvn 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 524 ---SGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDK-AREGRTTIVIAH--RLSTVRNADVIAGFDGGV 597
Cdd:CHL00131 150 egfSGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKlMTSENSIILITHyqRLLDYIKPDYVHVMQNGK 229
|
....*.
gi 25453402 598 IVEQGN 603
Cdd:CHL00131 230 IIKTGD 235
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
115-337 |
7.35e-12 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350009 [Multi-domain] Cd Length: 313 Bit Score: 67.98 E-value: 7.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 115 AGVLIVA--------YIQVSLWCLAAGRQIHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFF 186
Cdd:cd18565 57 GGLTVAAflleslfqYLSGVLWRRFAQRVQHDLRTDTYDHVQRLDMAFFEDRQTGDLMSVLNNDVNQLERFLDDGANSII 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 187 QAMATFFGGFIIGFTRGWKLTLVILAISPVLGLSAGIWAKILSSFTDKELQAYAKAGAVAEEVLAAIRTVIAFGGQKKEL 266
Cdd:cd18565 137 RVVVTVLGIGAILFYLNWQLALVALLPVPLIIAGTYWFQRRIEPRYRAVREAVGDLNARLENNLSGIAVIKAFTAEDFER 216
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 25453402 267 ERynnnLEEAKRLGIKKAITAnISMGAAF-----LLIYASYALAFWYGTSLVISKEYTIGQVLTVffsvliGAFSV 337
Cdd:cd18565 217 ER----VADASEEYRDANWRA-IRLRAAFfpvirLVAGAGFVATFVVGGYWVLDGPPLFTGTLTV------GTLVT 281
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
1043-1247 |
9.36e-12 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 66.65 E-value: 9.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1043 PVLQGLSLEVKKGQTLALVGSSGCGKS----TVVQLLERFYDPMAGTVFLDGKEIKQlnvQWLRA-HLGIVSQEPilfdc 1117
Cdd:PRK10418 17 PLVHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDGKPVAP---CALRGrKIATIMQNP----- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1118 siaeNIAYGDNSRVVSH--EEIVKAAKEANIHQFIDSLPEkyntrVG--DKGT-------QLSGGQKQRIAIARALVRQP 1186
Cdd:PRK10418 89 ----RSAFNPLHTMHTHarETCLALGKPADDATLTAALEA-----VGleNAARvlklypfEMSGGMLQRMMIALALLCEA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 25453402 1187 HILLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLSTIQN-ADLIVVIQNGQVKEHG 1247
Cdd:PRK10418 160 PFIIADEPTTDLDVVAQARILDLLESivQKRALGMLLVTHDMGVVARlADDVAVMSHGRIVEQG 223
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
139-335 |
1.21e-11 |
|
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: 67.09 E-value: 1.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 139 IRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINE----GIGDkigmFFQAMATFFGGFIIGFTRGWKLTLVILAIS 214
Cdd:cd18549 77 MRRDLFEHLQKLSFSFFDNNKTGQLMSRITNDLFDISElahhGPED----LFISIITIIGSFIILLTINVPLTLIVFALL 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 215 PVLGlsagiwakILSSFTDKEL-----QAYAKAG---AVAEEVLAAIRTVIAFGGQKKELERY---NNNLEEAKRLGIKk 283
Cdd:cd18549 153 PLMI--------IFTIYFNKKMkkafrRVREKIGeinAQLEDSLSGIRVVKAFANEEYEIEKFdegNDRFLESKKKAYK- 223
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 25453402 284 aITANISMGAAFL--LIYASyALAFwyGTSLVISKEYTIGQVLTvfFSVLIGAF 335
Cdd:cd18549 224 -AMAYFFSGMNFFtnLLNLV-VLVA--GGYFIIKGEITLGDLVA--FLLYVNVF 271
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1044-1226 |
1.35e-11 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 66.29 E-value: 1.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1044 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKeikqlnvqwLRahLGIVSQEpILFDCSIAENI 1123
Cdd:PRK09544 19 VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGK---------LR--IGYVPQK-LYLDTTLPLTV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1124 aygdnSRV------VSHEEIVKAAKEANIHQFIDSLPEKyntrvgdkgtqLSGGQKQRIAIARALVRQPHILLLDEATSA 1197
Cdd:PRK09544 87 -----NRFlrlrpgTKKEDILPALKRVQAGHLIDAPMQK-----------LSGGETQRVLLARALLNRPQLLVLDEPTQG 150
|
170 180 190
....*....|....*....|....*....|.
gi 25453402 1198 LDTESEKVVQEALDKAREGRTCIV--IAHRL 1226
Cdd:PRK09544 151 VDVNGQVALYDLIDQLRRELDCAVlmVSHDL 181
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
409-582 |
1.50e-11 |
|
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: 66.24 E-value: 1.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 409 VKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSiDGQDIRTInVRYLReiiGVVSQEpvLFATTIAENIRYGRENVT 488
Cdd:cd03236 23 PREGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFD-DPPDWDEI-LDEFR---GSELQN--YFTKLLEGDVKVIVKPQY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 489 MDEIEKAVKeANAYDFIMKLP--HKFDTLVG--------ERG-AQLSGGQKQRIAIARALVRNPKILLLDEATSALDTES 557
Cdd:cd03236 96 VDLIPKAVK-GKVGELLKKKDerGKLDELVDqlelrhvlDRNiDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQ 174
|
170 180
....*....|....*....|....*.
gi 25453402 558 EAVVQAALDK-AREGRTTIVIAHRLS 582
Cdd:cd03236 175 RLNAARLIRElAEDDNYVLVVEHDLA 200
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
1045-1241 |
1.61e-11 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 64.57 E-value: 1.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1045 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLL-ERFYD-PMAGTVFLDGKEIKQLnvqwLRAHLGIVSQEPILFDCS-IAE 1121
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESGAGKTTLLDVLaGRKTAgVITGEILINGRPLDKN----FQRSTGYVEQQDVHSPNLtVRE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1122 NIAYGDNSRvvsheeivkaakeanihqfidslpekyntrvgdkgtQLSGGQKQRIAIARALVRQPHILLLDEATSALDTE 1201
Cdd:cd03232 99 ALRFSALLR------------------------------------GLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQ 142
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 25453402 1202 SEKVVQEALDK-AREGRTCIVIAHRLS--TIQNADLIVVIQNG 1241
Cdd:cd03232 143 AAYNIVRFLKKlADSGQAILCTIHQPSasIFEKFDRLLLLKRG 185
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1046-1224 |
1.80e-11 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 64.83 E-value: 1.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1046 QGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIKQL------NVQWLRAHLGIVS----QEPILF 1115
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQrdeyhqDLLYLGHQPGIKTeltaLENLRF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1116 DCSIAeniaygdnsRVVSHEEIVKAAKEANIHQFIDsLPEKyntrvgdkgtQLSGGQKQRIAIARALVRQPHILLLDEAT 1195
Cdd:PRK13538 98 YQRLH---------GPGDDEALWEALAQVGLAGFED-VPVR----------QLSAGQQRRVALARLWLTRAPLWILDEPF 157
|
170 180 190
....*....|....*....|....*....|
gi 25453402 1196 SALDTESEKVVQEALDK-AREGRTCIVIAH 1224
Cdd:PRK13538 158 TAIDKQGVARLEALLAQhAEQGGMVILTTH 187
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1048-1255 |
1.92e-11 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 67.06 E-value: 1.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1048 LSLEVKKGQTLALVGSSGCGKS-TVVQLLERFYDP--MAGTVFLDGKEI-----KQLNVqwLRA-HLGIVSQEPIlfdCS 1118
Cdd:PRK09473 35 LNFSLRAGETLGIVGESGSGKSqTAFALMGLLAANgrIGGSATFNGREIlnlpeKELNK--LRAeQISMIFQDPM---TS 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1119 IAENIAYGDNSRVV--SHEEIVKA-AKEANIhQFIDS--LPEKyNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDE 1193
Cdd:PRK09473 110 LNPYMRVGEQLMEVlmLHKGMSKAeAFEESV-RMLDAvkMPEA-RKRMKMYPHEFSGGMRQRVMIAMALLCRPKLLIADE 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 25453402 1194 ATSALDTESEKVVQEALDK-AREGRTCIV-IAHRLSTIQN-ADLIVVIQNGQVKEHGTHQQLLAQ 1255
Cdd:PRK09473 188 PTTALDVTVQAQIMTLLNElKREFNTAIImITHDLGVVAGiCDKVLVMYAGRTMEYGNARDVFYQ 252
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
384-577 |
2.61e-11 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 67.74 E-value: 2.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 384 LEFKNIhfsypSRKDVqiLKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRTINVRY-LREII 462
Cdd:COG1129 257 LEVEGL-----SVGGV--VRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDaIRAGI 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 463 GVVS----QEPVLFATTIAENI------RYGReNVTMDEiEKAVKEANAY--DFIMKLPHKfDTLVGergaQLSGGQKQR 530
Cdd:COG1129 330 AYVPedrkGEGLVLDLSIRENItlasldRLSR-GGLLDR-RRERALAEEYikRLRIKTPSP-EQPVG----NLSGGNQQK 402
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 25453402 531 IAIARALVRNPKILLLDEATSALDTESEAVVQAALDK-AREGRTTIVI 577
Cdd:COG1129 403 VVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRElAAEGKAVIVI 450
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
387-558 |
2.76e-11 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 67.45 E-value: 2.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 387 KNIHFSYPSrkdVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRTINVRY-LREIIGVV 465
Cdd:PRK10982 2 SNISKSFPG---VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEaLENGISMV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 466 SQE-PVLFATTIAENI---RYGRENVTMDEiEKAVKEANAYdfimklphkFDTL-----VGERGAQLSGGQKQRIAIARA 536
Cdd:PRK10982 79 HQElNLVLQRSVMDNMwlgRYPTKGMFVDQ-DKMYRDTKAI---------FDELdididPRAKVATLSVSQMQMIEIAKA 148
|
170 180
....*....|....*....|..
gi 25453402 537 LVRNPKILLLDEATSALdTESE 558
Cdd:PRK10982 149 FSYNAKIVIMDEPTSSL-TEKE 169
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
1054-1235 |
4.30e-11 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 62.39 E-value: 4.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1054 KGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVfldgkeikqlnvqwlrahlgivsqepILFDCSIAENIAYGDNSrvvs 1133
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGV--------------------------IYIDGEDILEEVLDQLL---- 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1134 heeivkaakeanihqfidslpekyNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALD-- 1211
Cdd:smart00382 51 ------------------------LIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElr 106
|
170 180
....*....|....*....|....*....
gi 25453402 1212 -----KAREGRTCIVIAHRLSTIQNADLI 1235
Cdd:smart00382 107 lllllKSEKNLTVILTTNDEKDLGPALLR 135
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
1048-1253 |
4.47e-11 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 64.57 E-value: 4.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1048 LSLEVKKGQTLALVGSSGCGKSTvvqLLERfydpMAGT------VFLDGKEIKQLNVQWL---RAHLgiVSQEPILFDCS 1118
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKST---LLAR----MAGLlpgsgsIQFAGQPLEAWSAAELarhRAYL--SQQQTPPFAMP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1119 IAEniaYGDNSRvvsHEEIVKAAKEANIHQFIDSLpekyntRVGDK----GTQLSGGQKQRIAIArALVRQ------PH- 1187
Cdd:PRK03695 86 VFQ---YLTLHQ---PDKTRTEAVASALNEVAEAL------GLDDKlgrsVNQLSGGEWQRVRLA-AVVLQvwpdinPAg 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 25453402 1188 -ILLLDEATSALDtesekVVQE-ALDK-----AREGRTCIVIAHRLS-TIQNADLIVVIQNGQVKEHGTHQQLL 1253
Cdd:PRK03695 153 qLLLLDEPMNSLD-----VAQQaALDRllselCQQGIAVVMSSHDLNhTLRHADRVWLLKQGKLLASGRRDEVL 221
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
749-1000 |
6.01e-11 |
|
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: 64.80 E-value: 6.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 749 LLFLILGIISFITFFLQGFTFGKAGEILTKRLRYMVFKSMLRQDISWFDdpKNTTGALTTRLANDAAQVKGATGSRLAVI 828
Cdd:cd18589 40 TVMSLLTIASAVSEFVCDLIYNITMSRIHSRLQGLVFAAVLRQEIAFFD--SNQTGDIVSRVTTDTEDMSESLSENLSLL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 829 TQNIANLGTGIIISLIYGWQLTLLLLAIVPIIAIAGVVEMKMLSGQALKDKKELEGSGKIATEAIENFRTVVSLTREQKF 908
Cdd:cd18589 118 MWYLARGLFLFIFMLWLSPKLALLTALGLPLLLLVPKFVGKFQQSLAVQVQKSLARANQVAVETFSAMKTVRSFANEEGE 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 909 ETMYAQSLQIPYRNALKKAHVFGITfSFTQAMMYFSYAAC-FRFGAYLVAR------ELMTFENVLLVFSAivfgamAVG 981
Cdd:cd18589 198 AQRYRQRLQKTYRLNKKEAAAYAVS-MWTSSFSGLALKVGiLYYGGQLVTAgtvssgDLVTFVLYELQFTS------AVE 270
|
250
....*....|....*....
gi 25453402 982 QVSSFAPDYAKAKVSASHI 1000
Cdd:cd18589 271 VLLSYYPSVMKAVGSSEKI 289
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
399-604 |
7.35e-11 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 67.18 E-value: 7.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 399 VQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLL--QRLYDPIEGEVSIDG-----------------QDIRT--INVR- 456
Cdd:PLN03140 893 LQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLagRKTGGYIEGDIRISGfpkkqetfarisgyceqNDIHSpqVTVRe 972
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 457 ------YLREIIGVVSQEPVLFattiaenirygrenvtMDEIEKAVKEANAYDFIMKLPhkfdtlvGERGaqLSGGQKQR 530
Cdd:PLN03140 973 sliysaFLRLPKEVSKEEKMMF----------------VDEVMELVELDNLKDAIVGLP-------GVTG--LSTEQRKR 1027
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 25453402 531 IAIARALVRNPKILLLDEATSALDTESEAVVQAAL-DKAREGRTTIVIAHRLSTvrnaDVIAGFDGGVIVEQGNH 604
Cdd:PLN03140 1028 LTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVrNTVDTGRTVVCTIHQPSI----DIFEAFDELLLMKRGGQ 1098
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
746-1000 |
9.36e-11 |
|
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349990 [Multi-domain] Cd Length: 292 Bit Score: 64.43 E-value: 9.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 746 LFSLLFLILGIISFITFFLQGFTFGKAGEILTKRLRYMVFKSMLRQDISWFDdpKNTTGALTTRLANDAAQVKGATGSRL 825
Cdd:cd18546 40 LAAAAYLAVVLAGWVAQRAQTRLTGRTGERLLYDLRLRVFAHLQRLSLDFHE--RETSGRIMTRMTSDIDALSELLQTGL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 826 AVITQNIANLGTGIIISLIYGWQLTLLLLAIVPIIAIAGVVEMKmLSGQALKDKKElegsgKIAT------EAIENFRTV 899
Cdd:cd18546 118 VQLVVSLLTLVGIAVVLLVLDPRLALVALAALPPLALATRWFRR-RSSRAYRRARE-----RIAAvnadlqETLAGIRVV 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 900 VSLTREQKFETMYAQsLQIPYRNALKKAH-VFGITFSFTQAMMYFSYAACFRFGAYLVARELMTFeNVLLVF---SAIVF 975
Cdd:cd18546 192 QAFRRERRNAERFAE-LSDDYRDARLRAQrLVAIYFPGVELLGNLATAAVLLVGAWRVAAGTLTV-GVLVAFllyLRRFF 269
|
250 260
....*....|....*....|....*
gi 25453402 976 GAMavGQVSSFAPDYAKAKVSASHI 1000
Cdd:cd18546 270 API--QQLSQVFDSYQQARAALEKI 292
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1021-1229 |
1.10e-10 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 63.75 E-value: 1.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1021 NMLEGNVKFNGVMFNYptRPNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIKQLNVQW 1100
Cdd:PRK15056 1 MMQQAGIVVNDVTVTW--RNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1101 LRAHLGiVSQE-----PILFDcSIAENIAYGDNS---RVVSHE-EIVKAAKEAnihqfIDSLPEKYNtRVGdkgtQLSGG 1171
Cdd:PRK15056 79 LVAYVP-QSEEvdwsfPVLVE-DVVMMGRYGHMGwlrRAKKRDrQIVTAALAR-----VDMVEFRHR-QIG----ELSGG 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 25453402 1172 QKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKAR-EGRTCIVIAHRLSTI 1229
Cdd:PRK15056 147 QKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRdEGKTMLVSTHNLGSV 205
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
1044-1266 |
1.11e-10 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 66.06 E-value: 1.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1044 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLE-RFY-DPMAGTVFLDGKEIKQlnvQWLRaHLGIVSQEPILF-DCSIA 1120
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAgRIQgNNFTGTILANNRKPTK---QILK-RTGFVTQDDILYpHLTVR 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1121 ENIAYGDNSRV---VSHEEIVKAAkEANIHQFidSLPEKYNTRVGDKGTQ-LSGGQKQRIAIARALVRQPHILLLDEATS 1196
Cdd:PLN03211 159 ETLVFCSLLRLpksLTKQEKILVA-ESVISEL--GLTKCENTIIGNSFIRgISGGERKRVSIAHEMLINPSLLILDEPTS 235
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 25453402 1197 ALD-TESEKVVQEALDKAREGRTCIVIAHRLST--IQNADLIVVIQNGQVKEHGTHQQLLAqkgiYFSMVSVQ 1266
Cdd:PLN03211 236 GLDaTAAYRLVLTLGSLAQKGKTIVTSMHQPSSrvYQMFDSVLVLSEGRCLFFGKGSDAMA----YFESVGFS 304
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1040-1242 |
1.40e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 65.14 E-value: 1.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1040 PNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIK-QLNVQWLRAHLGIVSQE-PILFDC 1117
Cdd:PRK10982 9 PGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfKSSKEALENGISMVHQElNLVLQR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1118 SIAENIAYGDNSR---VVSHEEIVKAAKeanihQFIDSLPEKYNTRvgDKGTQLSGGQKQRIAIARALVRQPHILLLDEA 1194
Cdd:PRK10982 89 SVMDNMWLGRYPTkgmFVDQDKMYRDTK-----AIFDELDIDIDPR--AKVATLSVSQMQMIEIAKAFSYNAKIVIMDEP 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 25453402 1195 TSALdteSEKVVQ---EALDKAREgRTC--IVIAHRLSTI-QNADLIVVIQNGQ 1242
Cdd:PRK10982 162 TSSL---TEKEVNhlfTIIRKLKE-RGCgiVYISHKMEEIfQLCDEITILRDGQ 211
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
115-354 |
1.46e-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: 63.71 E-value: 1.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 115 AGVLIVAYI-QVSLWCL-------AAGRQIHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFF 186
Cdd:cd18778 43 ALLLLGAYLlRALLNFLriylnhvAEQKVVADLRSDLYDKLQRLSLRYFDDRQTGDLMSRVINDVANVERLIADGIPQGI 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 187 QAMATFFGGFIIGFTRGWKLTLVILAISPVLGLSAGIWAKILSSFTDKELQAYAKAGAVAEEVLAAIRTVIAFGGQKKEL 266
Cdd:cd18778 123 TNVLTLVGVAIILFSINPKLALLTLIPIPFLALGAWLYSKKVRPRYRKVREALGELNALLQDNLSGIREIQAFGREEEEA 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 267 ERYNnnlEEAKRLGiKKAITANISMGAAFLLIY----ASYALAFWYGTSLVISKEYTIGQVltVFFSVLIGAF--SVGQA 340
Cdd:cd18778 203 KRFE---ALSRRYR-KAQLRAMKLWAIFHPLMEfltsLGTVLVLGFGGRLVLAGELTIGDL--VAFLLYLGLFyePITSL 276
|
250
....*....|....
gi 25453402 341 SPNIEAFANARGAA 354
Cdd:cd18778 277 HGLNEMLQRALAGA 290
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
386-595 |
1.49e-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: 65.54 E-value: 1.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 386 FKNIHFSYPSrKDVQILKgLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDgqdiRTINVRYlreiigvV 465
Cdd:TIGR00954 454 FENIPLVTPN-GDVLIES-LSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKP----AKGKLFY-------V 520
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 466 SQEPVLFATTIAENIRYgrENVTMDEIEKAVKEAN--AYDFIMKLPHKFDTLVGERGAQ-----LSGGQKQRIAIARALV 538
Cdd:TIGR00954 521 PQRPYMTLGTLRDQIIY--PDSSEDMKRRGLSDKDleQILDNVQLTHILEREGGWSAVQdwmdvLSGGEKQRIAMARLFY 598
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 25453402 539 RNPKILLLDEATSALDTESEavvQAALDKARE-GRTTIVIAHRLSTVRNADVIAGFDG 595
Cdd:TIGR00954 599 HKPQFAILDECTSAVSVDVE---GYMYRLCREfGITLFSVSHRKSLWKYHEYLLYMDG 653
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
391-579 |
1.73e-10 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 62.81 E-value: 1.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 391 FSYPSRKdvQILKGLNLKVKSG-----QTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDI----------RTINV 455
Cdd:cd03237 1 YTYPTMK--KTLGEFTLEVEGGsisesEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVsykpqyikadYEGTV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 456 RY-LREIIGVVSQEPvLFATTIAEnirygrenvtmdeiekavkeanaydfimklPHKFDTLVGERGAQLSGGQKQRIAIA 534
Cdd:cd03237 79 RDlLSSITKDFYTHP-YFKTEIAK------------------------------PLQIEQILDREVPELSGGELQRVAIA 127
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 25453402 535 RALVRNPKILLLDEATSALDTESEAVVQAALDKAREG--RTTIVIAH 579
Cdd:cd03237 128 ACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFAENneKTAFVVEH 174
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
404-602 |
1.82e-10 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 62.70 E-value: 1.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 404 GLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDI--------------RTI-NVRYLREIIGV---- 464
Cdd:PRK11300 23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIeglpghqiarmgvvRTFqHVRLFREMTVIenll 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 465 VSQE--------PVLFATTiaeniRYGREnvtmdEIEKAVKEANAYDFIMKLPhkfdtLVGERGAQLSGGQKQRIAIARA 536
Cdd:PRK11300 103 VAQHqqlktglfSGLLKTP-----AFRRA-----ESEALDRAATWLERVGLLE-----HANRQAGNLAYGQQRRLEIARC 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 25453402 537 LVRNPKILLLDEATSALDTESEAVVQAALDKARE--GRTTIVIAHRLSTVRN-ADVIagfdggVIVEQG 602
Cdd:PRK11300 168 MVTQPEILMLDEPAAGLNPKETKELDELIAELRNehNVTVLLIEHDMKLVMGiSDRI------YVVNQG 230
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
402-603 |
2.31e-10 |
|
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: 62.63 E-value: 2.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 402 LKGLNLKVKSGQTVALVGNSGCGKSTTVQ-----LLQRL----------YDPIEGEVSIDgqdiRTINV------RYLRE 460
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLINdtlypALARRlhlkkeqpgnHDRIEGLEHID----KVIVIdqspigRTPRS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 461 I----IGVVSQEPVLFATtIAENIRYGRE-------NVTMDEI-EKAVKEAnaYDF---IMKLPHKFDTLV--------- 516
Cdd:cd03271 87 NpatyTGVFDEIRELFCE-VCKGKRYNREtlevrykGKSIADVlDMTVEEA--LEFfenIPKIARKLQTLCdvglgyikl 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 517 GERGAQLSGGQKQRIAIARALVR---NPKILLLDEATSALDTESEAVVQAALDKARE-GRTTIVIAHRLSTVRNADVI-- 590
Cdd:cd03271 164 GQPATTLSGGEAQRIKLAKELSKrstGKTLYILDEPTTGLHFHDVKKLLEVLQRLVDkGNTVVVIEHNLDVIKCADWIid 243
|
250
....*....|....*..
gi 25453402 591 ----AGFDGGVIVEQGN 603
Cdd:cd03271 244 lgpeGGDGGGQVVASGT 260
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1048-1248 |
2.51e-10 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 63.61 E-value: 2.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1048 LSLEVKKGQTLALVGSSGCGKS----TVVQLLERFYDPMAGTVFLDGKEIKQLNVQWLR----AHLGIVSQEPI--LFDC 1117
Cdd:PRK11022 26 ISYSVKQGEVVGIVGESGSGKSvsslAIMGLIDYPGRVMAEKLEFNGQDLQRISEKERRnlvgAEVAMIFQDPMtsLNPC 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1118 -----SIAENI-AYGDNSRVVSHEEIVKAAKEANIHQfidslPEkynTRVGDKGTQLSGGQKQRIAIARALVRQPHILLL 1191
Cdd:PRK11022 106 ytvgfQIMEAIkVHQGGNKKTRRQRAIDLLNQVGIPD-----PA---SRLDVYPHQLSGGMSQRVMIAMAIACRPKLLIA 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1192 DEATSALD-TESEKVVQEALD-KAREGRTCIVIAHRLSTI-QNADLIVVIQNGQVKEHGT 1248
Cdd:PRK11022 178 DEPTTALDvTIQAQIIELLLElQQKENMALVLITHDLALVaEAAHKIIVMYAGQVVETGK 237
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
393-557 |
3.64e-10 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 63.98 E-value: 3.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 393 YPSRKdvQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSI-DGqdirtINVRYLreiigvvSQEPVL 471
Cdd:PRK11819 16 VPPKK--QILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPaPG-----IKVGYL-------PQEPQL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 472 FAT-TIAENIRYGrenvtMDEIEKAVKEANAYDFIMKLPH-KFDTLVGERG----------------------------- 520
Cdd:PRK11819 82 DPEkTVRENVEEG-----VAEVKAALDRFNEIYAAYAEPDaDFDALAAEQGelqeiidaadawdldsqleiamdalrcpp 156
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 25453402 521 -----AQLSGGQKQRIAIARALVRNPKILLLDEATSALDTES 557
Cdd:PRK11819 157 wdakvTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES 198
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1043-1243 |
5.13e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 63.82 E-value: 5.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1043 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLerfydpmAGTVFLD-GKEIKQLNVqwlrahlgIVS---QEP------ 1112
Cdd:PRK11147 17 PLLDNAELHIEDNERVCLVGRNGAGKSTLMKIL-------NGEVLLDdGRIIYEQDL--------IVArlqQDPprnveg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1113 ILFDcSIAENIA--------YGDNSRVVSHEE----IVKAAK-------------EANIHQFIDSL---PEKyntrvgdK 1164
Cdd:PRK11147 82 TVYD-FVAEGIEeqaeylkrYHDISHLVETDPseknLNELAKlqeqldhhnlwqlENRINEVLAQLgldPDA-------A 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1165 GTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALdKAREGrTCIVIAHRLSTIQN-ADLIVVIQNGQV 1243
Cdd:PRK11147 154 LSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFL-KTFQG-SIIFISHDRSFIRNmATRIVDLDRGKL 231
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
1044-1248 |
7.19e-10 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 61.38 E-value: 7.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1044 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLE-RFYDPMA-------GTVFLDGKEIKQLNVQWL---RAHLGIVSQEP 1112
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAgDLTGGGAprgarvtGDVTLNGEPLAAIDAPRLarlRAVLPQAAQPA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1113 ILFdcSIAENIAYG-----DNSRVVSHE--EIVKAAKEAnihqfidslpEKYNTRVGDKGTQLSGGQKQRIAIARAL--- 1182
Cdd:PRK13547 96 FAF--SAREIVLLGryphaRRAGALTHRdgEIAWQALAL----------AGATALVGRDVTTLSGGELARVQFARVLaql 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 25453402 1183 ------VRQPHILLLDEATSALD-TESEKVVQEALDKAREGRT-CIVIAHRLS-TIQNADLIVVIQNGQVKEHGT 1248
Cdd:PRK13547 164 wpphdaAQPPRYLLLDEPTAALDlAHQHRLLDTVRRLARDWNLgVLAIVHDPNlAARHADRIAMLADGAIVAHGA 238
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
111-328 |
1.09e-09 |
|
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: 60.97 E-value: 1.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 111 TGIGAGVLIVAYIQVSLWCLAAGRQ----IHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFF 186
Cdd:cd18546 42 AAAYLAVVLAGWVAQRAQTRLTGRTgerlLYDLRLRVFAHLQRLSLDFHERETSGRIMTRMTSDIDALSELLQTGLVQLV 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 187 QAMATFFGGFIIGFTRGWKLTLVILAISPVLGLsAGIWAKILSSFtdkelqAYAKA-GAVAE------EVLAAIRTVIAF 259
Cdd:cd18546 122 VSLLTLVGIAVVLLVLDPRLALVALAALPPLAL-ATRWFRRRSSR------AYRRArERIAAvnadlqETLAGIRVVQAF 194
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 260 GGQKKELERYnNNLEEAKRLGIKKAITAN-ISMGAAFLLIYASYALAFWYGTSLVISKEYTIGqVLTVFF 328
Cdd:cd18546 195 RRERRNAERF-AELSDDYRDARLRAQRLVaIYFPGVELLGNLATAAVLLVGAWRVAAGTLTVG-VLVAFL 262
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
1043-1255 |
1.21e-09 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 60.19 E-value: 1.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1043 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLL--ERFYDPMAGTVFLDGKEIKQLNVQwLRAHLGI--VSQEPI----- 1113
Cdd:PRK09580 15 AILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLagREDYEVTGGTVEFKGKDLLELSPE-DRAGEGIfmAFQYPVeipgv 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1114 ----LFDCSIAENIAYGDNSRV--VSHEEIVkaakEANIHQFidSLPEKYNTRVGDKGtqLSGGQKQRIAIARALVRQPH 1187
Cdd:PRK09580 94 snqfFLQTALNAVRSYRGQEPLdrFDFQDLM----EEKIALL--KMPEDLLTRSVNVG--FSGGEKKRNDILQMAVLEPE 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 25453402 1188 ILLLDEATSALDTESEKVVQEALDKAREG-RTCIVIAH--RLSTIQNADLIVVIQNGQVKEHGTH---QQLLAQ 1255
Cdd:PRK09580 166 LCILDESDSGLDIDALKIVADGVNSLRDGkRSFIIVTHyqRILDYIKPDYVHVLYQGRIVKSGDFtlvKQLEEQ 239
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
743-962 |
1.40e-09 |
|
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: 60.67 E-value: 1.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 743 NSNLFSLLFLILGIISFITF-----FLQGFTFGKAGEILTKRLRYMVFKSMLRQDISWFDdpKNTTGALTTRLaNDAAQV 817
Cdd:cd18566 35 NESIPTLQVLVIGVVIAILLesllrLLRSYILAWIGARFDHRLSNAAFEHLLSLPLSFFE--REPSGAHLERL-NSLEQI 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 818 KGATGSRLAVITQNIANLGTGIIISLIYGWQLTLLLLAIVPIIAIAGVVEMKMLSgQALKDKKELEGS-GKIATEAIENF 896
Cdd:cd18566 112 REFLTGQALLALLDLPFVLIFLGLIWYLGGKLVLVPLVLLGLFVLVAILLGPILR-RALKERSRADERrQNFLIETLTGI 190
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 897 RTVVSLTREQ----KFETMYAQSLQIPYRNALKKAHVFGITFSFTQAMMyfsyAACFRFGAYLVARELMT 962
Cdd:cd18566 191 HTIKAMAMEPqmlrRYERLQANAAYAGFKVAKINAVAQTLGQLFSQVSM----VAVVAFGALLVINGDLT 256
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
397-584 |
1.42e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 62.82 E-value: 1.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 397 KDVQILKGLNLKVKSGQTVALVGNSGCGKST-----TVQLLQRLYDpIEGEVSIDGQDIRTINVRYLREIIGVVSQE--- 468
Cdd:TIGR00956 72 KTFDILKPMDGLIKPGELTVVLGRPGSGCSTllktiASNTDGFHIG-VEGVITYDGITPEEIKKHYRGDVVYNAETDvhf 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 469 PVLfatTIAE-----------NIRYgrENVtmDEIEKAVKEANAYDFIMKLPHKFDTLVGE---RGaqLSGGQKQRIAIA 534
Cdd:TIGR00956 151 PHL---TVGEtldfaarcktpQNRP--DGV--SREEYAKHIADVYMATYGLSHTRNTKVGNdfvRG--VSGGERKRVSIA 221
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 25453402 535 RALVRNPKILLLDEATSALDTESeavvqaALDKAREGRTTIVIAHRLSTV 584
Cdd:TIGR00956 222 EASLGGAKIQCWDNATRGLDSAT------ALEFIRALKTSANILDTTPLV 265
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1043-1233 |
1.50e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 59.19 E-value: 1.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1043 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIKQLNVQWLRAHLGIVSQEPILFDCSIAEN 1122
Cdd:PRK13540 15 PLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCFVGHRSGINPYLTLREN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1123 IAYG--DNSRVVSHEEIVKAAKEANIHQFIDSLpekyntrvgdkgtqLSGGQKQRIAIARALVRQPHILLLDEATSALDT 1200
Cdd:PRK13540 95 CLYDihFSPGAVGITELCRLFSLEHLIDYPCGL--------------LSSGQKRQVALLRLWMSKAKLWLLDEPLVALDE 160
|
170 180 190
....*....|....*....|....*....|....
gi 25453402 1201 ESEKVVQEALDKAR-EGRTCIVIAHRLSTIQNAD 1233
Cdd:PRK13540 161 LSLLTIITKIQEHRaKGGAVLLTSHQDLPLNKAD 194
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
388-611 |
1.63e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 62.28 E-value: 1.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 388 NIHFSYPSRKDVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQrlydpieGEVSID-GQDIRTINVrylreiigVVS 466
Cdd:PRK11147 5 SIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILN-------GEVLLDdGRIIYEQDL--------IVA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 467 ---QEPVLFATT-----IAENI--------RYGR--ENVTMDEIEKAVKE-ANAYDfimKLPH----KFDTLVGERGAQ- 522
Cdd:PRK11147 70 rlqQDPPRNVEGtvydfVAEGIeeqaeylkRYHDisHLVETDPSEKNLNElAKLQE---QLDHhnlwQLENRINEVLAQl 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 523 ----------LSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALdKAREGrTTIVIAHRLSTVRN-ADVIA 591
Cdd:PRK11147 147 gldpdaalssLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFL-KTFQG-SIIFISHDRSFIRNmATRIV 224
|
250 260
....*....|....*....|.
gi 25453402 592 GFDGGVIVE-QGNHDELMREK 611
Cdd:PRK11147 225 DLDRGKLVSyPGNYDQYLLEK 245
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
480-607 |
2.32e-09 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 61.95 E-value: 2.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 480 IRYGRENVTmDEIEKAVKEAnaYDFIMKLP---HKFDTLV---------GERGAQLSGGQKQRIAIARALVR---NPKIL 544
Cdd:TIGR00630 778 VKYKGKNIA-DVLDMTVEEA--YEFFEAVPsisRKLQTLCdvglgyirlGQPATTLSGGEAQRIKLAKELSKrstGRTLY 854
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 25453402 545 LLDEATSALDTESEA----VVQAALDKareGRTTIVIAHRLSTVRNADVI------AGFDGGVIVEQGNHDEL 607
Cdd:TIGR00630 855 ILDEPTTGLHFDDIKklleVLQRLVDK---GNTVVVIEHNLDVIKTADYIidlgpeGGDGGGTVVASGTPEEV 924
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1049-1253 |
3.09e-09 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 61.08 E-value: 3.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1049 SLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIKQLNV-QWLRAhlGIV------SQEPILFDCSIAE 1121
Cdd:PRK11288 273 SFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPrDAIRA--GIMlcpedrKAEGIIPVHSVAD 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1122 NIAYGDNSRVVSHEEIVKAAKEA-NIHQFIDSLPEKynTRVGD-KGTQLSGGQKQRIAIARALVRQPHILLLDEATSALD 1199
Cdd:PRK11288 351 NINISARRHHLRAGCLINNRWEAeNADRFIRSLNIK--TPSREqLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGID 428
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 25453402 1200 TESEKVVQEAL-DKAREGRTCIVIAHRLSTIQN-ADLIVVIQNGQV-----KEHGTHQQLL 1253
Cdd:PRK11288 429 VGAKHEIYNVIyELAAQGVAVLFVSSDLPEVLGvADRIVVMREGRIagelaREQATERQAL 489
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
745-997 |
3.17e-09 |
|
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette transporters; This group includes the 6-TMD of the peptidase-containing ATP-binding cassette transporters (PCATs) such as Clostridium thermocellum PCAT1, a polypeptide processing and secretion transporter, and LagD, a bacteriocin ABC transporter from Lactococcus lactis. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs. The transporters involved in protein secretion often contain additional peptidase domains essential for substrate processing. These peptidase domains belong to the cysteine protease superfamily, classified as family C39, bacteriocin-processing peptidase. LagD is highly similar to the peptidase-containing ATP-binding cassette transporters (PCATs). In Gram-positive bacteria, the PCATs are responsible for exporting quorum-sensing or antimicrobial peptides called bacteriocins.
Pssm-ID: 350014 [Multi-domain] Cd Length: 294 Bit Score: 59.77 E-value: 3.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 745 NLFSLLFLILGIISFITFFLQGFTFGKAGEILTKRLRYMVFKSMLRQDISWFDdpKNTTGALTTRLaNDAAQVKGATGSr 824
Cdd:cd18570 42 NIISIGLILLYLFQSLLSYIRSYLLLKLSQKLDIRLILGYFKHLLKLPLSFFE--TRKTGEIISRF-NDANKIREAISS- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 825 lAVITQnIANLGTGIIISLI---YGWQLTLLLLAIVPIIAIAGVVEMKMLSGqalKDKKELEGSGKIATEAIENFR---T 898
Cdd:cd18570 118 -TTISL-FLDLLMVIISGIIlffYNWKLFLITLLIIPLYILIILLFNKPFKK---KNREVMESNAELNSYLIESLKgieT 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 899 VVSLTREQKFetmyAQSLQIPYRNALKKAHVFGITF----SFTQAMMYFSYAACFRFGAYLVAR------ELMTFeNVLL 968
Cdd:cd18570 193 IKSLNAEEQF----LKKIEKKFSKLLKKSFKLGKLSnlqsSIKGLISLIGSLLILWIGSYLVIKgqlslgQLIAF-NALL 267
|
250 260
....*....|....*....|....*....
gi 25453402 969 VFsaivFGAmAVGQVSSFAPDYAKAKVSA 997
Cdd:cd18570 268 GY----FLG-PIENLINLQPKIQEAKVAA 291
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1040-1227 |
4.79e-09 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 58.53 E-value: 4.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1040 PNIPVLQGLSLeVKKGQTLALVGSSGCGKSTVVQLLerfydpmAGTvfldgkeikqlnvqwLRAHLGIVSQEPilfdcSI 1119
Cdd:cd03236 12 PNSFKLHRLPV-PREGQVLGLVGPNGIGKSTALKIL-------AGK---------------LKPNLGKFDDPP-----DW 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1120 AENIAYGDNSRVVSHEEIVKAAKEANIH--QFIDSLPEKYNTRVG-------DKGT-------------------QLSGG 1171
Cdd:cd03236 64 DEILDEFRGSELQNYFTKLLEGDVKVIVkpQYVDLIPKAVKGKVGellkkkdERGKldelvdqlelrhvldrnidQLSGG 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1172 QKQRIAIARALVRQPHILLLDEATSALDT----ESEKVVQEAldkAREGRTCIVIAHRLS 1227
Cdd:cd03236 144 ELQRVAIAAALARDADFYFFDEPSSYLDIkqrlNAARLIREL---AEDDNYVLVVEHDLA 200
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1048-1243 |
5.54e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 60.06 E-value: 5.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1048 LSLEVKKGQTLALVGSSGCGKStvvQLLERFY---DPMAGTVFLDGKEIKQLNVQwLRAHLGIV-----SQEPILF-DCS 1118
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRT---ELAETLYglrPARGGRIMLNGKEINALSTA-QRLARGLVylpedRQSSGLYlDAP 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1119 IAENI---AYGDNSRvvsheeIVKAAKEANIHqfidslpEKYNTRVGDKGTQ-------LSGGQKQRIAIARALVRQPHI 1188
Cdd:PRK15439 358 LAWNVcalTHNRRGF------WIKPARENAVL-------ERYRRALNIKFNHaeqaartLSGGNQQKVLIAKCLEASPQL 424
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 25453402 1189 LLLDEATSALDTESEK-VVQEALDKAREGRTCIVIAHRLSTI-QNADLIVVIQNGQV 1243
Cdd:PRK15439 425 LIVDEPTRGVDVSARNdIYQLIRSIAAQNVAVLFISSDLEEIeQMADRVLVMHQGEI 481
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
401-602 |
5.59e-09 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 60.66 E-value: 5.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 401 ILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQ-RLY-DPIEGEVSIDGqdiRTINVRYLREIiGVVSQEPVLFA-TTIA 477
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAgRIQgNNFTGTILANN---RKPTKQILKRT-GFVTQDDILYPhLTVR 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 478 ENIRYGRENVTMDEIEKAVKEANAYDFI--MKLPHKFDTLVGE---RGaqLSGGQKQRIAIARALVRNPKILLLDEATSA 552
Cdd:PLN03211 159 ETLVFCSLLRLPKSLTKQEKILVAESVIseLGLTKCENTIIGNsfiRG--ISGGERKRVSIAHEMLINPSLLILDEPTSG 236
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 25453402 553 LD-TESEAVVQAALDKAREGRTTIVIAHRLSTvrnaDVIAGFDGGVIVEQG 602
Cdd:PLN03211 237 LDaTAAYRLVLTLGSLAQKGKTIVTSMHQPSS----RVYQMFDSVLVLSEG 283
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
763-997 |
6.03e-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: 59.06 E-value: 6.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 763 FLQGFTFGKAGEILTKRLRYMVFKSMLRQDISWFDdpKNTTGALTTRLANDAAQVKGATGSRLAVITQNIANLG--TGII 840
Cdd:cd18564 72 YAGTYLTALVGQRVVLDLRRDLFAHLQRLSLSFHD--RRRTGDLLSRLTGDVGAIQDLLVSGVLPLLTNLLTLVgmLGVM 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 841 ISLiyGWQLTLLLLAIVPIIAIAGVV---EMKmlsgQALKDKKELEGS-GKIATEAIENFRTVVSLTREQKFETMYAQSL 916
Cdd:cd18564 150 FWL--DWQLALIALAVAPLLLLAARRfsrRIK----EASREQRRREGAlASVAQESLSAIRVVQAFGREEHEERRFAREN 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 917 QIPYRNALKKAH-------VFGITFSFTQAMMYFsyaacfrFGAYLVARELMTFeNVLLVFSAIVFGAMA-VGQVSSFAP 988
Cdd:cd18564 224 RKSLRAGLRAARlqallspVVDVLVAVGTALVLW-------FGAWLVLAGRLTP-GDLLVFLAYLKNLYKpVRDLAKLTG 295
|
....*....
gi 25453402 989 DYAKAKVSA 997
Cdd:cd18564 296 RIAKASASA 304
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
395-579 |
6.73e-09 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 57.55 E-value: 6.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 395 SRKDVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRTIN-VRYlreiIGVVSQEPVLFA 473
Cdd:PRK13543 20 SRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDrSRF----MAYLGHLPGLKA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 474 TTIA-ENIRY-----GRENVTMdeiekavkEANAYDfIMKLPHKFDTLVgergAQLSGGQKQRIAIARALVRNPKILLLD 547
Cdd:PRK13543 96 DLSTlENLHFlcglhGRRAKQM--------PGSALA-IVGLAGYEDTLV----RQLSAGQKKRLALARLWLSPAPLWLLD 162
|
170 180 190
....*....|....*....|....*....|...
gi 25453402 548 EATSALDTESEAVVQAALD-KAREGRTTIVIAH 579
Cdd:PRK13543 163 EPYANLDLEGITLVNRMISaHLRGGGAALVTTH 195
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
1027-1207 |
9.50e-09 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 59.87 E-value: 9.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1027 VKFNGVMFNYPTRPNIpvLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKE----IKQLNVQWLR 1102
Cdd:PLN03073 509 ISFSDASFGYPGGPLL--FKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKVrmavFSQHHVDGLD 586
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1103 ahlgiVSQEPILFdcsiaeniaygdnsrvvsHEEIVKAAKEANIHQFIDSLPEKYNTRVGDKGTqLSGGQKQRIAIARAL 1182
Cdd:PLN03073 587 -----LSSNPLLY------------------MMRCFPGVPEQKLRAHLGSFGVTGNLALQPMYT-LSGGQKSRVAFAKIT 642
|
170 180
....*....|....*....|....*.
gi 25453402 1183 VRQPHILLLDEATSALDTES-EKVVQ 1207
Cdd:PLN03073 643 FKKPHILLLDEPSNHLDLDAvEALIQ 668
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
384-613 |
1.05e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 59.52 E-value: 1.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 384 LEFKNIHFSYPSRKdvqILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIdgqdirTINVRylreiIG 463
Cdd:PRK15064 320 LEVENLTKGFDNGP---LFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKW------SENAN-----IG 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 464 VVSQEPVL-FATTIA---------------ENIR--YGRENVTMDEIEKAVKeanaydfimklphkfdtlvgergaQLSG 525
Cdd:PRK15064 386 YYAQDHAYdFENDLTlfdwmsqwrqegddeQAVRgtLGRLLFSQDDIKKSVK------------------------VLSG 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 526 GQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDKArEGrTTIVIAH------RLSTvrnaDVIAGFDGGVIV 599
Cdd:PRK15064 442 GEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESIESLNMALEKY-EG-TLIFVSHdrefvsSLAT----RIIEITPDGVVD 515
|
250
....*....|....
gi 25453402 600 EQGNHDELMREKGI 613
Cdd:PRK15064 516 FSGTYEEYLRSQGI 529
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
112-335 |
1.18e-08 |
|
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) and similar proteins. These transporter subunits include HylB, PrtD, CyaB, CvaB, RsaD, HasD, LipB, and LapB, among many others. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). Most targeted proteins are not cleaved at the N terminus, but rather carry signals located toward the extreme C terminus to direct type I secretion. However, the 10 kDa Escherichia coli colicin V (CvaB) targets the ABC transporter using a cleaved, N-terminal signal sequence. Almost all transport substrates of the type I system have critical functions in attacking host cells either directly or by being essential for host colonization. The ABC-dependent T1SS transports various molecules, from ions, drugs, to proteins of various sizes up to 900 kDa. The molecules secreted vary in size from the small Escherichia coli peptide colicin V, (10 kDa) to the Pseudomonas fluorescens cell adhesion protein LapA of 520 kDa. The best characterized are the RTX toxins such as the adenylate cyclase (CyaA) toxin from Bordetella pertussis, the causative agent of whooping cough, and the lipases such as LipA. Type I secretion is also involved in export of non-protein substrates such as cyclic beta-glucans and polysaccharides.
Pssm-ID: 349999 [Multi-domain] Cd Length: 294 Bit Score: 57.91 E-value: 1.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 112 GIGAGVLIVAYIQVSLwclAAGRQIHKIRQKFFHAIMNQEIG--------WFDVHDVGELNTRLtDDVSKINEGIGDKIG 183
Cdd:cd18555 45 GIGILILFLLYGLFSF---LRGYIIIKLQTKLDKSLMSDFFEhllklpysFFENRSSGDLLFRA-NSNVYIRQILSNQVI 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 184 MFFQAMATFFGGFIIGFTRGWKLTLVILAISPVLGLSAGIWAKILSSFTDKELQAYAKAGAVAEEVLAAIRTVIAFGGQK 263
Cdd:cd18555 121 SLIIDLLLLVIYLIYMLYYSPLLTLIVLLLGLLIVLLLLLTRKKIKKLNQEEIVAQTKVQSYLTETLYGIETIKSLGSEK 200
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 25453402 264 KELERYNNNLEEAKRLGIKKAITANISMGAAFLLIYASYALAFWYGTSLVISKEYTIGQVLTvfFSVLIGAF 335
Cdd:cd18555 201 NIYKKWENLFKKQLKAFKKKERLSNILNSISSSIQFIAPLLILWIGAYLVINGELTLGELIA--FSSLAGSF 270
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
405-581 |
1.46e-08 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 59.64 E-value: 1.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 405 LNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRTiNVRYLREIIGVVSQEPVLfattiaENIRYGR 484
Cdd:TIGR01257 1958 LCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT-NISDVHQNMGYCPQFDAI------DDLLTGR 2030
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 485 EN---------VTMDEIEKAvkeANAYDFIMKLPHKFDTLVGergaQLSGGQKQRIAIARALVRNPKILLLDEATSALDT 555
Cdd:TIGR01257 2031 EHlylyarlrgVPAEEIEKV---ANWSIQSLGLSLYADRLAG----TYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDP 2103
|
170 180
....*....|....*....|....*..
gi 25453402 556 ESEAVV-QAALDKAREGRTTIVIAHRL 581
Cdd:TIGR01257 2104 QARRMLwNTIVSIIREGRAVVLTSHSM 2130
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
402-579 |
1.54e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 59.05 E-value: 1.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 402 LKGLNLKVKSGQ-----TVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDgqdirtINVRYLREIIGVVSQEPV-LFATT 475
Cdd:PRK13409 350 LGDFSLEVEGGEiyegeVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE------LKISYKPQYIKPDYDGTVeDLLRS 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 476 IAENIRygrENVTMDEIEKAvkeanaydfiMKLPHKFDTLVGErgaqLSGGQKQRIAIARALVRNPKILLLDEATSALDT 555
Cdd:PRK13409 424 ITDDLG---SSYYKSEIIKP----------LQLERLLDKNVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLDV 486
|
170 180
....*....|....*....|....*.
gi 25453402 556 ESEAVVQAALDKAREGR--TTIVIAH 579
Cdd:PRK13409 487 EQRLAVAKAIRRIAEEReaTALVVDH 512
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
111-331 |
1.58e-08 |
|
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: 57.49 E-value: 1.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 111 TGIGAGVLIVAYIQvslWCLAAGRQI----------HKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINEGIGd 180
Cdd:cd18543 39 WPLVLLLLALGVAE---AVLSFLRRYlagrlslgveHDLRTDLFAHLQRLDGAFHDRWQSGQLLSRATSDLSLVQRFLA- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 181 KIGMFFQAMATFFGGFIIGFTRGWKLTLVILAISPVLGLSAGIWAKILSSFTdkeLQAYAKAGAVA---EEVLAAIRTVI 257
Cdd:cd18543 115 FGPFLLGNLLTLVVGLVVMLVLSPPLALVALASLPPLVLVARRFRRRYFPAS---RRAQDQAGDLAtvvEESVTGIRVVK 191
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 25453402 258 AFGGQKKELERYNNNLEEAKRLGIKKA-ITANISMgAAFLLIYASYALAFWYGTSLVISKEYTIGQvLTVFFSVL 331
Cdd:cd18543 192 AFGRERRELDRFEAAARRLRATRLRAArLRARFWP-LLEALPELGLAAVLALGGWLVANGSLTLGT-LVAFSAYL 264
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
385-556 |
1.75e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 58.81 E-value: 1.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 385 EFKNIHFSYPsrkDVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQdirtINVRYL---REI 461
Cdd:PRK11147 321 EMENVNYQID---GKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTK----LEVAYFdqhRAE 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 462 IgvvsqEPvlfATTIAENIRYGRENVTMDEIEKAVKeanAY--DFIMKlPHKFDTLVgergAQLSGGQKQRIAIARALVR 539
Cdd:PRK11147 394 L-----DP---EKTVMDNLAEGKQEVMVNGRPRHVL---GYlqDFLFH-PKRAMTPV----KALSGGERNRLLLARLFLK 457
|
170
....*....|....*..
gi 25453402 540 NPKILLLDEATSALDTE 556
Cdd:PRK11147 458 PSNLLILDEPTNDLDVE 474
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
47-322 |
1.95e-08 |
|
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: 57.21 E-value: 1.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 47 RFYMLLGTLAAIIHGIALPLMMLVFGDMtdsfanVGNNRSMSfynatdiyakledemttyAYYYTGIGAGVLIVAYI--- 123
Cdd:cd18566 4 LPQVLLASLFINILALATPLFILQVYDR------VIPNESIP------------------TLQVLVIGVVIAILLESllr 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 124 ----QVSLWclaAGRQI-HKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDdVSKINEgigdkigmFF--QAMAT----- 191
Cdd:cd18566 60 llrsYILAW---IGARFdHRLSNAAFEHLLSLPLSFFEREPSGAHLERLNS-LEQIRE--------FLtgQALLAlldlp 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 192 ----FFGgfIIGFTrGWKLTLVILAISPVLGLSAGIWAKILSSFTDKELQAYAKAGAVAEEVLAAIRTVIAFGGQKKELE 267
Cdd:cd18566 128 fvliFLG--LIWYL-GGKLVLVPLVLLGLFVLVAILLGPILRRALKERSRADERRQNFLIETLTGIHTIKAMAMEPQMLR 204
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 25453402 268 RYNNNLEEAKRLGIKKAITANISMGAAFLLIYASYALAFWYGTSLVISKEYTIGQ 322
Cdd:cd18566 205 RYERLQANAAYAGFKVAKINAVAQTLGQLFSQVSMVAVVAFGALLVINGDLTVGA 259
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
703-865 |
2.01e-08 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350051 [Multi-domain] Cd Length: 293 Bit Score: 57.16 E-value: 2.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 703 FVVGVFCAIINGGLQpafsIIFSKVVGVFTkNDTPEIQRQNSNLFSLLFLILG--IISFITFFLQGFTFGKAGEILTKRL 780
Cdd:cd18778 1 LILTLLCALLSTLLG----LVPPWLIRELV-DLVTIGSKSLGLLLGLALLLLGayLLRALLNFLRIYLNHVAEQKVVADL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 781 RYMVFKSMLRQDISWFDDPKntTGALTTRLANDAAQVKgatgsRLAV--ITQNIANLGT--GIIISLIY-GWQLTLLLLA 855
Cdd:cd18778 76 RSDLYDKLQRLSLRYFDDRQ--TGDLMSRVINDVANVE-----RLIAdgIPQGITNVLTlvGVAIILFSiNPKLALLTLI 148
|
170
....*....|
gi 25453402 856 IVPIIAIAGV 865
Cdd:cd18778 149 PIPFLALGAW 158
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1043-1257 |
2.36e-08 |
|
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: 58.87 E-value: 2.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1043 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIKQlNVQWLRAHLGIVSQEPILFDCSIA-E 1121
Cdd:TIGR01257 1953 PAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT-NISDVHQNMGYCPQFDAIDDLLTGrE 2031
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1122 NIAYGDNSRVVSHEEIVKAA----KEANIHQFIDSLPEKYntrvgdkgtqlSGGQKQRIAIARALVRQPHILLLDEATSA 1197
Cdd:TIGR01257 2032 HLYLYARLRGVPAEEIEKVAnwsiQSLGLSLYADRLAGTY-----------SGGNKRKLSTAIALIGCPPLVLLDEPTTG 2100
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 25453402 1198 LDTESEKVVQEAL-DKAREGRTCIVIAHRLSTIQN-ADLIVVIQNGQVKEHGTHQQLLAQKG 1257
Cdd:TIGR01257 2101 MDPQARRMLWNTIvSIIREGRAVVLTSHSMEECEAlCTRLAIMVKGAFQCLGTIQHLKSKFG 2162
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
384-584 |
2.53e-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: 2.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 384 LEFKNIHFSYPSRKDVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYD-PIEGEVSIDGQ--DIRT-------- 452
Cdd:TIGR02633 258 LEARNLTCWDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPgKFEGNVFINGKpvDIRNpaqairag 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 453 -INVRYLREIIGVVSQEPVLFATTIAENIRYGRENVTMDEIEKAVKEANAYDFIMKLPHKFDTLvgergAQLSGGQKQRI 531
Cdd:TIGR02633 338 iAMVPEDRKRHGIVPILGVGKNITLSVLKSFCFKMRIDAAAELQIIGSAIQRLKVKTASPFLPI-----GRLSGGNQQKA 412
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 25453402 532 AIARALVRNPKILLLDEATSALDTESEAVVQAALDK-AREGRTTIVIAHRLSTV 584
Cdd:TIGR02633 413 VLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQlAQEGVAIIVVSSELAEV 466
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
100-341 |
2.77e-08 |
|
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: 56.74 E-value: 2.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 100 EDEMTTYAYYYTGIGAGVLIVAYIQVSLW----CLAAGRQIHkirQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKIN 175
Cdd:cd18580 34 NSSSGYYLGVYAALLVLASVLLVLLRWLLfvlaGLRASRRLH---DKLLRSVLRAPMSFFDTTPSGRILNRFSKDIGLID 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 176 EGIGDKIGMFFQAMATFFGGFI-IGFTRGWkltlvILAISPVLGLSAGIWAKI-LSSFTD-KELQAYAKAGAVA--EEVL 250
Cdd:cd18580 111 EELPLALLDFLQSLFSVLGSLIvIAIVSPY-----FLIVLPPLLVVYYLLQRYyLRTSRQlRRLESESRSPLYShfSETL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 251 AAIRTVIAFGGQKKELERYNNNLeeakrlgikkaitaNISMGAAFLLIYASYALAFWYgtslviskeytigQVLTVFFSV 330
Cdd:cd18580 186 SGLSTIRAFGWQERFIEENLRLL--------------DASQRAFYLLLAVQRWLGLRL-------------DLLGALLAL 238
|
250
....*....|.
gi 25453402 331 LIGAFSVGQAS 341
Cdd:cd18580 239 VVALLAVLLRS 249
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
703-963 |
2.85e-08 |
|
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: 56.69 E-value: 2.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 703 FVVGVFCAIINGGLqpafSIIFSKVVGVFTKNDTPEiqrQNSNLFSLLFLILGIISFITFFLQgFTFGKAGEILTKR--- 779
Cdd:cd18549 4 FFLDLFCAVLIAAL----DLVFPLIVRYIIDDLLPS---KNLRLILIIGAILLALYILRTLLN-YFVTYWGHVMGARiet 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 780 -LRYMVFKSMLRQDISWFDdpKNTTGALTTRLANDAAQVkgatgSRLA-------VITqnIANLGTGIIISLIYGWQLTL 851
Cdd:cd18549 76 dMRRDLFEHLQKLSFSFFD--NNKTGQLMSRITNDLFDI-----SELAhhgpedlFIS--IITIIGSFIILLTINVPLTL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 852 LLLAIVPIIAIAGVVEMKMLSGQALKDKKELegsGKIATEAIENF---RTVVSLTRE----QKFETMYAQslqipYRNAL 924
Cdd:cd18549 147 IVFALLPLMIIFTIYFNKKMKKAFRRVREKI---GEINAQLEDSLsgiRVVKAFANEeyeiEKFDEGNDR-----FLESK 218
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 25453402 925 KKAH-VFGITFSFTQAMMYFSYAACFRFGAYLVARELMTF 963
Cdd:cd18549 219 KKAYkAMAYFFSGMNFFTNLLNLVVLVAGGYFIIKGEITL 258
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1042-1255 |
3.09e-08 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 57.02 E-value: 3.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1042 IPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIKQLNVQWLRaHLGIV----SQepILFDC 1117
Cdd:COG4586 35 VEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFKRRKEFAR-RIGVVfgqrSQ--LWWDL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1118 SIAENIAYgdNSRVVsheEIVKAAKEANIHQFID--SLPEKYNTRVgdkgTQLSGGQKQRIAIARALVRQPHILLLDEAT 1195
Cdd:COG4586 112 PAIDSFRL--LKAIY---RIPDAEYKKRLDELVEllDLGELLDTPV----RQLSLGQRMRCELAAALLHRPKILFLDEPT 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 25453402 1196 SALDTESEKVVQEALDK--AREGRTCIVIAHRLSTIQN-ADLIVVIQNGQVKEHGTHQQLLAQ 1255
Cdd:COG4586 183 IGLDVVSKEAIREFLKEynRERGTTILLTSHDMDDIEAlCDRVIVIDHGRIIYDGSLEELKER 245
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
737-863 |
3.33e-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: 350007 [Multi-domain] Cd Length: 296 Bit Score: 56.75 E-value: 3.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 737 PEIQRQNSNLFSLLFLILGIISFITFFLQ---GFTFGKAGEILTKRLRYMVFKSMLRQDISWFDdpKNTTGALTTRLAND 813
Cdd:cd18563 32 QLGPGGNTSLLLLLVLGLAGAYVLSALLGilrGRLLARLGERITADLRRDLYEHLQRLSLSFFD--KRQTGSLMSRVTSD 109
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 25453402 814 AAQVKGATGSRLAVITQNIANLgTGIIISLIY-GWQLTLLLLAIVPIIAIA 863
Cdd:cd18563 110 TDRLQDFLSDGLPDFLTNILMI-IGIGVVLFSlNWKLALLVLIPVPLVVWG 159
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
1053-1238 |
3.86e-08 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 57.49 E-value: 3.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1053 KKGQTLALVGSSGCGKSTVVQLLerfydpmAGTvfldgkeikqlnvqwLRAHLGIVSQEPilfdcSIAENIAYGDNSRVV 1132
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKIL-------SGE---------------LKPNLGDYDEEP-----SWDEVLKRFRGTELQ 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1133 SHEEIVKAAKEANIH--QFIDSLPEKYNTRVGD-------KG-------------------TQLSGGQKQRIAIARALVR 1184
Cdd:COG1245 150 DYFKKLANGEIKVAHkpQYVDLIPKVFKGTVREllekvdeRGkldelaeklglenildrdiSELSGGELQRVAIAAALLR 229
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 25453402 1185 QPHILLLDEATSALD----TESEKVVQEAldkAREGRTCIVIAHRLSTIQN-ADLIVVI 1238
Cdd:COG1245 230 DADFYFFDEPSSYLDiyqrLNVARLIREL---AEEGKYVLVVEHDLAILDYlADYVHIL 285
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1030-1202 |
3.90e-08 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 57.64 E-value: 3.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1030 NGVMFNYPtrPNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLlerfydpMAG--TVFlDGKEIKQLNVQwlrahLGI 1107
Cdd:TIGR03719 8 NRVSKVVP--PKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRI-------MAGvdKDF-NGEARPQPGIK-----VGY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1108 VSQEPILfDCS--IAENI-------------------AYGDNS--------RVVSHEEIVKAAK----EANIHQFIDSL- 1153
Cdd:TIGR03719 73 LPQEPQL-DPTktVRENVeegvaeikdaldrfneisaKYAEPDadfdklaaEQAELQEIIDAADawdlDSQLEIAMDALr 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 25453402 1154 -PEkyntrvGD-KGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTES 1202
Cdd:TIGR03719 152 cPP------WDaDVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAES 196
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
1160-1236 |
4.06e-08 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 56.08 E-value: 4.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1160 RVGDKGTQLSGGQKQRIAIARALVRQ---PHILLLDEATSALDTESEKVVQEALDKARE-GRTCIVIAHRLSTIQNADLI 1235
Cdd:cd03271 162 KLGQPATTLSGGEAQRIKLAKELSKRstgKTLYILDEPTTGLHFHDVKKLLEVLQRLVDkGNTVVVIEHNLDVIKCADWI 241
|
.
gi 25453402 1236 V 1236
Cdd:cd03271 242 I 242
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
1007-1233 |
4.53e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 57.33 E-value: 4.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1007 IPEIDSYST-EGLKPNmlEGNVKFNGVMFNYPTRPnipVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLE----RFYdp 1081
Cdd:PRK10938 242 LPEPDEPSArHALPAN--EPRIVLNNGVVSYNDRP---ILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITgdhpQGY-- 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1082 mAGTVFLDGK---------EIKQlnvqwlraHLGIVSQEPIL---FDCSIAENIAYG--DN---SRVVSHEEIVKAAkea 1144
Cdd:PRK10938 315 -SNDLTLFGRrrgsgetiwDIKK--------HIGYVSSSLHLdyrVSTSVRNVILSGffDSigiYQAVSDRQQKLAQ--- 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1145 nihQFIDSLpeKYNTRVGDKGTQ-LSGGQkQRIA-IARALVRQPHILLLDEATSALDTESEKVVQEALDK-AREGRT--- 1218
Cdd:PRK10938 383 ---QWLDIL--GIDKRTADAPFHsLSWGQ-QRLAlIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVlISEGETqll 456
|
250 260
....*....|....*....|....*.
gi 25453402 1219 -----------CivIAHRLSTIQNAD 1233
Cdd:PRK10938 457 fvshhaedapaC--ITHRLEFVPDGD 480
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
108-329 |
4.80e-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: 4.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 108 YYYTGIGAGVLIVAYIQVSLWCLAAGRQ----IHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINE----GIG 179
Cdd:cd18540 42 TGFILLYLGLILIQALSVFLFIRLAGKIemgvSYDLRKKAFEHLQTLSFSYFDKTPVGWIMARVTSDTQRLGEiiswGLV 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 180 DkigmFFQAMATFFGGFIIGFTRGWKLTLVILAISPVLGLSAGIwakilssFTDKELQAYAKAGAVAEEVLAA------- 252
Cdd:cd18540 122 D----LVWGITYMIGILIVMLILNWKLALIVLAVVPVLAVVSIY-------FQKKILKAYRKVRKINSRITGAfnegitg 190
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 25453402 253 IRTVIAFGGQKKELERYNNNLEEAKRLGIKKAITANISMGAAFLLIYASYALAFWYGTSLVISKEYTIGQvLTVFFS 329
Cdd:cd18540 191 AKTTKTLVREEKNLREFKELTEEMRRASVRAARLSALFLPIVLFLGSIATALVLWYGGILVLAGAITIGT-LVAFIS 266
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
703-956 |
6.51e-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: 56.04 E-value: 6.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 703 FVVGVFCAIINgglqPAFSIIFSKVVG-----VFTKNDT----------PEIQRQnsnlfslLFLILGIISFITF----- 762
Cdd:cd18565 1 LVLGLLASILN----RLFDLAPPLLIGvaidaVFNGEASflplvpaslgPADPRG-------QLWLLGGLTVAAFllesl 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 763 --FLQGFTFGKAGEILTKRLRYMVFKSMLRQDISWFDDpkNTTGALTTRLANDAAQVKGATGSRLAVITQNIANLGTGII 840
Cdd:cd18565 70 fqYLSGVLWRRFAQRVQHDLRTDTYDHVQRLDMAFFED--RQTGDLMSVLNNDVNQLERFLDDGANSIIRVVVTVLGIGA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 841 ISLIYGWQLTLLLLAIVPIIAIAGVVEMKMLSGQALKDKKELegsGKIAT---EAIENFRTVVSLTREQkFET--MYAQS 915
Cdd:cd18565 148 ILFYLNWQLALVALLPVPLIIAGTYWFQRRIEPRYRAVREAV---GDLNArleNNLSGIAVIKAFTAED-FERerVADAS 223
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 25453402 916 LQipYRNALKKAHVFGITFSFT-QAMMYFSYAACFRFGAYLV 956
Cdd:cd18565 224 EE--YRDANWRAIRLRAAFFPViRLVAGAGFVATFVVGGYWV 263
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
410-583 |
6.68e-08 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 56.72 E-value: 6.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 410 KSGQTVALVGNSGCGKSTTVQLLQRLYDP----IEGEVSIDgqDIrtinVRYLReiiGVVSQEpvLFATTIAENIRYGRE 485
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSGELKPnlgdYDEEPSWD--EV----LKRFR---GTELQD--YFKKLANGEIKVAHK 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 486 NVTMDEIEKAVKeANAYDFIMKlphkfdtlVGERGA-------------------QLSGGQKQRIAIARALVRNPKILLL 546
Cdd:COG1245 166 PQYVDLIPKVFK-GTVRELLEK--------VDERGKldelaeklglenildrdisELSGGELQRVAIAAALLRDADFYFF 236
|
170 180 190
....*....|....*....|....*....|....*...
gi 25453402 547 DEATSALD-TESEAVVQAALDKAREGRTTIVIAHRLST 583
Cdd:COG1245 237 DEPSSYLDiYQRLNVARLIRELAEEGKYVLVVEHDLAI 274
|
|
| ABC_6TM_CyaB_HlyB_like |
cd18588 |
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ... |
196-336 |
8.75e-08 |
|
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: 55.20 E-value: 8.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 196 FIIGFTRGWKLTLVILAISPVLGLSAGIWAKILSSFTDKELQAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNNNLEE 275
Cdd:cd18588 133 LAVMFYYSPTLTLIVLASLPLYALLSLLVTPILRRRLEEKFQRGAENQSFLVETVTGIETVKSLAVEPQFQRRWEELLAR 212
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 25453402 276 AKRLGIKKAITANISMGAAFLLIYASYALAFWYGTSLVISKEYTIGQVltVFFSVLIGAFS 336
Cdd:cd18588 213 YVKASFKTANLSNLASQIVQLIQKLTTLAILWFGAYLVMDGELTIGQL--IAFNMLAGQVS 271
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1052-1238 |
1.38e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 55.97 E-value: 1.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1052 VKKGQTLALVGSSGCGKSTVVQLLerfydpmAGTvfldgkeikqlnvqwLRAHLGIVSQEPilfdcSIAENIAYGDNSRV 1131
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKIL-------SGE---------------LIPNLGDYEEEP-----SWDEVLKRFRGTEL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1132 VSHEEIVKAAKEANIH--QFIDSLPEKYNTRVGD--KGT------------------------QLSGGQKQRIAIARALV 1183
Cdd:PRK13409 149 QNYFKKLYNGEIKVVHkpQYVDLIPKVFKGKVREllKKVdergkldevverlglenildrdisELSGGELQRVAIAAALL 228
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 25453402 1184 RQPHILLLDEATSALDtesekvVQEALDKAR------EGRTCIVIAHRLSTIQN-ADLIVVI 1238
Cdd:PRK13409 229 RDADFYFFDEPTSYLD------IRQRLNVARlirelaEGKYVLVVEHDLAVLDYlADNVHIA 284
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1051-1235 |
1.56e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 55.59 E-value: 1.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1051 EVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDgkeikqLNV----QWLRA-HLGIVSQepilFDCSIAENIay 1125
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE------LKIsykpQYIKPdYDGTVED----LLRSITDDL-- 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1126 gDNSRVVSheEIVKAAkeaNIHQFIDSlpekyntRVGDkgtqLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKV 1205
Cdd:PRK13409 429 -GSSYYKS--EIIKPL---QLERLLDK-------NVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLA 491
|
170 180 190
....*....|....*....|....*....|..
gi 25453402 1206 VQEALDKAREGR--TCIVIAHRLSTIqnaDLI 1235
Cdd:PRK13409 492 VAKAIRRIAEEReaTALVVDHDIYMI---DYI 520
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
419-554 |
1.61e-07 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 55.90 E-value: 1.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 419 GNSGCGKSTTVQLLQRLYDPIEGEV-----SIDGQDIRTinvrylREIIGVVSQEPVLfattiaenirYG----REN--- 486
Cdd:NF033858 299 GSNGCGKSTTMKMLTGLLPASEGEAwlfgqPVDAGDIAT------RRRVGYMSQAFSL----------YGeltvRQNlel 362
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 25453402 487 ------VTMDEIEKAVKEanaydfimkLPHKFD--TLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALD 554
Cdd:NF033858 363 harlfhLPAAEIAARVAE---------MLERFDlaDVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVD 429
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
143-333 |
1.74e-07 |
|
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: 54.49 E-value: 1.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 143 FFHAIMNQEIGWFDVHDVGELNTRLTDdvskiNEGI-----GDKIGMFFQAMATFFGGFIIgFTRGWKLTLVILAISPVL 217
Cdd:cd18568 81 FYKHLLSLPLSFFASRKVGDIITRFQE-----NQKIrrfltRSALTTILDLLMVFIYLGLM-FYYNLQLTLIVLAFIPLY 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 218 GLSAGIWAKILSSFTDKELQAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNNNLEEAKRLGIKKAITANISMGAAFLL 297
Cdd:cd18568 155 VLLTLLSSPKLKRNSREIFQANAEQQSFLVEALTGIATIKALAAERPIRWRWENKFAKALNTRFRGQKLSIVLQLISSLI 234
|
170 180 190
....*....|....*....|....*....|....*.
gi 25453402 298 IYASYALAFWYGTSLVISKEYTIGQVltVFFSVLIG 333
Cdd:cd18568 235 NHLGTIAVLWYGAYLVISGQLTIGQL--VAFNMLFG 268
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
1043-1258 |
1.75e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 55.28 E-value: 1.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1043 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVfldgkeikqlnvQWL-RAHLGIVSQEP--------I 1113
Cdd:PRK15064 333 PLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV------------KWSeNANIGYYAQDHaydfendlT 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1114 LFDCsIAENIAYGDNSRVV---------SHEEIVKAAKeanihqfidslpekyntrvgdkgtQLSGGQKQRIAIARALVR 1184
Cdd:PRK15064 401 LFDW-MSQWRQEGDDEQAVrgtlgrllfSQDDIKKSVK------------------------VLSGGEKGRMLFGKLMMQ 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1185 QPHILLLDEATSALDTESEKVVQEALDKArEGrTCIVIAH------RLSTiqnaDLIVVIQNGQVKEHGTHQQLLAQKGI 1258
Cdd:PRK15064 456 KPNVLVMDEPTNHMDMESIESLNMALEKY-EG-TLIFVSHdrefvsSLAT----RIIEITPDGVVDFSGTYEEYLRSQGI 529
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
1049-1255 |
1.81e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 55.41 E-value: 1.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1049 SLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAG--------TVFLDGKEIKQL-NVQWLRAHLGIVSQEPILFDCSI 1119
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGerqsqfshITRLSFEQLQKLvSDEWQRNNTDMLSPGEDDTGRTT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1120 AENIAYG--DNSRVvshEEIVKaakeanihQF-IDSL---PEKYntrvgdkgtqLSGGQKQRIAIARALVRQPHILLLDE 1193
Cdd:PRK10938 103 AEIIQDEvkDPARC---EQLAQ--------QFgITALldrRFKY----------LSTGETRKTLLCQALMSEPDLLILDE 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 25453402 1194 ATSALDTESEKVVQEALDK-AREGRTCIVIAHRLSTIQN-ADLIVVIQNGQVKEHGTHQQLLAQ 1255
Cdd:PRK10938 162 PFDGLDVASRQQLAELLASlHQSGITLVLVLNRFDEIPDfVQFAGVLADCTLAETGEREEILQQ 225
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1045-1248 |
2.00e-07 |
|
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: 53.57 E-value: 2.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1045 LQGLSLEVKKG-----QTLALVGSSGCGKSTVVQLLerfydpmAGTVFLDGKEIKQLNVQwlrahlgiVSQEP----ILF 1115
Cdd:cd03237 10 LGEFTLEVEGGsisesEVIGILGPNGIGKTTFIKML-------AGVLKPDEGDIEIELDT--------VSYKPqyikADY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1116 DCSIAENIAYGDNSRVVSHEEIVKAAKEANIHQFIDS-LPEkyntrvgdkgtqLSGGQKQRIAIARALVRQPHILLLDEA 1194
Cdd:cd03237 75 EGTVRDLLSSITKDFYTHPYFKTEIAKPLQIEQILDReVPE------------LSGGELQRVAIAACLSKDADIYLLDEP 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 25453402 1195 TSALDTESE----KVVQEALDKARegRTCIVIAHrlsTIQNADLI---VVIQNGQVKEHGT 1248
Cdd:cd03237 143 SAYLDVEQRlmasKVIRRFAENNE--KTAFVVEH---DIIMIDYLadrLIVFEGEPSVNGV 198
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
700-963 |
2.32e-07 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349984 [Multi-domain] Cd Length: 295 Bit Score: 54.02 E-value: 2.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 700 WPYFVVGVFCAIINGGLQPAFSIIFSKVVGVFTKNDTPEiqrqNSNLFSLLFLILGIISFITFFLQGFTFGKAGEILTKR 779
Cdd:cd18540 1 KKLLILLIILMLLVALLDAVFPLLTKYAIDHFITPGTLD----GLTGFILLYLGLILIQALSVFLFIRLAGKIEMGVSYD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 780 LRYMVFKSMLRQDISWFDdpKNTTGALTTRLANDAAQVKGATGSRLAVITQNIANLGTGIIISLIYGWQLTLLLLAIVPI 859
Cdd:cd18540 77 LRKKAFEHLQTLSFSYFD--KTPVGWIMARVTSDTQRLGEIISWGLVDLVWGITYMIGILIVMLILNWKLALIVLAVVPV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 860 IAIAGVV-EMKMLSGQALKDKKELEGSGKIaTEAIENFRTVVSLTREQK----F----ETMYAQSlqipYRNALKKAhvf 930
Cdd:cd18540 155 LAVVSIYfQKKILKAYRKVRKINSRITGAF-NEGITGAKTTKTLVREEKnlreFkeltEEMRRAS----VRAARLSA--- 226
|
250 260 270
....*....|....*....|....*....|...
gi 25453402 931 gITFSFTQAMMYFSYAACFRFGAYLVARELMTF 963
Cdd:cd18540 227 -LFLPIVLFLGSIATALVLWYGGILVLAGAITI 258
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
409-579 |
2.45e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 55.18 E-value: 2.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 409 VKSGQTVALVGNSGCGKSTTVQLLQrlydpieGEVSIDGQDIRTINVRYLreiiGVVSQE-PVLFATTIAENIRYGREnv 487
Cdd:PRK10636 24 INPGQKVGLVGKNGCGKSTLLALLK-------NEISADGGSYTFPGNWQL----AWVNQEtPALPQPALEYVIDGDRE-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 488 tMDEIEKAVKEANAYD---FIMKLPHKFDTL----VGERGAQL------------------SGGQKQRIAIARALVRNPK 542
Cdd:PRK10636 91 -YRQLEAQLHDANERNdghAIATIHGKLDAIdawtIRSRAASLlhglgfsneqlerpvsdfSGGWRMRLNLAQALICRSD 169
|
170 180 190
....*....|....*....|....*....|....*..
gi 25453402 543 ILLLDEATSALDTESEAVVQAALdKAREGrTTIVIAH 579
Cdd:PRK10636 170 LLLLDEPTNHLDLDAVIWLEKWL-KSYQG-TLILISH 204
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1166-1202 |
3.21e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 54.74 E-value: 3.21e-07
10 20 30
....*....|....*....|....*....|....*..
gi 25453402 1166 TQLSGGQKQRIAIARALVRQPHILLLDEATSALDTES 1202
Cdd:PRK11819 162 TKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES 198
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1043-1254 |
3.34e-07 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 54.62 E-value: 3.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1043 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIKQLNVQWLRAHlGIV------SQEPILFD 1116
Cdd:PRK10762 266 PGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDGLAN-GIVyisedrKRDGLVLG 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1117 CSIAENI---AYGDNSRVVSHeeIVKAAKEANIHQFIDSLPEKYNTRVGDKGtQLSGGQKQRIAIARALVRQPHILLLDE 1193
Cdd:PRK10762 345 MSVKENMsltALRYFSRAGGS--LKHADEQQAVSDFIRLFNIKTPSMEQAIG-LLSGGNQQKVAIARGLMTRPKVLILDE 421
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 25453402 1194 ATSALDTESEKVVQEALDKAR-EGRTCIVIAHRLSTIQN-ADLIVVIQNGQV-----KEHGTHQQLLA 1254
Cdd:PRK10762 422 PTRGVDVGAKKEIYQLINQFKaEGLSIILVSSEMPEVLGmSDRILVMHEGRIsgeftREQATQEKLMA 489
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
1141-1236 |
3.58e-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: 54.63 E-value: 3.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1141 AKEANIHQFIDSLPE---KYnTRVGDKGTQLSGGQKQRIAIARALVRQ---PHILLLDEATSALDTESEK----VVQEAL 1210
Cdd:TIGR00630 801 EAVPSISRKLQTLCDvglGY-IRLGQPATTLSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLHFDDIKklleVLQRLV 879
|
90 100
....*....|....*....|....*.
gi 25453402 1211 DKareGRTCIVIAHRLSTIQNADLIV 1236
Cdd:TIGR00630 880 DK---GNTVVVIEHNLDVIKTADYII 902
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
113-333 |
3.59e-07 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350055 [Multi-domain] Cd Length: 294 Bit Score: 53.37 E-value: 3.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 113 IGAGVLIVAYIQVSLWCL-------AAGRQIHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLtDDVSKINEGIGDKIGMF 185
Cdd:cd18782 44 IGVVMLVAALLEAVLTALrtylftdTANRIDLELGGTIIDHLLRLPLGFFDKRPVGELSTRI-SELDTIRGFLTGTALTT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 186 FQAMATFFGGFIIGFTRGWKLTLVILAISPVLGLSAGIWAKILSSFTDKELQAYAKAGAVAEEVLAAIRTVIAfggQKKE 265
Cdd:cd18782 123 LLDVLFSVIYIAVLFSYSPLLTLVVLATVPLQLLLTFLFGPILRRQIRRRAEASAKTQSYLVESLTGIQTVKA---QNAE 199
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 25453402 266 L-------ERYNNNLEEAKRLGIKKAITANISmgaaFLLIYASYALAFWYGTSLVISKEYTIGQVLTvfFSVLIG 333
Cdd:cd18782 200 LkarwrwqNRYARSLGEGFKLTVLGTTSGSLS----QFLNKLSSLLVLWVGAYLVLRGELTLGQLIA--FRILSG 268
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
745-972 |
4.61e-07 |
|
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: 52.86 E-value: 4.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 745 NLFSLLFLILGIISFITFFLQGFTFGKAGEILTKRLRYMVFKSMLRQDISWFDdpKNTTGALTTRLANDAAQVKGA-TGS 823
Cdd:cd18545 40 LIIALLFLALNLVNWVASRLRIYLMAKVGQRILYDLRQDLFSHLQKLSFSFFD--SRPVGKILSRVINDVNSLSDLlSNG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 824 RLAVITQNIANLGTgIIISLIYGWQLTLLLLAIVPIIAIAgvveMKMLSGQALKDKKELegSGKIAT------EAIENFR 897
Cdd:cd18545 118 LINLIPDLLTLVGI-VIIMFSLNVRLALVTLAVLPLLVLV----VFLLRRRARKAWQRV--RKKISNlnaylhESISGIR 190
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 25453402 898 TVVSLTREQK-FETMyaQSLQIPYRNA-LKKAHVFGITFSFTQAMMYFSYAACFRFGAYLVARELMTFeNVLLVFSA 972
Cdd:cd18545 191 VIQSFAREDEnEEIF--DELNRENRKAnMRAVRLNALFWPLVELISALGTALVYWYGGKLVLGGAITV-GVLVAFIG 264
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
409-581 |
4.86e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 54.04 E-value: 4.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 409 VKSGQTVALVGNSGCGKSTTVQLLQRLYDP----IEGEVSIDgqdirtiNVryLREIIGVVSQEpvLFATTIAENIRYGR 484
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSGELIPnlgdYEEEPSWD-------EV--LKRFRGTELQN--YFKKLYNGEIKVVH 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 485 ENVTMDEIEKAVKeANAYDFIMKLPH--KFDTLVGERG---------AQLSGGQKQRIAIARALVRNPKILLLDEATSAL 553
Cdd:PRK13409 165 KPQYVDLIPKVFK-GKVRELLKKVDErgKLDEVVERLGlenildrdiSELSGGELQRVAIAAALLRDADFYFFDEPTSYL 243
|
170 180
....*....|....*....|....*...
gi 25453402 554 DTESEAVVQAALDKAREGRTTIVIAHRL 581
Cdd:PRK13409 244 DIRQRLNVARLIRELAEGKYVLVVEHDL 271
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
1028-1199 |
5.13e-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: 51.49 E-value: 5.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1028 KFNGVMFNYPTRPNIPVLQGLSLEVKKGQTLALVGSSGCGKST----VVQLLERFYDPmAGTVFLDGKEIKQLNVQWlRA 1103
Cdd:cd03233 6 WRNISFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTllkaLANRTEGNVSV-EGDIHYNGIPYKEFAEKY-PG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1104 HLGIVSQEpilfDCSIAEniaygdnsrvVSHEEIVKAAKEANIHQFIdslpekyntrvgdKGtqLSGGQKQRIAIARALV 1183
Cdd:cd03233 84 EIIYVSEE----DVHFPT----------LTVRETLDFALRCKGNEFV-------------RG--ISGGERKRVSIAEALV 134
|
170
....*....|....*.
gi 25453402 1184 RQPHILLLDEATSALD 1199
Cdd:cd03233 135 SRASVLCWDNSTRGLD 150
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
1051-1235 |
5.26e-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: 54.02 E-value: 5.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1051 EVKKGQTLALVGSSGCGKSTVVQLLerfydpmAGTVFLDGKEI-KQLNV----QWL--------RAHLGIVSQEPilFDC 1117
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKIL-------AGVLKPDEGEVdEDLKIsykpQYIspdydgtvEEFLRSANTDD--FGS 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1118 SIAEniaygdnsrvvshEEIVKAAKeanihqfIDSLPEKYntrVGDkgtqLSGGQKQRIAIARALVRQPHILLLDEATSA 1197
Cdd:COG1245 433 SYYK-------------TEIIKPLG-------LEKLLDKN---VKD----LSGGELQRVAIAACLSRDADLYLLDEPSAH 485
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 25453402 1198 LDTESEKVVQEALDKAREGR--TCIVIAHRLSTIqnaDLI 1235
Cdd:COG1245 486 LDVEQRLAVAKAIRRFAENRgkTAMVVDHDIYLI---DYI 522
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
406-626 |
6.73e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 53.38 E-value: 6.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 406 NLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQdirTINVRYLREII--GVV------SQEPVLFATTIA 477
Cdd:PRK11288 273 SFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGK---PIDIRSPRDAIraGIMlcpedrKAEGIIPVHSVA 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 478 ENIRYG--RENVTMDEIEKAVKEA-NAYDFIMKL----PHKfDTLVGergaQLSGGQKQRIAIARALVRNPKILLLDEAT 550
Cdd:PRK11288 350 DNINISarRHHLRAGCLINNRWEAeNADRFIRSLniktPSR-EQLIM----NLSGGNQQKAILGRWLSEDMKVILLDEPT 424
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 25453402 551 SALDTESEAVVQAAL-DKAREGRTTIVIAHRLSTVRN-ADVIAGFDGGVIVEQGNHDELMREKGIyfKLVMTQTAGNE 626
Cdd:PRK11288 425 RGIDVGAKHEIYNVIyELAAQGVAVLFVSSDLPEVLGvADRIVVMREGRIAGELAREQATERQAL--SLALPRTSAAV 500
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
384-562 |
8.11e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 53.71 E-value: 8.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 384 LEFKNIHFSYPSRKdvQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVsidgqdIRTINVRylreiIG 463
Cdd:PLN03073 509 ISFSDASFGYPGGP--LLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTV------FRSAKVR-----MA 575
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 464 VVSQEPVLFATTIAENIRYgrenvtMDEIEKAVKEanaydfiMKLPHKFDT--LVGERGAQ----LSGGQKQRIAIARAL 537
Cdd:PLN03073 576 VFSQHHVDGLDLSSNPLLY------MMRCFPGVPE-------QKLRAHLGSfgVTGNLALQpmytLSGGQKSRVAFAKIT 642
|
170 180
....*....|....*....|....*.
gi 25453402 538 VRNPKILLLDEATSALDTES-EAVVQ 562
Cdd:PLN03073 643 FKKPHILLLDEPSNHLDLDAvEALIQ 668
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
384-554 |
1.03e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 53.01 E-value: 1.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 384 LEFKNIHFSYPSRKDVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYD-PIEGEVSIDGQDIRTINVR-YLREI 461
Cdd:PRK13549 260 LEVRNLTAWDPVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGKPVKIRNPQqAIAQG 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 462 IGVVSQE-------PVLfatTIAENI------RYGRENVtmdeIEKAVKEANAYDFIMKLPHKFDTLVgERGAQLSGGQK 528
Cdd:PRK13549 340 IAMVPEDrkrdgivPVM---GVGKNItlaaldRFTGGSR----IDDAAELKTILESIQRLKVKTASPE-LAIARLSGGNQ 411
|
170 180
....*....|....*....|....*.
gi 25453402 529 QRIAIARALVRNPKILLLDEATSALD 554
Cdd:PRK13549 412 QKAVLAKCLLLNPKILILDEPTRGID 437
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1049-1211 |
1.10e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 53.03 E-value: 1.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1049 SLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKeikqLNVQWL---RAHLgivsqEPilfDCSIAENIAY 1125
Cdd:PRK11147 339 SAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTK----LEVAYFdqhRAEL-----DP---EKTVMDNLAE 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1126 GDnsrvvshEEIVKAAKEANIHQFI-DSL--PEKYNTRVgdkgTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTES 1202
Cdd:PRK11147 407 GK-------QEVMVNGRPRHVLGYLqDFLfhPKRAMTPV----KALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVET 475
|
....*....
gi 25453402 1203 EKVVQEALD 1211
Cdd:PRK11147 476 LELLEELLD 484
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
391-579 |
1.43e-06 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 52.48 E-value: 1.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 391 FSYPS-RKDvqiLKGLNLKVKSGQ-----TVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDgqdirtINVRYLREIIGV 464
Cdd:COG1245 342 VEYPDlTKS---YGGFSLEVEGGEiregeVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDED------LKISYKPQYISP 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 465 VSQEPV--LFATTIAENIRYGRENVtmdEIEKAvkeanaydfiMKLPHKFDTLVGErgaqLSGGQKQRIAIARALVRNPK 542
Cdd:COG1245 413 DYDGTVeeFLRSANTDDFGSSYYKT---EIIKP----------LGLEKLLDKNVKD----LSGGELQRVAIAACLSRDAD 475
|
170 180 190
....*....|....*....|....*....|....*....
gi 25453402 543 ILLLDEATSALDTESEAVVQAALDKAREGR--TTIVIAH 579
Cdd:COG1245 476 LYLLDEPSAHLDVEQRLAVAKAIRRFAENRgkTAMVVDH 514
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
745-862 |
1.58e-06 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349994 [Multi-domain] Cd Length: 294 Bit Score: 51.33 E-value: 1.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 745 NLFSLLFLILGIISFITFFLQGFTFGKAGEILTKRLRYMVFKSMLRQDISWFDDPKntTGALTTRLANDAAQVKGATGSR 824
Cdd:cd18550 39 VLLALGMVAVAVASALLGVVQTYLSARIGQGVMYDLRVQLYAHLQRMSLAFFTRTR--TGEIQSRLNNDVGGAQSVVTGT 116
|
90 100 110
....*....|....*....|....*....|....*...
gi 25453402 825 LAVITQNIANLGTGIIISLIYGWQLTLLLLAIVPIIAI 862
Cdd:cd18550 117 LTSVVSNVVTLVATLVAMLALDWRLALLSLVLLPLFVL 154
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1044-1210 |
1.80e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 52.48 E-value: 1.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1044 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLdGKEIK-----QLNVQWLRAhlgivSQEPIlfdcs 1118
Cdd:PRK10636 327 ILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL-AKGIKlgyfaQHQLEFLRA-----DESPL----- 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1119 iaeniaygdnsrvvshEEIVKAAKEANIHQFIDSLpEKYNTRvGDKGT----QLSGGQKQRIAIARALVRQPHILLLDEA 1194
Cdd:PRK10636 396 ----------------QHLARLAPQELEQKLRDYL-GGFGFQ-GDKVTeetrRFSGGEKARLVLALIVWQRPNLLLLDEP 457
|
170
....*....|....*.
gi 25453402 1195 TSALDTESEKVVQEAL 1210
Cdd:PRK10636 458 TNHLDLDMRQALTEAL 473
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
1062-1235 |
1.94e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 49.87 E-value: 1.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1062 GSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIKQLNVQWLRAhlgIVSQEPILFDCSIAENIAYGdnSRVVSHEEIVKAA 1141
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPYCTY---IGHNLGLKLEMTVFENLKFW--SEIYNSAETLYAA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1142 keanIHQFidslpeKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALD-KAREGRTCI 1220
Cdd:PRK13541 108 ----IHYF------KLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLIVmKANSGGIVL 177
|
170
....*....|....*
gi 25453402 1221 VIAHRLSTIQNADLI 1235
Cdd:PRK13541 178 LSSHLESSIKSAQIL 192
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
368-611 |
3.24e-06 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 51.32 E-value: 3.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 368 DSFSKSGHKPDNIQGN--LEFKNIhfsypSRKDVQILKGLNLKVKSGQTVALVGNSGCGKSttvQLLQRLY--DPI-EGE 442
Cdd:PRK09700 248 NRFNAMKENVSNLAHEtvFEVRNV-----TSRDRKKVRDISFSVCRGEILGFAGLVGSGRT---ELMNCLFgvDKRaGGE 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 443 VSIDGQDIrTINVRY--LREIIGVVSQ---EPVLFAT-TIAENI------RYGRENVTM----DEIEKAVKEANAYDFIM 506
Cdd:PRK09700 320 IRLNGKDI-SPRSPLdaVKKGMAYITEsrrDNGFFPNfSIAQNMaisrslKDGGYKGAMglfhEVDEQRTAENQRELLAL 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 507 KLpHKFDTLVGErgaqLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDK-AREGRTTIVIAHRLSTVR 585
Cdd:PRK09700 399 KC-HSVNQNITE----LSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQlADDGKVILMVSSELPEII 473
|
250 260
....*....|....*....|....*...
gi 25453402 586 NA-DVIAGFDGGVIVEQ-GNHDELMREK 611
Cdd:PRK09700 474 TVcDRIAVFCEGRLTQIlTNRDDMSEEE 501
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
1149-1248 |
3.34e-06 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 48.86 E-value: 3.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1149 FIDSLPEKYNT-----RVGDKGTQLSGGQKQRIAIARALVRQPH--ILLLDEATSALDTESEKVVQEALDKAR-EGRTCI 1220
Cdd:cd03238 64 FIDQLQFLIDVglgylTLGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLIdLGNTVI 143
|
90 100
....*....|....*....|....*...
gi 25453402 1221 VIAHRLSTIQNADLIVVIQNGQVKEHGT 1248
Cdd:cd03238 144 LIEHNLDVLSSADWIIDFGPGSGKSGGK 171
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
384-606 |
3.52e-06 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 51.09 E-value: 3.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 384 LEFKNIHFSYPSRkdvQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIdGQDIRTINVRYLREIIg 463
Cdd:TIGR03719 323 IEAENLTKAFGDK---LLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETVKLAYVDQSRDAL- 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 464 vvsqEPvlfATTIAENIRYGrenvtMDEIEKAVKEANAYDFIMKLPHKF---DTLVGergaQLSGGQKQRIAIARALVRN 540
Cdd:TIGR03719 398 ----DP---NKTVWEEISGG-----LDIIKLGKREIPSRAYVGRFNFKGsdqQKKVG----QLSGGERNRVHLAKTLKSG 461
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 541 PKILLLDEATSALDTES-EAVVQAALDKAreGrTTIVIAH-RLSTVRNADVIAGFDGGVIVE--QGNHDE 606
Cdd:TIGR03719 462 GNVLLLDEPTNDLDVETlRALEEALLNFA--G-CAVVISHdRWFLDRIATHILAFEGDSHVEwfEGNFSE 528
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
523-602 |
4.78e-06 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 48.47 E-value: 4.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 523 LSGGQKQRIAIARALVRNPK--ILLLDEATSALDTESEAVVQAALDKAR-EGRTTIVIAHRLSTVRNADVI------AGF 593
Cdd:cd03238 88 LSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLIdLGNTVILIEHNLDVLSSADWIidfgpgSGK 167
|
....*....
gi 25453402 594 DGGVIVEQG 602
Cdd:cd03238 168 SGGKVVFSG 176
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
397-637 |
5.17e-06 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 49.43 E-value: 5.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 397 KDVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQ-DIRTINVRYLREIIGVvsqepvlfatt 475
Cdd:PRK13546 35 KTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEvSVIAISAGLSGQLTGI----------- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 476 iaENIRYGR--ENVTMDEIEKAVKEANAY----DFIMKLPHKFdtlvgergaqlSGGQKQRIAIARALVRNPKILLLDEA 549
Cdd:PRK13546 104 --ENIEFKMlcMGFKRKEIKAMTPKIIEFselgEFIYQPVKKY-----------SSGMRAKLGFSINITVNPDILVIDEA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 550 TSALDtesEAVVQAALDKARE----GRTTIVIAHRLSTVRN-ADVIAGFDGGVIVEQGNHDELMREKGIYFKLVMTQTAG 624
Cdd:PRK13546 171 LSVGD---QTFAQKCLDKIYEfkeqNKTIFFVSHNLGQVRQfCTKIAWIEGGKLKDYGELDDVLPKYEAFLNDFKKKSKA 247
|
250
....*....|...
gi 25453402 625 NEIELGNEACESK 637
Cdd:PRK13546 248 EQKEFRNKLDESR 260
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1038-1245 |
6.89e-06 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 50.17 E-value: 6.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1038 TRPNIPVLQGLSLEVKKGQTLALVGSSGCGKStvvQLLERFY--DPMA-GTVFLDGKEIKQLN-VQWLRAHLGIVSQ--- 1110
Cdd:PRK09700 272 TSRDRKKVRDISFSVCRGEILGFAGLVGSGRT---ELMNCLFgvDKRAgGEIRLNGKDISPRSpLDAVKKGMAYITEsrr 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1111 EPILF-DCSIAENIA---------YGDNSRVVSHEEIVKAAKEANihqfiDSLPEKYNTrVGDKGTQLSGGQKQRIAIAR 1180
Cdd:PRK09700 349 DNGFFpNFSIAQNMAisrslkdggYKGAMGLFHEVDEQRTAENQR-----ELLALKCHS-VNQNITELSGGNQQKVLISK 422
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 25453402 1181 ALVRQPHILLLDEATSALDTESEKVVQEALDK-AREGRTCIVIAHRLSTIQNA-DLIVVIQNGQVKE 1245
Cdd:PRK09700 423 WLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQlADDGKVILMVSSELPEIITVcDRIAVFCEGRLTQ 489
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
405-609 |
1.24e-05 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 49.28 E-value: 1.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 405 LNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRTINVR--------YL---REIIGVVSQEPVLFA 473
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAqrlarglvYLpedRQSSGLYLDAPLAWN 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 474 T-TIAEN-----IRYGRENVTMDEIEKAVKeanaydfiMKLPHKfDTLVGergaQLSGGQKQRIAIARALVRNPKILLLD 547
Cdd:PRK15439 362 VcALTHNrrgfwIKPARENAVLERYRRALN--------IKFNHA-EQAAR----TLSGGNQQKVLIAKCLEASPQLLIVD 428
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 25453402 548 EATSALDTESEA-VVQAALDKAREGRTTIVIAHRLSTVRN-ADVIAGFDGGVIV-----EQGNHDELMR 609
Cdd:PRK15439 429 EPTRGVDVSARNdIYQLIRSIAAQNVAVLFISSDLEEIEQmADRVLVMHQGEISgaltgAAINVDTIMR 497
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
419-590 |
1.37e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 47.17 E-value: 1.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 419 GNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRTInvrylreiigvvsQEPvlFATTIAENIRYGRENVTMDEIEKAVKE 498
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNI-------------AKP--YCTYIGHNLGLKLEMTVFENLKFWSEI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 499 ANAYDFIMKLPH--KFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALD-KAREGRTTI 575
Cdd:PRK13541 98 YNSAETLYAAIHyfKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLIVmKANSGGIVL 177
|
170
....*....|....*
gi 25453402 576 VIAHRLSTVRNADVI 590
Cdd:PRK13541 178 LSSHLESSIKSAQIL 192
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
480-596 |
1.37e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 49.83 E-value: 1.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 480 IRYGRENVTmDEIEKAVKEANayDFIMKLPH---KFDTL---------VGERGAQLSGGQKQRIAIARAL---VRNPKIL 544
Cdd:PRK00635 758 VRYKGKNIA-DILEMTAYEAE--KFFLDEPSiheKIHALcslgldylpLGRPLSSLSGGEIQRLKLAYELlapSKKPTLY 834
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 25453402 545 LLDEATSALDTES-EAVVQAALDKAREGRTTIVIAHRLSTVRNADVIA--GFDGG 596
Cdd:PRK00635 835 VLDEPTTGLHTHDiKALIYVLQSLTHQGHTVVIIEHNMHVVKVADYVLelGPEGG 889
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
1128-1242 |
1.50e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 49.72 E-value: 1.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1128 NSRVVSHEEIVKAAKEANIHQFIDSLPEKYNTRVGD---KGtqLSGGQKQRIAIARALVRQPHILLLDEATSALDTESek 1204
Cdd:TIGR00956 169 QNRPDGVSREEYAKHIADVYMATYGLSHTRNTKVGNdfvRG--VSGGERKRVSIAEASLGGAKIQCWDNATRGLDSAT-- 244
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 25453402 1205 vvqeALDKAREGRTCIVIAHRLSTI------QNA----DLIVVIQNGQ 1242
Cdd:TIGR00956 245 ----ALEFIRALKTSANILDTTPLVaiyqcsQDAyelfDKVIVLYEGY 288
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
409-595 |
1.78e-05 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 46.80 E-value: 1.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 409 VKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGqdirtinvrylreiigvvsqepvlfattiaenirygrenvt 488
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDG----------------------------------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 489 mdeIEKAVKeanaydfimklPHKFDtlvgergaqLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDKA 568
Cdd:cd03222 61 ---ITPVYK-----------PQYID---------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRL 117
|
170 180 190
....*....|....*....|....*....|
gi 25453402 569 RE--GRTTIVIAHRLSTVRN-ADVIAGFDG 595
Cdd:cd03222 118 SEegKKTALVVEHDLAVLDYlSDRIHVFEG 147
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1044-1228 |
1.80e-05 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 48.78 E-value: 1.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1044 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLdGKEIKQLNVQWLRAHLgivsqEPilfDCSIAENI 1123
Cdd:TIGR03719 337 LIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETVKLAYVDQSRDAL-----DP---NKTVWEEI 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1124 AYGdnsrvvsHEEIVKAAKEANIHQFIDSlpekYNTRVGD---KGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDT 1200
Cdd:TIGR03719 408 SGG-------LDIIKLGKREIPSRAYVGR----FNFKGSDqqkKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDV 476
|
170 180 190
....*....|....*....|....*....|....
gi 25453402 1201 ESEKVVQEALDKAreGRTCIVIAH------RLST 1228
Cdd:TIGR03719 477 ETLRALEEALLNF--AGCAVVISHdrwfldRIAT 508
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
378-554 |
1.95e-05 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 48.85 E-value: 1.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 378 DNIQGNLEFKNIHFSYPSRKDVqilkglNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRTIN--- 454
Cdd:PRK10762 250 DKAPGEVRLKVDNLSGPGVNDV------SFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSpqd 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 455 -----VRYLRE-------IIGV-VSQEPVLFA----TTIAENIRYGRENVTMDeiekavkeanayDFIM----KLPHKfD 513
Cdd:PRK10762 324 glangIVYISEdrkrdglVLGMsVKENMSLTAlryfSRAGGSLKHADEQQAVS------------DFIRlfniKTPSM-E 390
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 25453402 514 TLVGErgaqLSGGQKQRIAIARALVRNPKILLLDEATSALD 554
Cdd:PRK10762 391 QAIGL----LSGGNQQKVAIARGLMTRPKVLILDEPTRGVD 427
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
398-610 |
2.19e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 48.47 E-value: 2.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 398 DVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRTINVRYLREIigvVSQEpvlfattia 477
Cdd:PRK10938 15 DTKTLQLPSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQLQKL---VSDE--------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 478 enirYGRENVTM---DE----------IEKAVKEANAYDFIMKLPHkFDTLVGERGAQLSGGQKQRIAIARALVRNPKIL 544
Cdd:PRK10938 83 ----WQRNNTDMlspGEddtgrttaeiIQDEVKDPARCEQLAQQFG-ITALLDRRFKYLSTGETRKTLLCQALMSEPDLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 25453402 545 LLDEATSALDTESEAVVQAALDK-AREGRTTIVIAHRLSTVRN-ADVIAGFDGGVIVEQGNHDELMRE 610
Cdd:PRK10938 158 ILDEPFDGLDVASRQQLAELLASlHQSGITLVLVLNRFDEIPDfVQFAGVLADCTLAETGEREEILQQ 225
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
384-577 |
2.24e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 48.63 E-value: 2.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 384 LEFKNIHFSYPSRKDVQILKGLNLKVKSGQTVALVGNSGCGKS-TTVQLLQRLYDP-IEGEVSIDGQDIRTINVR----- 456
Cdd:NF040905 258 FEVKNWTVYHPLHPERKVVDDVSLNVRRGEIVGIAGLMGAGRTeLAMSVFGRSYGRnISGTVFKDGKEVDVSTVSdaida 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 457 ---YL---REIIGVVSQEPVLFATTIAENIRYGRENVtMDEIEKaVKEANAY--DFIMKLPHkfdtlVGERGAQLSGGQK 528
Cdd:NF040905 338 glaYVtedRKGYGLNLIDDIKRNITLANLGKVSRRGV-IDENEE-IKVAEEYrkKMNIKTPS-----VFQKVGNLSGGNQ 410
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 25453402 529 QRIAIARALVRNPKILLLDEATSALDT----ESEAVVQaalDKAREGRTTIVI 577
Cdd:NF040905 411 QKVVLSKWLFTDPDVLILDEPTRGIDVgakyEIYTIIN---ELAAEGKGVIVI 460
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
398-612 |
3.39e-05 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 47.81 E-value: 3.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 398 DVQILKGLNLKVKSGQTVALVGNSGCGKSTTVqLLQRLYDPIEGEVSIDGQdIRTINVRYLREIIGVvsQEPVLFATTIA 477
Cdd:NF000106 25 EVKAVDGVDLDVREGTVLGVLGP*GAA**RGA-LPAHV*GPDAGRRPWRF*-TWCANRRALRRTIG*--HRPVR*GRRES 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 478 ENiryGRENVTM--DEIEKAVKEANAYDFIMKLPHKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDT 555
Cdd:NF000106 101 FS---GRENLYMigR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDP 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 25453402 556 ESE-AVVQAALDKAREGRTTIVIAHRLSTVRN-ADVIAGFDGGVIVEQGNHDELMREKG 612
Cdd:NF000106 178 RTRnEVWDEVRSMVRDGATVLLTTQYMEEAEQlAHELTVIDRGRVIADGKVDELKTKVG 236
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
1168-1248 |
4.00e-05 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 45.64 E-value: 4.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1168 LSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTIQNADLIVVIQNGQVKE 1245
Cdd:cd03222 72 LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEegKKTALVVEHDLAVLDYLSDRIHVFEGEPGV 151
|
...
gi 25453402 1246 HGT 1248
Cdd:cd03222 152 YGI 154
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1167-1254 |
4.73e-05 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 47.10 E-value: 4.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1167 QLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTI-QNADLIVVIQNGQV 1243
Cdd:PRK15093 158 ELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQnnNTTILLISHDLQMLsQWADKINVLYCGQT 237
|
90
....*....|.
gi 25453402 1244 KEHGTHQQLLA 1254
Cdd:PRK15093 238 VETAPSKELVT 248
|
|
| ABC_6TM_VMR1_D2_like |
cd18604 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
107-223 |
5.32e-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: 46.69 E-value: 5.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 107 AYY---YTGIGAGVLIVAYIQVSLWC---LAAGRQIHkirQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINEGIGD 180
Cdd:cd18604 43 LYYlgiYALISLLSVLLGTLRYLLFFfgsLRASRKLH---ERLLHSVLRAPLRWLDTTPVGRILNRFSKDIETIDSELAD 119
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 25453402 181 KIGMFFQAMATFFGGFIigftrgwkltlVILAISPVLGLSAGI 223
Cdd:cd18604 120 SLSSLLESTLSLLVILI-----------AIVVVSPAFLLPAVV 151
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
1044-1241 |
6.68e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 47.41 E-value: 6.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1044 VLQGLSLEVKKGQTLALVGSSGCGKSTvvqLLERFYDPMAGTVFLDGKEI---KQLNVQWLRAhLGIVSQEPI-LFDCSI 1119
Cdd:TIGR00956 778 ILNNVDGWVKPGTLTALMGASGAGKTT---LLNVLAERVTTGVITGGDRLvngRPLDSSFQRS-IGYVQQQDLhLPTSTV 853
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1120 AENIAYgdNSRVVSHEEIVKAAKEANIHQFIDSLP-EKY-NTRVGDKGTQLSGGQKQRIAIARALVRQPHILL-LDEATS 1196
Cdd:TIGR00956 854 RESLRF--SAYLRQPKSVSKSEKMEYVEEVIKLLEmESYaDAVVGVPGEGLNVEQRKRLTIGVELVAKPKLLLfLDEPTS 931
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 25453402 1197 ALDTESEKVVQEALDK-AREGRTCIVIAHRLSTI--QNADLIVVIQNG 1241
Cdd:TIGR00956 932 GLDSQTAWSICKLMRKlADHGQAILCTIHQPSAIlfEEFDRLLLLQKG 979
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
522-593 |
7.18e-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: 44.66 E-value: 7.18e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 25453402 522 QLSGGQKQRIAIARAL----VRNPKILLLDEATSALDTES-EAVVQAALDKAREGRTTIVIAHRLSTVRNADVIAGF 593
Cdd:cd03227 77 QLSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDgQALAEAILEHLVKGAQVIVITHLPELAELADKLIHI 153
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
1160-1236 |
9.03e-05 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 46.99 E-value: 9.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1160 RVGDKGTQLSGGQKQRIAIARALVRQPH---ILLLDEATSALDTES----EKVVQEALDKareGRTCIVIAHRLSTIQNA 1232
Cdd:PRK00349 823 KLGQPATTLSGGEAQRVKLAKELSKRSTgktLYILDEPTTGLHFEDirklLEVLHRLVDK---GNTVVVIEHNLDVIKTA 899
|
....
gi 25453402 1233 DLIV 1236
Cdd:PRK00349 900 DWII 903
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
707-963 |
9.11e-05 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350055 [Multi-domain] Cd Length: 294 Bit Score: 46.05 E-value: 9.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 707 VFCAIINGGLQPAFSIIFSKVVGVFtkndtpeIQRQNSN-LFSLLFLILGIISFITFF--LQGFTFGKAGEILTKRLRYM 783
Cdd:cd18782 8 LALSFVVQLLGLANPLLFQVIIDKV-------LVQQDLAtLYVIGVVMLVAALLEAVLtaLRTYLFTDTANRIDLELGGT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 784 VFKSMLRQDISWFDdpKNTTGALTTRLaNDAAQVKG-ATGSRLAVITQNIANLGTgIIISLIYGWQLTLLLLAIVPIIAI 862
Cdd:cd18782 81 IIDHLLRLPLGFFD--KRPVGELSTRI-SELDTIRGfLTGTALTTLLDVLFSVIY-IAVLFSYSPLLTLVVLATVPLQLL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 863 AGVVEMKMLSGQaLKDKKELEGSGKIA-TEAIENFRTVVSLTRE----QKFETMYAQSLQIPYrnalkKAHVFGITFSFT 937
Cdd:cd18782 157 LTFLFGPILRRQ-IRRRAEASAKTQSYlVESLTGIQTVKAQNAElkarWRWQNRYARSLGEGF-----KLTVLGTTSGSL 230
|
250 260
....*....|....*....|....*..
gi 25453402 938 QAMM-YFSYAACFRFGAYLVARELMTF 963
Cdd:cd18782 231 SQFLnKLSSLLVLWVGAYLVLRGELTL 257
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
1167-1224 |
9.68e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 46.78 E-value: 9.68e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 25453402 1167 QLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKARegRTCIVIAH 1224
Cdd:PLN03073 344 TFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWP--KTFIVVSH 399
|
|
| ABC_6TM_CvaB_RaxB_like |
cd18567 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ... |
204-329 |
1.14e-04 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 secretion systems, CvaB and RaxB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the peptidase-containing ABC transporter subunit of T1SS (Type 1 secretion systems), such as Escherichia coli colicin V secretion/processing ATP-binding protein CvaB and putative ABC transporter RaxB. These ABC-transporter proteins carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion. RaxB is part of the T1SS RaxABC, which is responsible for the type 1-dependent secretion of the bacterial quorum-sensing molecule AvrXa21. Both CvaB and RaxB belong to a subgroup of T1SS ABC transporters that contain a C39 peptidase domain. T1SS are found in pathogenic Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium.
Pssm-ID: 350011 [Multi-domain] Cd Length: 294 Bit Score: 45.53 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 204 WKLTLVILAISPVLGLSAGIWAKILSSFTDKELQAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNNNLEEAKRLGIKK 283
Cdd:cd18567 141 PKLALIVLAAVALYALLRLALYPPLRRATEEQIVASAKEQSHFLETIRGIQTIKLFGREAEREARWLNLLVDAINADIRL 220
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 25453402 284 AITANISMGAAFLLIYASYALAFWYGTSLVISKEYTIGqVLTVFFS 329
Cdd:cd18567 221 QRLQILFSAANGLLFGLENILVIYLGALLVLDGEFTVG-MLFAFLA 265
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
365-588 |
1.32e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 46.16 E-value: 1.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 365 PSIDSFSKSGHKPDNiQGNLEFKNIHFSYPSRKdvqILKGLNLKVKSGQTVALVGNSGCGKSTTVQLlqrlydpIEGE-- 442
Cdd:PRK10938 243 PEPDEPSARHALPAN-EPRIVLNNGVVSYNDRP---ILHNLSWQVNPGEHWQIVGPNGAGKSTLLSL-------ITGDhp 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 443 --VSID----------GQDIRTInvrylREIIGVVSQEPVL---FATTIAENIRYGrenvTMDEI--EKAVKEANaydfi 505
Cdd:PRK10938 312 qgYSNDltlfgrrrgsGETIWDI-----KKHIGYVSSSLHLdyrVSTSVRNVILSG----FFDSIgiYQAVSDRQ----- 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 506 MKLPHKFDTLVGERGAQ-------LSGGQkQRIA-IARALVRNPKILLLDEATSALDTESEAVVQAALDK-AREGRTTIV 576
Cdd:PRK10938 378 QKLAQQWLDILGIDKRTadapfhsLSWGQ-QRLAlIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVlISEGETQLL 456
|
250 260
....*....|....*....|....
gi 25453402 577 ------------IAHRLSTVRNAD 588
Cdd:PRK10938 457 fvshhaedapacITHRLEFVPDGD 480
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
1151-1257 |
1.35e-04 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 45.88 E-value: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1151 DSLPEKYN--TRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESE-KVVQEALDKAREGRTCIVIAHRLS 1227
Cdd:NF000106 126 DELLERFSltEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRnEVWDEVRSMVRDGATVLLTTQYME 205
|
90 100 110
....*....|....*....|....*....|.
gi 25453402 1228 TI-QNADLIVVIQNGQVKEHGTHQQLLAQKG 1257
Cdd:NF000106 206 EAeQLAHELTVIDRGRVIADGKVDELKTKVG 236
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
522-579 |
1.35e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 46.39 E-value: 1.35e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 25453402 522 QLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDKARegRTTIVIAH 579
Cdd:PLN03073 344 TFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWP--KTFIVVSH 399
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
501-614 |
1.44e-04 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 46.22 E-value: 1.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 501 AYDF---IMKLPHKFDTLV---------GERGAQLSGGQKQRIAIARALVRNP--KIL-LLDEATSALDTESEA----VV 561
Cdd:PRK00349 797 ALEFfeaIPKIARKLQTLVdvglgyiklGQPATTLSGGEAQRVKLAKELSKRStgKTLyILDEPTTGLHFEDIRklleVL 876
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 25453402 562 QAALDKareGRTTIVIAHRLSTVRNADVI------AGFDGGVIVEQGNHDELMREKGIY 614
Cdd:PRK00349 877 HRLVDK---GNTVVVIEHNLDVIKTADWIidlgpeGGDGGGEIVATGTPEEVAKVEASY 932
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
839-962 |
1.61e-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: 45.24 E-value: 1.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 839 IIISLIYGWQLTLLLLAIVPIIAIAGVV---EMKMLSGQALKDKKELEGSgkiATEAIENFRTVVSLTREQKF----ETM 911
Cdd:cd18568 133 LGLMFYYNLQLTLIVLAFIPLYVLLTLLsspKLKRNSREIFQANAEQQSF---LVEALTGIATIKALAAERPIrwrwENK 209
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 25453402 912 YAQSLQIPYRnALKKAHVFGITFSFtqaMMYFSYAACFRFGAYLVARELMT 962
Cdd:cd18568 210 FAKALNTRFR-GQKLSIVLQLISSL---INHLGTIAVLWYGAYLVISGQLT 256
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
1037-1222 |
1.65e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 45.94 E-value: 1.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1037 PTRPNIPVLQGLSLEVKKGQTLALVGSSGCGKS-TVVQLLERFYDP-MAGTVFLDGKEIKQLNVQWL-----------RA 1103
Cdd:NF040905 268 PLHPERKVVDDVSLNVRRGEIVGIAGLMGAGRTeLAMSVFGRSYGRnISGTVFKDGKEVDVSTVSDAidaglayvtedRK 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1104 HLGIVSQEPILFDCSIA--ENIAygdNSRVVSHEEIVKAAKEanihqFIDSLpekyNTR---VGDKGTQLSGGQKQRIAI 1178
Cdd:NF040905 348 GYGLNLIDDIKRNITLAnlGKVS---RRGVIDENEEIKVAEE-----YRKKM----NIKtpsVFQKVGNLSGGNQQKVVL 415
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 25453402 1179 ARALVRQPHILLLDEATSALDT----ESEKVVQEAldkAREGRTCIVI 1222
Cdd:NF040905 416 SKWLFTDPDVLILDEPTRGIDVgakyEIYTIINEL---AAEGKGVIVI 460
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
402-602 |
2.67e-04 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 43.79 E-value: 2.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 402 LKGLNLKVKSGQTVALVGNSGCGKSTTVqllqrlYDPIEGEvsidGQD--IRTINVrYLREIIGVVSQEPVLFAT----T 475
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLA------FDTIYAE----GQRryVESLSA-YARQFLGQMDKPDVDSIEglspA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 476 IAENIRYGRENV-----TMDEIekavkeanaYDFI------------------MKLPHkfdtLVGERGAQ-LSGGQKQRI 531
Cdd:cd03270 80 IAIDQKTTSRNPrstvgTVTEI---------YDYLrllfarvgirerlgflvdVGLGY----LTLSRSAPtLSGGEAQRI 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 532 AIARALVRNPK--ILLLDEATSALDTESEAVVQAALDKARE-GRTTIVIAHRLSTVRNADVI------AGFDGGVIVEQG 602
Cdd:cd03270 147 RLATQIGSGLTgvLYVLDEPSIGLHPRDNDRLIETLKRLRDlGNTVLVVEHDEDTIRAADHVidigpgAGVHGGEIVAQG 226
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
523-614 |
2.69e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 45.40 E-value: 2.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 523 LSGGQKQRIAIARALVR--NPKIL-LLDEATSALDTESEAVVQAALDKARE-GRTTIVIAHRLSTVRNAD-VI-----AG 592
Cdd:COG0178 827 LSGGEAQRVKLASELSKrsTGKTLyILDEPTTGLHFHDIRKLLEVLHRLVDkGNTVVVIEHNLDVIKTADwIIdlgpeGG 906
|
90 100
....*....|....*....|..
gi 25453402 593 FDGGVIVEQGNHDELMREKGIY 614
Cdd:COG0178 907 DGGGEIVAEGTPEEVAKVKASY 928
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
1161-1243 |
4.00e-04 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 44.84 E-value: 4.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1161 VGDKG-TQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEAL-DKAREGRTCIVIAHRLST-IQNA--DLI 1235
Cdd:PLN03140 1012 VGLPGvTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVrNTVDTGRTVVCTIHQPSIdIFEAfdELL 1091
|
....*...
gi 25453402 1236 VVIQNGQV 1243
Cdd:PLN03140 1092 LMKRGGQV 1099
|
|
| ABC_6TM_T1SS_like |
cd18779 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding ... |
187-335 |
4.88e-04 |
|
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: 43.69 E-value: 4.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 187 QAMATFF-GGFIIGFTrgwkltLVILAISP-----VLGLSAGIWAKILSSF------TDKELQAYAKAGAVAEEVLAAIR 254
Cdd:cd18779 118 QTLSALLdGTLVLGYL------ALLFAQSPllglvVLGLAALQVALLLATRrrvrelMARELAAQAEAQSYLVEALSGIE 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 255 TVIAFGGQKKELERYNNNLEEAKRLGIKKAITANISMGAAFLLIYASYALAFWYGTSLVISKEYTIGQVLTvfFSVLIGA 334
Cdd:cd18779 192 TLKASGAEDRALDRWSNLFVDQLNASLRRGRLDALVDALLATLRLAAPLVLLWVGAWQVLDGQLSLGTMLA--LNALAGA 269
|
.
gi 25453402 335 F 335
Cdd:cd18779 270 F 270
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
131-328 |
6.05e-04 |
|
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar proteins; This group represents the homodimeric bacterial ABC multidrug exporter Sav1866, which is homologous to the lipid flippase MsbA, and both of which are functionally related to the human P-glycoprotein multidrug transporter (ABCB1 or MDR1). This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 349998 [Multi-domain] Cd Length: 299 Bit Score: 43.56 E-value: 6.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 131 AAGRQIHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFFQAMATFFGGFIIGFTRGWKLTLVI 210
Cdd:cd18554 73 IANKILYDIRKDLFDHLQKLSLRYYANNRSGEIISRVINDVEQTKDFITTGLMNIWLDMITIIIAICIMLVLNPKLTFVS 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 211 LAISPVLGLSAGIWAKILSSFTDKELQAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNNNLEEAKRLGIKKAITANIS 290
Cdd:cd18554 153 LVIFPFYILAVKYFFGRLRKLTKERSQALAEVQGFLHERIQGMSVIKSFALEKHEQKQFDKRNGHFLTRALKHTRWNAKT 232
|
170 180 190
....*....|....*....|....*....|....*...
gi 25453402 291 MGAAFLLIYASYALAFWYGTSLVISKEYTIGQvLTVFF 328
Cdd:cd18554 233 FSAVNTITDLAPLLVIGFAAYLVIEGNLTVGT-LVAFV 269
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
523-578 |
6.23e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 43.95 E-value: 6.23e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 25453402 523 LSGGQKQRIAIARALVRNPKILLLDEATSALDTESE-AVVQAALDKAREGRTTIVIA 578
Cdd:PRK10982 392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKfEIYQLIAELAKKDKGIIIIS 448
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
740-973 |
6.77e-04 |
|
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: 43.27 E-value: 6.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 740 QRQNSNLFSLLFLILGIISFITFFLQGFTFGKAGEILTKRLRYMVFKSMLRQDISWFDdpKNTTGALTTRlANDAAQVKG 819
Cdd:cd18555 37 NLNLLNVLGIGILILFLLYGLFSFLRGYIIIKLQTKLDKSLMSDFFEHLLKLPYSFFE--NRSSGDLLFR-ANSNVYIRQ 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 820 ATGSRLAVITQNIANLGTGIIISLIYGWQLTLLLLAIVPIIAIAGVVEMKMLSGqalKDKKELEGSGK---IATEAIENF 896
Cdd:cd18555 114 ILSNQVISLIIDLLLLVIYLIYMLYYSPLLTLIVLLLGLLIVLLLLLTRKKIKK---LNQEEIVAQTKvqsYLTETLYGI 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 897 RTVVSLTREQKFET----MYAQSLQIpyrnALKKAHVFGITFSFTQAMMYFSYAACFRFGAYLVARELMTFeNVLLVFSA 972
Cdd:cd18555 191 ETIKSLGSEKNIYKkwenLFKKQLKA----FKKKERLSNILNSISSSIQFIAPLLILWIGAYLVINGELTL-GELIAFSS 265
|
.
gi 25453402 973 I 973
Cdd:cd18555 266 L 266
|
|
| ABC_6TM_AarD_CydDC_like |
cd18561 |
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and ... |
131-328 |
8.25e-04 |
|
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: 43.04 E-value: 8.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 131 AAGRQIHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFFQAMATFFGGFIIGFTRGWKLTLVI 210
Cdd:cd18561 63 AAQRVKQHLRRRLFAKLLKLGPGYLEGERTGELQTTVVDGVEALEAYYGRYLPQLLVALLGPLLILIYLFFLDPLVALIL 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 211 LAISPVLGLSAGIWAKILSSFTDKELQAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNNNLEEAKRLGIKKAITANIS 290
Cdd:cd18561 143 LVFALLIPLSPALWDRLAKDTGRRHWAAYGRLSAQFLDSLQGMTTLKAFGASKRRGNELAARAEDLRQATMKVLAVSLLS 222
|
170 180 190
....*....|....*....|....*....|....*...
gi 25453402 291 MGAAFLLIYASYALAFWYGTSLVISKEYTIGQVLTVFF 328
Cdd:cd18561 223 SGIMGLATALGTALALGVGALRVLGGQLTLSSLLLILF 260
|
|
| ABC_6TM_YOR1_D2_like |
cd18606 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ... |
754-862 |
8.81e-04 |
|
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC subfamily; This group includes the six-transmembrane domain 1 (TMD1) of the yeast Yor1p, an oligomycin resistance ABC transporter, and similar proteins. Members of this group belong to the MRP (multidrug resistance-associated protein) subfamily (ABCC). In addition to Yor1p, yeast ABCC (also termed MRP/CFTR) subfamily also comprises five other members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, and Vmr1p), which are not included in this group. Yor1p is a plasma membrane ATP-binding transporter that mediates export of many different organic anions including oligomycin. While Yor1p has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane.
Pssm-ID: 350050 [Multi-domain] Cd Length: 290 Bit Score: 42.85 E-value: 8.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 754 LGIISFITFFLQGFTFGKAGEILTKRLRYMVFKSMLRQDISWFDdpknTT--GALTTRLANDAAQVKGATGSRLAVITQN 831
Cdd:cd18606 44 LGVLQAIFLFLFGLLLAYLGIRASKRLHNKALKRVLRAPMSFFD----TTplGRILNRFSKDTDVLDNELPDSLRMFLYT 119
|
90 100 110
....*....|....*....|....*....|.
gi 25453402 832 IANLGTGIIISLIYgwqLTLLLLAIVPIIAI 862
Cdd:cd18606 120 LSSIIGTFILIIIY---LPWFAIALPPLLVL 147
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
1166-1236 |
1.06e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 43.48 E-value: 1.06e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 25453402 1166 TQLSGGQKQRIAIARALVR---QPHILLLDEATSALDTESEKVVQEALDKARE-GRTCIVIAHRLSTIQNADLIV 1236
Cdd:COG0178 825 TTLSGGEAQRVKLASELSKrstGKTLYILDEPTTGLHFHDIRKLLEVLHRLVDkGNTVVVIEHNLDVIKTADWII 899
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
1167-1236 |
1.29e-03 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 40.81 E-value: 1.29e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 25453402 1167 QLSGGQKQRIAIARALVRQPH----ILLLDEATSALDTESEKVVQEALDKAR-EGRTCIVIAHRLSTIQNADLIV 1236
Cdd:cd03227 77 QLSGGEKELSALALILALASLkprpLYILDEIDRGLDPRDGQALAEAILEHLvKGAQVIVITHLPELAELADKLI 151
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
522-608 |
1.79e-03 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 42.10 E-value: 1.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 522 QLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDKARE--GRTTIVIAHRLSTVRN-ADVIAGFDGGVI 598
Cdd:PRK15093 158 ELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQnnNTTILLISHDLQMLSQwADKINVLYCGQT 237
|
90
....*....|
gi 25453402 599 VEQGNHDELM 608
Cdd:PRK15093 238 VETAPSKELV 247
|
|
| PRK01889 |
PRK01889 |
GTPase RsgA; Reviewed |
1040-1075 |
1.93e-03 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234988 [Multi-domain] Cd Length: 356 Bit Score: 41.84 E-value: 1.93e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 25453402 1040 PNIPV-----LQGLSLEV-----KKGQTLALVGSSGCGKSTVV-QLL 1075
Cdd:PRK01889 170 PGVPVlavsaLDGEGLDVlaawlSGGKTVALLGSSGVGKSTLVnALL 216
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
383-590 |
2.14e-03 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 41.05 E-value: 2.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 383 NLEFKNIHfSYPSRKDVQILKGLNLkvksgqtvaLVGNSGCGKSTTVQLLqrlydpiegEVSIDGQ-DIRTINVRYLREI 461
Cdd:cd03240 3 KLSIRNIR-SFHERSEIEFFSPLTL---------IVGQNGAGKTTIIEAL---------KYALTGElPPNSKGGAHDPKL 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 462 IGVvsqepvlfATTIAEnIRYGRENVTMDEIeKAVKEANAYDFIMKLPH-KFDTLVGERGAQLSGGQKQ------RIAIA 534
Cdd:cd03240 64 IRE--------GEVRAQ-VKLAFENANGKKY-TITRSLAILENVIFCHQgESNWPLLDMRGRCSGGEKVlasliiRLALA 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 25453402 535 RALVRNPKILLLDEATSALDTESEAVVQAALDKAREG---RTTIVIAHRLSTVRNADVI 590
Cdd:cd03240 134 ETFGSNCGILALDEPTTNLDEENIEESLAEIIEERKSqknFQLIVITHDEELVDAADHI 192
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
406-608 |
2.99e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 41.80 E-value: 2.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 406 NLKVK--SGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDgqdirtINVRylreiIGVVSQEPVLFattiaENIRYg 483
Cdd:PRK15064 19 NISVKfgGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLD------PNER-----LGKLRQDQFAF-----EEFTV- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 484 RENVTM--DEIEKAVKEANA-Y-------DFIMK---LPHKF---DTLVGERGA-------------------QLSGGQK 528
Cdd:PRK15064 82 LDTVIMghTELWEVKQERDRiYalpemseEDGMKvadLEVKFaemDGYTAEARAgelllgvgipeeqhyglmsEVAPGWK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 529 QRIAIARALVRNPKILLLDEATSALDTESEAVVQAALdKAREGrTTIVIAH-R--LSTV--RNADViagfDGGVI-VEQG 602
Cdd:PRK15064 162 LRVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVL-NERNS-TMIIISHdRhfLNSVctHMADL----DYGELrVYPG 235
|
....*.
gi 25453402 603 NHDELM 608
Cdd:PRK15064 236 NYDEYM 241
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
1161-1265 |
3.56e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 41.74 E-value: 3.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453402 1161 VGDKGTQLSGGQKQRIAIARALV---RQPHILLLDEATSALDTESEKVVQEALDK-AREGRTCIVIAHRLSTIQNADLIV 1236
Cdd:PRK00635 1693 LGQNLSSLSLSEKIAIKIAKFLYlppKHPTLFLLDEIATSLDNQQKSALLVQLRTlVSLGHSVIYIDHDPALLKQADYLI 1772
|
90 100 110
....*....|....*....|....*....|..
gi 25453402 1237 VIQNGQVKEHGthqQLL---AQKGIYFSMVSV 1265
Cdd:PRK00635 1773 EMGPGSGKTGG---KILfsgPPKDISASKDSL 1801
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
1168-1236 |
7.75e-03 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 39.55 E-value: 7.75e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 25453402 1168 LSGGQKQRIAIARAL------VrqphILLLDEATSALDTESEKVVQEALDKARE-GRTCIVIAHRLSTIQNADLIV 1236
Cdd:cd03270 138 LSGGEAQRIRLATQIgsgltgV----LYVLDEPSIGLHPRDNDRLIETLKRLRDlGNTVLVVEHDEDTIRAADHVI 209
|
|
| |
