|
Name |
Accession |
Description |
Interval |
E-value |
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
39-632 |
1.21e-178 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 539.75 E-value: 1.21e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 39 LLTLFRYSdWQDKLFMFLGTLMAIAHGSGLPLMMIVFGEMTDKFVDNtGNFSLpvnfslsmlnpgrileeeMTRYAYYYS 118
Cdd:COG1132 9 LRRLLRYL-RPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAG-GDLSA------------------LLLLLLLLL 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 119 GLGGGVLVAAYIQVSFWTLAAGRQIKKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDDVSKISEGIGDKVGMFFQAIAT 198
Cdd:COG1132 69 GLALLRALLSYLQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVT 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 199 FFAGFIVGFIRGWKLTLVIMAISPILGLSTAVWAKILSTFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKELERYQK 278
Cdd:COG1132 149 LIGALVVLFVIDWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFRE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 279 HLENAKKIGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTIGNAMTVFFSILIGAFSVGQAAPCIDAFANAR 358
Cdd:COG1132 229 ANEELRRANLRAARLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRAL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 359 GAAYVIFDIIDNNPKIDSfSERGHKPDNIKGNLEFSDVHFSYPSraNIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQL 438
Cdd:COG1132 309 ASAERIFELLDEPPEIPD-PPGAVPLPPVRGEIEFENVSFSYPG--DRPVLKDISLTIPPGETVALVGPSGSGKSTLVNL 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 439 LQRLYDPTEGKISIDGQDIRNFNVRCLREIIGVVSQEPVLFSTTIAENIRYGRGNVTMDEIEKAVKEANAYDFIMKLPQK 518
Cdd:COG1132 386 LLRFYDPTSGRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDG 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 519 FDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTIRNADVIA 598
Cdd:COG1132 466 YDTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRIL 545
|
570 580 590
....*....|....*....|....*....|....
gi 338817954 599 GFEDGVIVEQGSHSELMKKEGIYFRLVNMQTAGS 632
Cdd:COG1132 546 VLDDGRIVEQGTHEELLARGGLYARLYRLQFGEE 579
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
30-1269 |
2.11e-178 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 566.97 E-value: 2.11e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 30 KKKKVNLIGLLTLFRYSDWQDKLFMFLGTLMAIAHGSGLPLMMIVFGEMTDKFvdNTGNFSLPVNFSLSMLnpgrileee 109
Cdd:PTZ00265 38 KKIKTQKIPFFLPFKCLPASHRKLLGVSFVCATISGGTLPFFVSVFGVIMKNM--NLGENVNDIIFSLVLI--------- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 110 mtryayyysglGGGVLVAAYIQVSFWTLAAGRQIKKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDDVSKISEGIGDKV 189
Cdd:PTZ00265 107 -----------GIFQFILSFISSFCMDVVTTKILKTLKLEFLKSVFYQDGQFHDNNPGSKLTSDLDFYLEQVNAGIGTKF 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 190 GMFFQAIATFFAGFIVGFIRGWKLTLVIMAISPILGLSTAVWAKILSTFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQ 269
Cdd:PTZ00265 176 ITIFTYASAFLGLYIWSLFKNARLTLCITCVFPLIYICGVICNKKVKINKKTSLLYNNNTMSIIEEALVGIRTVVSYCGE 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 270 NKELERYQKHLENAKKIGIKKAISANISMGIAFLLIYASYALAFWYGSTLVIS--------KEYTIGNAMTVFFSILIGA 341
Cdd:PTZ00265 256 KTILKKFNLSEKLYSKYILKANFMESLHIGMINGFILASYAFGFWYGTRIIISdlsnqqpnNDFHGGSVISILLGVLISM 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 342 FSVGQAAPCIDAFANARGAAYVIFDIIDNNPKIDSfSERGHKPDNIKgNLEFSDVHFSYPSRANIKILKGLNLKVKSGQT 421
Cdd:PTZ00265 336 FMLTIILPNITEYMKSLEATNSLYEIINRKPLVEN-NDDGKKLKDIK-KIQFKNVRFHYDTRKDVEIYKDLNFTLTEGKT 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 422 VALVGNSGCGKSTTVQLLQRLYDPTEGKISI-DGQDIRNFNVRCLREIIGVVSQEPVLFSTTIAENIRYG---------- 490
Cdd:PTZ00265 414 YAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKYSlyslkdleal 493
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 491 ------RGNVTMD-----------------------------------------EIEKAVKEANAYDFIMKLPQKFDTLV 523
Cdd:PTZ00265 494 snyyneDGNDSQEnknkrnscrakcagdlndmsnttdsneliemrknyqtikdsEVVDVSKKVLIHDFVSALPDKYETLV 573
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 524 GDRGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALD--KAREGRTTIVIAHRLSTIRNADVI---- 597
Cdd:PTZ00265 574 GSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINnlKGNENRITIIIAHRLSTIRYANTIfvls 653
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 598 -------------------------------------------AGFEDGVIVEQGSHSELMK-KEGIYFRLVNMQTAGSQ 633
Cdd:PTZ00265 654 nrergstvdvdiigedptkdnkennnknnkddnnnnnnnnnnkINNAGSYIIEQGTHDALMKnKNGIYYTMINNQKVSSK 733
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 634 ILSEEFEVELSDEKAAG-DVAPNGWKARIFRNSTKKSLKSPHQNR----LDEETNELDANvPPVSFLKVLKLNKTEWPY- 707
Cdd:PTZ00265 734 KSSNNDNDKDSDMKSSAyKDSERGYDPDEMNGNSKHENESASNKKsckmSDENASENNAG-GKLPFLRNLFKRKPKAPNn 812
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 708 --------------FVVGTVCAIANGALQPAFSIILSEMIA-IFgpgDDAVKQQKCNMFSLVFLGLGVLSFFTFFLQGFT 772
Cdd:PTZ00265 813 lrivyreifsykkdVTIIALSILVAGGLYPVFALLYAKYVStLF---DFANLEANSNKYSLYILVIAIAMFISETLKNYY 889
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 773 FGKAGEILTTRLRSMAFKAMLRQDMSWFDDHKNSTGALSTRLATDAAQVQGATGTRLALIAQNTANLGTGIIISFiYGWQ 852
Cdd:PTZ00265 890 NNVIGEKVEKTMKRRLFENILYQEISFFDQDKHAPGLLSAHINRDVHLLKTGLVNNIVIFTHFIVLFLVSMVMSF-YFCP 968
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 853 LTLLLLSVVPFIAVAGIVEMKMLAGNAKRDKKEMEAAGKI----------------ATEAIENIRTVVSLTQERKFESMY 916
Cdd:PTZ00265 969 IVAAVLTGTYFIFMRVFAIRARLTANKDVEKKEINQPGTVfaynsddeifkdpsflIQEAFYNMNTVIIYGLEDYFCNLI 1048
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 917 VEKLHGPYRNSVRKAHIYGITFSISQAFMYFSYAGCFRFGSYLIVNGHMRFKDVI-LVFSAIVLGAVAlGHASSFAPDYA 995
Cdd:PTZ00265 1049 EKAIDYSNKGQKRKTLVNSMLWGFSQSAQLFINSFAYWFGSFLIRRGTILVDDFMkSLFTFLFTGSYA-GKLMSLKGDSE 1127
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 996 KAKLSAAYLFSLFERQPLIDSYSGEGLW---PDKFEGSVTFNEVVFNYPTRANVPVLQGLSLEVKKGQTLALVGSSGCGK 1072
Cdd:PTZ00265 1128 NAKLSFEKYYPLIIRKSNIDVRDNGGIRiknKNDIKGKIEIMDVNFRYISRPNVPIYKDLTFSCDSKKTTAIVGETGSGK 1207
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1073 STVVQLLERFYD------------------------------------------------------PMAGSVLLDGQEAK 1098
Cdd:PTZ00265 1208 STVMSLLMRFYDlkndhhivfknehtndmtneqdyqgdeeqnvgmknvnefsltkeggsgedstvfKNSGKILLDGVDIC 1287
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1099 KLNVQWLRAQLGIVSQEPILFDCSIAENIAYG--DNSRvvphDEIVRAAKEANIHPFIETLPQKYNTRVGDKGTQLSGGQ 1176
Cdd:PTZ00265 1288 DYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGkeDATR----EDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQ 1363
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1177 KQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEAL----DKAreGRTCIVIAHRLSTIQNADLIVVIENGK-----V 1247
Cdd:PTZ00265 1364 KQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIvdikDKA--DKTIITIAHRIASIKRSDKIVVFNNPDrtgsfV 1441
|
1450 1460
....*....|....*....|...
gi 338817954 1248 KEHGTHQQLL-AQKGIYFSMVNI 1269
Cdd:PTZ00265 1442 QAHGTHEELLsVQDGVYKKYVKL 1464
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
693-1274 |
7.22e-169 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 514.33 E-value: 7.22e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 693 SFLKVLKLNKTEWPYFVVGTVCAIANGALQPAFSIILSEMI-AIFGPGDdavkQQKCNMFSLVFLGLGVLSFFTFFLQGF 771
Cdd:COG1132 8 LLRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIdALLAGGD----LSALLLLLLLLLGLALLRALLSYLQRY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 772 TFGKAGEILTTRLRSMAFKAMLRQDMSWFDDHknSTGALSTRLATDAAQVQGATGTRLALIAQNTANLGTGIIISFIYGW 851
Cdd:COG1132 84 LLARLAQRVVADLRRDLFEHLLRLPLSFFDRR--RTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDW 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 852 QLTLLLLSVVPFIAVAGIVEMKMLAGNAKRDKKEMEAAGKIATEAIENIRTVVSLTQERKFESMYVEKLHGPYRNSVRKA 931
Cdd:COG1132 162 RLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 932 HIYGITFSISQAFMYFSYAGCFRFGSYLIVNGHMRFKDVILVFSAIVLGAVALGHASSFAPDYAKAKLSAAYLFSLFERQ 1011
Cdd:COG1132 242 RLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEP 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1012 PLIDSYSGEGLwPDKFEGSVTFNEVVFNYPtrANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVL 1091
Cdd:COG1132 322 PEIPDPPGAVP-LPPVRGEIEFENVSFSYP--GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRIL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1092 LDGQEAKKLNVQWLRAQLGIVSQEPILFDCSIAENIAYGDNSrvVPHDEIVRAAKEANIHPFIETLPQKYNTRVGDKGTQ 1171
Cdd:COG1132 399 IDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPD--ATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVN 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1172 LSGGQKQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIENGKVKEHG 1251
Cdd:COG1132 477 LSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQG 556
|
570 580
....*....|....*....|...
gi 338817954 1252 THQQLLAQKGIYFSMVNIQAGTQ 1274
Cdd:COG1132 557 THEELLARGGLYARLYRLQFGEE 579
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
392-628 |
3.77e-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: 459.31 E-value: 3.77e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 392 EFSDVHFSYPSRANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLREIIGV 471
Cdd:cd03249 2 EFKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 472 VSQEPVLFSTTIAENIRYGRGNVTMDEIEKAVKEANAYDFIMKLPQKFDTLVGDRGAQLSGGQKQRIAIARALVRNPKIL 551
Cdd:cd03249 82 VSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKIL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 338817954 552 LLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTIRNADVIAGFEDGVIVEQGSHSELMKKEGIYFRLVNMQ 628
Cdd:cd03249 162 LLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKAQ 238
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
1031-1270 |
3.92e-150 |
|
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: 451.61 E-value: 3.92e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1031 VTFNEVVFNYPTRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQWLRAQLG 1110
Cdd:cd03249 1 IEFKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1111 IVSQEPILFDCSIAENIAYGDNSRVVphDEIVRAAKEANIHPFIETLPQKYNTRVGDKGTQLSGGQKQRIAIARALIRQP 1190
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYGKPDATD--EEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1191 RVLLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIENGKVKEHGTHQQLLAQKGIYFSMVNIQ 1270
Cdd:cd03249 159 KILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKAQ 238
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
120-629 |
3.72e-143 |
|
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: 451.21 E-value: 3.72e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 120 LGGGVLVAAYIQV------SFWTLAAGRQI-KKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDdVSKISEGIGDKVGMF 192
Cdd:COG2274 198 LAIGLLLALLFEGllrllrSYLLLRLGQRIdLRLSSRFFRHLLRLPLSFFESRSVGDLASRFRD-VESIREFLTGSLLTA 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 193 FQAIATFFAGFIVGFIRGWKLTLVIMAISPILGLSTAVWAKILSTFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKE 272
Cdd:COG2274 277 LLDLLFVLIFLIVLFFYSPPLALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRF 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 273 LERYQKHLENAKKIGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTIGnaMTVFFSILIGAF--SVGQAAPC 350
Cdd:COG2274 357 RRRWENLLAKYLNARFKLRRLSNLLSTLSGLLQQLATVALLWLGAYLVIDGQLTLG--QLIAFNILSGRFlaPVAQLIGL 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 351 IDAFANARGAAYVIFDIIDNNPKIDSFSERGHKPdNIKGNLEFSDVHFSYPSRANiKILKGLNLKVKSGQTVALVGNSGC 430
Cdd:COG2274 435 LQRFQDAKIALERLDDILDLPPEREEGRSKLSLP-RLKGDIELENVSFRYPGDSP-PVLDNISLTIKPGERVAIVGRSGS 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 431 GKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLREIIGVVSQEPVLFSTTIAENIRYGRGNVTMDEIEKAVKEANAYD 510
Cdd:COG2274 513 GKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPDATDEEIIEAARLAGLHD 592
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 511 FIMKLPQKFDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLST 590
Cdd:COG2274 593 FIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLST 672
|
490 500 510
....*....|....*....|....*....|....*....
gi 338817954 591 IRNADVIAGFEDGVIVEQGSHSELMKKEGIYFRLVNMQT 629
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; ... |
698-1014 |
2.78e-140 |
|
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: 428.79 E-value: 2.78e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 698 LKLNKTEWPYFVVGTVCAIANGALQPAFSIILSEMIAIFGPGDDAVKQQKCNMFSLVFLGLGVLSFFTFFLQGFTFGKAG 777
Cdd:cd18578 1 LKLNKPEWPLLLLGLIGAIIAGAVFPVFAILFSKLISVFSLPDDDELRSEANFWALMFLVLAIVAGIAYFLQGYLFGIAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 778 EILTTRLRSMAFKAMLRQDMSWFDDHKNSTGALSTRLATDAAQVQGATGTRLALIAQNTANLGTGIIISFIYGWQLTLLL 857
Cdd:cd18578 81 ERLTRRLRKLAFRAILRQDIAWFDDPENSTGALTSRLSTDASDVRGLVGDRLGLILQAIVTLVAGLIIAFVYGWKLALVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 858 LSVVPFIAVAGIVEMKMLAGNAKRDKKEMEAAGKIATEAIENIRTVVSLTQERKFESMYVEKLHGPYRNSVRKAHIYGIT 937
Cdd:cd18578 161 LATVPLLLLAGYLRMRLLSGFEEKNKKAYEESSKIASEAVSNIRTVASLTLEDYFLEKYEEALEEPLKKGLRRALISGLG 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 338817954 938 FSISQAFMYFSYAGCFRFGSYLIVNGHMRFKDVILVFSAIVLGAVALGHASSFAPDYAKAKLSAAYLFSLFERQPLI 1014
Cdd:cd18578 241 FGLSQSLTFFAYALAFWYGGRLVANGEYTFEQFFIVFMALIFGAQSAGQAFSFAPDIAKAKAAAARIFRLLDRKPEI 317
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
54-364 |
1.22e-136 |
|
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: 419.37 E-value: 1.22e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 54 MFLGTLMAIAHGSGLPLMMIVFGEMTDKFVdNTGNFSLPVNFS--LSMLNPGRILEEEMTRYAYYYSGLGGGVLVAAYIQ 131
Cdd:cd18558 1 MVVGILCAIIHGGLLPAFMVIFGDMTDSFT-NGGMTNITGNSSglNSSAGPFEKLEEEMTLYAYYYLIIGAIVLITAYIQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 132 VSFWTLAAGRQIKKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDDVSKISEGIGDKVGMFFQAIATFFAGFIVGFIRGW 211
Cdd:cd18558 80 GSFWGLAAGRQTKKIRYKFFHAIMRQEIGWFDVNDTGELNTRLADDVSKINEGIGDKIGVIFQNIATFGTGFIIGFIRGW 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 212 KLTLVIMAISPILGLSTAVWAKILSTFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKELERYQKHLENAKKIGIKKA 291
Cdd:cd18558 160 KLTLVILAISPVLGLSAVVWAKILSGFTDKEKKAYAKAGAVAEEVLEAFRTVIAFGGQQKEETRYAQNLEIAKRNGIKKA 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 338817954 292 ISANISMGIAFLLIYASYALAFWYGSTLVISKEYTIGNAMTVFFSILIGAFSVGQAAPCIDAFANARGAAYVI 364
Cdd:cd18558 240 ITFNISMGAAFLLIYASYALAFWYGTYLVTQQEYSIGEVLTVFFSVLIGAFSAGQQVPSIEAFANARGAAYHI 312
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
39-625 |
4.54e-133 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 424.52 E-value: 4.54e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 39 LLTLFRYSDWQDKLFMFLGTLMAIahgSGLPLMMIVF--GEMTDKFVDNTGNFSLPVN-FSLSMLNPGRILEEemtryay 115
Cdd:TIGR00958 149 LFRLLGLSGRDWPWLISAFVFLTL---SSLGEMFIPFytGRVIDTLGGDKGPPALASAiFFMCLLSIASSVSA------- 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 116 yysGLGGGVLvaayiqvsfwTLAAGRQIKKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDDVSKISEGIGDKVGMFFQA 195
Cdd:TIGR00958 219 ---GLRGGSF----------NYTMARINLRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNVLLRN 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 196 IATFFAGFIVGFIRGWKLTLVIMAISPILGLSTAVWAKILSTFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKELER 275
Cdd:TIGR00958 286 LVMLLGLLGFMLWLSPRLTMVTLINLPLVFLAEKVFGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFAAEEGEASR 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 276 YQKHLENAKKIGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTIGNamtvFFSILIGAFSVGQAAPCIDAFA 355
Cdd:TIGR00958 366 FKEALEETLQLNKRKALAYAGYLWTTSVLGMLIQVLVLYYGGQLVLTGKVSSGN----LVSFLLYQEQLGEAVRVLSYVY 441
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 356 N----ARGAAYVIFDIIDNNPKIDSfsERGHKPDNIKGNLEFSDVHFSYPSRANIKILKGLNLKVKSGQTVALVGNSGCG 431
Cdd:TIGR00958 442 SgmmqAVGASEKVFEYLDRKPNIPL--TGTLAPLNLEGLIEFQDVSFSYPNRPDVPVLKGLTFTLHPGEVVALVGPSGSG 519
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 432 KSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLREIIGVVSQEPVLFSTTIAENIRYGRGNVTMDEIEKAVKEANAYDF 511
Cdd:TIGR00958 520 KSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDF 599
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 512 IMKLPQKFDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAalDKAREGRTTIVIAHRLSTI 591
Cdd:TIGR00958 600 IMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQE--SRSRASRTVLLIAHRLSTV 677
|
570 580 590
....*....|....*....|....*....|....
gi 338817954 592 RNADVIAGFEDGVIVEQGSHSELMKKEGIYFRLV 625
Cdd:TIGR00958 678 ERADQILVLKKGSVVEMGTHKQLMEDQGCYKHLV 711
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
690-1271 |
6.76e-131 |
|
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: 418.47 E-value: 6.76e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 690 PPVSFLKVLKLNKTEWPYFVVGTVCAIANGALQPAFSIILseMIAIfgpgDDAVKQQkcNMFSLVFLGLGVLSFFTF--- 766
Cdd:COG2274 140 KPFGLRWFLRLLRRYRRLLLQVLLASLLINLLALATPLFT--QVVI----DRVLPNQ--DLSTLWVLAIGLLLALLFegl 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 767 --FLQGFTFGKAGEILTTRLRSMAFKAMLRQDMSWFDdhKNSTGALSTRLaTDAAQVQGATGTRLALIAQNTANLGTGII 844
Cdd:COG2274 212 lrLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFE--SRSVGDLASRF-RDVESIREFLTGSLLTALLDLLFVLIFLI 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 845 ISFIYGWQLTLLLLSVVPFIAVAGIVEMKMLAgnaKRDKKEMEAAGKIAT---EAIENIRTVVSLTQERKFESMYVEKLH 921
Cdd:COG2274 289 VLFFYSPPLALVVLLLIPLYVLLGLLFQPRLR---RLSREESEASAKRQSllvETLRGIETIKALGAESRFRRRWENLLA 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 922 GPYRNSVRKAHIYGITFSISQAFMYFSYAGCFRFGSYLIVNGHMRFkDVILVFSAIVLGAVA-LGHASSFAPDYAKAKLS 1000
Cdd:COG2274 366 KYLNARFKLRRLSNLLSTLSGLLQQLATVALLWLGAYLVIDGQLTL-GQLIAFNILSGRFLApVAQLIGLLQRFQDAKIA 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1001 AAYLFSLFERQPliDSYSGEG-LWPDKFEGSVTFNEVVFNYPtRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLL 1079
Cdd:COG2274 445 LERLDDILDLPP--EREEGRSkLSLPRLKGDIELENVSFRYP-GDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLL 521
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1080 ERFYDPMAGSVLLDGQEAKKLNVQWLRAQLGIVSQEPILFDCSIAENIAYGDNSrvVPHDEIVRAAKEANIHPFIETLPQ 1159
Cdd:COG2274 522 LGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPD--ATDEEIIEAARLAGLHDFIEALPM 599
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1160 KYNTRVGDKGTQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLI 1239
Cdd:COG2274 600 GYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRI 679
|
570 580 590
....*....|....*....|....*....|..
gi 338817954 1240 VVIENGKVKEHGTHQQLLAQKGIYFSMVNIQA 1271
Cdd:COG2274 680 IVLDKGRIVEDGTHEELLARKGLYAELVQQQL 711
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
116-628 |
3.94e-126 |
|
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ATP transporter that exports lipid A and to eukaryotic P-glycoproteins.
Pssm-ID: 131259 [Multi-domain] Cd Length: 576 Bit Score: 401.39 E-value: 3.94e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 116 YYSGLGGGVLVAA---YIQVSFWTLAAGRQIKKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDDVSKISEGIGDKVGMF 192
Cdd:TIGR02204 60 YFAFLLVVALVLAlgtAARFYLVTWLGERVVADIRRAVFAHLISLSPSFFDKNRSGEVVSRLTTDTTLLQSVIGSSLSMA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 193 FQAIATFFAGFIVGFIRGWKLTLVIMAISPILGLSTAVWAKILSTFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKE 272
Cdd:TIGR02204 140 LRNALMCIGGLIMMFITSPKLTSLVLLAVPLVLLPILLFGRRVRKLSRESQDRIADAGSYAGETLGAIRTVQAFGHEDAE 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 273 LERYQKHLENAKKIGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTIGN-AMTVFFSILIGAfSVGQAAPCI 351
Cdd:TIGR02204 220 RSRFGGAVEKAYEAARQRIRTRALLTAIVIVLVFGAIVGVLWVGAHDVIAGKMSAGTlGQFVFYAVMVAG-SIGTLSEVW 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 352 DAFANARGAAYVIFDIIDNNPKIDSFSERGHKPDNIKGNLEFSDVHFSYPSRANIKILKGLNLKVKSGQTVALVGNSGCG 431
Cdd:TIGR02204 299 GELQRAAGAAERLIELLQAEPDIKAPAHPKTLPVPLRGEIEFEQVNFAYPARPDQPALDGLNLTVRPGETVALVGPSGAG 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 432 KSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLREIIGVVSQEPVLFSTTIAENIRYGRGNVTMDEIEKAVKEANAYDF 511
Cdd:TIGR02204 379 KSTLFQLLLRFYDPQSGRILLDGVDLRQLDPAELRARMALVPQDPVLFAASVMENIRYGRPDATDEEVEAAARAAHAHEF 458
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 512 IMKLPQKFDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTI 591
Cdd:TIGR02204 459 ISALPEGYDTYLGERGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDAESEQLVQQALETLMKGRTTLIIAHRLATV 538
|
490 500 510
....*....|....*....|....*....|....*..
gi 338817954 592 RNADVIAGFEDGVIVEQGSHSELMKKEGIYFRLVNMQ 628
Cdd:TIGR02204 539 LKADRIVVMDQGRIVAQGTHAELIAKGGLYARLARLQ 575
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
681-1267 |
3.69e-123 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 397.94 E-value: 3.69e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 681 ETNELDANVPPVSFlKVLKLNKTEWPYFVVGTV---CAIANGALQPAFSiilSEMIAIFGpGDDAVKQQKCNMFSLVFLG 757
Cdd:TIGR00958 137 EAEQGQSETADLLF-RLLGLSGRDWPWLISAFVfltLSSLGEMFIPFYT---GRVIDTLG-GDKGPPALASAIFFMCLLS 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 758 LGvlSFFTFFLQGFTFGKAGEILTTRLRSMAFKAMLRQDMSWFDDHKnsTGALSTRLATDAAQVQGATGTRLALIAQNTA 837
Cdd:TIGR00958 212 IA--SSVSAGLRGGSFNYTMARINLRIREDLFRSLLRQDLGFFDENK--TGELTSRLSSDTQTMSRSLSLNVNVLLRNLV 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 838 NLGTGIIISFIYGWQLTLLLLSVVPFIAVAGIVEMKMLAGNAKRDKKEMEAAGKIATEAIENIRTVVSLTQERKFESMYV 917
Cdd:TIGR00958 288 MLLGLLGFMLWLSPRLTMVTLINLPLVFLAEKVFGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFAAEEGEASRFK 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 918 EKLHGPYRNSVRKAHIYGITFSISQAFMYFSYAGCFRFGSYLIVNGHMRfKDVILVFsaiVLGAVALGHA----SSFAPD 993
Cdd:TIGR00958 368 EALEETLQLNKRKALAYAGYLWTTSVLGMLIQVLVLYYGGQLVLTGKVS-SGNLVSF---LLYQEQLGEAvrvlSYVYSG 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 994 YAKAKLSAAYLFSLFERQPLIdSYSGEgLWPDKFEGSVTFNEVVFNYPTRANVPVLQGLSLEVKKGQTLALVGSSGCGKS 1073
Cdd:TIGR00958 444 MMQAVGASEKVFEYLDRKPNI-PLTGT-LAPLNLEGLIEFQDVSFSYPNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKS 521
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1074 TVVQLLERFYDPMAGSVLLDGQEAKKLNVQWLRAQLGIVSQEPILFDCSIAENIAYGDNSrvVPHDEIVRAAKEANIHPF 1153
Cdd:TIGR00958 522 TVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTD--TPDEEIMAAAKAANAHDF 599
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1154 IETLPQKYNTRVGDKGTQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEalDKAREGRTCIVIAHRLSTI 1233
Cdd:TIGR00958 600 IMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQE--SRSRASRTVLLIAHRLSTV 677
|
570 580 590
....*....|....*....|....*....|....
gi 338817954 1234 QNADLIVVIENGKVKEHGTHQQLLAQKGIYFSMV 1267
Cdd:TIGR00958 678 ERADQILVLKKGSVVEMGTHKQLMEDQGCYKHLV 711
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
54-364 |
1.65e-120 |
|
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: 375.66 E-value: 1.65e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 54 MFLGTLMAIAHGSGLPLMMIVFGEMTDKFVDNTGNFSLPVNFslsmlnpgrilEEEMTRYAYYYSGLGGGVLVAAYIQVS 133
Cdd:cd18577 1 LIIGLLAAIAAGAALPLMTIVFGDLFDAFTDFGSGESSPDEF-----------LDDVNKYALYFVYLGIGSFVLSYIQTA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 134 FWTLAAGRQIKKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDDVSKISEGIGDKVGMFFQAIATFFAGFIVGFIRGWKL 213
Cdd:cd18577 70 CWTITGERQARRIRKRYLKALLRQDIAWFDKNGAGELTSRLTSDTNLIQDGIGEKLGLLIQSLSTFIAGFIIAFIYSWKL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 214 TLVIMAISPILGLSTAVWAKILSTFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKELERYQKHLENAKKIGIKKAIS 293
Cdd:cd18577 150 TLVLLATLPLIAIVGGIMGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKALEKARKAGIKKGLV 229
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 338817954 294 ANISMGIAFLLIYASYALAFWYGSTLVISKEYTIGNAMTVFFSILIGAFSVGQAAPCIDAFANARGAAYVI 364
Cdd:cd18577 230 SGLGLGLLFFIIFAMYALAFWYGSRLVRDGEISPGDVLTVFFAVLIGAFSLGQIAPNLQAFAKARAAAAKI 300
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
126-628 |
3.04e-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: 374.44 E-value: 3.04e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 126 VAAYIQVSFWTLAAGRQIKKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDDVSKISEGIGDKVGMFFQAIATFFAGFIV 205
Cdd:TIGR02203 69 ICSFVSTYLLSWVSNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIV 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 206 GFIRGWKLTLVIMAISPILGLSTAVWAKILSTFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKELERYQKHLENAKK 285
Cdd:TIGR02203 149 LLYYSWQLTLIVVVMLPVLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFDAVSNRNRR 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 286 IGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTIGNaMTVFFSiligafSVGQAAPCIDAFANARG------ 359
Cdd:TIGR02203 229 LAMKMTSAGSISSPITQLIASLALAVVLFIALFQAQAGSLTAGD-FTAFIT------AMIALIRPLKSLTNVNApmqrgl 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 360 -AAYVIFDIIDNNPKIDsfsERGHKPDNIKGNLEFSDVHFSYPSRaNIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQL 438
Cdd:TIGR02203 302 aAAESLFTLLDSPPEKD---TGTRAIERARGDVEFRNVTFRYPGR-DRPALDSISLVIEPGETVALVGRSGSGKSTLVNL 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 439 LQRLYDPTEGKISIDGQDIRNFNVRCLREIIGVVSQEPVLFSTTIAENIRYGR-GNVTMDEIEKAVKEANAYDFIMKLPQ 517
Cdd:TIGR02203 378 IPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRtEQADRAEIERALAAAYAQDFVDKLPL 457
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 518 KFDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTIRNADVI 597
Cdd:TIGR02203 458 GLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRI 537
|
490 500 510
....*....|....*....|....*....|.
gi 338817954 598 AGFEDGVIVEQGSHSELMKKEGIYFRLVNMQ 628
Cdd:TIGR02203 538 VVMDDGRIVERGTHNELLARNGLYAQLHNMQ 568
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
736-1270 |
2.06e-114 |
|
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ATP transporter that exports lipid A and to eukaryotic P-glycoproteins.
Pssm-ID: 131259 [Multi-domain] Cd Length: 576 Bit Score: 369.80 E-value: 2.06e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 736 FGPGDDAVKQQKCNMFSLVFLGLGVLSFFTFFLqgftFGKAGEILTTRLRSMAFKAMLRQDMSWFDdhKNSTGALSTRLA 815
Cdd:TIGR02204 49 FSKDSSGLLNRYFAFLLVVALVLALGTAARFYL----VTWLGERVVADIRRAVFAHLISLSPSFFD--KNRSGEVVSRLT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 816 TDAAQVQGATGTRLALIAQNTANLGTGIIISFIYGWQLTLLLLSVVPFIAVAGIVEMKMLAGNAKRDKKEMEAAGKIATE 895
Cdd:TIGR02204 123 TDTTLLQSVIGSSLSMALRNALMCIGGLIMMFITSPKLTSLVLLAVPLVLLPILLFGRRVRKLSRESQDRIADAGSYAGE 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 896 AIENIRTVVSLTQERKFESMYVEKLHGPYRNSVRKAHIYGITFSISQAFMYFSYAGCFRFGSYLIVNGHMRFKDV-ILVF 974
Cdd:TIGR02204 203 TLGAIRTVQAFGHEDAERSRFGGAVEKAYEAARQRIRTRALLTAIVIVLVFGAIVGVLWVGAHDVIAGKMSAGTLgQFVF 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 975 SAIVLGAvALGHASSFAPDYAKAKLSAAYLFSLFERQPLIDSYSGEGLWPDKFEGSVTFNEVVFNYPTRANVPVLQGLSL 1054
Cdd:TIGR02204 283 YAVMVAG-SIGTLSEVWGELQRAAGAAERLIELLQAEPDIKAPAHPKTLPVPLRGEIEFEQVNFAYPARPDQPALDGLNL 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1055 EVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQWLRAQLGIVSQEPILFDCSIAENIAYG--DN 1132
Cdd:TIGR02204 362 TVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDLRQLDPAELRARMALVPQDPVLFAASVMENIRYGrpDA 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1133 SRvvphDEIVRAAKEANIHPFIETLPQKYNTRVGDKGTQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTESEKVVQE 1212
Cdd:TIGR02204 442 TD----EEVEAAARAAHAHEFISALPEGYDTYLGERGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDAESEQLVQQ 517
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 338817954 1213 ALDKAREGRTCIVIAHRLSTIQNADLIVVIENGKVKEHGTHQQLLAQKGIYFSMVNIQ 1270
Cdd:TIGR02204 518 ALETLMKGRTTLIIAHRLATVLKADRIVVMDQGRIVAQGTHAELIAKGGLYARLARLQ 575
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
391-624 |
2.68e-114 |
|
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: 356.54 E-value: 2.68e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 391 LEFSDVHFSYPSRANiKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLREIIG 470
Cdd:cd03251 1 VEFKNVTFRYPGDGP-PVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 471 VVSQEPVLFSTTIAENIRYGRGNVTMDEIEKAVKEANAYDFIMKLPQKFDTLVGDRGAQLSGGQKQRIAIARALVRNPKI 550
Cdd:cd03251 80 LVSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 338817954 551 LLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTIRNADVIAGFEDGVIVEQGSHSELMKKEGIYFRL 624
Cdd:cd03251 160 LILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKL 233
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
262-633 |
1.26e-113 |
|
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: 368.76 E-value: 1.26e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 262 TVIAFGGQNKELERYQKHLENAKKIGIKKAISAN---------ISMGIAFLLIYASYAlafwygstlVISKEYTIGNamt 332
Cdd:COG5265 230 TVKYFGNEAREARRYDEALARYERAAVKSQTSLAllnfgqaliIALGLTAMMLMAAQG---------VVAGTMTVGD--- 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 333 vfFsILIGAFSVGQAAPCidafaNARGAAY-----------VIFDIIDNNPKIDSfserghKPDNI-----KGNLEFSDV 396
Cdd:COG5265 298 --F-VLVNAYLIQLYIPL-----NFLGFVYreirqaladmeRMFDLLDQPPEVAD------APDAPplvvgGGEVRFENV 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 397 HFSY-PSRaniKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLREIIGVVSQE 475
Cdd:COG5265 364 SFGYdPER---PILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQD 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 476 PVLFSTTIAENIRYGRGNVTMDEIEKAVKEANAYDFIMKLPQKFDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDE 555
Cdd:COG5265 441 TVLFNDTIAYNIAYGRPDASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDE 520
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 338817954 556 ATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTIRNADVIAGFEDGVIVEQGSHSELMKKEGIYFRLVNMQTAGSQ 633
Cdd:COG5265 521 ATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLYAQMWARQQEEEE 598
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
139-628 |
7.02e-109 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 355.10 E-value: 7.02e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 139 AGRQIKKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDD------------VSKISEGigdkvgmffqaiATFFAGFIVG 206
Cdd:PRK11176 93 SGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDseqvassssgalITVVREG------------ASIIGLFIMM 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 207 FIRGWKLTLVIMAISPILGLSTAVWAKILSTFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKELERYQKHLENAKKI 286
Cdd:PRK11176 161 FYYSWQLSLILIVIAPIVSIAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNRMRQQ 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 287 GIKKAISANISMGIAFLLiyASYALAF--WYGSTLVISKEYTIGnAMTVFFSILIGAFSVGQAAPCIDA-FANARGAAYV 363
Cdd:PRK11176 241 GMKMVSASSISDPIIQLI--ASLALAFvlYAASFPSVMDTLTAG-TITVVFSSMIALMRPLKSLTNVNAqFQRGMAACQT 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 364 IFDIIDNNPKIDsfsERGHKPDNIKGNLEFSDVHFSYPSRaNIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLY 443
Cdd:PRK11176 318 LFAILDLEQEKD---EGKRVIERAKGDIEFRNVTFTYPGK-EVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFY 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 444 DPTEGKISIDGQDIRNFNVRCLREIIGVVSQEPVLFSTTIAENIRYGRGNV-TMDEIEKAVKEANAYDFIMKLPQKFDTL 522
Cdd:PRK11176 394 DIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYARTEQySREQIEEAARMAYAMDFINKMDNGLDTV 473
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 523 VGDRGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTIRNADVIAGFED 602
Cdd:PRK11176 474 IGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVED 553
|
490 500
....*....|....*....|....*.
gi 338817954 603 GVIVEQGSHSELMKKEGIYFRLVNMQ 628
Cdd:PRK11176 554 GEIVERGTHAELLAQNGVYAQLHKMQ 579
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
391-628 |
4.44e-107 |
|
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: 337.28 E-value: 4.44e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 391 LEFSDVHFSY-PSRaniKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLREII 469
Cdd:cd03253 1 IEFENVTFAYdPGR---PVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 470 GVVSQEPVLFSTTIAENIRYGRGNVTMDEIEKAVKEANAYDFIMKLPQKFDTLVGDRGAQLSGGQKQRIAIARALVRNPK 549
Cdd:cd03253 78 GVVPQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 338817954 550 ILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTIRNADVIAGFEDGVIVEQGSHSELMKKEGIYFRLVNMQ 628
Cdd:cd03253 158 ILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMWKAQ 236
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
693-1273 |
3.42e-106 |
|
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: 347.47 E-value: 3.42e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 693 SFLKVLKLNKTEWPYFVVGTVCAIANGALQPAFSIILSEMI-AIFGPGDdavkQQKCNMFSLVFLGLGVLSFFTFFLQGF 771
Cdd:TIGR02203 1 TFRRLWSYVRPYKAGLVLAGVAMILVAATESTLAALLKPLLdDGFGGRD----RSVLWWVPLVVIGLAVLRGICSFVSTY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 772 TFGKAGEILTTRLRSMAFKAMLRQDMSWFDdhKNSTGALSTRLATDAAQVQGATGTRLALIAQNTANLGTGIIISFIYGW 851
Cdd:TIGR02203 77 LLSWVSNKVVRDIRVRMFEKLLGLPVSFFD--RQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIVLLYYSW 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 852 QLTLLLLSVVPFIAVAGIVEMKMLAGNAKRDKKEMEAAGKIATEAIENIRTVVSLTQE----RKFESMYVEKLhgpyRNS 927
Cdd:TIGR02203 155 QLTLIVVVMLPVLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQayetRRFDAVSNRNR----RLA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 928 VRKAHIYGITFSISQAFMYFSYAGCFRFGSYLIVNGHMRFKDVILVFSAIVLGAVALGHASSFAPDYAKAKLSAAYLFSL 1007
Cdd:TIGR02203 231 MKMTSAGSISSPITQLIASLALAVVLFIALFQAQAGSLTAGDFTAFITAMIALIRPLKSLTNVNAPMQRGLAAAESLFTL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1008 FERQPLIDSysgEGLWPDKFEGSVTFNEVVFNYPTRaNVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMA 1087
Cdd:TIGR02203 311 LDSPPEKDT---GTRAIERARGDVEFRNVTFRYPGR-DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDS 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1088 GSVLLDGQEAKKLNVQWLRAQLGIVSQEPILFDCSIAENIAYGDnSRVVPHDEIVRAAKEANIHPFIETLPQKYNTRVGD 1167
Cdd:TIGR02203 387 GQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGR-TEQADRAEIERALAAAYAQDFVDKLPLGLDTPIGE 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1168 KGTQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIENGKV 1247
Cdd:TIGR02203 466 NGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRI 545
|
570 580
....*....|....*....|....*.
gi 338817954 1248 KEHGTHQQLLAQKGIYFSMVNIQAGT 1273
Cdd:TIGR02203 546 VERGTHNELLARNGLYAQLHNMQFRE 571
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
1031-1263 |
4.36e-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: 4.36e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1031 VTFNEVVFNYPTRANvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQWLRAQLG 1110
Cdd:cd03251 1 VEFKNVTFRYPGDGP-PVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1111 IVSQEPILFDCSIAENIAYGDnsRVVPHDEIVRAAKEANIHPFIETLPQKYNTRVGDKGTQLSGGQKQRIAIARALIRQP 1190
Cdd:cd03251 80 LVSQDVFLFNDTVAENIAYGR--PGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 338817954 1191 RVLLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIENGKVKEHGTHQQLLAQKGIY 1263
Cdd:cd03251 158 PILILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVY 230
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
708-1004 |
2.39e-103 |
|
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: 330.01 E-value: 2.39e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 708 FVVGTVCAIANGALQPAFSIILSEMIAIFGPGDDAVK-----------------QQKCNMFSLVFLGLGVLSFFTFFLQG 770
Cdd:cd18558 1 MVVGILCAIIHGGLLPAFMVIFGDMTDSFTNGGMTNItgnssglnssagpfeklEEEMTLYAYYYLIIGAIVLITAYIQG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 771 FTFGKAGEILTTRLRSMAFKAMLRQDMSWFDdhKNSTGALSTRLATDAAQVQGATGTRLALIAQNTANLGTGIIISFIYG 850
Cdd:cd18558 81 SFWGLAAGRQTKKIRYKFFHAIMRQEIGWFD--VNDTGELNTRLADDVSKINEGIGDKIGVIFQNIATFGTGFIIGFIRG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 851 WQLTLLLLSVVPFIAVAGIVEMKMLAGNAKRDKKEMEAAGKIATEAIENIRTVVSLTQERKFESMYVEKLHGPYRNSVRK 930
Cdd:cd18558 159 WKLTLVILAISPVLGLSAVVWAKILSGFTDKEKKAYAKAGAVAEEVLEAFRTVIAFGGQQKEETRYAQNLEIAKRNGIKK 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 338817954 931 AHIYGITFSISQAFMYFSYAGCFRFGSYLIVNGHMR-FKDVILVFSAIVLGAVALGHASSFAPdYAKAKLSAAYL 1004
Cdd:cd18558 239 AITFNISMGAAFLLIYASYALAFWYGTYLVTQQEYSiGEVLTVFFSVLIGAFSAGQQVPSIEA-FANARGAAYHI 312
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
1004-1271 |
3.72e-103 |
|
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: 340.26 E-value: 3.72e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1004 LFSLFERQPLI-DSYSGEGLWPDkfEGSVTFNEVVFNY-PTRanvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLER 1081
Cdd:COG5265 332 MFDLLDQPPEVaDAPDAPPLVVG--GGEVRFENVSFGYdPER---PILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFR 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1082 FYDPMAGSVLLDGQEAKKLNVQWLRAQLGIVSQEPILFDCSIAENIAYG--DNSRvvphDEIVRAAKEANIHPFIETLPQ 1159
Cdd:COG5265 407 FYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAYGrpDASE----EEVEAAARAAQIHDFIESLPD 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1160 KYNTRVGDKGTQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLI 1239
Cdd:COG5265 483 GYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEI 562
|
250 260 270
....*....|....*....|....*....|..
gi 338817954 1240 VVIENGKVKEHGTHQQLLAQKGIYFSMVNIQA 1271
Cdd:COG5265 563 LVLEAGRIVERGTHAELLAQGGLYAQMWARQQ 594
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
389-619 |
4.17e-100 |
|
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: 318.02 E-value: 4.17e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 389 GNLEFSDVHFSYpsRANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLREI 468
Cdd:cd03254 1 GEIEFENVNFSY--DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 469 IGVVSQEPVLFSTTIAENIRYGRGNVTMDEIEKAVKEANAYDFIMKLPQKFDTLVGDRGAQLSGGQKQRIAIARALVRNP 548
Cdd:cd03254 79 IGVVLQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 338817954 549 KILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTIRNADVIAGFEDGVIVEQGSHSELMKKEG 619
Cdd:cd03254 159 KILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
1031-1270 |
4.41e-100 |
|
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: 318.02 E-value: 4.41e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1031 VTFNEVVFNYPTraNVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQWLRAQLG 1110
Cdd:cd03253 1 IEFENVTFAYDP--GRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1111 IVSQEPILFDCSIAENIAYGDNSrvVPHDEIVRAAKEANIHPFIETLPQKYNTRVGDKGTQLSGGQKQRIAIARALIRQP 1190
Cdd:cd03253 79 VVPQDTVLFNDTIGYNIRYGRPD--ATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1191 RVLLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIENGKVKEHGTHQQLLAQKGIYFSMVNIQ 1270
Cdd:cd03253 157 PILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMWKAQ 236
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
292-628 |
5.77e-97 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 322.68 E-value: 5.77e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 292 ISANISMGIAFLLiyasyalafwyGSTLVISKEYTIGN--AMTVFFSILIG------AF--SVGQAAPCIDAFanargaa 361
Cdd:PRK13657 248 AASTITMLAILVL-----------GAALVQKGQLRVGEvvAFVGFATLLIGrldqvvAFinQVFMAAPKLEEF------- 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 362 yviFDIIDNNPKIDsfsERGHKPD--NIKGNLEFSDVHFSYPSRAniKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLL 439
Cdd:PRK13657 310 ---FEVEDAVPDVR---DPPGAIDlgRVKGAVEFDDVSFSYDNSR--QGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLL 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 440 QRLYDPTEGKISIDGQDIRNFNVRCLREIIGVVSQEPVLFSTTIAENIRYGRGNVTMDEIEKAVKEANAYDFIMKLPQKF 519
Cdd:PRK13657 382 QRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIERKPDGY 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 520 DTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTIRNADVIAG 599
Cdd:PRK13657 462 DTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILV 541
|
330 340
....*....|....*....|....*....
gi 338817954 600 FEDGVIVEQGSHSELMKKEGIYFRLVNMQ 628
Cdd:PRK13657 542 FDNGRVVESGSFDELVARGGRFAALLRAQ 570
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
355-619 |
1.60e-95 |
|
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: 317.86 E-value: 1.60e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 355 ANARGAAYVIFDIIDNNPKIdsfSERGHKPDNIKGN--LEFSDVHFSYPSRANIkiLKGLNLKVKSGQTVALVGNSGCGK 432
Cdd:COG4988 302 ANGIAAAEKIFALLDAPEPA---APAGTAPLPAAGPpsIELEDVSFSYPGGRPA--LDGLSLTIPPGERVALVGPSGAGK 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 433 STTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLREIIGVVSQEPVLFSTTIAENIRYGRGNVTMDEIEKAVKEANAYDFI 512
Cdd:COG4988 377 STLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPDASDEELEAALEAAGLDEFV 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 513 MKLPQKFDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTIR 592
Cdd:COG4988 457 AALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLA 536
|
250 260
....*....|....*....|....*..
gi 338817954 593 NADVIAGFEDGVIVEQGSHSELMKKEG 619
Cdd:COG4988 537 QADRILVLDDGRIVEQGTHEELLAKNG 563
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
1029-1261 |
2.19e-95 |
|
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: 304.92 E-value: 2.19e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1029 GSVTFNEVVFNYptRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQWLRAQ 1108
Cdd:cd03254 1 GEIEFENVNFSY--DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1109 LGIVSQEPILFDCSIAENIAYGDNSrvVPHDEIVRAAKEANIHPFIETLPQKYNTRVGDKGTQLSGGQKQRIAIARALIR 1188
Cdd:cd03254 79 IGVVLQDTFLFSGTIMENIRLGRPN--ATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLR 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 338817954 1189 QPRVLLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIENGKVKEHGTHQQLLAQKG 1261
Cdd:cd03254 157 DPKILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
135-624 |
5.99e-92 |
|
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: 308.23 E-value: 5.99e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 135 WTLaagRQIKKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDDVskisegigDKVGMFF-QAIATFFAGFIVGFIrgwkL 213
Cdd:COG4987 82 ATL---RLLADLRVRLYRRLEPLAPAGLARLRSGDLLNRLVADV--------DALDNLYlRVLLPLLVALLVILA----A 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 214 TLVIMAISPILGLSTA-------VWAKILSTFSDKELAAYAKAG-----AVAEEALGAIRTVIAFGGQNKELERYQKHLE 281
Cdd:COG4987 147 VAFLAFFSPALALVLAlglllagLLLPLLAARLGRRAGRRLAAAraalrARLTDLLQGAAELAAYGALDRALARLDAAEA 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 282 NAKKIGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTiGNAMTVFFSILIGAFSVgqAAPCIDAFAN---AR 358
Cdd:COG4987 227 RLAAAQRRLARLSALAQALLQLAAGLAVVAVLWLAAPLVAAGALS-GPLLALLVLAALALFEA--LAPLPAAAQHlgrVR 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 359 GAAYVIFDIIDNNPKIDSFSERGHKPDNikGNLEFSDVHFSYPSRANIkILKGLNLKVKSGQTVALVGNSGCGKSTTVQL 438
Cdd:COG4987 304 AAARRLNELLDAPPAVTEPAEPAPAPGG--PSLELEDVSFRYPGAGRP-VLDGLSLTLPPGERVAIVGPSGSGKSTLLAL 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 439 LQRLYDPTEGKISIDGQDIRNFNVRCLREIIGVVSQEPVLFSTTIAENIRYGRGNVTMDEIEKAVKEANAYDFIMKLPQK 518
Cdd:COG4987 381 LLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPDATDEELWAALERVGLGDWLAALPDG 460
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 519 FDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTIRNADVIA 598
Cdd:COG4987 461 LDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRIL 540
|
490 500
....*....|....*....|....*.
gi 338817954 599 GFEDGVIVEQGSHSELMKKEGIYFRL 624
Cdd:COG4987 541 VLEDGRIVEQGTHEELLAQNGRYRQL 566
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
784-1272 |
1.06e-91 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 307.72 E-value: 1.06e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 784 LRSMAFKAMLRQDMSWFDdhKNSTGALSTRLATDAAQVQGATGTRLALIAQNTANLGTGIIISFIYGWQLTLLLLSVVPF 863
Cdd:PRK11176 100 MRRRLFGHMMGMPVSFFD--KQSTGTLLSRITYDSEQVASSSSGALITVVREGASIIGLFIMMFYYSWQLSLILIVIAPI 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 864 IAVAgiveMKMLAGNAKRDKKEMEAA-GKIATEAIENIR--TVVSLTQERKFESMYVEKLHGPYR-NSVRKAHIYGITFS 939
Cdd:PRK11176 178 VSIA----IRVVSKRFRNISKNMQNTmGQVTTSAEQMLKghKEVLIFGGQEVETKRFDKVSNRMRqQGMKMVSASSISDP 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 940 ISQAFMYFSYAGCFRFGSYLIVNGHMRFKDVILVFSAIVLGAVALGHASSFAPDYAKAKLSAAYLFSLFERQPLIDSYSG 1019
Cdd:PRK11176 254 IIQLIASLALAFVLYAASFPSVMDTLTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGMAACQTLFAILDLEQEKDEGKR 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1020 EglwPDKFEGSVTFNEVVFNYPTRaNVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKK 1099
Cdd:PRK11176 334 V---IERAKGDIEFRNVTFTYPGK-EVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRD 409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1100 LNVQWLRAQLGIVSQEPILFDCSIAENIAYGDN---SRvvphDEIVRAAKEANIHPFIETLPQKYNTRVGDKGTQLSGGQ 1176
Cdd:PRK11176 410 YTLASLRNQVALVSQNVHLFNDTIANNIAYARTeqySR----EQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQ 485
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1177 KQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIENGKVKEHGTHQQL 1256
Cdd:PRK11176 486 RQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAEL 565
|
490
....*....|....*.
gi 338817954 1257 LAQKGIYFSMVNIQAG 1272
Cdd:PRK11176 566 LAQNGVYAQLHKMQFG 581
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
986-1261 |
5.31e-88 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 297.05 E-value: 5.31e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 986 HASsfapdyAKAKLSAAYLFSLFErQPLIDSYSGEGLWPDKFEGSVTFNEVVFNYPTRAnvPVLQGLSLEVKKGQTLALV 1065
Cdd:COG4988 299 HAR------ANGIAAAEKIFALLD-APEPAAPAGTAPLPAAGPPSIELEDVSFSYPGGR--PALDGLSLTIPPGERVALV 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1066 GSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQWLRAQLGIVSQEPILFDCSIAENIAYGDnsRVVPHDEIVRAA 1145
Cdd:COG4988 370 GPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGR--PDASDEELEAAL 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1146 KEANIHPFIETLPQKYNTRVGDKGTQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEALDKAREGRTCIV 1225
Cdd:COG4988 448 EAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVIL 527
|
250 260 270
....*....|....*....|....*....|....*.
gi 338817954 1226 IAHRLSTIQNADLIVVIENGKVKEHGTHQQLLAQKG 1261
Cdd:COG4988 528 ITHRLALLAQADRILVLDDGRIVEQGTHEELLAKNG 563
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
1022-1247 |
2.05e-87 |
|
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: 282.82 E-value: 2.05e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1022 LWPDKFEGSVTFNEVVFNYPTRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLN 1101
Cdd:cd03248 3 LAPDHLKGIVKFQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1102 VQWLRAQLGIVSQEPILFDCSIAENIAYGDNSrvVPHDEIVRAAKEANIHPFIETLPQKYNTRVGDKGTQLSGGQKQRIA 1181
Cdd:cd03248 83 HKYLHSKVSLVGQEPVLFARSLQDNIAYGLQS--CSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 338817954 1182 IARALIRQPRVLLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIENGKV 1247
Cdd:cd03248 161 IARALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
198-629 |
5.51e-85 |
|
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: 292.42 E-value: 5.51e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 198 TFFAgfiVGFIRGWKLTLVIMAISPILGLSTAVWAKILSTFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKELERYQ 277
Cdd:TIGR01846 268 VFLA---VMFFYSPTLTGVVIGSLVCYALLSVFVGPILRKRVEDKFERSAAATSFLVESVTGIETIKATATEPQFQNRWD 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 278 KHLENAKKIGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTIGNamTVFFSILIGAFS--VGQAAPCIDAFA 355
Cdd:TIGR01846 345 RQLAAYVAASFRVTNLGNIAGQAIELIQKLTFAILLWFGAHLVIGGALSPGQ--LVAFNMLAGRVTqpVLRLAQLWQDFQ 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 356 NARGAAYVIFDIIdNNPKIDSFSERGHKPdNIKGNLEFSDVHFSYPSRANiKILKGLNLKVKSGQTVALVGNSGCGKSTT 435
Cdd:TIGR01846 423 QTGIALERLGDIL-NSPTEPRSAGLAALP-ELRGAITFENIRFRYAPDSP-EVLSNLNLDIKPGEFIGIVGPSGSGKSTL 499
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 436 VQLLQRLYDPTEGKISIDGQDIRNFNVRCLREIIGVVSQEPVLFSTTIAENIRYGRGNVTMDEIEKAVKEANAYDFIMKL 515
Cdd:TIGR01846 500 TKLLQRLYTPQHGQVLVDGVDLAIADPAWLRRQMGVVLQENVLFSRSIRDNIALCNPGAPFEHVIHAAKLAGAHDFISEL 579
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 516 PQKFDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTIRNAD 595
Cdd:TIGR01846 580 PQGYNTEVGEKGANLSGGQRQRIAIARALVGNPRILIFDEATSALDYESEALIMRNMREICRGRTVIIIAHRLSTVRACD 659
|
410 420 430
....*....|....*....|....*....|....
gi 338817954 596 VIAGFEDGVIVEQGSHSELMKKEGIYFRLVNMQT 629
Cdd:TIGR01846 660 RIIVLEKGQIAESGRHEELLALQGLYARLWQQQS 693
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
391-603 |
3.07e-83 |
|
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: 268.87 E-value: 3.07e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 391 LEFSDVHFSYPSRANiKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLREIIG 470
Cdd:cd03228 1 IEFKNVSFSYPGRPK-PVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 471 VVSQEPVLFSTTIAENIrygrgnvtmdeiekavkeanaydfimklpqkfdtlvgdrgaqLSGGQKQRIAIARALVRNPKI 550
Cdd:cd03228 80 YVPQDPFLFSGTIRENI------------------------------------------LSGGQRQRIAIARALLRDPPI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 338817954 551 LLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTIRNADVIAGFEDG 603
Cdd:cd03228 118 LILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDG 170
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
391-628 |
8.59e-83 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 270.51 E-value: 8.59e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 391 LEFSDVHFSYPSRANIkILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLREIIG 470
Cdd:cd03252 1 ITFEHVRFRYKPDGPV-ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 471 VVSQEPVLFSTTIAENIRYGRGNVTMDEIEKAVKEANAYDFIMKLPQKFDTLVGDRGAQLSGGQKQRIAIARALVRNPKI 550
Cdd:cd03252 80 VVLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 338817954 551 LLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTIRNADVIAGFEDGVIVEQGSHSELMKKEGIYFRLVNMQ 628
Cdd:cd03252 160 LIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQLQ 237
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
780-1269 |
9.00e-83 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 282.43 E-value: 9.00e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 780 LTTRLRSMAFKAMLRQDMSWFddHKNSTGALSTRLATDAAQVQGATgtrLALIAQNTANLGTGIIISFIYGWQLTLLLLS 859
Cdd:COG4987 86 LLADLRVRLYRRLEPLAPAGL--ARLRSGDLLNRLVADVDALDNLY---LRVLLPLLVALLVILAAVAFLAFFSPALALV 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 860 VVPFIAVAGIVeMKMLAG--NAKRDKKEMEAAGKIATEAIENIRTVVSLT----QERKFESmyVEKLHGPYRNSVRKAHI 933
Cdd:COG4987 161 LALGLLLAGLL-LPLLAArlGRRAGRRLAAARAALRARLTDLLQGAAELAaygaLDRALAR--LDAAEARLAAAQRRLAR 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 934 Y-GITFSISQAFMYFSYAGCFRFGSYLIVNGHMRFKDV-ILVFSAIVLGAVALGHASSFApDYAKAKLSAAYLFSLFERQ 1011
Cdd:COG4987 238 LsALAQALLQLAAGLAVVAVLWLAAPLVAAGALSGPLLaLLVLAALALFEALAPLPAAAQ-HLGRVRAAARRLNELLDAP 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1012 PLIdSYSGEGLWPDKFeGSVTFNEVVFNYPTrANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVL 1091
Cdd:COG4987 317 PAV-TEPAEPAPAPGG-PSLELEDVSFRYPG-AGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSIT 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1092 LDGQEAKKLNVQWLRAQLGIVSQEPILFDCSIAENIAYGDNSrvVPHDEIVRAAKEANIHPFIETLPQKYNTRVGDKGTQ 1171
Cdd:COG4987 394 LGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPD--ATDEELWAALERVGLGDWLAALPDGLDTWLGEGGRR 471
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1172 LSGGQKQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIENGKVKEHG 1251
Cdd:COG4987 472 LSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQG 551
|
490
....*....|....*...
gi 338817954 1252 THQQLLAQKGIYFSMVNI 1269
Cdd:COG4987 552 THEELLAQNGRYRQLYQR 569
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
384-605 |
4.03e-82 |
|
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: 268.18 E-value: 4.03e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 384 PDNIKGNLEFSDVHFSYPSRANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVR 463
Cdd:cd03248 5 PDHLKGIVKFQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 464 CLREIIGVVSQEPVLFSTTIAENIRYGRGNVTMDEIEKAVKEANAYDFIMKLPQKFDTLVGDRGAQLSGGQKQRIAIARA 543
Cdd:cd03248 85 YLHSKVSLVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 338817954 544 LVRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTIRNADVIAGFEDGVI 605
Cdd:cd03248 165 LIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
708-1004 |
1.40e-81 |
|
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: 269.73 E-value: 1.40e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 708 FVVGTVCAIANGALQPAFSIILSEMIAIF-----GPGDDAVKQQKCNMFSLVFLGLGVLSFFTFFLQGFTFGKAGEILTT 782
Cdd:cd18577 1 LIIGLLAAIAAGAALPLMTIVFGDLFDAFtdfgsGESSPDEFLDDVNKYALYFVYLGIGSFVLSYIQTACWTITGERQAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 783 RLRSMAFKAMLRQDMSWFDdhKNSTGALSTRLATDAAQVQGATGTRLALIAQNTANLGTGIIISFIYGWQLTLLLLSVVP 862
Cdd:cd18577 81 RIRKRYLKALLRQDIAWFD--KNGAGELTSRLTSDTNLIQDGIGEKLGLLIQSLSTFIAGFIIAFIYSWKLTLVLLATLP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 863 FIAVAGIVEMKMLAGNAKRDKKEMEAAGKIATEAIENIRTVVSLTQERKFESMYVEKLHGPYRNSVRKAHIYGITFSISQ 942
Cdd:cd18577 159 LIAIVGGIMGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKALEKARKAGIKKGLVSGLGLGLLF 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 338817954 943 AFMYFSYAGCFRFGSYLIVNGHMRFKDVILVFSAIVLGAVALGHASSFAPDYAKAKLSAAYL 1004
Cdd:cd18577 239 FIIFAMYALAFWYGSRLVRDGEISPGDVLTVFFAVLIGAFSLGQIAPNLQAFAKARAAAAKI 300
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
1031-1270 |
1.57e-81 |
|
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: 267.04 E-value: 1.57e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1031 VTFNEVVFNYptRANVP-VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQWLRAQL 1109
Cdd:cd03252 1 ITFEHVRFRY--KPDGPvILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1110 GIVSQEPILFDCSIAENIAYGDNSrvVPHDEIVRAAKEANIHPFIETLPQKYNTRVGDKGTQLSGGQKQRIAIARALIRQ 1189
Cdd:cd03252 79 GVVLQENVLFNRSIRDNIALADPG--MSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1190 PRVLLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIENGKVKEHGTHQQLLAQKGIYFSMVNI 1269
Cdd:cd03252 157 PRILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQL 236
|
.
gi 338817954 1270 Q 1270
Cdd:cd03252 237 Q 237
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
845-1261 |
2.33e-79 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 273.38 E-value: 2.33e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 845 ISFIYGWQLTLLLLS-VVPFIAVAGIVEMKMLAGNAKRDKKEMEAAGKiATEAIENIRTVVSLTQERKfesmYVEKLHGp 923
Cdd:PRK13657 150 LALFMNWRLSLVLVVlGIVYTLITTLVMRKTKDGQAAVEEHYHDLFAH-VSDAIGNVSVVQSYNRIEA----ETQALRD- 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 924 YRNSVRKAHI-----YGITFSISQAFMYFSYAGCFRFGSYLIVNGHMRFKDVILVFSAIVLGAVALGHASSFApdyAKAK 998
Cdd:PRK13657 224 IADNLLAAQMpvlswWALASVLNRAASTITMLAILVLGAALVQKGQLRVGEVVAFVGFATLLIGRLDQVVAFI---NQVF 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 999 LSAAYLFSLF----------ERQPLIDsysgeglwPDKFEGSVTFNEVVFNYPTRAnvPVLQGLSLEVKKGQTLALVGSS 1068
Cdd:PRK13657 301 MAAPKLEEFFevedavpdvrDPPGAID--------LGRVKGAVEFDDVSFSYDNSR--QGVEDVSFEAKPGQTVAIVGPT 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1069 GCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQWLRAQLGIVSQEPILFDCSIAENIAYGDNSrvVPHDEIVRAAKEA 1148
Cdd:PRK13657 371 GAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRPD--ATDEEMRAAAERA 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1149 NIHPFIETLPQKYNTRVGDKGTQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEALDKAREGRTCIVIAH 1228
Cdd:PRK13657 449 QAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAH 528
|
410 420 430
....*....|....*....|....*....|...
gi 338817954 1229 RLSTIQNADLIVVIENGKVKEHGTHQQLLAQKG 1261
Cdd:PRK13657 529 RLSTVRNADRILVFDNGRVVESGSFDELVARGG 561
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
1031-1246 |
1.15e-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: 256.16 E-value: 1.15e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1031 VTFNEVVFNYPTRANvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQWLRAQLG 1110
Cdd:cd03228 1 IEFKNVSFSYPGRPK-PVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1111 IVSQEPILFDCSIAENIaygdnsrvvphdeivraakeanihpfietlpqkyntrvgdkgtqLSGGQKQRIAIARALIRQP 1190
Cdd:cd03228 80 YVPQDPFLFSGTIRENI--------------------------------------------LSGGQRQRIAIARALLRDP 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 338817954 1191 RVLLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIENGK 1246
Cdd:cd03228 116 PILILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
706-1263 |
2.02e-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: 274.13 E-value: 2.02e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 706 PYFVVGTVCAIANGALQPAFSIILSEMIAIfgpgddavkQQKCNMFSLVFLGLGVLSFFTFFLQGFTfgkagEILTTRLR 785
Cdd:TIGR03796 157 LYLLLAGLLLVLPGLVIPAFSQIFVDEILV---------QGRQDWLRPLLLGMGLTALLQGVLTWLQ-----LYYLRRLE 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 786 ---SMAFKA-----MLRQDMSWFDdhKNSTGALSTRLATdAAQVQGATGTRLALIAQNTANLGTGIIISFIYGWQLTLLL 857
Cdd:TIGR03796 223 iklAVGMSArflwhILRLPVRFFA--QRHAGDIASRVQL-NDQVAEFLSGQLATTALDAVMLVFYALLMLLYDPVLTLIG 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 858 lsvvpfIAVAGIVEMKMLAGNAKR---DKKEMEAAGKIATEAIENIRTVVSLtQERKFESMYVEKLHGPYRNSVRKAHIY 934
Cdd:TIGR03796 300 ------IAFAAINVLALQLVSRRRvdaNRRLQQDAGKLTGVAISGLQSIETL-KASGLESDFFSRWAGYQAKLLNAQQEL 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 935 GITFSI----SQAFMYFSYAGCFRFGSYLIVNGHMR------FKDVILVFSAIVLGAVALGHA-SSFAPDYAKAKLSAAY 1003
Cdd:TIGR03796 373 GVLTQIlgvlPTLLTSLNSALILVVGGLRVMEGQLTigmlvaFQSLMSSFLEPVNNLVGFGGTlQELEGDLNRLDDVLRN 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1004 -LFSLFERQPLIDSYSGEglwPDKFEGSVTFNEVVFNYpTRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERF 1082
Cdd:TIGR03796 453 pVDPLLEEPEGSAATSEP---PRRLSGYVELRNITFGY-SPLEPPLIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGL 528
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1083 YDPMAGSVLLDGQEAKKLNVQWLRAQLGIVSQEPILFDCSIAENIAYGDNSrvVPHDEIVRAAKEANIHPFIETLPQKYN 1162
Cdd:TIGR03796 529 YQPWSGEILFDGIPREEIPREVLANSVAMVDQDIFLFEGTVRDNLTLWDPT--IPDADLVRACKDAAIHDVITSRPGGYD 606
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1163 TRVGDKGTQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEALdkAREGRTCIVIAHRLSTIQNADLIVVI 1242
Cdd:TIGR03796 607 AELAEGGANLSGGQRQRLEIARALVRNPSILILDEATSALDPETEKIIDDNL--RRRGCTCIIVAHRLSTIRDCDEIIVL 684
|
570 580
....*....|....*....|.
gi 338817954 1243 ENGKVKEHGTHQQLLAQKGIY 1263
Cdd:TIGR03796 685 ERGKVVQRGTHEELWAVGGAY 705
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
54-342 |
6.23e-77 |
|
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: 255.65 E-value: 6.23e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 54 MFLGTLMAIAHGSGLPLMMIVFGEMTDKFVDNtgnfslpvnfslsmlnpGRILEEEMTRYAYYYSGLGGGVLVAAYIQVS 133
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLPD-----------------GDPETQALNVYSLALLLLGLAQFILSFLQSY 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 134 FWTLAAGRQIKKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDDVSKISEGIGDKVGMFFQAIATFFAGFIVGFIRGWKL 213
Cdd:pfam00664 64 LLNHTGERLSRRLRRKLFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 214 TLVIMAISPILGLSTAVWAKILSTFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKELERYQKHLENAKKIGIKKAIS 293
Cdd:pfam00664 144 TLVLLAVLPLYILVSAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVA 223
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 338817954 294 ANISMGIAFLLIYASYALAFWYGSTLVISKEYTIGN--AMTVFFSILIGAF 342
Cdd:pfam00664 224 NGLSFGITQFIGYLSYALALWFGAYLVISGELSVGDlvAFLSLFAQLFGPL 274
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
48-374 |
6.49e-77 |
|
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: 257.00 E-value: 6.49e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 48 WQDKLFMFLGTLMAIAHGSGLPLMMIVFGEMTDkfvdntgNFSLPvnfslsmlnPGRILEEEMTRYAYYYSGLGGGVLVA 127
Cdd:cd18578 5 KPEWPLLLLGLIGAIIAGAVFPVFAILFSKLIS-------VFSLP---------DDDELRSEANFWALMFLVLAIVAGIA 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 128 AYIQVSFWTLAAGRQIKKIRQKFFHAILRQEMGWFDIKG--TTELNTRLTDDVSKISEGIGDKVGMFFQAIATFFAGFIV 205
Cdd:cd18578 69 YFLQGYLFGIAGERLTRRLRKLAFRAILRQDIAWFDDPEnsTGALTSRLSTDASDVRGLVGDRLGLILQAIVTLVAGLII 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 206 GFIRGWKLTLVIMAISPILGLSTAVWAKILSTFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKELERYQKHLENAKK 285
Cdd:cd18578 149 AFVYGWKLALVGLATVPLLLLAGYLRMRLLSGFEEKNKKAYEESSKIASEAVSNIRTVASLTLEDYFLEKYEEALEEPLK 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 286 IGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTIGNAMTVFFSILIGAFSVGQAAPCIDAFANARGAAYVIF 365
Cdd:cd18578 229 KGLRRALISGLGFGLSQSLTFFAYALAFWYGGRLVANGEYTFEQFFIVFMALIFGAQSAGQAFSFAPDIAKAKAAAARIF 308
|
....*....
gi 338817954 366 DIIDNNPKI 374
Cdd:cd18578 309 RLLDRKPEI 317
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
847-1272 |
1.96e-76 |
|
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: 268.15 E-value: 1.96e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 847 FIYGWQLTLLLLSVVPF-----IAVAGIVEMKMlagnakRDKKEMEAAGK-IATEAIENIRTVVSLTQERKFESMYVEKL 920
Cdd:TIGR01846 274 FFYSPTLTGVVIGSLVCyallsVFVGPILRKRV------EDKFERSAAATsFLVESVTGIETIKATATEPQFQNRWDRQL 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 921 HGPYRNSVRKAHIYGITFSISQAFMYFSYAGCFRFGSYLIVNGHMRFKDVIL--VFSAIVLGAVAlgHASSFAPDYAKAK 998
Cdd:TIGR01846 348 AAYVAASFRVTNLGNIAGQAIELIQKLTFAILLWFGAHLVIGGALSPGQLVAfnMLAGRVTQPVL--RLAQLWQDFQQTG 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 999 LSAAYLFSLFErQPLIDSYSGEGLWPdKFEGSVTFNEVVFNYPTRAnVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQL 1078
Cdd:TIGR01846 426 IALERLGDILN-SPTEPRSAGLAALP-ELRGAITFENIRFRYAPDS-PEVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKL 502
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1079 LERFYDPMAGSVLLDGQEAKKLNVQWLRAQLGIVSQEPILFDCSIAENIAYGDNSrvVPHDEIVRAAKEANIHPFIETLP 1158
Cdd:TIGR01846 503 LQRLYTPQHGQVLVDGVDLAIADPAWLRRQMGVVLQENVLFSRSIRDNIALCNPG--APFEHVIHAAKLAGAHDFISELP 580
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1159 QKYNTRVGDKGTQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADL 1238
Cdd:TIGR01846 581 QGYNTEVGEKGANLSGGQRQRIAIARALVGNPRILIFDEATSALDYESEALIMRNMREICRGRTVIIIAHRLSTVRACDR 660
|
410 420 430
....*....|....*....|....*....|....
gi 338817954 1239 IVVIENGKVKEHGTHQQLLAQKGIYFSMVNIQAG 1272
Cdd:TIGR01846 661 IIVLEKGQIAESGRHEELLALQGLYARLWQQQSG 694
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
710-1275 |
9.34e-74 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 270.36 E-value: 9.34e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 710 VGTVCAIANGALQPAFSIILSEMIAIFGPGDDAVKQqkcnMFSLVFLGLG--VLSFFTFFLQGFTFGKageILTTrLRSM 787
Cdd:PTZ00265 64 VSFVCATISGGTLPFFVSVFGVIMKNMNLGENVNDI----IFSLVLIGIFqfILSFISSFCMDVVTTK---ILKT-LKLE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 788 AFKAMLRQDMSWFDDHKNSTgaLSTRLATDAAQVQGATGTRLALIAQNTANLGTGIIISFIYGWQLTLLLLSVVPFIAVA 867
Cdd:PTZ00265 136 FLKSVFYQDGQFHDNNPGSK--LTSDLDFYLEQVNAGIGTKFITIFTYASAFLGLYIWSLFKNARLTLCITCVFPLIYIC 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 868 GIVEMKMLAGNAKRDKKEMEAAGKIATEAIENIRTVVSLTQERKFESMY--VEKLHGPY---RNSVRKAHIYGItfsisQ 942
Cdd:PTZ00265 214 GVICNKKVKINKKTSLLYNNNTMSIIEEALVGIRTVVSYCGEKTILKKFnlSEKLYSKYilkANFMESLHIGMI-----N 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 943 AFMYFSYAGCFRFGSYLIV--------NGHMRFKDVILVFSAIVLGAVALGHASSFAPDYAKAKLSAAYLFSLFERQPLI 1014
Cdd:PTZ00265 289 GFILASYAFGFWYGTRIIIsdlsnqqpNNDFHGGSVISILLGVLISMFMLTIILPNITEYMKSLEATNSLYEIINRKPLV 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1015 DSYS-GEGLWPDKfegSVTFNEVVFNYPTRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLL- 1092
Cdd:PTZ00265 369 ENNDdGKKLKDIK---KIQFKNVRFHYDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIn 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1093 DGQEAKKLNVQWLRAQLGIVSQEPILFDCSIAENIAY------------------------GDNSR-------------- 1134
Cdd:PTZ00265 446 DSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKYslyslkdlealsnyynedgndsqeNKNKRnscrakcagdlndm 525
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1135 -----------------VVPHDEIVRAAKEANIHPFIETLPQKYNTRVGDKGTQLSGGQKQRIAIARALIRQPRVLLLDE 1197
Cdd:PTZ00265 526 snttdsneliemrknyqTIKDSEVVDVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDE 605
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1198 ATSALDTESEKVVQEALD--KAREGRTCIVIAHRLSTIQNADLIVVIENGK----------------------------- 1246
Cdd:PTZ00265 606 ATSSLDNKSEYLVQKTINnlKGNENRITIIIAHRLSTIRYANTIFVLSNRErgstvdvdiigedptkdnkennnknnkdd 685
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 338817954 1247 ------------------VKEHGTHQQLLAQK-GIYFSMVNIQAGTQN 1275
Cdd:PTZ00265 686 nnnnnnnnnnkinnagsyIIEQGTHDALMKNKnGIYYTMINNQKVSSK 733
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
292-625 |
1.29e-73 |
|
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: 257.12 E-value: 1.29e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 292 ISANISMgIAFLLIyasyalafwyGSTLVISKEYTIGNAMTV--FFSILIGAFSvgQAAPCIDAFANARGAAYVIFDIID 369
Cdd:TIGR01192 248 MASTISM-MCILVI----------GTVLVIKGELSVGEVIAFigFANLLIGRLD--QMSGFITQIFEARAKLEDFFDLED 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 370 NNPKIDSFSERGHKPdNIKGNLEFSDVHFSYPSRAniKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGK 449
Cdd:TIGR01192 315 SVFQREEPADAPELP-NVKGAVEFRHITFEFANSS--QGVFDVSFEAKAGQTVAIVGPTGAGKTTLINLLQRVYDPTVGQ 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 450 ISIDGQDIRNFNVRCLREIIGVVSQEPVLFSTTIAENIRYGRGNVTMDEIEKAVKEANAYDFIMKLPQKFDTLVGDRGAQ 529
Cdd:TIGR01192 392 ILIDGIDINTVTRESLRKSIATVFQDAGLFNRSIRENIRLGREGATDEEVYEAAKAAAAHDFILKRSNGYDTLVGERGNR 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 530 LSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTIRNADVIAGFEDGVIVEQG 609
Cdd:TIGR01192 472 LSGGERQRLAIARAILKNAPILVLDEATSALDVETEARVKNAIDALRKNRTTFIIAHRLSTVRNADLVLFLDQGRLIEKG 551
|
330
....*....|....*.
gi 338817954 610 SHSELMKKEGIYFRLV 625
Cdd:TIGR01192 552 SFQELIQKDGRFYKLL 567
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
118-625 |
4.35e-70 |
|
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: 249.86 E-value: 4.35e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 118 SGLGGGVLVAAYIQVSfwTLAAGRqikkirqkFFHAILRQEMGWF------DIKGTTELNTRLTDDVS-KISEGIGDKVG 190
Cdd:TIGR03796 211 TWLQLYYLRRLEIKLA--VGMSAR--------FLWHILRLPVRFFaqrhagDIASRVQLNDQVAEFLSgQLATTALDAVM 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 191 MFFQAIATFfagfivgfIRGWKLTLVIMAISPILGLSTAVWAKILSTFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQN 270
Cdd:TIGR03796 281 LVFYALLML--------LYDPVLTLIGIAFAAINVLALQLVSRRRVDANRRLQQDAGKLTGVAISGLQSIETLKASGLES 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 271 KELER---YQKHLENA-KKIGIKKAISANISMGIAFLliyaSYALAFWYGSTLVISKEYTIGnaMTVFFSILIGAFS--- 343
Cdd:TIGR03796 353 DFFSRwagYQAKLLNAqQELGVLTQILGVLPTLLTSL----NSALILVVGGLRVMEGQLTIG--MLVAFQSLMSSFLepv 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 344 ---VGQAAPCIDAFAN-ARgaayviFDIIDNNPKIDSFSERGHKPDN------IKGNLEFSDVHFSYpSRANIKILKGLN 413
Cdd:TIGR03796 427 nnlVGFGGTLQELEGDlNR------LDDVLRNPVDPLLEEPEGSAATsepprrLSGYVELRNITFGY-SPLEPPLIENFS 499
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 414 LKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLREIIGVVSQEPVLFSTTIAENIRYGRGN 493
Cdd:TIGR03796 500 LTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIPREVLANSVAMVDQDIFLFEGTVRDNLTLWDPT 579
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 494 VTMDEIEKAVKEANAYDFIMKLPQKFDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALd 573
Cdd:TIGR03796 580 IPDADLVRACKDAAIHDVITSRPGGYDAELAEGGANLSGGQRQRLEIARALVRNPSILILDEATSALDPETEKIIDDNL- 658
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 338817954 574 kAREGRTTIVIAHRLSTIRNADVIAGFEDGVIVEQGSHSELMKKEGIYFRLV 625
Cdd:TIGR03796 659 -RRRGCTCIIVAHRLSTIRDCDEIIVLERGKVVQRGTHEELWAVGGAYARLI 709
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
708-982 |
1.44e-69 |
|
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: 234.84 E-value: 1.44e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 708 FVVGTVCAIANGALQPAFSIILSEMIAIFGPGDDAVKQqKCNMFSLVFLGLGVLSFFTFFLQGFTFGKAGEILTTRLRSM 787
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLPDGDPETQ-ALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 788 AFKAMLRQDMSWFDdhKNSTGALSTRLATDAAQVQGATGTRLALIAQNTANLGTGIIISFIYGWQLTLLLLSVVPFIAVA 867
Cdd:pfam00664 80 LFKKILRQPMSFFD--TNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 868 GIVEMKMLAGNAKRDKKEMEAAGKIATEAIENIRTVVSLTQERKFESMYVEKLHGPYRNSVRKAHIYGITFSISQAFMYF 947
Cdd:pfam00664 158 SAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYL 237
|
250 260 270
....*....|....*....|....*....|....*..
gi 338817954 948 SYAGCFRFGSYLIVNGHMRFKDVI--LVFSAIVLGAV 982
Cdd:pfam00664 238 SYALALWFGAYLVISGELSVGDLVafLSLFAQLFGPL 274
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
847-1270 |
5.55e-69 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 246.02 E-value: 5.55e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 847 FIYGWQLTL----LLLSVVPFIAVAGIVEMKMLagnakrdKKEMEAAGKIATEAIENIRTVVSL----TQERKFesMYVE 918
Cdd:TIGR03797 271 FYYSWKLALvavaLALVAIAVTLVLGLLQVRKE-------RRLLELSGKISGLTVQLINGISKLrvagAENRAF--ARWA 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 919 KLHGPYRNSVRKAH-IYGITFSISQAFMYFSYAGCFRFGSYLIVNGHMRFKDvILVFSAivlgavALGHASSFAPDYAKA 997
Cdd:TIGR03797 342 KLFSRQRKLELSAQrIENLLTVFNAVLPVLTSAALFAAAISLLGGAGLSLGS-FLAFNT------AFGSFSGAVTQLSNT 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 998 KLSAAYLFSLFER-QPLIDS---YSGEGLWPDKFEGSVTFNEVVFNYptRANVP-VLQGLSLEVKKGQTLALVGSSGCGK 1072
Cdd:TIGR03797 415 LISILAVIPLWERaKPILEAlpeVDEAKTDPGKLSGAIEVDRVTFRY--RPDGPlILDDVSLQIEPGEFVAIVGPSGSGK 492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1073 STVVQLLERFYDPMAGSVLLDGQEAKKLNVQWLRAQLGIVSQEPILFDCSIAENIAYGDnsrVVPHDEIVRAAKEANIHP 1152
Cdd:TIGR03797 493 STLLRLLLGFETPESGSVFYDGQDLAGLDVQAVRRQLGVVLQNGRLMSGSIFENIAGGA---PLTLDEAWEAARMAGLAE 569
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1153 FIETLPQKYNTRVGDKGTQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEALDKAREGRtcIVIAHRLST 1232
Cdd:TIGR03797 570 DIRAMPMGMHTVISEGGGTLSGGQRQRLLIARALVRKPRILLFDEATSALDNRTQAIVSESLERLKVTR--IVIAHRLST 647
|
410 420 430
....*....|....*....|....*....|....*...
gi 338817954 1233 IQNADLIVVIENGKVKEHGTHQQLLAQKGIYFSMVNIQ 1270
Cdd:TIGR03797 648 IRNADRIYVLDAGRVVQQGTYDELMAREGLFAQLARRQ 685
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
389-609 |
1.99e-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: 229.40 E-value: 1.99e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 389 GNLEFSDVHFSYPSrANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLREI 468
Cdd:cd03245 1 GRIEFRNVSFSYPN-QEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 469 IGVVSQEPVLFSTTIAENIRYGRGNVTMDEIEKAVKEANAYDFIMKLPQKFDTLVGDRGAQLSGGQKQRIAIARALVRNP 548
Cdd:cd03245 80 IGYVPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 338817954 549 KILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTIRNADVIAGFEDGVIVEQG 609
Cdd:cd03245 160 PILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
353-597 |
9.88e-67 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 235.26 E-value: 9.88e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 353 AFANARGAAYVIFDIIDNNPKIdsFSERGHKPDNIKGNLEFSDVHFSYPSRANIkiLKGLNLKVKSGQTVALVGNSGCGK 432
Cdd:TIGR02857 286 ARADGVAAAEALFAVLDAAPRP--LAGKAPVTAAPASSLEFSGVSVAYPGRRPA--LRPVSFTVPPGERVALVGPSGAGK 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 433 STTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLREIIGVVSQEPVLFSTTIAENIRYGRGNVTMDEIEKAVKEANAYDFI 512
Cdd:TIGR02857 362 STLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLARPDASDAEIREALERAGLDEFV 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 513 MKLPQKFDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTIR 592
Cdd:TIGR02857 442 AALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAA 521
|
....*
gi 338817954 593 NADVI 597
Cdd:TIGR02857 522 LADRI 526
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
155-628 |
6.69e-66 |
|
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: 237.16 E-value: 6.69e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 155 LRQEMGWFDIKGTTELNTRlTDDVSKISEGIGDKvgMFFQAIATFFAGFIVG--FIRGWKLTLVIMAISPILGLSTAVWA 232
Cdd:TIGR03797 220 LRLPVSFFRQYSTGDLASR-AMGISQIRRILSGS--TLTTLLSGIFALLNLGlmFYYSWKLALVAVALALVAIAVTLVLG 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 233 KILSTFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKELERYQKHLENAKKIGIKKAISANI-SMGIAFLLIYASYAL 311
Cdd:TIGR03797 297 LLQVRKERRLLELSGKISGLTVQLINGISKLRVAGAENRAFARWAKLFSRQRKLELSAQRIENLlTVFNAVLPVLTSAAL 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 312 aFWYGSTLVISKEYTIGNAMTvfFSILIGAFSVGqaapcIDAFANARGAAYVIF-------DIIDNNPKIDsfsERGHKP 384
Cdd:TIGR03797 377 -FAAAISLLGGAGLSLGSFLA--FNTAFGSFSGA-----VTQLSNTLISILAVIplwerakPILEALPEVD---EAKTDP 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 385 DNIKGNLEFSDVHFSYPSRANIkILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRC 464
Cdd:TIGR03797 446 GKLSGAIEVDRVTFRYRPDGPL-ILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLDVQA 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 465 LREIIGVVSQEPVLFSTTIAENIrYGRGNVTMDEIEKAVKEANAYDFIMKLPQKFDTLVGDRGAQLSGGQKQRIAIARAL 544
Cdd:TIGR03797 525 VRRQLGVVLQNGRLMSGSIFENI-AGGAPLTLDEAWEAARMAGLAEDIRAMPMGMHTVISEGGGTLSGGQRQRLLIARAL 603
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 545 VRNPKILLLDEATSALDTESEAEVQAALDKAREGRttIVIAHRLSTIRNADVIAGFEDGVIVEQGSHSELMKKEGIYFRL 624
Cdd:TIGR03797 604 VRKPRILLFDEATSALDNRTQAIVSESLERLKVTR--IVIAHRLSTIRNADRIYVLDAGRVVQQGTYDELMAREGLFAQL 681
|
....
gi 338817954 625 VNMQ 628
Cdd:TIGR03797 682 ARRQ 685
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
389-610 |
6.82e-66 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 221.98 E-value: 6.82e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 389 GNLEFSDVHFSYpsRANIK-ILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLRE 467
Cdd:cd03244 1 GDIEFKNVSLRY--RPNLPpVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 468 IIGVVSQEPVLFSTTIAENI----RYgrgnvTMDEIEKAVKEANAYDFIMKLPQKFDTLVGDRGAQLSGGQKQRIAIARA 543
Cdd:cd03244 79 RISIIPQDPVLFSGTIRSNLdpfgEY-----SDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 338817954 544 LVRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTIRNADVIAGFEDGVIVEQGS 610
Cdd:cd03244 154 LLRKSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
19-627 |
3.50e-65 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 243.40 E-value: 3.50e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 19 ELGSISNQGREKKKKVNLIGLLTLFRYSDWQDKLFMFLGTLMAiahGSGLPLMMIVFGemtdKFVDNTGNFSlpvnfsls 98
Cdd:PTZ00265 795 KLPFLRNLFKRKPKAPNNLRIVYREIFSYKKDVTIIALSILVA---GGLYPVFALLYA----KYVSTLFDFA-------- 859
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 99 mlnpgrILEEEMTRYAYYYSGLGGGVLVAAYIQvSFWTLAAGRQIKK-IRQKFFHAILRQEMGWFDIKGTTE--LNTRLT 175
Cdd:PTZ00265 860 ------NLEANSNKYSLYILVIAIAMFISETLK-NYYNNVIGEKVEKtMKRRLFENILYQEISFFDQDKHAPglLSAHIN 932
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 176 DDVSKISEGIGDKVGMFFQAIATFFAGFIVGF----IRGWKLTLV------IMAISPILGLSTAVWAK-------ILSTF 238
Cdd:PTZ00265 933 RDVHLLKTGLVNNIVIFTHFIVLFLVSMVMSFyfcpIVAAVLTGTyfifmrVFAIRARLTANKDVEKKeinqpgtVFAYN 1012
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 239 SDKELAAYAKAGAvaEEALGAIRTVIAFGGQNKELERYQKHLENAKKIGIKKAISANISMGIAFLLIYASYALAFWYGST 318
Cdd:PTZ00265 1013 SDDEIFKDPSFLI--QEAFYNMNTVIIYGLEDYFCNLIEKAIDYSNKGQKRKTLVNSMLWGFSQSAQLFINSFAYWFGSF 1090
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 319 LVISKEYTIGNAMTVFFSILIGAFSVGQAAPCIDAFANARGAAYVIFDIIDNNPKIDSFSERGHKPDN---IKGNLEFSD 395
Cdd:PTZ00265 1091 LIRRGTILVDDFMKSLFTFLFTGSYAGKLMSLKGDSENAKLSFEKYYPLIIRKSNIDVRDNGGIRIKNkndIKGKIEIMD 1170
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 396 VHFSYPSRANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYD------------------------------- 444
Cdd:PTZ00265 1171 VNFRYISRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDlkndhhivfknehtndmtneqdyqgdeeqnv 1250
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 445 -----------------------PTEGKISIDGQDIRNFNVRCLREIIGVVSQEPVLFSTTIAENIRYGRGNVTMDEIEK 501
Cdd:PTZ00265 1251 gmknvnefsltkeggsgedstvfKNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKEDATREDVKR 1330
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 502 AVKEANAYDFIMKLPQKFDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAAL----DKAre 577
Cdd:PTZ00265 1331 ACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIvdikDKA-- 1408
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 338817954 578 GRTTIVIAHRLSTIRNADVIAGFED----GVIVE-QGSHSELMK-KEGIYFRLVNM 627
Cdd:PTZ00265 1409 DKTIITIAHRIASIKRSDKIVVFNNpdrtGSFVQaHGTHEELLSvQDGVYKKYVKL 1464
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
1029-1247 |
4.22e-65 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 219.77 E-value: 4.22e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1029 GSVTFNEVVFNYPTRANvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQWLRAQ 1108
Cdd:cd03245 1 GRIEFRNVSFSYPNQEI-PALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1109 LGIVSQEPILFDCSIAENIAYGDnsRVVPHDEIVRAAKEANIHPFIETLPQKYNTRVGDKGTQLSGGQKQRIAIARALIR 1188
Cdd:cd03245 80 IGYVPQDVTLFYGTLRDNITLGA--PLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLN 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 338817954 1189 QPRVLLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIENGKV 1247
Cdd:cd03245 158 DPPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
126-656 |
2.89e-64 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 229.21 E-value: 2.89e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 126 VAAYIQVSFWTL----AAGRQIKKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDDVSKISEGIGDKVGMFFQAIATFFA 201
Cdd:PRK10789 47 VVVYLLRYVWRVllfgASYQLAVELREDFYRQLSRQHPEFYLRHRTGDLMARATNDVDRVVFAAGEGVLTLVDSLVMGCA 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 202 GFIVGFIR-GWKLTLVIMAISPILGLSTAVWAKIL-----------STFSDKelaayakagavAEEALGAIRTVIAFGgq 269
Cdd:PRK10789 127 VLIVMSTQiSWQLTLLALLPMPVMAIMIKRYGDQLherfklaqaafSSLNDR-----------TQESLTSIRMIKAFG-- 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 270 nkeLERYQKHL--ENAKKIGIKKA----ISANISMGIaFLLIYASYALAFWYGSTLVISKEYTIGnAMTVFFSILigafs 343
Cdd:PRK10789 194 ---LEDRQSALfaADAEDTGKKNMrvarIDARFDPTI-YIAIGMANLLAIGGGSWMVVNGSLTLG-QLTSFVMYL----- 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 344 vGQAAPCIDAFA---N--ARG-AAYV-IFDIIDNNPKIDSfserGHKP-DNIKGNLEFSDVHFSYPsRANIKILKGLNLK 415
Cdd:PRK10789 264 -GLMIWPMLALAwmfNivERGsAAYSrIRAMLAEAPVVKD----GSEPvPEGRGELDVNIRQFTYP-QTDHPALENVNFT 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 416 VKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLREIIGVVSQEPVLFSTTIAENIRYGRGNVT 495
Cdd:PRK10789 338 LKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNIALGRPDAT 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 496 MDEIEKAVKEANAYDFIMKLPQKFDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKA 575
Cdd:PRK10789 418 QQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQW 497
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 576 REGRTTIVIAHRLSTIRNADVIAGFEDGVIVEQGSHSELMKKEGIYFRLVNMQtagsqilseEFEVELSDEKAAGDVAPN 655
Cdd:PRK10789 498 GEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSGWYRDMYRYQ---------QLEAALDDAPEIREEAVD 568
|
.
gi 338817954 656 G 656
Cdd:PRK10789 569 A 569
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
993-1242 |
1.65e-63 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 226.01 E-value: 1.65e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 993 DYAKAKLSAAYLFSLFERQPLIDSYSGEGLWPDkfEGSVTFNEVVFNYPTRAnvPVLQGLSLEVKKGQTLALVGSSGCGK 1072
Cdd:TIGR02857 286 ARADGVAAAEALFAVLDAAPRPLAGKAPVTAAP--ASSLEFSGVSVAYPGRR--PALRPVSFTVPPGERVALVGPSGAGK 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1073 STVVQLLERFYDPMAGSVLLDGQEAKKLNVQWLRAQLGIVSQEPILFDCSIAENIAYGDnsRVVPHDEIVRAAKEANIHP 1152
Cdd:TIGR02857 362 STLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLAR--PDASDAEIREALERAGLDE 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1153 FIETLPQKYNTRVGDKGTQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLST 1232
Cdd:TIGR02857 440 FVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLAL 519
|
250
....*....|
gi 338817954 1233 IQNADLIVVI 1242
Cdd:TIGR02857 520 AALADRIVVL 529
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
1028-1259 |
1.94e-63 |
|
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: 226.55 E-value: 1.94e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1028 EGSVTFNEVVFNYPtRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKklnvQWLRA 1107
Cdd:COG4618 328 KGRLSVENLTVVPP-GSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLS----QWDRE 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1108 QLG--I--VSQEPILFDCSIAENIA-YGDnsrvVPHDEIVRAAKEANIHPFIETLPQKYNTRVGDKGTQLSGGQKQRIAI 1182
Cdd:COG4618 403 ELGrhIgyLPQDVELFDGTIAENIArFGD----ADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGL 478
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 338817954 1183 ARALIRQPRVLLLDEATSALDTESEKVVQEALDKARE-GRTCIVIAHRLSTIQNADLIVVIENGKVKEHGTHQQLLAQ 1259
Cdd:COG4618 479 ARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKArGATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
780-1270 |
1.26e-62 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 224.59 E-value: 1.26e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 780 LTTRLRSMAFKAMLRQDMSWFDDHKnsTGALSTRLATDAAQVQGATGTR-LALIAQNTANLGTGIIISFIYGWQLTLLLL 858
Cdd:PRK10789 67 LAVELREDFYRQLSRQHPEFYLRHR--TGDLMARATNDVDRVVFAAGEGvLTLVDSLVMGCAVLIVMSTQISWQLTLLAL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 859 SVVPFIAVAgivemkmlagnAKRDKKEMEAAGKIATEAIE--NIRTVVSLTQERKFESMYVEKLHGPY---------RNS 927
Cdd:PRK10789 145 LPMPVMAIM-----------IKRYGDQLHERFKLAQAAFSslNDRTQESLTSIRMIKAFGLEDRQSALfaadaedtgKKN 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 928 VRKAHI---YGITFSISQAFMYFSYAGCfrfGSYLIVNGHMrfkdvilvfsaivlgavALGHASSFA--------PDYAK 996
Cdd:PRK10789 214 MRVARIdarFDPTIYIAIGMANLLAIGG---GSWMVVNGSL-----------------TLGQLTSFVmylglmiwPMLAL 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 997 AKL-------SAAY--LFSLFERQPLIDSysGEGLWPDKfEGSVTFNEVVFNYPTrANVPVLQGLSLEVKKGQTLALVGS 1067
Cdd:PRK10789 274 AWMfnivergSAAYsrIRAMLAEAPVVKD--GSEPVPEG-RGELDVNIRQFTYPQ-TDHPALENVNFTLKPGQMLGICGP 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1068 SGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQWLRAQLGIVSQEPILFDCSIAENIAYG--DNSRvvphDEIVRAA 1145
Cdd:PRK10789 350 TGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNIALGrpDATQ----QEIEHVA 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1146 KEANIHPFIETLPQKYNTRVGDKGTQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEALDKAREGRTCIV 1225
Cdd:PRK10789 426 RLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVII 505
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 338817954 1226 IAHRLSTIQNADLIVVIENGKVKEHGTHQQLLAQKGIYFSMVNIQ 1270
Cdd:PRK10789 506 SAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSGWYRDMYRYQ 550
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
126-626 |
1.89e-62 |
|
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: 227.31 E-value: 1.89e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 126 VAAYIQVSFWTLAAGRQIKKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDdVSKISEGIGDKV-GMFFQAIATFFAGFI 204
Cdd:TIGR01193 211 ILSYIQIFLLNVLGQRLSIDIILSYIKHLFELPMSFFSTRRTGEIVSRFTD-ASSIIDALASTIlSLFLDMWILVIVGLF 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 205 VGFiRGWKLTLVIMAISPILGLSTAVWAKILSTFSDKELAAYAKAGAVAEEALGAIRTVIAFGGqnkELERYQK------ 278
Cdd:TIGR01193 290 LVR-QNMLLFLLSLLSIPVYAVIIILFKRTFNKLNHDAMQANAVLNSSIIEDLNGIETIKSLTS---EAERYSKidsefg 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 279 -HLENAKKIGIKKAISANISMGIAFLLIyasyALAFWYGSTLVISKEYTIGNAMTvfFSILIGAFsvgqaapcIDAFANa 357
Cdd:TIGR01193 366 dYLNKSFKYQKADQGQQAIKAVTKLILN----VVILWTGAYLVMRGKLTLGQLIT--FNALLSYF--------LTPLEN- 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 358 rgaayvifdIIDNNPK----------------IDSFSERGHKPD---NIKGNLEFSDVHFSYPSRANIkiLKGLNLKVKS 418
Cdd:TIGR01193 431 ---------IINLQPKlqaarvannrlnevylVDSEFINKKKRTelnNLNGDIVINDVSYSYGYGSNI--LSDISLTIKM 499
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 419 GQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLREIIGVVSQEPVLFSTTIAENIRYG-RGNVTMD 497
Cdd:TIGR01193 500 NSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLGaKENVSQD 579
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 498 EIEKAVKEANAYDFIMKLPQKFDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKARE 577
Cdd:TIGR01193 580 EIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQD 659
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 338817954 578 gRTTIVIAHRLSTIRNADVIAGFEDGVIVEQGSHSELMKKEGIYFRLVN 626
Cdd:TIGR01193 660 -KTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYASLIH 707
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
330-624 |
9.46e-62 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 222.01 E-value: 9.46e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 330 AMTVF-----FSILI---GAFS-VGQaapCIdafanarGAAYVIFDIIDNNPKIdSFSERgHKPDNIKGNLEFSDVHFSY 400
Cdd:PRK11160 281 ALFVFaalaaFEALMpvaGAFQhLGQ---VI-------ASARRINEITEQKPEV-TFPTT-STAAADQVSLTLNNVSFTY 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 401 PSRANiKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLREIIGVVSQEPVLFS 480
Cdd:PRK11160 349 PDQPQ-PVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFS 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 481 TTIAENIRYGRGNVTmDEIEKAVKEANAYDFIMKLPQKFDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEATSAL 560
Cdd:PRK11160 428 ATLRDNLLLAAPNAS-DEALIEVLQQVGLEKLLEDDKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGL 506
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 338817954 561 DTESEAEVQAALDKAREGRTTIVIAHRLSTIRNADVIAGFEDGVIVEQGSHSELMKKEGIYFRL 624
Cdd:PRK11160 507 DAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQGRYYQL 570
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
388-617 |
3.11e-61 |
|
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: 220.39 E-value: 3.11e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 388 KGNLEFSDVHFSYPSRANIkILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLRE 467
Cdd:COG4618 328 KGRLSVENLTVVPPGSKRP-ILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGR 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 468 IIGVVSQEPVLFSTTIAENI-RYGrgNVTMDEIEKAVKEANAYDFIMKLPQKFDTLVGDRGAQLSGGQKQRIAIARALVR 546
Cdd:COG4618 407 HIGYLPQDVELFDGTIAENIaRFG--DADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYG 484
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 338817954 547 NPKILLLDEATSALDTESEAEVQAALDKARE-GRTTIVIAHRLSTIRNADVIAGFEDGVIVEQGSHSELMKK 617
Cdd:COG4618 485 DPRLVVLDEPNSNLDDEGEAALAAAIRALKArGATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
397-1275 |
3.19e-61 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 230.63 E-value: 3.19e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 397 HFSYPSRANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKiSIDgqdirnfnvrcLREIIGVVSQEP 476
Cdd:PLN03232 621 YFSWDSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETS-SVV-----------IRGSVAYVPQVS 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 477 VLFSTTIAENIRYGrGNVTMDEIEKAVK-EANAYDFIMkLPQKFDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDE 555
Cdd:PLN03232 689 WIFNATVRENILFG-SDFESERYWRAIDvTALQHDLDL-LPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDD 766
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 556 ATSALDTESEAEV-QAALDKAREGRTTIVIAHRLSTIRNADVIAGFEDGVIVEQGSHSELMKKEGIYFRLvnMQTAGSqi 634
Cdd:PLN03232 767 PLSALDAHVAHQVfDSCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELSKSGSLFKKL--MENAGK-- 842
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 635 LSEEFEVELSDEKAA--GDVAPNGWKARIFRNSTK-KSLKSPHQNRLDEETNELDANVppvsflkVLKLNKTEWPYFVVG 711
Cdd:PLN03232 843 MDATQEVNTNDENILklGPTVTIDVSERNLGSTKQgKRGRSVLVKQEERETGIISWNV-------LMRYNKAVGGLWVVM 915
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 712 T--VCAIANGALQPAFSIILSemiaiFGPGDDAVKQQKCNMFSLVFLGLGVLSFFTFFLQGFTFGKAGEILTTRLRSMAF 789
Cdd:PLN03232 916 IllVCYLTTEVLRVSSSTWLS-----IWTDQSTPKSYSPGFYIVVYALLGFGQVAVTFTNSFWLISSSLHAAKRLHDAML 990
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 790 KAMLRQDMSWFddHKNSTGALSTRLATDAAQvqgatgtrlalIAQNTANLGTGIIISFiygWQL--TLLLLSVVPFIAVA 867
Cdd:PLN03232 991 NSILRAPMLFF--HTNPTGRVINRFSKDIGD-----------IDRNVANLMNMFMNQL---WQLlsTFALIGTVSTISLW 1054
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 868 GIVEMKML-------AGNAKRDKKEMEAAGKIATEAI--ENIRTVVSLTQERKFESMyvEKLHGPYRN------------ 926
Cdd:PLN03232 1055 AIMPLLILfyaaylyYQSTSREVRRLDSVTRSPIYAQfgEALNGLSSIRAYKAYDRM--AKINGKSMDnnirftlantss 1132
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 927 ----SVRKAHIYGITFSISQAFMYFSYAGcfrfgsyliVNGHMRFKDVI-LVFSAIV----LGAVALGHASSFAPDYAKA 997
Cdd:PLN03232 1133 nrwlTIRLETLGGVMIWLTATFAVLRNGN---------AENQAGFASTMgLLLSYTLnittLLSGVLRQASKAENSLNSV 1203
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 998 KLSAAYLFSLFERQPLIDSYSGEGLWPDKfeGSVTFNEVVFNYptRANVP-VLQGLSLEVKKGQTLALVGSSGCGKSTVV 1076
Cdd:PLN03232 1204 ERVGNYIDLPSEATAIIENNRPVSGWPSR--GSIKFEDVHLRY--RPGLPpVLHGLSFFVSPSEKVGVVGRTGAGKSSML 1279
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1077 QLLERFYDPMAGSVLLDGQEAKKLNVQWLRAQLGIVSQEPILFDCSIAENIAygdnsrvvPHDE-----IVRAAKEANIH 1151
Cdd:PLN03232 1280 NALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNID--------PFSEhndadLWEALERAHIK 1351
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1152 PFIETLPQKYNTRVGDKGTQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLS 1231
Cdd:PLN03232 1352 DVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLN 1431
|
890 900 910 920
....*....|....*....|....*....|....*....|....
gi 338817954 1232 TIQNADLIVVIENGKVKEHGTHQQLLAQKGIYFSMVNIQAGTQN 1275
Cdd:PLN03232 1432 TIIDCDKILVLSSGQVLEYDSPQELLSRDTSAFFRMVHSTGPAN 1475
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
409-1266 |
3.34e-61 |
|
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: 230.60 E-value: 3.34e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 409 LKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQdirnfnvrclreiIGVVSQEPVLFSTTIAENIR 488
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS-------------VAYVPQQAWIQNDSLRENIL 720
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 489 YGRGnvTMDEIEKAVKEANAY--DFIMkLPQKFDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEA 566
Cdd:TIGR00957 721 FGKA--LNEKYYQQVLEACALlpDLEI-LPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGK 797
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 567 EVqaaLDKA------REGRTTIVIAHRLSTIRNADVIAGFEDGVIVEQGSHSELMKKEGIYFR-LVNMQTAGSQILSEEF 639
Cdd:TIGR00957 798 HI---FEHVigpegvLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAFAEfLRTYAPDEQQGHLEDS 874
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 640 EVEL-SDEKAAGDVAPNGW------KARIFRNSTKKSLKSPHQNRLDEETNELDANVPPVSFLKVLKLNKTE-------- 704
Cdd:TIGR00957 875 WTALvSGEGKEAKLIENGMlvtdvvGKQLQRQLSASSSDSGDQSRHHGSSAELQKAEAKEETWKLMEADKAQtgqvelsv 954
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 705 -WPY---------------FVVGTVCAIANGALQPAFSiilsemiaifgpgDDAV---KQQKCNMFSLVFLGLGVLSFFT 765
Cdd:TIGR00957 955 yWDYmkaiglfitflsiflFVCNHVSALASNYWLSLWT-------------DDPMvngTQNNTSLRLSVYGALGILQGFA 1021
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 766 FFLQGFTFGKAGEILTTRLRSMAFKAMLRQDMSWFDdhKNSTGALSTRLATDAAQVQGATGTRLALIAQNTAN-LGTGII 844
Cdd:TIGR00957 1022 VFGYSMAVSIGGIQASRVLHQDLLHNKLRSPMSFFE--RTPSGNLVNRFSKELDTVDSMIPPVIKMFMGSLFNvIGALIV 1099
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 845 ISFIygwqlTLLLLSVVPFIAVAGIVEMKMLAGNAkRDKKEMEAAGKIATEAIENiRTVVSLTQERKFEsmyveklhgpy 924
Cdd:TIGR00957 1100 ILLA-----TPIAAVIIPPLGLLYFFVQRFYVASS-RQLKRLESVSRSPVYSHFN-ETLLGVSVIRAFE----------- 1161
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 925 rNSVRKAHIYGITFSISQAfMYFSYAGCFRF---GSYLIVNGHMRFKDVILVFSAIVLGAVALGHASSFA---------- 991
Cdd:TIGR00957 1162 -EQERFIHQSDLKVDENQK-AYYPSIVANRWlavRLECVGNCIVLFAALFAVISRHSLSAGLVGLSVSYSlqvtfylnwl 1239
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 992 -----------------PDYAKAKLSAAYLfslferqplIDSYSGEGLWPDKfeGSVTFNEVVFNYPTRANVpVLQGLSL 1054
Cdd:TIGR00957 1240 vrmssemetnivaverlKEYSETEKEAPWQ---------IQETAPPSGWPPR--GRVEFRNYCLRYREDLDL-VLRHINV 1307
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1055 EVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQWLRAQLGIVSQEPILFDCSIAENI----AYG 1130
Cdd:TIGR00957 1308 TIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLdpfsQYS 1387
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1131 DnsrvvphDEIVRAAKEANIHPFIETLPQKYNTRVGDKGTQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTESEKVV 1210
Cdd:TIGR00957 1388 D-------EEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLI 1460
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|....*.
gi 338817954 1211 QEALDKAREGRTCIVIAHRLSTIQNADLIVVIENGKVKEHGTHQQLLAQKGIYFSM 1266
Cdd:TIGR00957 1461 QSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRGIFYSM 1516
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
1029-1252 |
1.72e-60 |
|
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: 206.58 E-value: 1.72e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1029 GSVTFNEVVFNYptRAN-VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQWLRA 1107
Cdd:cd03244 1 GDIEFKNVSLRY--RPNlPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1108 QLGIVSQEPILFDCSIAENIA----YGDnsrvvphDEIVRAAKEANIHPFIETLPQKYNTRVGDKGTQLSGGQKQRIAIA 1183
Cdd:cd03244 79 RISIIPQDPVLFSGTIRSNLDpfgeYSD-------EELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 338817954 1184 RALIRQPRVLLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIENGKVKEHGT 1252
Cdd:cd03244 152 RALLRKSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1000-1266 |
5.22e-58 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 211.22 E-value: 5.22e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1000 SAAYLFSLFERQPLIdSYSGEGLWPDKfEGSVTFNEVVFNYPTRANvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLL 1079
Cdd:PRK11160 310 SARRINEITEQKPEV-TFPTTSTAAAD-QVSLTLNNVSFTYPDQPQ-PVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLL 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1080 ERFYDPMAGSVLLDGQEAKKLNVQWLRAQLGIVSQEPILFDCSIAENIAYgdnsrvvphdeivrAAKEANIHPFIETL-- 1157
Cdd:PRK11160 387 TRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLL--------------AAPNASDEALIEVLqq 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1158 ---------PQKYNTRVGDKGTQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEALDKAREGRTCIVIAH 1228
Cdd:PRK11160 453 vgleklledDKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITH 532
|
250 260 270
....*....|....*....|....*....|....*...
gi 338817954 1229 RLSTIQNADLIVVIENGKVKEHGTHQQLLAQKGIYFSM 1266
Cdd:PRK11160 533 RLTGLEQFDRICVMDNGQIIEQGTHQELLAQQGRYYQL 570
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
755-1276 |
9.55e-58 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 210.73 E-value: 9.55e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 755 FLGLGVLSFFTFFLQGFTFGKAGEILTTRLRSMAFKAMLRQDMSWFDDHknSTGALSTRLATDAAQVQGATGTRLALIAQ 834
Cdd:PRK10790 71 YVGLQLLAAGLHYAQSLLFNRAAVGVVQQLRTDVMDAALRQPLSAFDTQ--PVGQLISRVTNDTEVIRDLYVTVVATVLR 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 835 NTANLGTGIIISFIYGWQLTLLLLSVVPFIAVAGIVEMKMLAGNAKRDKKEMEAAGKIATEAIENIRTVVSLTQERKF-E 913
Cdd:PRK10790 149 SAALIGAMLVAMFSLDWRMALVAIMIFPAVLVVMVIYQRYSTPIVRRVRAYLADINDGFNEVINGMSVIQQFRQQARFgE 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 914 SMyveklhgpyrNSVRKAHiygitfsisqafmYFSYAGCFRFGSYLIvnghmrfKDVILVFSAIVL------------GA 981
Cdd:PRK10790 229 RM----------GEASRSH-------------YMARMQTLRLDGFLL-------RPLLSLFSALILcgllmlfgfsasGT 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 982 VALGHASSFApdyakaklsaAYLFSLFErqPLID-----------SYSGEGLwpdkFE------------------GSVT 1032
Cdd:PRK10790 279 IEVGVLYAFI----------SYLGRLNE--PLIElttqqsmlqqaVVAGERV----FElmdgprqqygnddrplqsGRID 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1033 FNEVVFNYptRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQWLRAQLGIV 1112
Cdd:PRK10790 343 IDNVSFAY--RDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMV 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1113 SQEPILFDCSIAENIAYGdnsRVVPHDEIVRAAKEANIHPFIETLPQKYNTRVGDKGTQLSGGQKQRIAIARALIRQPRV 1192
Cdd:PRK10790 421 QQDPVVLADTFLANVTLG---RDISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQI 497
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1193 LLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIENGKVKEHGTHQQLLAQKGIYFSMVNIQAG 1272
Cdd:PRK10790 498 LILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQGRYWQMYQLQLA 577
|
....
gi 338817954 1273 TQNL 1276
Cdd:PRK10790 578 GEEL 581
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
395-1267 |
2.72e-57 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 218.45 E-value: 2.72e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 395 DVHFSYPSRANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQ-LLQRLYDPTEGKISIDGQdirnfnvrclreiIGVVS 473
Cdd:PLN03130 619 NGYFSWDSKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISaMLGELPPRSDASVVIRGT-------------VAYVP 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 474 QEPVLFSTTIAENIRYGrGNVTMDEIEKAVKEANAYDFIMKLPQKFDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLL 553
Cdd:PLN03130 686 QVSWIFNATVRDNILFG-SPFDPERYERAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIF 764
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 554 DEATSALDTESEAEV-QAALDKAREGRTTIVIAHRLSTIRNADVIAGFEDGVIVEQGSHSELMKKEGIYFRLvnMQTAGS 632
Cdd:PLN03130 765 DDPLSALDAHVGRQVfDKCIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSNNGPLFQKL--MENAGK 842
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 633 QILSEEFEVELSDEKAAGDVAPNGWKARIFRNSTKKSlKSPHQNRLDEETNELDANVppVSFlKVLKLNKTEWP-YFVVG 711
Cdd:PLN03130 843 MEEYVEENGEEEDDQTSSKPVANGNANNLKKDSSSKK-KSKEGKSVLIKQEERETGV--VSW-KVLERYKNALGgAWVVM 918
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 712 TV--CAIANGALQPAFSIILSEMIAIFGPgddavKQQKCNMFSLVFlglGVLSFftfflqgftfgkaGEILTT------- 782
Cdd:PLN03130 919 ILflCYVLTEVFRVSSSTWLSEWTDQGTP-----KTHGPLFYNLIY---ALLSF-------------GQVLVTllnsywl 977
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 783 ---------RLRSMAFKAMLRQDMSWFddHKNSTGALSTRLATDaaqvqgatgtrLALIAQNTANLGTGIIISFiygWQL 853
Cdd:PLN03130 978 imsslyaakRLHDAMLGSILRAPMSFF--HTNPLGRIINRFAKD-----------LGDIDRNVAVFVNMFLGQI---FQL 1041
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 854 --TLLLLSVVPFIAVAGIveMKMLAG---------NAKRDKKEMEaagkiateaienirtvvSLTQERKFeSMYVEKLHG 922
Cdd:PLN03130 1042 lsTFVLIGIVSTISLWAI--MPLLVLfygaylyyqSTAREVKRLD-----------------SITRSPVY-AQFGEALNG 1101
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 923 -----PYRNSVRKAHIYGITFSISQAFMYFSYAGCFRFGSYL-IVNGHMrfkdVILVFSAIVLGAVALGHASSFAP---- 992
Cdd:PLN03130 1102 lstirAYKAYDRMAEINGRSMDNNIRFTLVNMSSNRWLAIRLeTLGGLM----IWLTASFAVMQNGRAENQAAFAStmgl 1177
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 993 --DYA-------KAKLSAAYL----FSLFER-----------QPLIDSYSGEGLWPDKfeGSVTFNEVVFNYptRANVP- 1047
Cdd:PLN03130 1178 llSYAlnitsllTAVLRLASLaensLNAVERvgtyidlpseaPLVIENNRPPPGWPSS--GSIKFEDVVLRY--RPELPp 1253
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1048 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQWLRAQLGIVSQEPILFDCSIAENI 1127
Cdd:PLN03130 1254 VLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNL 1333
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1128 -AYGDNSRVvphdEIVRAAKEANIHPFIETLPQKYNTRVGDKGTQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTES 1206
Cdd:PLN03130 1334 dPFNEHNDA----DLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRT 1409
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 338817954 1207 EKVVQEALDKarEGRTC--IVIAHRLSTIQNADLIVVIENGKVKEHGTHQQLLAQKGIYFS-MV 1267
Cdd:PLN03130 1410 DALIQKTIRE--EFKSCtmLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEGSAFSkMV 1471
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
721-1268 |
2.33e-56 |
|
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: 209.21 E-value: 2.33e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 721 LQPAFSIILSEMIAIFGPgddavkQQKCNMFSLVFLGL-------GVLSFFtfflQGFTFGKAGEILTTRLRSMAFKAML 793
Cdd:TIGR01193 171 ISIAGSYYLQKIIDTYIP------HKMMGTLGIISIGLiiayiiqQILSYI----QIFLLNVLGQRLSIDIILSYIKHLF 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 794 RQDMSWFDDHKnsTGALSTRLaTDAAQVQGATG-TRLALIAqntaNLGTGIIISFIYGWQ---LTLLLLSVVPFIAVAGI 869
Cdd:TIGR01193 241 ELPMSFFSTRR--TGEIVSRF-TDASSIIDALAsTILSLFL----DMWILVIVGLFLVRQnmlLFLLSLLSIPVYAVIII 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 870 VEMKMLAgnaKRDKKEMEAAGKIATEAIEN---IRTVVSLTQE----RKFESMYVEKLHGPYRNS----VRKAHIYGITF 938
Cdd:TIGR01193 314 LFKRTFN---KLNHDAMQANAVLNSSIIEDlngIETIKSLTSEaerySKIDSEFGDYLNKSFKYQkadqGQQAIKAVTKL 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 939 SISQAFMYFsyagcfrfGSYLIVNGHMRFKDVIlVFSAIV-LGAVALGHASSFAPDYAKAK-----LSAAYLF-SLFERQ 1011
Cdd:TIGR01193 391 ILNVVILWT--------GAYLVMRGKLTLGQLI-TFNALLsYFLTPLENIINLQPKLQAARvannrLNEVYLVdSEFINK 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1012 PLIDSYSgeglwpdKFEGSVTFNEVVFNYPTraNVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVL 1091
Cdd:TIGR01193 462 KKRTELN-------NLNGDIVINDVSYSYGY--GSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEIL 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1092 LDGQEAKKLNVQWLRAQLGIVSQEPILFDCSIAENIAYGdNSRVVPHDEIVRAAKEANIHPFIETLPQKYNTRVGDKGTQ 1171
Cdd:TIGR01193 533 LNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLG-AKENVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSS 611
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1172 LSGGQKQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEALDKAREgRTCIVIAHRLSTIQNADLIVVIENGKVKEHG 1251
Cdd:TIGR01193 612 ISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQD-KTIIFVAHRLSVAKQSDKIIVLDHGKIIEQG 690
|
570
....*....|....*..
gi 338817954 1252 THQQLLAQKGIYFSMVN 1268
Cdd:TIGR01193 691 SHDELLDRNGFYASLIH 707
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
389-644 |
5.46e-55 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 202.64 E-value: 5.46e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 389 GNLEFSDVHFSYpsRANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLREI 468
Cdd:PRK10790 339 GRIDIDNVSFAY--RDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQG 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 469 IGVVSQEPVLFSTTIAENIRYGRgNVTMDEIEKAVKEANAYDFIMKLPQKFDTLVGDRGAQLSGGQKQRIAIARALVRNP 548
Cdd:PRK10790 417 VAMVQQDPVVLADTFLANVTLGR-DISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTP 495
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 549 KILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTIRNADVIAGFEDGVIVEQGSHSELMKKEGIYFRLVNMQ 628
Cdd:PRK10790 496 QILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQGRYWQMYQLQ 575
|
250
....*....|....*.
gi 338817954 629 TAGSQILSEEFEVELS 644
Cdd:PRK10790 576 LAGEELAASVREEESL 591
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
138-588 |
3.90e-54 |
|
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: 198.74 E-value: 3.90e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 138 AAGRQIKKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDDVskisEGIGDkvgMFFQAIATFFAGFIVGFIrgwkLTLVI 217
Cdd:TIGR02868 80 AALRSLGALRVRVYERLARQALAGRRRLRRGDLLGRLGADV----DALQD---LYVRVIVPAGVALVVGAA----AVAAI 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 218 MAISP----ILGLSTAVWAKILSTFS-----DKELAAYAKAGAVAEEALGAIR---TVIAFGGQNKELERYQKHLENAKK 285
Cdd:TIGR02868 149 AVLSVpaalILAAGLLLAGFVAPLVSlraarAAEQALARLRGELAAQLTDALDgaaELVASGALPAALAQVEEADRELTR 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 286 IGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTiGNAMTVFFSILIGAFSVGQAAP-CIDAFANARGAAYVI 364
Cdd:TIGR02868 229 AERRAAAATALGAALTLLAAGLAVLGALWAGGPAVADGRLA-PVTLAVLVLLPLAAFEAFAALPaAAQQLTRVRAAAERI 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 365 FDIIDNNPKIDSFSERGHKPDNIKG-NLEFSDVHFSYPSRAniKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLY 443
Cdd:TIGR02868 308 VEVLDAAGPVAEGSAPAAGAVGLGKpTLELRDLSAGYPGAP--PVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLL 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 444 DPTEGKISIDGQDIRNFNVRCLREIIGVVSQEPVLFSTTIAENIRYGRGNVTMDEIEKAVKEANAYDFIMKLPQKFDTLV 523
Cdd:TIGR02868 386 DPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPDATDEELWAALERVGLADWLRALPDGLDTVL 465
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 338817954 524 GDRGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRL 588
Cdd:TIGR02868 466 GEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
255-617 |
5.63e-54 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 198.34 E-value: 5.63e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 255 EALGAIRTViafggQNKELERYQKHLENAKKIGIKKAISANISMgiAFLLIYASYALAFwyGSTLVISKEYTIGnaMTVF 334
Cdd:TIGR01842 194 EAMGMMGNL-----TKRWGRFHSKYLSAQSAASDRAGMLSNLSK--YFRIVLQSLVLGL--GAYLAIDGEITPG--MMIA 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 335 FSILigafsVGQAAPCID-------AFANARGAAYVIFDIIDNNPkidsFSERGHKPDNIKGNLEFSDVHFSYPSrANIK 407
Cdd:TIGR01842 263 GSIL-----VGRALAPIDgaiggwkQFSGARQAYKRLNELLANYP----SRDPAMPLPEPEGHLSVENVTIVPPG-GKKP 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 408 ILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLREIIGVVSQEPVLFSTTIAENI 487
Cdd:TIGR01842 333 TLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKHIGYLPQDVELFPGTVAENI 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 488 -RYGRgNVTMDEIEKAVKEANAYDFIMKLPQKFDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEA 566
Cdd:TIGR01842 413 aRFGE-NADPEKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQ 491
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 338817954 567 EVQAALDKAR-EGRTTIVIAHRLSTIRNADVIAGFEDGVIVEQGSHSELMKK 617
Cdd:TIGR01842 492 ALANAIKALKaRGITVVVITHRPSLLGCVDKILVLQDGRIARFGERDEVLAK 543
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
353-624 |
1.07e-53 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 198.53 E-value: 1.07e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 353 AFANARGAAYVIFDIIDNNpkiDSFSERGHKPDNIKGNLEFSDVHFSYPSRANIKILKGLNLKVKSGQTVALVGNSGCGK 432
Cdd:PRK11174 313 AKAQAVGAAESLVTFLETP---LAHPQQGEKELASNDPVTIEAEDLEILSPDGKTLAGPLNFTLPAGQRIALVGPSGAGK 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 433 STTVQLLqrL-YDPTEGKISIDGQDIRNFNVRCLREIIGVVSQEPVLFSTTIAENIRYGRGNVTMDEIEKAVKEANAYDF 511
Cdd:PRK11174 390 TSLLNAL--LgFLPYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGNPDASDEQLQQALENAWVSEF 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 512 IMKLPQKFDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTI 591
Cdd:PRK11174 468 LPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLEDL 547
|
250 260 270
....*....|....*....|....*....|...
gi 338817954 592 RNADVIAGFEDGVIVEQGSHSELMKKEGIYFRL 624
Cdd:PRK11174 548 AQWDQIWVMQDGQIVQQGDYAELSQAGGLFATL 580
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
391-614 |
2.21e-52 |
|
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: 183.54 E-value: 2.21e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 391 LEFSDVHFSYpsrANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYD-----PTEGKISIDGQDIR--NFNVR 463
Cdd:cd03260 1 IELRDLNVYY---GDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYdlDVDVL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 464 CLREIIGVVSQEPVLFSTTIAENIRYG---RGNVTMDEIEKAVKEANAydfIMKLPQKfdtlVGDR--GAQLSGGQKQRI 538
Cdd:cd03260 78 ELRRRVGMVFQKPNPFPGSIYDNVAYGlrlHGIKLKEELDERVEEALR---KAALWDE----VKDRlhALGLSGGQQQRL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 338817954 539 AIARALVRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLS-TIRNADVIAGFEDGVIVEQGSHSEL 614
Cdd:cd03260 151 CLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQqAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1052-1266 |
1.22e-51 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 192.75 E-value: 1.22e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1052 LSLEVKKGQTLALVGSSGCGKSTVVQLLERFYdPMAGSVLLDGQEAKKLNVQWLRAQLGIVSQEPILFDCSIAENIAYGD 1131
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGN 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1132 NSrvVPHDEIVRAAKEANIHPFIETLPQKYNTRVGDKGTQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTESEKVVQ 1211
Cdd:PRK11174 448 PD--ASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVM 525
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 338817954 1212 EALDKAREGRTCIVIAHRLSTIQNADLIVVIENGKVKEHGTHQQLLAQKGIYFSM 1266
Cdd:PRK11174 526 QALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATL 580
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
391-618 |
1.31e-51 |
|
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: 181.38 E-value: 1.31e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 391 LEFSDVHFSYPSraNIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLREIIG 470
Cdd:COG1122 1 IELENLSFSYPG--GTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 471 VVSQEPV--LFSTTIAENIRYG---RGnVTMDEIEKAVKEA----NAYDFIMKLPQkfdtlvgdrgaQLSGGQKQRIAIA 541
Cdd:COG1122 79 LVFQNPDdqLFAPTVEEDVAFGpenLG-LPREEIRERVEEAlelvGLEHLADRPPH-----------ELSGGQKQRVAIA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 338817954 542 RALVRNPKILLLDEATSALDTESEAEVQAALDK-AREGRTTIVIAHRLSTI-RNADVIAGFEDGVIVEQGSHSELMKKE 618
Cdd:COG1122 147 GVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRlNKEGKTVIIVTHDLDLVaELADRVIVLDDGRIVADGTPREVFSDY 225
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
749-1259 |
3.77e-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: 190.25 E-value: 3.77e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 749 NMFSLVFLGLGVLSFFTFF-----LQGFTFGKAGEILTTRLRSMAFKAMLRQDMswfddhkNSTGALSTRLATDAAQVQG 823
Cdd:TIGR01842 41 SVPTLLMLTVLALGLYLFLglldaLRSFVLVRIGEKLDGALNQPIFAASFSATL-------RRGSGDGLQALRDLDQLRQ 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 824 ATGtrlaliaqntanlGTGIIISFIYGWQLTLLLLSVV--PFIAVAGIVEMKMLAG----NAKRDKKEME-------AAG 890
Cdd:TIGR01842 114 FLT-------------GPGLFAFFDAPWMPIYLLVCFLlhPWIGILALGGAVVLVGlallNNRATKKPLKeateasiRAN 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 891 KIATEAIENIRTVVSLTQERKFESMYvEKLHGPYRNSVRKAHIYGITFS-ISQAFMYFSYAGCFRFGSYLIVNGHMRFKD 969
Cdd:TIGR01842 181 NLADSALRNAEVIEAMGMMGNLTKRW-GRFHSKYLSAQSAASDRAGMLSnLSKYFRIVLQSLVLGLGAYLAIDGEITPGM 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 970 VILvfSAIVLGAvALG---HASSFAPDYAKAKLSAAYLFSLFERQPLIDsysgEGLWPDKFEGSVTFNEVVFnYPTRANV 1046
Cdd:TIGR01842 260 MIA--GSILVGR-ALApidGAIGGWKQFSGARQAYKRLNELLANYPSRD----PAMPLPEPEGHLSVENVTI-VPPGGKK 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1047 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKklnvQWLRAQLG----IVSQEPILFDCS 1122
Cdd:TIGR01842 332 PTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLK----QWDRETFGkhigYLPQDVELFPGT 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1123 IAENIA-YGDNsrvVPHDEIVRAAKEANIHPFIETLPQKYNTRVGDKGTQLSGGQKQRIAIARALIRQPRVLLLDEATSA 1201
Cdd:TIGR01842 408 VAENIArFGEN---ADPEKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSN 484
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 338817954 1202 LDTESEKVVQEALDKAR-EGRTCIVIAHRLSTIQNADLIVVIENGKVKEHGTHQQLLAQ 1259
Cdd:TIGR01842 485 LDEEGEQALANAIKALKaRGITVVVITHRPSLLGCVDKILVLQDGRIARFGERDEVLAK 543
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
391-615 |
4.00e-51 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 189.34 E-value: 4.00e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 391 LEFSDVHFSYPSRAN--IKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLREI 468
Cdd:COG1123 261 LEVRNLSKRYPVRGKggVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 469 ---IGVVSQEPV--LF-STTIAENIRYG---RGNVTMDEIEKAVKEAnaydfiMK---LPQKFdtlvGDR-GAQLSGGQK 535
Cdd:COG1123 341 rrrVQMVFQDPYssLNpRMTVGDIIAEPlrlHGLLSRAERRERVAEL------LErvgLPPDL----ADRyPHELSGGQR 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 536 QRIAIARALVRNPKILLLDEATSALDTESEAEVQAALD--KAREGRTTIVIAHRLSTIRN-ADVIAGFEDGVIVEQGSHS 612
Cdd:COG1123 411 QRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRdlQRELGLTYLFISHDLAVVRYiADRVAVMYDGRIVEDGPTE 490
|
...
gi 338817954 613 ELM 615
Cdd:COG1123 491 EVF 493
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
392-603 |
1.11e-50 |
|
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: 178.04 E-value: 1.11e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 392 EFSDVHFSYPSRANiKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLREIIGV 471
Cdd:cd03225 1 ELKNLSFSYPDGAR-PALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 472 VSQEP--VLFSTTIAENIRYGRGN--VTMDEIEKAVKEANAydfimklpqkfdtLVGDRG------AQLSGGQKQRIAIA 541
Cdd:cd03225 80 VFQNPddQFFGPTVEEEVAFGLENlgLPEEEIEERVEEALE-------------LVGLEGlrdrspFTLSGGQKQRVAIA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 338817954 542 RALVRNPKILLLDEATSALDTESEAEVQAALDK-AREGRTTIVIAHRLSTIRN-ADVIAGFEDG 603
Cdd:cd03225 147 GVLAMDPDILLLDEPTAGLDPAGRRELLELLKKlKAEGKTIIIVTHDLDLLLElADRVIVLEDG 210
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
391-605 |
3.20e-49 |
|
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: 172.40 E-value: 3.20e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 391 LEFSDVHFSYPSRANiKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLREIIG 470
Cdd:cd03246 1 LEVENVSFRYPGAEP-PVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 471 VVSQEPVLFSTTIAENIrygrgnvtmdeiekavkeanaydfimklpqkfdtlvgdrgaqLSGGQKQRIAIARALVRNPKI 550
Cdd:cd03246 80 YLPQDDELFSGSIAENI------------------------------------------LSGGQRQRLGLARALYGNPRI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 338817954 551 LLLDEATSALDTESEAEVQAALDKARE-GRTTIVIAHRLSTIRNADVIAGFEDGVI 605
Cdd:cd03246 118 LVLDEPNSHLDVEGERALNQAIAALKAaGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
1031-1260 |
4.22e-48 |
|
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: 171.36 E-value: 4.22e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1031 VTFNEVVFNYPTraNVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQWLRAQLG 1110
Cdd:COG1122 1 IELENLSFSYPG--GTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1111 IVSQEPI--LFDCSIAENIAYGDNSRVVPHDEIVRAAKEA----NIHPFIETLPQkyntrvgdkgtQLSGGQKQRIAIAR 1184
Cdd:COG1122 79 LVFQNPDdqLFAPTVEEDVAFGPENLGLPREEIRERVEEAlelvGLEHLADRPPH-----------ELSGGQKQRVAIAG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 338817954 1185 ALIRQPRVLLLDEATSALDTESEKVVQEALDK-AREGRTCIVIAHRLSTI-QNADLIVVIENGKVKEHGTHQQLLAQK 1260
Cdd:COG1122 148 VLAMEPEVLVLDEPTAGLDPRGRRELLELLKRlNKEGKTVIIVTHDLDLVaELADRVIVLDDGRIVADGTPREVFSDY 225
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
1036-1247 |
5.05e-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: 168.93 E-value: 5.05e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1036 VVFNYPTRANvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQWLRAQLGIVSQE 1115
Cdd:cd03246 6 VSFRYPGAEP-PVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGYLPQD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1116 PILFDCSIAENIaygdnsrvvphdeivraakeanihpfietlpqkyntrvgdkgtqLSGGQKQRIAIARALIRQPRVLLL 1195
Cdd:cd03246 85 DELFSGSIAENI--------------------------------------------LSGGQRQRLGLARALYGNPRILVL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 338817954 1196 DEATSALDTESEKVVQEALDKARE-GRTCIVIAHRLSTIQNADLIVVIENGKV 1247
Cdd:cd03246 121 DEPNSHLDVEGERALNQAIAALKAaGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
1048-1256 |
6.95e-48 |
|
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: 170.82 E-value: 6.95e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1048 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYD-----PMAGSVLLDGQE--AKKLNVQWLRAQLGIVSQEPILFD 1120
Cdd:cd03260 15 ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDiyDLDVDVLELRRRVGMVFQKPNPFP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1121 CSIAENIAYGDNSR-VVPH---DEIVRAA-KEANIHPfietlpqkyntRVGDK--GTQLSGGQKQRIAIARALIRQPRVL 1193
Cdd:cd03260 95 GSIYDNVAYGLRLHgIKLKeelDERVEEAlRKAALWD-----------EVKDRlhALGLSGGQQQRLCLARALANEPEVL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 338817954 1194 LLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHGTHQQL 1256
Cdd:cd03260 164 LLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARvADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
409-558 |
1.57e-47 |
|
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: 166.67 E-value: 1.57e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 409 LKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLREIIGVVSQEPVLFS-TTIAENI 487
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPrLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 338817954 488 RYGRgnvTMDEIEKAVKEANAYDFIMKLPQKF--DTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEATS 558
Cdd:pfam00005 81 RLGL---LLKGLSKREKDARAEEALEKLGLGDlaDRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
391-610 |
1.81e-47 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 173.34 E-value: 1.81e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 391 LEFSDVHFSYPSRAN-IKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLREI- 468
Cdd:COG1135 2 IELENLSKTFPTKGGpVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAAr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 469 --IGVVSQEPVLFST-TIAENIRY-----GrgnVTMDEIEKAVKE----------ANAYdfimklPqkfdtlvgdrgAQL 530
Cdd:COG1135 82 rkIGMIFQHFNLLSSrTVAENVALpleiaG---VPKAEIRKRVAEllelvglsdkADAY------P-----------SQL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 531 SGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKARE--GRTTIVIAHRLSTIRN-ADVIAGFEDGVIVE 607
Cdd:COG1135 142 SGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRelGLTIVLITHEMDVVRRiCDRVAVLENGRIVE 221
|
...
gi 338817954 608 QGS 610
Cdd:COG1135 222 QGP 224
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
391-609 |
2.27e-47 |
|
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: 167.49 E-value: 2.27e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 391 LEFSDVHFSYPSRaNIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNvRCLREIIG 470
Cdd:cd03247 1 LSINNVSFSYPEQ-EQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 471 VVSQEPVLFSTTIAENIrygrgnvtmdeiekavkeanaydfimklpqkfdtlvgdrGAQLSGGQKQRIAIARALVRNPKI 550
Cdd:cd03247 79 VLNQRPYLFDTTLRNNL---------------------------------------GRRFSGGERQRLALARILLQDAPI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 338817954 551 LLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTIRNADVIAGFEDGVIVEQG 609
Cdd:cd03247 120 VLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
391-586 |
2.94e-47 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 168.07 E-value: 2.94e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 391 LEFSDVHFSYPSRaniKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLREIIG 470
Cdd:COG4619 1 LELEGLSFRVGGK---PILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 471 VVSQEPVLFSTTIAENI----RYGRGNVTMDEIEKAVKEANaydfimkLPQKF-DTLVgdrgAQLSGGQKQRIAIARALV 545
Cdd:COG4619 78 YVPQEPALWGGTVRDNLpfpfQLRERKFDRERALELLERLG-------LPPDIlDKPV----ERLSGGERQRLALIRALL 146
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 338817954 546 RNPKILLLDEATSALDTESEAEVQAALDK--AREGRTTIVIAH 586
Cdd:COG4619 147 LQPDVLLLDEPTSALDPENTRRVEELLREylAEEGRAVLWVSH 189
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
391-614 |
3.44e-47 |
|
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: 168.91 E-value: 3.44e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 391 LEFSDVHFSYPSRAN-IKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDI---RNFNVRCLR 466
Cdd:cd03258 2 IELKNVSKVFGDTGGkVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLtllSGKELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 467 EIIGVVSQEPVLFST-TIAENIRYGR--GNVTMDEIEKAVKEanaydfimklpqkFDTLVG--DRG----AQLSGGQKQR 537
Cdd:cd03258 82 RRIGMIFQHFNLLSSrTVFENVALPLeiAGVPKAEIEERVLE-------------LLELVGleDKAdaypAQLSGGQKQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 538 IAIARALVRNPKILLLDEATSALDTESEAEVQAALDK--AREGRTTIVIAHRLSTIRN-ADVIAGFEDGVIVEQGSHSEL 614
Cdd:cd03258 149 VGIARALANNPKVLLCDEATSALDPETTQSILALLRDinRELGLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEEV 228
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
391-609 |
4.76e-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: 168.45 E-value: 4.76e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 391 LEFSDVHFSYPSRAN-IKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLREI- 468
Cdd:cd03257 2 LEVKNLSVSFPTGGGsVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIRr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 469 --IGVVSQEPV-----LFS--TTIAENIRYGRGNVTMDEIEKAVKEA-----NAYDFIMKLPqkfdtlvgdrgAQLSGGQ 534
Cdd:cd03257 82 keIQMVFQDPMsslnpRMTigEQIAEPLRIHGKLSKKEARKEAVLLLlvgvgLPEEVLNRYP-----------HELSGGQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 338817954 535 KQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKARE--GRTTIVIAHRLSTIRN-ADVIAGFEDGVIVEQG 609
Cdd:cd03257 151 RQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEelGLTLLFITHDLGVVAKiADRVAVMYAGKIVEEG 228
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1031-1259 |
5.50e-47 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 177.02 E-value: 5.50e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1031 VTFNEVVFNYPTRAN--VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLN---VQWL 1105
Cdd:COG1123 261 LEVRNLSKRYPVRGKggVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSrrsLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1106 RAQLGIVSQEPIL-FDC--SIAENIAYG-DNSRVVPHDEIVRAAKE-----------ANIHPFietlpqkyntrvgdkgt 1170
Cdd:COG1123 341 RRRVQMVFQDPYSsLNPrmTVGDIIAEPlRLHGLLSRAERRERVAEllervglppdlADRYPH----------------- 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1171 QLSGGQKQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEALD--KAREGRTCIVIAHRLSTIQN-ADLIVVIENGKV 1247
Cdd:COG1123 404 ELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRdlQRELGLTYLFISHDLAVVRYiADRVAVMYDGRI 483
|
250
....*....|..
gi 338817954 1248 KEHGTHQQLLAQ 1259
Cdd:COG1123 484 VEDGPTEEVFAN 495
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
1033-1246 |
2.26e-46 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 165.72 E-value: 2.26e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1033 FNEVVFNYPTRaNVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQWLRAQLGIV 1112
Cdd:cd03225 2 LKNLSFSYPDG-ARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1113 SQEP--ILFDCSIAENIAYGDNSRVVPHDEIVRAAKEA----NIHPFIETLPQkyntrvgdkgtQLSGGQKQRIAIARAL 1186
Cdd:cd03225 81 FQNPddQFFGPTVEEEVAFGLENLGLPEEEIEERVEEAlelvGLEGLRDRSPF-----------TLSGGQKQRVAIAGVL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 338817954 1187 IRQPRVLLLDEATSALDTESEKVVQEALDK-AREGRTCIVIAHRLSTIQN-ADLIVVIENGK 1246
Cdd:cd03225 150 AMDPDILLLDEPTAGLDPAGRRELLELLKKlKAEGKTIIIVTHDLDLLLElADRVIVLEDGK 211
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
1047-1247 |
3.04e-46 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 165.37 E-value: 3.04e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1047 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQWLRAQLGIVSQEPILFDCSIAEN 1126
Cdd:COG4619 14 PILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYVPQEPALWGGTVRDN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1127 IAYGDNSRVVPHDE--IVRAAKEANIHPFIetlpqkYNTRVgdkgTQLSGGQKQRIAIARALIRQPRVLLLDEATSALDT 1204
Cdd:COG4619 94 LPFPFQLRERKFDRerALELLERLGLPPDI------LDKPV----ERLSGGERQRLALIRALLLQPDVLLLDEPTSALDP 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 338817954 1205 ESEKVVQEALDK--AREGRTCIVIAHRLSTIQN-ADLIVVIENGKV 1247
Cdd:COG4619 164 ENTRRVEELLREylAEEGRAVLWVSHDPEQIERvADRVLTLEAGRL 209
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
1023-1252 |
3.54e-46 |
|
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: 164.89 E-value: 3.54e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1023 WPDkfEGSVTFNEVVFNYptRANVP-VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLN 1101
Cdd:cd03369 1 WPE--HGEIEVENLSVRY--APDLPpVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1102 VQWLRAQLGIVSQEPILFDCSIAENI-AYGDNSrvvphDEIVRAAkeanihpfietlpqkynTRVGDKGTQLSGGQKQRI 1180
Cdd:cd03369 77 LEDLRSSLTIIPQDPTLFSGTIRSNLdPFDEYS-----DEEIYGA-----------------LRVSEGGLNLSQGQRQLL 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 338817954 1181 AIARALIRQPRVLLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIENGKVKEHGT 1252
Cdd:cd03369 135 CLARALLKRPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
391-614 |
1.28e-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: 164.40 E-value: 1.28e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 391 LEFSDVHFSYpsrANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDI--RNFNVRCLREI 468
Cdd:COG1126 2 IEIENLHKSF---GDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLtdSKKDINKLRRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 469 IGVVSQEPVLFS-TTIAENIRYG----RGnvtMDEiEKAVKEAnaydfiMKLPQKfdtlVG--DRG----AQLSGGQKQR 537
Cdd:COG1126 79 VGMVFQQFNLFPhLTVLENVTLApikvKK---MSK-AEAEERA------MELLER----VGlaDKAdaypAQLSGGQQQR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 338817954 538 IAIARALVRNPKILLLDEATSALDTESEAEVQAAL-DKAREGRTTIVIAHRLSTIRN-ADVIAGFEDGVIVEQGSHSEL 614
Cdd:COG1126 145 VAIARALAMEPKVMLFDEPTSALDPELVGEVLDVMrDLAKEGMTMVVVTHEMGFAREvADRVVFMDGGRIVEEGPPEEF 223
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
391-608 |
1.63e-45 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 163.68 E-value: 1.63e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 391 LEFSDVHFSYPSRAN-IKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLREI- 468
Cdd:COG1136 5 LELRNLTKSYGTGEGeVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELARLr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 469 ---IGVVSQEPVLFST-TIAENIRYGR--GNVTMDEIEKAVKEANAY----DFIMKLPqkfdtlvgdrgAQLSGGQKQRI 538
Cdd:COG1136 85 rrhIGFVFQFFNLLPElTALENVALPLllAGVSRKERRERARELLERvglgDRLDHRP-----------SQLSGGQQQRV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 338817954 539 AIARALVRNPKILLLDEATSALDTESEAEVQAALDK-AREGRTTIVIA-HRLSTIRNADVIAGFEDGVIVEQ 608
Cdd:COG1136 154 AIARALVNRPKLILADEPTGNLDSKTGEEVLELLRElNRELGTTIVMVtHDPELAARADRVIRLRDGRIVSD 225
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
1031-1251 |
1.67e-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: 162.10 E-value: 1.67e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1031 VTFNEVVFNYPTRaNVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQwLRAQLG 1110
Cdd:cd03247 1 LSINNVSFSYPEQ-EQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKA-LSSLIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1111 IVSQEPILFDCSIAENIaygdnsrvvphdeivraakeanihpfietlpqkyntrvgdkGTQLSGGQKQRIAIARALIRQP 1190
Cdd:cd03247 79 VLNQRPYLFDTTLRNNL-----------------------------------------GRRFSGGERQRLALARILLQDA 117
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 338817954 1191 RVLLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIENGKVKEHG 1251
Cdd:cd03247 118 PIVLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
391-626 |
1.80e-45 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 164.08 E-value: 1.80e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 391 LEFSDVHFSYpsrANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRcLREIIG 470
Cdd:COG1131 1 IEVRGLTKRY---GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAE-VRRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 471 VVSQEPVLFST-TIAENIRYGRG--NVTMDEIEKAVKEANAydfIMKLPQKFDTLVGdrgaQLSGGQKQRIAIARALVRN 547
Cdd:COG1131 77 YVPQEPALYPDlTVRENLRFFARlyGLPRKEARERIDELLE---LFGLTDAADRKVG----TLSGGMKQRLGLALALLHD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 548 PKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIA-HRLSTI-RNADVIAGFEDGVIVEQGSHSELMKK--EGIYFR 623
Cdd:COG1131 150 PELLILDEPTSGLDPEARRELWELLRELAAEGKTVLLStHYLEEAeRLCDRVAIIDKGRIVADGTPDELKARllEDVFLE 229
|
...
gi 338817954 624 LVN 626
Cdd:COG1131 230 LTG 232
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
389-610 |
7.64e-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: 161.04 E-value: 7.64e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 389 GNLEFSDVHFSYpsRANI-KILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLRE 467
Cdd:cd03369 5 GEIEVENLSVRY--APDLpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 468 IIGVVSQEPVLFSTTIAENI-RYGRgnVTMDEIEKAVKeanaydfimklpqkfdtlVGDRGAQLSGGQKQRIAIARALVR 546
Cdd:cd03369 83 SLTIIPQDPTLFSGTIRSNLdPFDE--YSDEEIYGALR------------------VSEGGLNLSQGQRQLLCLARALLK 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 338817954 547 NPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTIRNADVIAGFEDGVIVEQGS 610
Cdd:cd03369 143 RPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
391-616 |
9.83e-45 |
|
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: 162.07 E-value: 9.83e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 391 LEFSDVHFSYPSRaniKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLREI-- 468
Cdd:COG1127 6 IEVRNLTKSFGDR---VVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYELrr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 469 -IGVVSQEPVLFST-TIAENIRYG---RGNVTMDEIEKAVkeanaydfIMKLpqkfdTLVGDRGA------QLSGGQKQR 537
Cdd:COG1127 83 rIGMLFQGGALFDSlTVFENVAFPlreHTDLSEAEIRELV--------LEKL-----ELVGLPGAadkmpsELSGGMRKR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 538 IAIARALVRNPKILLLDEATSALDTESEAEVQAALDKARE--GRTTIVIAHRLSTIRN-ADVIAGFEDGVIVEQGSHSEL 614
Cdd:COG1127 150 VALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDelGLTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPEEL 229
|
..
gi 338817954 615 MK 616
Cdd:COG1127 230 LA 231
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
391-609 |
1.32e-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: 160.76 E-value: 1.32e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 391 LEFSDVHFSYPSranIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRclREIIG 470
Cdd:cd03259 1 LELKGLSKTYGS---VRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE--RRNIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 471 VVSQEPVLFST-TIAENIRYG--RGNVTMDEIEKAVKEANAydfimklpqkfdtLVGDRG------AQLSGGQKQRIAIA 541
Cdd:cd03259 76 MVFQDYALFPHlTVAENIAFGlkLRGVPKAEIRARVRELLE-------------LVGLEGllnrypHELSGGQQQRVALA 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 338817954 542 RALVRNPKILLLDEATSALDTESEAEVQAALDK--AREGRTTIVIAHRLS-TIRNADVIAGFEDGVIVEQG 609
Cdd:cd03259 143 RALAREPSLLLLDEPLSALDAKLREELREELKElqRELGITTIYVTHDQEeALALADRIAVMNEGRIVQVG 213
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
391-603 |
1.62e-44 |
|
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: 159.27 E-value: 1.62e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 391 LEFSDVHFSYpsrANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIR--NFNVRCLREI 468
Cdd:cd03229 1 LELKNVSKRY---GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTdlEDELPPLRRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 469 IGVVSQEPVLFST-TIAENIRYGrgnvtmdeiekavkeanaydfimklpqkfdtlvgdrgaqLSGGQKQRIAIARALVRN 547
Cdd:cd03229 78 IGMVFQDFALFPHlTVLENIALG---------------------------------------LSGGQQQRVALARALAMD 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 338817954 548 PKILLLDEATSALDTESEAEVQAALD--KAREGRTTIVIAHRLS-TIRNADVIAGFEDG 603
Cdd:cd03229 119 PDVLLLDEPTSALDPITRREVRALLKslQAQLGITVVLVTHDLDeAARLADRVVVLRDG 177
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
113-636 |
4.84e-44 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 175.55 E-value: 4.84e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 113 YAYYYSGLGGGvLVAAYIQVSFWTLAAG-RQIKKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDDVSKISEGIGDKVGM 191
Cdd:PLN03232 952 YIVVYALLGFG-QVAVTFTNSFWLISSSlHAAKRLHDAMLNSILRAPMLFFHTNPTGRVINRFSKDIGDIDRNVANLMNM 1030
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 192 F----FQAIATFFAGFIVGFIRGWkltlvimAISPILGLSTAVWAKILSTFSD-KELAAYAKAGAVAE--EALGAIRTVI 264
Cdd:PLN03232 1031 FmnqlWQLLSTFALIGTVSTISLW-------AIMPLLILFYAAYLYYQSTSREvRRLDSVTRSPIYAQfgEALNGLSSIR 1103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 265 AFGGQNKELERYQKHLENAKKIGIKkAISAN-------ISMGIAFLLIYASYALAFW--------YGSTLVISKEYTIgN 329
Cdd:PLN03232 1104 AYKAYDRMAKINGKSMDNNIRFTLA-NTSSNrwltirlETLGGVMIWLTATFAVLRNgnaenqagFASTMGLLLSYTL-N 1181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 330 AMTVFFSILIGAFSVGQAAPCIDAFANARGAAYVIFDIIDNNPKIDSFSERGhkpdnikgNLEFSDVHFSYpsRANIK-I 408
Cdd:PLN03232 1182 ITTLLSGVLRQASKAENSLNSVERVGNYIDLPSEATAIIENNRPVSGWPSRG--------SIKFEDVHLRY--RPGLPpV 1251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 409 LKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLREIIGVVSQEPVLFSTTIAENIR 488
Cdd:PLN03232 1252 LHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNID 1331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 489 -YGRGNVTmdEIEKAVKEANAYDFIMKLPQKFDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAE 567
Cdd:PLN03232 1332 pFSEHNDA--DLWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSL 1409
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 338817954 568 VQAALDKAREGRTTIVIAHRLSTIRNADVIAGFEDGVIVEQGSHSELMKKEG-IYFRLVNMQ-TAGSQILS 636
Cdd:PLN03232 1410 IQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTsAFFRMVHSTgPANAQYLS 1480
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
391-615 |
4.94e-44 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 168.16 E-value: 4.94e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 391 LEFSDVHFSYPSRANiKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPT---EGKISIDGQDIRNFNVRCLRE 467
Cdd:COG1123 5 LEVRDLSVRYPGGDV-PAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 468 IIGVVSQEP--VLFSTTIAENIRYG--RGNVTMDEIEKAVKEANAYDFImklpqkfDTLVGDRGAQLSGGQKQRIAIARA 543
Cdd:COG1123 84 RIGMVFQDPmtQLNPVTVGDQIAEAleNLGLSRAEARARVLELLEAVGL-------ERRLDRYPHQLSGGQRQRVAIAMA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 338817954 544 LVRNPKILLLDEATSALDTESEAEVQAALDK--AREGRTTIVIAHRLSTI-RNADVIAGFEDGVIVEQGSHSELM 615
Cdd:COG1123 157 LALDPDLLIADEPTTALDVTTQAEILDLLRElqRERGTTVLLITHDLGVVaEIADRVVVMDDGRIVEDGPPEEIL 231
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
1042-1251 |
7.89e-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: 158.45 E-value: 7.89e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1042 TRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQwlRAQLGIVSQEPILFD- 1120
Cdd:cd03259 9 TYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE--RRNIGMVFQDYALFPh 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1121 CSIAENIAYGDNSRVVPHDEIVRAAKEA----NIHPFIETLPqkyntrvgdkgTQLSGGQKQRIAIARALIRQPRVLLLD 1196
Cdd:cd03259 87 LTVAENIAFGLKLRGVPKAEIRARVRELlelvGLEGLLNRYP-----------HELSGGQQQRVALARALAREPSLLLLD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 338817954 1197 EATSALDTESEKVVQEALDK--AREGRTCIVIAHRLS-TIQNADLIVVIENGKVKEHG 1251
Cdd:cd03259 156 EPLSALDAKLREELREELKElqRELGITTIYVTHDQEeALALADRIAVMNEGRIVQVG 213
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
391-615 |
9.66e-44 |
|
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: 159.39 E-value: 9.66e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 391 LEFSDVHFSYPSRAniKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLREIIG 470
Cdd:cd03295 1 IEFENVTKRYGGGK--KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 471 VVSQEPVLFS-TTIAENIrygrGNV-TMDEIEKAVKEANAYDfIMKL----PQKFdtlvGDR-GAQLSGGQKQRIAIARA 543
Cdd:cd03295 79 YVIQQIGLFPhMTVEENI----ALVpKLLKWPKEKIRERADE-LLALvgldPAEF----ADRyPHELSGGQQQRVGVARA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 338817954 544 LVRNPKILLLDEATSALDTESEAEVQAALDKARE--GRTTIVIAHRL-STIRNADVIAGFEDGVIVEQGSHSELM 615
Cdd:cd03295 150 LAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQelGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEIL 224
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
973-1230 |
1.21e-43 |
|
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: 167.54 E-value: 1.21e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 973 VFSAIVLGAVALGHASSFAPDYA----KAKLSAAYLFSLFERQPLIDSYSG---EGLWPDKFegSVTFNEVVFNYPTRAn 1045
Cdd:TIGR02868 272 TLAVLVLLPLAAFEAFAALPAAAqqltRVRAAAERIVEVLDAAGPVAEGSApaaGAVGLGKP--TLELRDLSAGYPGAP- 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1046 vPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQWLRAQLGIVSQEPILFDCSIAE 1125
Cdd:TIGR02868 349 -PVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRE 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1126 N--IAYGDnsrvVPHDEIVRAAKEANIHPFIETLPQKYNTRVGDKGTQLSGGQKQRIAIARALIRQPRVLLLDEATSALD 1203
Cdd:TIGR02868 428 NlrLARPD----ATDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLD 503
|
250 260
....*....|....*....|....*..
gi 338817954 1204 TESEKVVQEALDKAREGRTCIVIAHRL 1230
Cdd:TIGR02868 504 AETADELLEDLLAALSGRTVVLITHHL 530
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
391-605 |
1.32e-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: 158.04 E-value: 1.32e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 391 LEFSDVHFSYPSRAN-IKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLREI- 468
Cdd:cd03255 1 IELKNLSKTYGGGGEkVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 469 ---IGVVSQEPVLFST-TIAENIRYGrgnVTMDEIEKAVKEANAYDFI--MKLPQKFDTLVgdrgAQLSGGQKQRIAIAR 542
Cdd:cd03255 81 rrhIGFVFQSFNLLPDlTALENVELP---LLLAGVPKKERRERAEELLerVGLGDRLNHYP----SELSGGQQQRVAIAR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 338817954 543 ALVRNPKILLLDEATSALDTESEAEVQAAL-DKAREGRTTIVIA-HRLSTIRNADVIAGFEDGVI 605
Cdd:cd03255 154 ALANDPKIILADEPTGNLDSETGKEVMELLrELNKEAGTTIVVVtHDPELAEYADRIIELRDGKI 218
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
391-618 |
1.84e-43 |
|
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: 159.05 E-value: 1.84e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 391 LEFSDVHFSYPSRAnikILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLREIIG 470
Cdd:COG1120 2 LEAENLSVGYGGRP---VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 471 VVSQEPVL-FSTTIAENIRYGR-------GNVT---MDEIEKAVKEANAYDFIMKLpqkFDTlvgdrgaqLSGGQKQRIA 539
Cdd:COG1120 79 YVPQEPPApFGLTVRELVALGRyphlglfGRPSaedREAVEEALERTGLEHLADRP---VDE--------LSGGERQRVL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 540 IARALVRNPKILLLDEATSALDTESEAEVQAALDK--AREGRTTIVIAHRLS-TIRNADVIAGFEDGVIVEQGSHSELMK 616
Cdd:COG1120 148 IARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRlaRERGRTVVMVLHDLNlAARYADRLVLLKDGRIVAQGPPEEVLT 227
|
..
gi 338817954 617 KE 618
Cdd:COG1120 228 PE 229
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
391-614 |
1.96e-43 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 162.19 E-value: 1.96e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 391 LEFSDVHFSYpsrANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDI-------RNfnvr 463
Cdd:COG3842 6 LELENVSKRY---GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVtglppekRN---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 464 clreiIGVVSQEPVLFS-TTIAENIRYG---RGnVTMDEIEKAVKEANAydfIMKLPQkfdtlVGDRG-AQLSGGQKQRI 538
Cdd:COG3842 79 -----VGMVFQDYALFPhLTVAENVAFGlrmRG-VPKAEIRARVAELLE---LVGLEG-----LADRYpHQLSGGQQQRV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 539 AIARALVRNPKILLLDEATSALDTESEAEVQAALDK--AREGRTTIVIAHRLS---TIrnADVIAGFEDGVIVEQGSHSE 613
Cdd:COG3842 145 ALARALAPEPRVLLLDEPLSALDAKLREEMREELRRlqRELGITFIYVTHDQEealAL--ADRIAVMNDGRIEQVGTPEE 222
|
.
gi 338817954 614 L 614
Cdd:COG3842 223 I 223
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
392-603 |
2.18e-43 |
|
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: 155.10 E-value: 2.18e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 392 EFSDVHFSYPSRaniKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLREIIGV 471
Cdd:cd00267 1 EIENLSFRYGGR---TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 472 VSQepvlfsttiaenirygrgnvtmdeiekavkeanaydfimklpqkfdtlvgdrgaqLSGGQKQRIAIARALVRNPKIL 551
Cdd:cd00267 78 VPQ-------------------------------------------------------LSGGQRQRVALARALLLNPDLL 102
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 338817954 552 LLDEATSALDTESEAEVQAALDK-AREGRTTIVIAHRLSTIRNA-DVIAGFEDG 603
Cdd:cd00267 103 LLDEPTSGLDPASRERLLELLRElAEEGRTVIIVTHDPELAELAaDRVIVLKDG 156
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
391-620 |
3.39e-43 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 158.75 E-value: 3.39e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 391 LEFSDVHFSYPSrANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNF-NVRCLREII 469
Cdd:TIGR04520 1 IEVENVSFSYPE-SEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEeNLWEIRKKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 470 GVVSQEP--VLFSTTIAENIRYGRGN--VTMDEIEKAVKEA----NAYDFIMKLPQKfdtlvgdrgaqLSGGQKQRIAIA 541
Cdd:TIGR04520 80 GMVFQNPdnQFVGATVEDDVAFGLENlgVPREEMRKRVDEAlklvGMEDFRDREPHL-----------LSGGQKQRVAIA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 542 RALVRNPKILLLDEATSALDTESEAEVQAALDKAR--EGRTTIVIAHRLSTIRNADVIAGFEDGVIVEQG------SHSE 613
Cdd:TIGR04520 149 GVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNkeEGITVISITHDMEEAVLADRVIVMNKGKIVAEGtpreifSQVE 228
|
....*..
gi 338817954 614 LMKKEGI 620
Cdd:TIGR04520 229 LLKEIGL 235
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
391-616 |
3.71e-43 |
|
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: 157.66 E-value: 3.71e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 391 LEFSDVHFSYPSRA-NIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLREII 469
Cdd:COG1124 2 LEVRNLSVSYGQGGrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 470 GVVSQEPVL-----FS--TTIAENIR-YGRGNVtMDEIEKAVKEANaydfimkLPqkfDTLVGDRGAQLSGGQKQRIAIA 541
Cdd:COG1124 82 QMVFQDPYAslhprHTvdRILAEPLRiHGLPDR-EERIAELLEQVG-------LP---PSFLDRYPHQLSGGQRQRVAIA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 338817954 542 RALVRNPKILLLDEATSALDTESEAEVQAALD--KAREGRTTIVIAHRLSTI-RNADVIAGFEDGVIVEQGSHSELMK 616
Cdd:COG1124 151 RALILEPELLLLDEPTSALDVSVQAEILNLLKdlREERGLTYLFVSHDLAVVaHLCDRVAVMQNGRIVEELTVADLLA 228
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1040-1251 |
8.65e-43 |
|
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: 156.13 E-value: 8.65e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1040 YPTRAN-VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQWL---RAQLGIVSQE 1115
Cdd:cd03257 11 FPTGGGsVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRkirRKEIQMVFQD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1116 PI-----LFdcSIAENIAygdnsrvvphdEIVRAAKEANIHPFIETLPQKYNTRVGDKGT-------QLSGGQKQRIAIA 1183
Cdd:cd03257 91 PMsslnpRM--TIGEQIA-----------EPLRIHGKLSKKEARKEAVLLLLVGVGLPEEvlnryphELSGGQRQRVAIA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 338817954 1184 RALIRQPRVLLLDEATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHG 1251
Cdd:cd03257 158 RALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEelGLTLLFITHDLGVVAKiADRVAVMYAGKIVEEG 228
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
1031-1249 |
1.82e-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: 154.94 E-value: 1.82e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1031 VTFNEVVFNYPT-RANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEakklnVQWLRAQL 1109
Cdd:cd03293 1 LEVRNVSKTYGGgGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEP-----VTGPGPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1110 GIVSQEPILFD-CSIAENIAYGDNSRVVPHDEIVRAAKEAnihpfIEtlpqkyntRVGDKGT------QLSGGQKQRIAI 1182
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNVALGLELQGVPKAEARERAEEL-----LE--------LVGLSGFenayphQLSGGMRQRVAL 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 338817954 1183 ARALIRQPRVLLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLS-TIQNADLIVVIEN--GKVKE 1249
Cdd:cd03293 143 ARALAVDPDVLLLDEPFSALDALTREQLQEELLDiwRETGKTVLLVTHDIDeAVFLADRVVVLSArpGRIVA 214
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
1049-1200 |
2.29e-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: 152.03 E-value: 2.29e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1049 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQWLRAQLGIVSQEPILF-DCSIAENI 1127
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFpRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 338817954 1128 AYGdnsrvVPHDEIVRAAKEANIHPFIETLPQKY--NTRVGDKGTQLSGGQKQRIAIARALIRQPRVLLLDEATS 1200
Cdd:pfam00005 81 RLG-----LLLKGLSKREKDARAEEALEKLGLGDlaDRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1043-1258 |
5.81e-42 |
|
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: 154.58 E-value: 5.81e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1043 RANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQWLRAQLGIVSQEPIL---- 1118
Cdd:COG1124 15 GRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRVQMVFQDPYAslhp 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1119 ---FDCSIAE--NIAYGDNSRvvphDEIVRAAKEANIHP-FIETLPQkyntrvgdkgtQLSGGQKQRIAIARALIRQPRV 1192
Cdd:COG1124 95 rhtVDRILAEplRIHGLPDRE----ERIAELLEQVGLPPsFLDRYPH-----------QLSGGQRQRVAIARALILEPEL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 338817954 1193 LLLDEATSALDTesekVVQ-EALD-----KAREGRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHGTHQQLLA 1258
Cdd:COG1124 160 LLLDEPTSALDV----SVQaEILNllkdlREERGLTYLFVSHDLAVVAHlCDRVAVMQNGRIVEELTVADLLA 228
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1045-1259 |
1.20e-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: 153.23 E-value: 1.20e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1045 NVPVLQGLSLEVKKGQTLALVGSSGCGKSTV---VQLLERfydPMAGSVLLDGQE--AKKLNVQWLRAQLGIVSQEPILF 1119
Cdd:COG1126 13 DLEVLKGISLDVEKGEVVVIIGPSGSGKSTLlrcINLLEE---PDSGTITVDGEDltDSKKDINKLRRKVGMVFQQFNLF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1120 -DCSIAENIAYGdnSRVV---PHDEIVRAAKEAnihpfietLpqkynTRVG--DKG----TQLSGGQKQRIAIARALIRQ 1189
Cdd:COG1126 90 pHLTVLENVTLA--PIKVkkmSKAEAEERAMEL--------L-----ERVGlaDKAdaypAQLSGGQQQRVAIARALAME 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 338817954 1190 PRVLLLDEATSALDTEsekVVQEALD--K--AREGRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHGTHQQLLAQ 1259
Cdd:COG1126 155 PKVMLFDEPTSALDPE---LVGEVLDvmRdlAKEGMTMVVVTHEMGFAREvADRVVFMDGGRIVEEGPPEEFFEN 226
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
391-586 |
1.70e-41 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 153.32 E-value: 1.70e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 391 LEFSDVHFSYPSRAN-IKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRclreiI 469
Cdd:COG1116 8 LELRGVSKRFPTGGGgVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPD-----R 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 470 GVVSQEPVLFS-TTIAENIRYGrgnVTMDEIEKAVKEANAYDFImklpqkfdTLVGDRGA------QLSGGQKQRIAIAR 542
Cdd:COG1116 83 GVVFQEPALLPwLTVLDNVALG---LELRGVPKAERRERARELL--------ELVGLAGFedayphQLSGGMRQRVAIAR 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 338817954 543 ALVRNPKILLLDEATSALDTESEAEVQAALDK--AREGRTTIVIAH 586
Cdd:COG1116 152 ALANDPEVLLMDEPFGALDALTRERLQDELLRlwQETGKTVLFVTH 197
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
391-586 |
3.03e-41 |
|
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: 151.47 E-value: 3.03e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 391 LEFSDVHFSYPS-RANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRclreiI 469
Cdd:cd03293 1 LEVRNVSKTYGGgGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD-----R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 470 GVVSQEPVLFS-TTIAENIRYG---RGnVTMDEIEKAVKEANA----YDFIMKLPqkfdtlvgdrgAQLSGGQKQRIAIA 541
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNVALGlelQG-VPKAEARERAEELLElvglSGFENAYP-----------HQLSGGMRQRVALA 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 338817954 542 RALVRNPKILLLDEATSALDTESEAEVQAALDK--AREGRTTIVIAH 586
Cdd:cd03293 144 RALAVDPDVLLLDEPFSALDALTREQLQEELLDiwRETGKTVLLVTH 190
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1031-1249 |
4.59e-41 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 150.96 E-value: 4.59e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1031 VTFNEVVFNYPTRAN-VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQL---LERfydPMAGSVLLDGQEAKKLN----V 1102
Cdd:COG1136 5 LELRNLTKSYGTGEGeVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNIlggLDR---PTSGEVLIDGQDISSLSerelA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1103 QWLRAQLGIVSQEPILFDC-SIAENIA----YGDNSRVVPHDEIVRAAKEANIHPFIETLPqkyntrvgdkgTQLSGGQK 1177
Cdd:COG1136 82 RLRRRHIGFVFQFFNLLPElTALENVAlpllLAGVSRKERRERARELLERVGLGDRLDHRP-----------SQLSGGQQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 338817954 1178 QRIAIARALIRQPRVLLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLSTIQNADLIVVIENGKVKE 1249
Cdd:COG1136 151 QRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRElnRELGTTIVMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
391-616 |
5.07e-41 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 151.12 E-value: 5.07e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 391 LEFSDVHFSYPSRaniKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLREI-- 468
Cdd:cd03261 1 IELRGLTKSFGGR---TVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLrr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 469 -IGVVSQEPVLF-STTIAENIRYG---RGNVTMDEIEKAVKeanaydfiMKLpqkfdTLVGDRG------AQLSGGQKQR 537
Cdd:cd03261 78 rMGMLFQSGALFdSLTVFENVAFPlreHTRLSEEEIREIVL--------EKL-----EAVGLRGaedlypAELSGGMKKR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 538 IAIARALVRNPKILLLDEATSALDTESEAEVQA-ALD-KAREGRTTIVIAHRLSTIRN-ADVIAGFEDGVIVEQGSHSEL 614
Cdd:cd03261 145 VALARALALDPELLLYDEPTAGLDPIASGVIDDlIRSlKKELGLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPEEL 224
|
..
gi 338817954 615 MK 616
Cdd:cd03261 225 RA 226
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1030-1252 |
9.82e-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: 154.10 E-value: 9.82e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1030 SVTFNEVVFNYptrANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQwlRAQL 1109
Cdd:COG3842 5 ALELENVSKRY---GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPE--KRNV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1110 GIVSQEPILF-DCSIAENIAYGDNSRVVPHDEIVRAAKEA----NIHPFIETLPqkyntrvgdkgTQLSGGQKQRIAIAR 1184
Cdd:COG3842 80 GMVFQDYALFpHLTVAENVAFGLRMRGVPKAEIRARVAELlelvGLEGLADRYP-----------HQLSGGQQQRVALAR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 338817954 1185 ALIRQPRVLLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLS---TIqnADLIVVIENGKVKEHGT 1252
Cdd:COG3842 149 ALAPEPRVLLLDEPLSALDAKLREEMREELRRlqRELGITFIYVTHDQEealAL--ADRIAVMNDGRIEQVGT 219
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1031-1259 |
1.07e-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: 158.53 E-value: 1.07e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1031 VTFNEVVFNYPTRAnVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDP---MAGSVLLDGQEAKKLNVQWLRA 1107
Cdd:COG1123 5 LEVRDLSVRYPGGD-VPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHggrISGEVLLDGRDLLELSEALRGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1108 QLGIVSQEPI--LFDCSIAENIAYGDNSRVVPHDEIVRAAKEANIHPFIETLPQKYNTrvgdkgtQLSGGQKQRIAIARA 1185
Cdd:COG1123 84 RIGMVFQDPMtqLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPH-------QLSGGQRQRVAIAMA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 338817954 1186 LIRQPRVLLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLSTI-QNADLIVVIENGKVKEHGTHQQLLAQ 1259
Cdd:COG1123 157 LALDPDLLIADEPTTALDVTTQAEILDLLRElqRERGTTVLLITHDLGVVaEIADRVVVMDDGRIVEDGPPEEILAA 233
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
391-605 |
1.07e-40 |
|
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: 149.60 E-value: 1.07e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 391 LEFSDVHFSYpsrANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRN--FNVRCLREI 468
Cdd:cd03262 1 IEIKNLHKSF---GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDdkKNINELRQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 469 IGVVSQEPVLFS-TTIAENIRYGRgnVTMDEIEKAVKEANAYDFIMK--LPQKFDtlvgDRGAQLSGGQKQRIAIARALV 545
Cdd:cd03262 78 VGMVFQQFNLFPhLTVLENITLAP--IKVKGMSKAEAEERALELLEKvgLADKAD----AYPAQLSGGQQQRVAIARALA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 338817954 546 RNPKILLLDEATSALDTESEAEVQAAL-DKAREGRTTIVIAHRLSTIRN-ADVIAGFEDGVI 605
Cdd:cd03262 152 MNPKVMLFDEPTSALDPELVGEVLDVMkDLAEEGMTMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1031-1259 |
3.08e-40 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 148.88 E-value: 3.08e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1031 VTFNEVVFNYPTRAN-VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQ---LLERfydPMAGSVLLDGQEAKKLN---VQ 1103
Cdd:cd03258 2 IELKNVSKVFGDTGGkVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRcinGLER---PTSGSVLVDGTDLTLLSgkeLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1104 WLRAQLGIVSQEPILFDC-SIAENIAYGDNSRVVPHDEIVRAAKEanihpfieTLPQkyntrVG--DKG----TQLSGGQ 1176
Cdd:cd03258 79 KARRRIGMIFQHFNLLSSrTVFENVALPLEIAGVPKAEIEERVLE--------LLEL-----VGleDKAdaypAQLSGGQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1177 KQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHGTH 1253
Cdd:cd03258 146 KQRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDinRELGLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTV 225
|
....*.
gi 338817954 1254 QQLLAQ 1259
Cdd:cd03258 226 EEVFAN 231
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
1031-1260 |
4.42e-40 |
|
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: 149.50 E-value: 4.42e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1031 VTFNEVVFNYPtRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAK-KLNVQWLRAQL 1109
Cdd:TIGR04520 1 IEVENVSFSYP-ESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLdEENLWEIRKKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1110 GIVSQEPilfD----CSIAEN-IAYGDNSRVVPHDEIVR----AAKEANIHPFIETLPQKyntrvgdkgtqLSGGQKQRI 1180
Cdd:TIGR04520 80 GMVFQNP---DnqfvGATVEDdVAFGLENLGVPREEMRKrvdeALKLVGMEDFRDREPHL-----------LSGGQKQRV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1181 AIARALIRQPRVLLLDEATSALDTESEKVVQEALDKAR--EGRTCIVIAHRLSTIQNADLIVVIENGKVKEHGTHQQLLA 1258
Cdd:TIGR04520 146 AIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNkeEGITVISITHDMEEAVLADRVIVMNKGKIVAEGTPREIFS 225
|
..
gi 338817954 1259 QK 1260
Cdd:TIGR04520 226 QV 227
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
1045-1259 |
5.28e-40 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 148.29 E-value: 5.28e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1045 NVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQWlRAQLGIVSQEPILF-DCSI 1123
Cdd:COG1131 12 DKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEV-RRRIGYVPQEPALYpDLTV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1124 AENIAYGDNSRVVPHDEIVRAAKEAnihpfIET--LPQKYNTRVGdkgtQLSGGQKQRIAIARALIRQPRVLLLDEATSA 1201
Cdd:COG1131 91 RENLRFFARLYGLPRKEARERIDEL-----LELfgLTDAADRKVG----TLSGGMKQRLGLALALLHDPELLILDEPTSG 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1202 LDTESEKVVQEALDK-AREGRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHGTHQQLLAQ 1259
Cdd:COG1131 162 LDPEARRELWELLRElAAEGKTVLLSTHYLEEAERlCDRVAIIDKGRIVADGTPDELKAR 221
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
391-631 |
6.12e-40 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 151.76 E-value: 6.12e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 391 LEFSDVHFSYpsrANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDI-------RNfnvr 463
Cdd:COG3839 4 LELENVSKSY---GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVtdlppkdRN---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 464 clreiIGVVSQEPVLF-STTIAENIRYG---RGnVTMDEIEKAVKEANAydfIMKLpqkfDTLVGDRGAQLSGGQKQRIA 539
Cdd:COG3839 77 -----IAMVFQSYALYpHMTVYENIAFPlklRK-VPKAEIDRRVREAAE---LLGL----EDLLDRKPKQLSGGQRQRVA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 540 IARALVRNPKILLLDEATSALD------TESE-AEVQAALdkareGRTTIVIAHRLS---TIrnADVIAGFEDGVIVEQG 609
Cdd:COG3839 144 LGRALVREPKVFLLDEPLSNLDaklrveMRAEiKRLHRRL-----GTTTIYVTHDQVeamTL--ADRIAVMNDGRIQQVG 216
|
250 260
....*....|....*....|..
gi 338817954 610 SHSELmkkegiYFRLVNMQTAG 631
Cdd:COG3839 217 TPEEL------YDRPANLFVAG 232
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
111-364 |
1.25e-39 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This group includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins.
Pssm-ID: 350001 [Multi-domain] Cd Length: 289 Bit Score: 149.25 E-value: 1.25e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 111 TRYAYYYSGLGGGVLVAAYIQVSFWTLAAGRQIKKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDDVSKISEGIGDKVG 190
Cdd:cd18557 36 NELALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFSSLLRQEIAFFDKHKTGELTSRLSSDTSVLQSAVTDNLS 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 191 MFFQAIATFFAGFIVGFIRGWKLTLVIMAISPILGLSTAVWAKILSTFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQN 270
Cdd:cd18557 116 QLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASKIYGRYIRKLSKEVQDALAKAGQVAEESLSNIRTVRSFSAEE 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 271 KELERYQKHLENAKKIGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTIGNAMT-VFFSILIgAFSVGQAAP 349
Cdd:cd18557 196 KEIRRYSEALDRSYRLARKKALANALFQGITSLLIYLSLLLVLWYGGYLVLSGQLTVGELTSfILYTIMV-ASSVGGLSS 274
|
250
....*....|....*
gi 338817954 350 CIDAFANARGAAYVI 364
Cdd:cd18557 275 LLADIMKALGASERV 289
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
391-609 |
1.37e-39 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 147.88 E-value: 1.37e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 391 LEFSDVHFSYpsrANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYD--P---TEGKISIDGQDI--RNFNVR 463
Cdd:COG1117 12 IEVRNLNVYY---GDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDliPgarVEGEILLDGEDIydPDVDVV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 464 CLREIIGVVSQEPVLFSTTIAENIRYG------RGNVTMDEI-EKAVKEANAYDfimklpqkfdtLVGDR----GAQLSG 532
Cdd:COG1117 89 ELRRRVGMVFQKPNPFPKSIYDNVAYGlrlhgiKSKSELDEIvEESLRKAALWD-----------EVKDRlkksALGLSG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 533 GQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKAREgRTTIVI-------AHRLStirnaDVIAGFEDGVI 605
Cdd:COG1117 158 GQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKK-DYTIVIvthnmqqAARVS-----DYTAFFYLGEL 231
|
....
gi 338817954 606 VEQG 609
Cdd:COG1117 232 VEFG 235
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1036-1257 |
1.81e-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: 147.50 E-value: 1.81e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1036 VVFNYPTRanvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQWLRAQLGIVSQE 1115
Cdd:COG1120 7 LSVGYGGR---PVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYVPQE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1116 PIL-FDCSIAENIAYG------DNSRVVPHD-EIVRAA-KEANIHPFIEtlpQKYntrvgdkgTQLSGGQKQRIAIARAL 1186
Cdd:COG1120 84 PPApFGLTVRELVALGryphlgLFGRPSAEDrEAVEEAlERTGLEHLAD---RPV--------DELSGGERQRVLIARAL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 338817954 1187 IRQPRVLLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLS-TIQNADLIVVIENGKVKEHGTHQQLL 1257
Cdd:COG1120 153 AQEPPLLLLDEPTSHLDLAHQLEVLELLRRlaRERGRTVVMVLHDLNlAARYADRLVLLKDGRIVAQGPPEEVL 226
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1031-1249 |
3.01e-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: 147.16 E-value: 3.01e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1031 VTFNEVVFNYPTRAN-VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEakklnVQWLRAQL 1109
Cdd:COG1116 8 LELRGVSKRFPTGGGgVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKP-----VTGPGPDR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1110 GIVSQEPILFD-CSIAENIAYGDNSRVVPHDEIVRAAKEAnihpfIEtlpqkyntRVGDKG------TQLSGGQKQRIAI 1182
Cdd:COG1116 83 GVVFQEPALLPwLTVLDNVALGLELRGVPKAERRERAREL-----LE--------LVGLAGfedaypHQLSGGMRQRVAI 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 338817954 1183 ARALIRQPRVLLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAH------RLstiqnADLIVVIEN--GKVKE 1249
Cdd:COG1116 150 ARALANDPEVLLMDEPFGALDALTRERLQDELLRlwQETGKTVLFVTHdvdeavFL-----ADRVVVLSArpGRIVE 221
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
398-1263 |
3.32e-39 |
|
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: 159.69 E-value: 3.32e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 398 FSYPSRANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQdirnfnvrclreiIGVVSQEPV 477
Cdd:TIGR01271 431 FSNFSLYVTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR-------------ISFSPQTSW 497
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 478 LFSTTIAENIRYGrgnVTMDEIE--KAVKEANAYDFIMKLPQKFDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDE 555
Cdd:TIGR01271 498 IMPGTIKDNIIFG---LSYDEYRytSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDS 574
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 556 ATSALDTESEAEV-QAALDKAREGRTTIVIAHRLSTIRNADVIAGFEDGVIVEQGSHSELMKKEGIY------------- 621
Cdd:TIGR01271 575 PFTHLDVVTEKEIfESCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAKRPDFsslllgleafdnf 654
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 622 ------------------------------------------------------------FRLVNMQTAGSQILSEEFEV 641
Cdd:TIGR01271 655 saerrnsiltetlrrvsidgdstvfsgpetikqsfkqpppefaekrkqsiilnpiasarkFSFVQMGPQKAQATTIEDAV 734
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 642 -ELSDEKAA--------------GDVAPNGW----------------------KARIFRNSTKKSLKSPHQNRL------ 678
Cdd:TIGR01271 735 rEPSERKFSlvpedeqgeeslprGNQYHHGLqhqaqrrqsvlqlmthsnrgenRREQLQTSFRKKSSITQQNELaseldi 814
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 679 -------------DEETNELD---------ANVPPVS----FLKVLKLNKTEWPYFVVGTVCAIANGALQPAFSIILSEM 732
Cdd:TIGR01271 815 ysrrlskdsvyeiSEEINEEDlkecfaderENVFETTtwntYLRYITTNRNLVFVLIFCLVIFLAEVAASLLGLWLITDN 894
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 733 IAIFG--PGDDAVKQQKCNMFSL------------VFLGLGVLSFFTFFLQGFTFGKAGEILTTRLRSMAFKAMLRQDMS 798
Cdd:TIGR01271 895 PSAPNyvDQQHANASSPDVQKPViitptsayyifyIYVGTADSVLALGFFRGLPLVHTLLTVSKRLHEQMLHSVLQAPMA 974
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 799 WFDDHKnsTGALSTRLATDAAQVQGATG-TRLALIAQNTANLGTGIIISFIYGWqltlLLLSVVPFIAVAGIVEMKMLAG 877
Cdd:TIGR01271 975 VLNTMK--AGRILNRFTKDMAIIDDMLPlTLFDFIQLTLIVLGAIFVVSVLQPY----IFIAAIPVAVIFIMLRAYFLRT 1048
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 878 NAKRDKKEMEAAGKIATEAIENIR---TVVSLTQERKFESMYVEKLHGPYRN-SVRKAHIYGITFSISQAFMYFSYAGCF 953
Cdd:TIGR01271 1049 SQQLKQLESEARSPIFSHLITSLKglwTIRAFGRQSYFETLFHKALNLHTANwFLYLSTLRWFQMRIDIIFVFFFIAVTF 1128
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 954 -RFGSYLIVNGHMrfkDVILVFSAIVLGAVALGHASSFAPDYAKAKLSAAYLF-SLFERQP---------------LIDS 1016
Cdd:TIGR01271 1129 iAIGTNQDGEGEV---GIILTLAMNILSTLQWAVNSSIDVDGLMRSVSRVFKFiDLPQEEPrpsggggkyqlstvlVIEN 1205
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1017 YSGEGLWPDkfEGSVTFNEVVFNYpTRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDpMAGSVLLDGQE 1096
Cdd:TIGR01271 1206 PHAQKCWPS--GGQMDVQGLTAKY-TEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVS 1281
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1097 AKKLNVQWLRAQLGIVSQEPILFDCSIAENIaygDNSRVVPHDEIVRAAKEANIHPFIETLPQKYNTRVGDKGTQLSGGQ 1176
Cdd:TIGR01271 1282 WNSVTLQTWRKAFGVIPQKVFIFSGTFRKNL---DPYEQWSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGH 1358
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1177 KQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIENGKVKEHGTHQQL 1256
Cdd:TIGR01271 1359 KQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKL 1438
|
....*..
gi 338817954 1257 LAQKGIY 1263
Cdd:TIGR01271 1439 LNETSLF 1445
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
391-616 |
3.44e-39 |
|
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: 148.66 E-value: 3.44e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 391 LEFSDVHFSYPSRAN-IKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDP---TEGKISIDGQDIRNFNVRCLR 466
Cdd:COG0444 2 LEVRNLKVYFPTRRGvVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 467 EI----IGVVSQEPvlFS---------TTIAENIRYGRGnVTMDEIEKAVKEA-------NAYDFIMKLPQkfdtlvgdr 526
Cdd:COG0444 82 KIrgreIQMIFQDP--MTslnpvmtvgDQIAEPLRIHGG-LSKAEARERAIELlervglpDPERRLDRYPH--------- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 527 gaQLSGGQKQRIAIARALVRNPKILLLDEATSALDteseAEVQAA-LD-----KAREGRTTIVIAHRLSTIRN-ADVIA- 598
Cdd:COG0444 150 --ELSGGMRQRVMIARALALEPKLLIADEPTTALD----VTIQAQiLNllkdlQRELGLAILFITHDLGVVAEiADRVAv 223
|
250 260
....*....|....*....|
gi 338817954 599 --GfedGVIVEQGSHSELMK 616
Cdd:COG0444 224 myA---GRIVEEGPVEELFE 240
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
391-619 |
3.57e-39 |
|
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: 146.16 E-value: 3.57e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 391 LEFSDVHFSYPSRaniKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLREIiG 470
Cdd:COG4555 2 IEVENLSKKYGKV---PALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQI-G 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 471 VVSQEPVLFST-TIAENIRY-GRGNvtmdEIEKAVKEANAYDFI--MKLPQKFDTLVGDrgaqLSGGQKQRIAIARALVR 546
Cdd:COG4555 78 VLPDERGLYDRlTVRENIRYfAELY----GLFDEELKKRIEELIelLGLEEFLDRRVGE----LSTGMKKKVALARALVH 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 338817954 547 NPKILLLDEATSALDTESEAEVQAALDKAR-EGRTTIVIAHRLSTIRN-ADVIAGFEDGVIVEQGSHSELMKKEG 619
Cdd:COG4555 150 DPKVLLLDEPTNGLDVMARRLLREILRALKkEGKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEIG 224
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1040-1252 |
5.68e-39 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 148.69 E-value: 5.68e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1040 YPTRAN-VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQ---LLERfydPMAGSVLLDGQEAKKLNVQWLRA---QLGIV 1112
Cdd:COG1135 11 FPTKGGpVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRcinLLER---PTSGSVLVDGVDLTALSERELRAarrKIGMI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1113 SQEPILFD-CSIAENIAY-----GdnsrvVPHDEIvraakEANIHPFIEtlpqkyntRVG--DKG----TQLSGGQKQRI 1180
Cdd:COG1135 88 FQHFNLLSsRTVAENVALpleiaG-----VPKAEI-----RKRVAELLE--------LVGlsDKAdaypSQLSGGQKQRV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 338817954 1181 AIARALIRQPRVLLLDEATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHGT 1252
Cdd:COG1135 150 GIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRelGLTIVLITHEMDVVRRiCDRVAVLENGRIVEQGP 224
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
1031-1246 |
5.73e-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: 144.15 E-value: 5.73e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1031 VTFNEVVFNYPTRANV--PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLL--ErfYDPMAGSVLLDGQEAkklnvqwlr 1106
Cdd:cd03250 1 ISVEDASFTWDSGEQEtsFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALlgE--LEKLSGSVSVPGSIA--------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1107 aqlgIVSQEPILFDCSIAENIAYG---DNSRVvphDEIVRAAKeanIHPFIETLPQKYNTRVGDKGTQLSGGQKQRIAIA 1183
Cdd:cd03250 70 ----YVSQEPWIQNGTIRENILFGkpfDEERY---EKVIKACA---LEPDLEILPDGDLTEIGEKGINLSGGQKQRISLA 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 338817954 1184 RALIRQPRVLLLDEATSALDTES-----EKVVQEALdkaREGRTCIVIAHRLSTIQNADLIVVIENGK 1246
Cdd:cd03250 140 RAVYSDADIYLLDDPLSAVDAHVgrhifENCILGLL---LNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
391-605 |
9.81e-39 |
|
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: 142.54 E-value: 9.81e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 391 LEFSDVHFSYPSRaniKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNfNVRCLREIIG 470
Cdd:cd03230 1 IEVRNLSKRYGKK---TALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 471 VVSQEPVLFST-TIAENIRYgrgnvtmdeiekavkeanaydfimklpqkfdtlvgdrgaqlSGGQKQRIAIARALVRNPK 549
Cdd:cd03230 77 YLPEEPSLYENlTVRENLKL-----------------------------------------SGGMKQRLALAQALLHDPE 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 338817954 550 ILLLDEATSALDTESEAEVQAALDK-AREGRTTIVIAHRLSTIRN-ADVIAGFEDGVI 605
Cdd:cd03230 116 LLILDEPTSGLDPESRREFWELLRElKKEGKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1034-1259 |
1.20e-38 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 145.93 E-value: 1.20e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1034 NEVVFNYPtRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQWLRAQLGIVS 1113
Cdd:PRK13635 9 EHISFRYP-DAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGMVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1114 QEPilfD-----CSIAENIAYGDNSRVVPHDEIVR----AAKEANIHPFIETLPQKyntrvgdkgtqLSGGQKQRIAIAR 1184
Cdd:PRK13635 88 QNP---DnqfvgATVQDDVAFGLENIGVPREEMVErvdqALRQVGMEDFLNREPHR-----------LSGGQKQRVAIAG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1185 ALIRQPRVLLLDEATSALDTESEkvvQEALD-----KAREGRTCIVIAHRLSTIQNADLIVVIENGKVKEHGTHQQLLAQ 1259
Cdd:PRK13635 154 VLALQPDIIILDEATSMLDPRGR---REVLEtvrqlKEQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFKS 230
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
391-614 |
1.99e-38 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 144.04 E-value: 1.99e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 391 LEFSDVHFSYPSRAniKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLREI-- 468
Cdd:COG3638 3 LELRNLSKRYPGGT--PALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRLrr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 469 -IGVVSQEPVLFS-TTIAENI-----------RYGRGNVTMDEIEKAvkeanaydfimklpqkFDTL--VG------DRG 527
Cdd:COG3638 81 rIGMIFQQFNLVPrLSVLTNVlagrlgrtstwRSLLGLFPPEDRERA----------------LEALerVGladkayQRA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 528 AQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAAL-DKARE-GRTTIVIAHRLSTIRN-ADVIAGFEDGV 604
Cdd:COG3638 145 DQLSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLrRIAREdGITVVVNLHQVDLARRyADRIIGLRDGR 224
|
250
....*....|
gi 338817954 605 IVEQGSHSEL 614
Cdd:COG3638 225 VVFDGPPAEL 234
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
392-620 |
3.35e-38 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 144.36 E-value: 3.35e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 392 EFSDVHFSYPSRANIkILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLREIIGV 471
Cdd:PRK13632 9 KVENVSFSYPNSENN-ALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 472 VSQEP---VLFSTT---IA---ENIRYGRgNVTMDEIEKAVKEANAYDFIMKLPQKfdtlvgdrgaqLSGGQKQRIAIAR 542
Cdd:PRK13632 88 IFQNPdnqFIGATVeddIAfglENKKVPP-KKMKDIIDDLAKKVGMEDYLDKEPQN-----------LSGGQKQRVAIAS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 543 ALVRNPKILLLDEATSALDTESEAEVQAALDKAREGR--TTIVIAHRLSTIRNADVIAGFEDGVIVEQGSHSELMKKEGI 620
Cdd:PRK13632 156 VLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRkkTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEILNNKEI 235
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
392-613 |
4.43e-38 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 146.10 E-value: 4.43e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 392 EFSDVHFSYPSRAN-IKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLREI-- 468
Cdd:PRK11153 3 ELKNISKVFPQGGRtIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKArr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 469 -IGVVSQE-PVLFSTTIAENIRYGR--GNVTMDEIEKAVKE----------ANAYdfimklPqkfdtlvgdrgAQLSGGQ 534
Cdd:PRK11153 83 qIGMIFQHfNLLSSRTVFDNVALPLelAGTPKAEIKARVTEllelvglsdkADRY------P-----------AQLSGGQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 535 KQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKA-REGRTTIV-IAHRLSTIRN-ADVIAGFEDGVIVEQGSH 611
Cdd:PRK11153 146 KQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDInRELGLTIVlITHEMDVVKRiCDRVAVIDAGRLVEQGTV 225
|
..
gi 338817954 612 SE 613
Cdd:PRK11153 226 SE 227
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
391-607 |
7.05e-38 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 141.73 E-value: 7.05e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 391 LEFSDVHFSYPsrANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQD---IRNFNVRCLRE 467
Cdd:COG2884 2 IRFENVSKRYP--GGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDlsrLKRREIPYLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 468 IIGVVSQE-PVLFSTTIAENIRY-----GRgnvTMDEIEKAVKEAnaydfIMK--LPQKFDTLVgdrgAQLSGGQKQRIA 539
Cdd:COG2884 80 RIGVVFQDfRLLPDRTVYENVALplrvtGK---SRKEIRRRVREV-----LDLvgLSDKAKALP----HELSGGEQQRVA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 338817954 540 IARALVRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIA-HRLSTIRNAD--VIAgFEDGVIVE 607
Cdd:COG2884 148 IARALVNRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIAtHDLELVDRMPkrVLE-LEDGRLVR 217
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1048-1256 |
1.17e-37 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 142.48 E-value: 1.17e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1048 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYD--P---MAGSVLLDGQE--AKKLNVQWLRAQLGIVSQEPILFD 1120
Cdd:COG1117 26 ALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDliPgarVEGEILLDGEDiyDPDVDVVELRRRVGMVFQKPNPFP 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1121 CSIAENIAYG-----DNSRVVpHDEIVRAA-KEANihpfietLPQKYNTRVGDKGTQLSGGQKQRIAIARALIRQPRVLL 1194
Cdd:COG1117 106 KSIYDNVAYGlrlhgIKSKSE-LDEIVEESlRKAA-------LWDEVKDRLKKSALGLSGGQQQRLCIARALAVEPEVLL 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 338817954 1195 LDEATSALDTESEKVVQEALDKAREgRTCIVI-------AHRLStiqnaDLIVVIENGKVKEHGTHQQL 1256
Cdd:COG1117 178 MDEPTSALDPISTAKIEELILELKK-DYTIVIvthnmqqAARVS-----DYTAFFYLGELVEFGPTEQI 240
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1032-1261 |
1.43e-37 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 141.53 E-value: 1.43e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1032 TFNEVVFNYPtraNVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNvQWLRAQLGI 1111
Cdd:COG4555 3 EVENLSKKYG---KVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEP-REARRQIGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1112 VSQEPILFD-CSIAENIAYGDNSRVVPHDEIVRAAKEanihpFIE--TLPQKYNTRVGDkgtqLSGGQKQRIAIARALIR 1188
Cdd:COG4555 79 LPDERGLYDrLTVRENIRYFAELYGLFDEELKKRIEE-----LIEllGLEEFLDRRVGE----LSTGMKKKVALARALVH 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 338817954 1189 QPRVLLLDEATSALDTESEKVVQEALDKAREGRTCIVIA-HRLSTIQN-ADLIVVIENGKVKEHGTHQQLLAQKG 1261
Cdd:COG4555 150 DPKVLLLDEPTNGLDVMARRLLREILRALKKEGKTVLFSsHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEIG 224
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
413-615 |
1.58e-37 |
|
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: 142.40 E-value: 1.58e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 413 NLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLREI----IGVVSQEPVLF-STTIAENI 487
Cdd:cd03294 44 SLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELrrkkISMVFQSFALLpHRTVLENV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 488 RYG---RGNVTMDEIEKAVKEANAY---DFIMKLPQkfdtlvgdrgaQLSGGQKQRIAIARALVRNPKILLLDEATSALD 561
Cdd:cd03294 124 AFGlevQGVPRAEREERAAEALELVgleGWEHKYPD-----------ELSGGMQQRVGLARALAVDPDILLMDEAFSALD 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 338817954 562 TESEAEVQAALDK--AREGRTTIVIAHRLS-TIRNADVIAGFEDGVIVEQGSHSELM 615
Cdd:cd03294 193 PLIRREMQDELLRlqAELQKTIVFITHDLDeALRLGDRIAIMKDGRLVQVGTPEEIL 249
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
1031-1247 |
1.88e-37 |
|
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: 140.32 E-value: 1.88e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1031 VTFNEVVFNYPTRAN-VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQWL---- 1105
Cdd:cd03255 1 IELKNLSKTYGGGGEkVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1106 RAQLGIVSQE----PILfdcSIAENIAYGDNSRVVPHDEIVRAAKEAnihpfIET--LPQKYNTRVGdkgtQLSGGQKQR 1179
Cdd:cd03255 81 RRHIGFVFQSfnllPDL---TALENVELPLLLAGVPKKERRERAEEL-----LERvgLGDRLNHYPS----ELSGGQQQR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1180 IAIARALIRQPRVLLLDEATSALDTESEKVVQEAL-DKAREGRTCIVIA-HRLSTIQNADLIVVIENGKV 1247
Cdd:cd03255 149 VAIARALANDPKIILADEPTGNLDSETGKEVMELLrELNKEAGTTIVVVtHDPELAEYADRIIELRDGKI 218
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1032-1246 |
1.96e-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: 138.15 E-value: 1.96e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1032 TFNEVVFNYPTRanvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQWLRAQLGI 1111
Cdd:cd00267 1 EIENLSFRYGGR---TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1112 VSQepilfdcsiaeniaygdnsrvvphdeivraakeanihpfietlpqkyntrvgdkgtqLSGGQKQRIAIARALIRQPR 1191
Cdd:cd00267 78 VPQ---------------------------------------------------------LSGGQRQRVALARALLLNPD 100
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 338817954 1192 VLLLDEATSALDTESEKVVQEALDK-AREGRTCIVIAHRLSTIQNA-DLIVVIENGK 1246
Cdd:cd00267 101 LLLLDEPTSGLDPASRERLLELLRElAEEGRTVIIVTHDPELAELAaDRVIVLKDGK 157
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
1042-1246 |
2.23e-37 |
|
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: 138.86 E-value: 2.23e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1042 TRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLN--VQWLRAQLGIVSQEPILF 1119
Cdd:cd03229 9 RYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEdeLPPLRRRIGMVFQDFALF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1120 -DCSIAENIAYGdnsrvvphdeivraakeanihpfietlpqkyntrvgdkgtqLSGGQKQRIAIARALIRQPRVLLLDEA 1198
Cdd:cd03229 89 pHLTVLENIALG-----------------------------------------LSGGQQQRVALARALAMDPDVLLLDEP 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 338817954 1199 TSALDTESEKVVQEALD--KAREGRTCIVIAHRLSTIQN-ADLIVVIENGK 1246
Cdd:cd03229 128 TSALDPITRREVRALLKslQAQLGITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
388-624 |
2.61e-37 |
|
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: 153.56 E-value: 2.61e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 388 KGNLEFSDVHFSYPSRANIkILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLRE 467
Cdd:TIGR00957 1282 RGRVEFRNYCLRYREDLDL-VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRF 1360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 468 IIGVVSQEPVLFSTTIAENIRyGRGNVTMDEIEKAVKEANAYDFIMKLPQKFDTLVGDRGAQLSGGQKQRIAIARALVRN 547
Cdd:TIGR00957 1361 KITIIPQDPVLFSGSLRMNLD-PFSQYSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRK 1439
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 338817954 548 PKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTIRNADVIAGFEDGVIVEQGSHSELMKKEGIYFRL 624
Cdd:TIGR00957 1440 TKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRGIFYSM 1516
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
391-614 |
2.95e-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: 140.78 E-value: 2.95e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 391 LEFSDVHFSYPSraNIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLREI-- 468
Cdd:cd03256 1 IEVENLSKTYPN--GKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLrr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 469 -IGVVSQEPVLFS-TTIAENIRYGR-----------GNVTMDEIEKAVKEANAYDFIMKLPQkfdtlvgdRGAQLSGGQK 535
Cdd:cd03256 79 qIGMIFQQFNLIErLSVLENVLSGRlgrrstwrslfGLFPKEEKQRALAALERVGLLDKAYQ--------RADQLSGGQQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 536 QRIAIARALVRNPKILLLDEATSALDTESEAEVQAAL-DKARE-GRTTIVIAHRLSTIR-NADVIAGFEDGVIVEQGSHS 612
Cdd:cd03256 151 QRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLkRINREeGITVIVSLHQVDLAReYADRIVGLKDGRIVFDGPPA 230
|
..
gi 338817954 613 EL 614
Cdd:cd03256 231 EL 232
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
105-361 |
1.05e-36 |
|
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: 140.76 E-value: 1.05e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 105 ILEEEMTRYAYYYSGLGGGVLVAA---YIQVSFWTLAAGRQIKKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDDVSKI 181
Cdd:cd07346 30 IPAGDLSLLLWIALLLLLLALLRAllsYLRRYLAARLGQRVVFDLRRDLFRHLQRLSLSFFDRNRTGDLMSRLTSDVDAV 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 182 SEGIGDKVGMFFQAIATFFAGFIVGFIRGWKLTLVIMAISPILGLSTAVWAKILSTFSDKELAAYAKAGAVAEEALGAIR 261
Cdd:cd07346 110 QNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILRYFRRRIRKASREVRESLAELSAFLQESLSGIR 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 262 TVIAFGGQNKELERYQKHLENAKKIGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTIGnAMTVFFSILIGA 341
Cdd:cd07346 190 VVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTALGTALVLLYGGYLVLQGSLTIG-ELVAFLAYLGML 268
|
250 260
....*....|....*....|.
gi 338817954 342 FS-VGQAAPCIDAFANARGAA 361
Cdd:cd07346 269 FGpIQRLANLYNQLQQALASL 289
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
113-622 |
1.06e-36 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 151.81 E-value: 1.06e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 113 YAYYYSGLG-GGVLVAayIQVSFW----TLAAGrqiKKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDDVSKISEGIGD 187
Cdd:PLN03130 955 YNLIYALLSfGQVLVT--LLNSYWlimsSLYAA---KRLHDAMLGSILRAPMSFFHTNPLGRIINRFAKDLGDIDRNVAV 1029
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 188 KVGMF----FQAIATFFagfIVGFIRgwklTLVIMAISPILGLSTAVWAKILSTFSD-KELAAYAKAGAVAE--EALGAI 260
Cdd:PLN03130 1030 FVNMFlgqiFQLLSTFV---LIGIVS----TISLWAIMPLLVLFYGAYLYYQSTAREvKRLDSITRSPVYAQfgEALNGL 1102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 261 RTVIAFGGQNKELERYQKHLENAKKIGIKKaISANISMGIAF-----LLIY--ASYAL----------AFWYGSTLVISK 323
Cdd:PLN03130 1103 STIRAYKAYDRMAEINGRSMDNNIRFTLVN-MSSNRWLAIRLetlggLMIWltASFAVmqngraenqaAFASTMGLLLSY 1181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 324 EYTIGNAMTvffsiligafSVGQAAPCIDAFANA--RGAAYVifDIIDNNPKIdsfsERGHKPDN---IKGNLEFSDVHF 398
Cdd:PLN03130 1182 ALNITSLLT----------AVLRLASLAENSLNAveRVGTYI--DLPSEAPLV----IENNRPPPgwpSSGSIKFEDVVL 1245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 399 SYpsRANIK-ILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLREIIGVVSQEPV 477
Cdd:PLN03130 1246 RY--RPELPpVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPV 1323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 478 LFSTTIAENIR-YGRGNVTmdEIEKAVKEANAYDFIMKLPQKFDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEA 556
Cdd:PLN03130 1324 LFSGTVRFNLDpFNEHNDA--DLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEA 1401
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 338817954 557 TSALDTESEAEVQAALDKAREGRTTIVIAHRLSTIRNADVIAGFEDGVIVEQGSHSELMKKEGIYF 622
Cdd:PLN03130 1402 TAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEGSAF 1467
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
711-1003 |
1.66e-36 |
|
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: 140.00 E-value: 1.66e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 711 GTVCAIANGALQPAFSIILSEMIAIFGPGDDavkQQKCNMFSLVFLGLGVLSFFTFFLQGFTFGKAGEILTTRLRSMAFK 790
Cdd:cd18557 1 GLLFLLISSAAQLLLPYLIGRLIDTIIKGGD---LDVLNELALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 791 AMLRQDMSWFDDHKnsTGALSTRLATDAAQVQGATGTRLALIAQNTANLGTGIIISFIYGWQLTLLLLSVVPFIAVAGIV 870
Cdd:cd18557 78 SLLRQEIAFFDKHK--TGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASKI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 871 EMKMLAGNAKRDKKEMEAAGKIATEAIENIRTVVSLTQERKFESMYVEKLHGPYRNSVRKAHIYGITFSISQAFMYFSYA 950
Cdd:cd18557 156 YGRYIRKLSKEVQDALAKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQGITSLLIYLSLL 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 338817954 951 GCFRFGSYLIVNGHMRFKDVI--LVFSAIVlgAVALGHASSFAPDYAKAkLSAAY 1003
Cdd:cd18557 236 LVLWYGGYLVLSGQLTVGELTsfILYTIMV--ASSVGGLSSLLADIMKA-LGASE 287
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
708-1001 |
1.95e-36 |
|
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: 139.99 E-value: 1.95e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 708 FVVGTVCAIANGALQPAFSIILSEMIAIFGPGDDavkQQKCNMFSLVFLGLGVLSFFTFFLQGFTFGKAGEILTTRLRSM 787
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLLIDDVIPAGD---LSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 788 AFKAMLRQDMSWFDdhKNSTGALSTRLATDAAQVQGATGTRLALIAQNTANLGTGIIISFIYGWQLTLLLLSVVPFIAVA 867
Cdd:cd07346 78 LFRHLQRLSLSFFD--RNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 868 GIVEMKMLAGNAKRDKKEMEAAGKIATEAIENIRTVVSLTQERKFESMYVEKLHGPYRNSVRKAHIYGITFSISQAFMYF 947
Cdd:cd07346 156 LRYFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTAL 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 338817954 948 SYAGCFRFGSYLIVNGHMRFKDVILVFSAIVLGAVALGHASSFAPDYAKAKLSA 1001
Cdd:cd07346 236 GTALVLLYGGYLVLQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASL 289
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1047-1258 |
2.57e-36 |
|
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: 137.80 E-value: 2.57e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1047 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNV---QWLRAQLGIVSQEPILFDC-S 1122
Cdd:COG1127 19 VVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEkelYELRRRIGMLFQGGALFDSlT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1123 IAENIAYG-DNSRVVPHDEIVRAAKEAnihpfIEtlpqkyntRVGDKGT------QLSGGQKQRIAIARALIRQPRVLLL 1195
Cdd:COG1127 99 VFENVAFPlREHTDLSEAEIRELVLEK-----LE--------LVGLPGAadkmpsELSGGMRKRVALARALALDPEILLY 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 338817954 1196 DEATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHGTHQQLLA 1258
Cdd:COG1127 166 DEPTAGLDPITSAVIDELIRELRDelGLTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPEELLA 231
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
391-603 |
2.63e-36 |
|
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: 136.45 E-value: 2.63e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 391 LEFSDVHFSYPSRANI--KILKGLNLKVKSGQTVALVGNSGCGKSTtvqLLQRL---YDPTEGKISIDGQdirnfnvrcl 465
Cdd:cd03250 1 ISVEDASFTWDSGEQEtsFTLKDINLEVPKGELVAIVGPVGSGKSS---LLSALlgeLEKLSGSVSVPGS---------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 466 reiIGVVSQEPVLFSTTIAENIRYGRgnvTMDEIE-KAVKEANA--YDFIMkLPQKFDTLVGDRGAQLSGGQKQRIAIAR 542
Cdd:cd03250 68 ---IAYVSQEPWIQNGTIRENILFGK---PFDEERyEKVIKACAlePDLEI-LPDGDLTEIGEKGINLSGGQKQRISLAR 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 338817954 543 ALVRNPKILLLDEATSALDTESEAEV--QAALDKAREGRTTIVIAHRLSTIRNADVIAGFEDG 603
Cdd:cd03250 141 AVYSDADIYLLDDPLSAVDAHVGRHIfeNCILGLLLNNKTRILVTHQLQLLPHADQIVVLDNG 203
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
389-625 |
3.99e-36 |
|
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: 138.12 E-value: 3.99e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 389 GNLEFSDVHFSYPSraNIK-ILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLRE 467
Cdd:cd03288 18 GEIKIHDLCVRYEN--NLKpVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 468 IIGVVSQEPVLFSTTIAENIRYGRgNVTMDEIEKAVKEANAYDFIMKLPQKFDTLVGDRGAQLSGGQKQRIAIARALVRN 547
Cdd:cd03288 96 RLSIILQDPILFSGSIRFNLDPEC-KCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRK 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 338817954 548 PKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTIRNADVIAGFEDGVIVEQGSHSELM-KKEGIYFRLV 625
Cdd:cd03288 175 SSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLaQEDGVFASLV 253
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1033-1262 |
4.95e-36 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 138.20 E-value: 4.95e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1033 FNEVVFNYPTRANvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQWLRAQLGIV 1112
Cdd:PRK13632 10 VENVSFSYPNSEN-NALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGII 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1113 SQEPilfD-----CSIAENIAYGDNSRVVPHDE----IVRAAKEANIHPFIETLPQKyntrvgdkgtqLSGGQKQRIAIA 1183
Cdd:PRK13632 89 FQNP---DnqfigATVEDDIAFGLENKKVPPKKmkdiIDDLAKKVGMEDYLDKEPQN-----------LSGGQKQRVAIA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1184 RALIRQPRVLLLDEATSALDTESEKVVQEALDKAREGR--TCIVIAHRLSTIQNADLIVVIENGKVKEHGTHQQLLAQKG 1261
Cdd:PRK13632 155 SVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRkkTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEILNNKE 234
|
.
gi 338817954 1262 I 1262
Cdd:PRK13632 235 I 235
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
395-586 |
5.71e-36 |
|
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: 135.46 E-value: 5.71e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 395 DVHFSYpsRANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGqdiRNFNVRCLREIIGVVSQ 474
Cdd:cd03226 4 NISFSY--KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNG---KPIKAKERRKSIGYVMQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 475 EP--VLFSTTIAENIRYGRGNVTMD--EIEKAVKEANAYDFIMKLPQkfdtlvgdrgaQLSGGQKQRIAIARALVRNPKI 550
Cdd:cd03226 79 DVdyQLFTDSVREELLLGLKELDAGneQAETVLKDLDLYALKERHPL-----------SLSGGQKQRLAIAAALLSGKDL 147
|
170 180 190
....*....|....*....|....*....|....*..
gi 338817954 551 LLLDEATSALDTESEAEVQAALDK-AREGRTTIVIAH 586
Cdd:cd03226 148 LIFDEPTSGLDYKNMERVGELIRElAAQGKAVIVITH 184
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
1047-1267 |
6.57e-36 |
|
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: 137.35 E-value: 6.57e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1047 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQWLRAQLGIVSQEPILFDCSIAEN 1126
Cdd:cd03288 35 PVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFN 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1127 IaygDNSRVVPHDEIVRAAKEANIHPFIETLPQKYNTRVGDKGTQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTES 1206
Cdd:cd03288 115 L---DPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMAT 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 338817954 1207 EKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIENGKVKEHGTHQQLLAQK-GIYFSMV 1267
Cdd:cd03288 192 ENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEdGVFASLV 253
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
391-618 |
7.88e-36 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 136.76 E-value: 7.88e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 391 LEFSDVHFSYPSRaniKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNfnvrcLREIIG 470
Cdd:COG1121 7 IELENLTVSYGGR---PVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRR-----ARRRIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 471 VVSQEPVL---FSTTIAENI---RYGRGNVTM-------DEIEKAVKEANAYDFImklpqkfDTLVGdrgaQLSGGQKQR 537
Cdd:COG1121 79 YVPQRAEVdwdFPITVRDVVlmgRYGRRGLFRrpsradrEAVDEALERVGLEDLA-------DRPIG----ELSGGQQQR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 538 IAIARALVRNPKILLLDEATSALDTESEAEVQAALDK-AREGRTTIVIAHRLSTIR-NADVIAGFEDGVIVEqGSHSELM 615
Cdd:COG1121 148 VLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRElRREGKTILVVTHDLGAVReYFDRVLLLNRGLVAH-GPPEEVL 226
|
...
gi 338817954 616 KKE 618
Cdd:COG1121 227 TPE 229
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1030-1259 |
1.46e-35 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 139.13 E-value: 1.46e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1030 SVTFNEVVFNYPTRanvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQL---LERfydPMAGSVLLDGQEAK-KLNVQwl 1105
Cdd:COG1118 2 SIEVRNISKRFGSF---TLLDDVSLEIASGELVALLGPSGSGKTTLLRIiagLET---PDSGRIVLNGRDLFtNLPPR-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1106 RAQLGIVSQEPILF-DCSIAENIAYGDNSRVVPHDEIVRAAKE----ANIHPFIETLPqkyntrvgdkgTQLSGGQKQRI 1180
Cdd:COG1118 74 ERRVGFVFQHYALFpHMTVAENIAFGLRVRPPSKAEIRARVEEllelVQLEGLADRYP-----------SQLSGGQRQRV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1181 AIARALIRQPRVLLLDEATSALDT----ESEKVVQEALDkaREGRTCIVIAH------RLstiqnADLIVVIENGKVKEH 1250
Cdd:COG1118 143 ALARALAVEPEVLLLDEPFGALDAkvrkELRRWLRRLHD--ELGGTTVFVTHdqeealEL-----ADRVVVMNQGRIEQV 215
|
....*....
gi 338817954 1251 GTHQQLLAQ 1259
Cdd:COG1118 216 GTPDEVYDR 224
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
108-329 |
2.18e-35 |
|
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: 136.90 E-value: 2.18e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 108 EEMTRYAYYYSGLGGGVLVAAYIQVSFWTLAAGRQIKKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDDVSKISEGIGD 187
Cdd:cd18572 33 EAFYRAVLLLLLLSVLSGLFSGLRGGCFSYAGTRLVRRLRRDLFRSLLRQDIAFFDATKTGELTSRLTSDCQKVSDPLST 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 188 KVGMFFQAIATFFAGFIVGFIRGWKLTLVIMAISPILGLSTAVWAKILSTFSDKELAAYAKAGAVAEEALGAIRTVIAFG 267
Cdd:cd18572 113 NLNVFLRNLVQLVGGLAFMFSLSWRLTLLAFITVPVIALITKVYGRYYRKLSKEIQDALAEANQVAEEALSNIRTVRSFA 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 338817954 268 GQNKELERYQKHLENAKKIGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTIGN 329
Cdd:cd18572 193 TEEREARRYERALDKALKLSVRQALAYAGYVAVNTLLQNGTQVLVLFYGGHLVLSGRMSAGQ 254
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
1031-1258 |
2.29e-35 |
|
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: 134.94 E-value: 2.29e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1031 VTFNEVVFNYPTRanvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNV---QWLRA 1107
Cdd:cd03261 1 IELRGLTKSFGGR---TVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEaelYRLRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1108 QLGIVSQEPILFDC-SIAENIAYG--DNSRVVPH--DEIVRAAKEA-NIHPFIETLPqkyntrvgdkgTQLSGGQKQRIA 1181
Cdd:cd03261 78 RMGMLFQSGALFDSlTVFENVAFPlrEHTRLSEEeiREIVLEKLEAvGLRGAEDLYP-----------AELSGGMKKRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1182 IARALIRQPRVLLLDEATSALD-TESEKVVQEALD-KAREGRTCIVIAHRLSTI-QNADLIVVIENGKVKEHGTHQQLLA 1258
Cdd:cd03261 147 LARALALDPELLLYDEPTAGLDpIASGVIDDLIRSlKKELGLTSIMVTHDLDTAfAIADRIAVLYDGKIVAEGTPEELRA 226
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
107-347 |
3.29e-35 |
|
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 and similar proteins; This group includes Arabidopsis ABC transporter B family member 27 (also known as AtABCB27, aluminum tolerance-related ATP-binding cassette transporter, transporter associated with antigen processing-like protein 2, AtTAP2, and ALS1) which may play a role in aluminum resistance. The ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family.
Pssm-ID: 350053 [Multi-domain] Cd Length: 295 Bit Score: 136.61 E-value: 3.29e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 107 EEEMTRYAYYYSGLGGGVLVAAYIQVSFWTLAAGRQIKKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDDVSKISEGIG 186
Cdd:cd18780 38 LRALNQAVLILLGVVLIGSIATFLRSWLFTLAGERVVARLRKRLFSAIIAQEIAFFDVTRTGELLNRLSSDTQVLQNAVT 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 187 DKVGMFFQAIATFFAGFIVGFIRGWKLTLVIMAISPILGLSTAVWAKILSTFSDKELAAYAKAGAVAEEALGAIRTVIAF 266
Cdd:cd18780 118 VNLSMLLRYLVQIIGGLVFMFTTSWKLTLVMLSVVPPLSIGAVIYGKYVRKLSKKFQDALAAASTVAEESISNIRTVRSF 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 267 GGQNKELERYQKHLENAKKIGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTIGnAMTVFfsiLIGAFSVGQ 346
Cdd:cd18780 198 AKETKEVSRYSEKINESYLLGKKLARASGGFNGFMGAAAQLAIVLVLWYGGRLVIDGELTTG-LLTSF---LLYTLTVAM 273
|
.
gi 338817954 347 A 347
Cdd:cd18780 274 S 274
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
1048-1247 |
4.71e-35 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 133.42 E-value: 4.71e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1048 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQE--AKKLNVQWLRAQLGIVSQEPILF-DCSIA 1124
Cdd:cd03262 15 VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKltDDKKNINELRQKVGMVFQQFNLFpHLTVL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1125 ENIAYGdnSRVVPHdeivRAAKEAnihpfiETLPQKYNTRVG--DKGT----QLSGGQKQRIAIARALIRQPRVLLLDEA 1198
Cdd:cd03262 95 ENITLA--PIKVKG----MSKAEA------EERALELLEKVGlaDKADaypaQLSGGQQQRVAIARALAMNPKVMLFDEP 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 338817954 1199 TSALDTEsekVVQEALDK----AREGRTCIVIAHRLSTIQN-ADLIVVIENGKV 1247
Cdd:cd03262 163 TSALDPE---LVGEVLDVmkdlAEEGMTMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
403-615 |
4.92e-35 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 136.79 E-value: 4.92e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 403 RANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLREI---IGVVSQEPvlF 479
Cdd:COG4608 28 VGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELRPLrrrMQMVFQDP--Y 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 480 S---------TTIAENIRYgRGNVTMDEIEKAVKEanaydfIMklpqkfdTLVG------DRGA-QLSGGQKQRIAIARA 543
Cdd:COG4608 106 AslnprmtvgDIIAEPLRI-HGLASKAERRERVAE------LL-------ELVGlrpehaDRYPhEFSGGQRQRIGIARA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 544 LVRNPKILLLDEATSALDTESEAEV-------QAALdkareGRTTIVIAHRLSTIRN-ADVIAGFEDGVIVEQGSHSELM 615
Cdd:COG4608 172 LALNPKLIVCDEPVSALDVSIQAQVlnlledlQDEL-----GLTYLFISHDLSVVRHiSDRVAVMYLGKIVEIAPRDELY 246
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
1031-1258 |
5.96e-35 |
|
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: 133.97 E-value: 5.96e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1031 VTFNEVVFNYPTRAnvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQWLRAQLG 1110
Cdd:cd03295 1 IEFENVTKRYGGGK--KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1111 IVSQEPILF-DCSIAENIAygdnsrVVPHDEIV-RAAKEANIHPFIETL---PQKYNTRVGDkgtQLSGGQKQRIAIARA 1185
Cdd:cd03295 79 YVIQQIGLFpHMTVEENIA------LVPKLLKWpKEKIRERADELLALVgldPAEFADRYPH---ELSGGQQQRVGVARA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 338817954 1186 LIRQPRVLLLDEATSALDTESEKVVQEALDKARE--GRTCIVIAHRL-STIQNADLIVVIENGKVKEHGTHQQLLA 1258
Cdd:cd03295 150 LAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQelGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEILR 225
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
392-594 |
6.04e-35 |
|
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: 133.04 E-value: 6.04e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 392 EFSDVHFSYPSRaniKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRclreiIGV 471
Cdd:cd03235 1 EVEDLTVSYGGH---PVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKR-----IGY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 472 VSQEPVL---FSTTIAENIRYGR----------GNVTMDEIEKAVKEANAYDFImklpqkfdtlvgDRG-AQLSGGQKQR 537
Cdd:cd03235 73 VPQRRSIdrdFPISVRDVVLMGLyghkglfrrlSKADKAKVDEALERVGLSELA------------DRQiGELSGGQQQR 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 338817954 538 IAIARALVRNPKILLLDEATSALDTESEAEVQAALDK-AREGRTTIVIAHRLSTIRNA 594
Cdd:cd03235 141 VLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRElRREGMTILVVTHDLGLVLEY 198
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
392-609 |
7.16e-35 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 131.40 E-value: 7.16e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 392 EFSDVHFSYPSRaniKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLREIIGV 471
Cdd:cd03214 1 EVENLSVGYGGR---TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 472 VSQepvlfsttiaenirygrgnvtmdeiekAVKEANAYDFIMKLpqkFDTlvgdrgaqLSGGQKQRIAIARALVRNPKIL 551
Cdd:cd03214 78 VPQ---------------------------ALELLGLAHLADRP---FNE--------LSGGERQRVLLARALAQEPPIL 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 338817954 552 LLDEATSALDTESEAEVQAALDK--AREGRTTIVIAHRLS-TIRNADVIAGFEDGVIVEQG 609
Cdd:cd03214 120 LLDEPTSHLDIAHQIELLELLRRlaRERGKTVVMVLHDLNlAARYADRVILLKDGRIVAQG 180
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
391-596 |
8.48e-35 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 132.53 E-value: 8.48e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 391 LEFSDVHFSYPsrANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRC---LRE 467
Cdd:cd03292 1 IEFINVTKTYP--NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAipyLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 468 IIGVVSQEPVLFST-TIAENIRYGR--GNVTMDEIEKAVKEANAydfIMKLPQKFDTLvgdrGAQLSGGQKQRIAIARAL 544
Cdd:cd03292 79 KIGVVFQDFRLLPDrNVYENVAFALevTGVPPREIRKRVPAALE---LVGLSHKHRAL----PAELSGGEQQRVAIARAI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 338817954 545 VRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIA-----------HRLSTIRNADV 596
Cdd:cd03292 152 VNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVAthakelvdttrHRVIALERGKL 214
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1029-1256 |
1.16e-34 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 136.36 E-value: 1.16e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1029 GSVTFNEVVFNYptrANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQeakklNVQWLRAQ 1108
Cdd:COG3839 2 ASLELENVSKSY---GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGR-----DVTDLPPK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1109 ---LGIVSQEPILFD-CSIAENIAYGDNSRVVPHDEIVRAAKEA----NIHPFIETLPqkyntrvgdkgTQLSGGQKQRI 1180
Cdd:COG3839 74 drnIAMVFQSYALYPhMTVYENIAFPLKLRKVPKAEIDRRVREAaellGLEDLLDRKP-----------KQLSGGQRQRV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1181 AIARALIRQPRVLLLDEATSALD------TESE-KVVQEALdkareGRTCIVIAHRLS---TIqnADLIVVIENGKVKEH 1250
Cdd:COG3839 143 ALGRALVREPKVFLLDEPLSNLDaklrveMRAEiKRLHRRL-----GTTTIYVTHDQVeamTL--ADRIAVMNDGRIQQV 215
|
....*.
gi 338817954 1251 GTHQQL 1256
Cdd:COG3839 216 GTPEEL 221
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
391-614 |
1.43e-34 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 136.04 E-value: 1.43e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 391 LEFSDVHFSYPSRaniKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIrNFNVRCLREIIG 470
Cdd:COG1118 3 IEVRNISKRFGSF---TLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDL-FTNLPPRERRVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 471 VVSQEPVLF-STTIAENIRYG--RGNVTMDEIEKAVKE----------ANAYdfimklPqkfdtlvgdrgAQLSGGQKQR 537
Cdd:COG1118 79 FVFQHYALFpHMTVAENIAFGlrVRPPSKAEIRARVEEllelvqleglADRY------P-----------SQLSGGQRQR 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 538 IAIARALVRNPKILLLDEATSALDTESEAEVQAALDK--AREGRTTIVIAH-RLSTIRNADVIAGFEDGVIVEQGSHSEL 614
Cdd:COG1118 142 VALARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRlhDELGGTTVFVTHdQEEALELADRVVVMNQGRIEQVGTPDEV 221
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
1031-1247 |
1.58e-34 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 132.87 E-value: 1.58e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1031 VTFNEVVFNYPtrANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLN---VQWLRA 1107
Cdd:COG3638 3 LELRNLSKRYP--GGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRgraLRRLRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1108 QLGIVSQEPILFD-CSIAENI---AYGDNS------RVVPHDEIVRAAkEAnihpfIET--LPQKYNTRVGdkgtQLSGG 1175
Cdd:COG3638 81 RIGMIFQQFNLVPrLSVLTNVlagRLGRTStwrsllGLFPPEDRERAL-EA-----LERvgLADKAYQRAD----QLSGG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 338817954 1176 QKQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEAL-DKARE-GRTCIVIAHRLSTIQN-ADLIVVIENGKV 1247
Cdd:COG3638 151 QQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLrRIAREdGITVVVNLHQVDLARRyADRIIGLRDGRV 225
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1031-1251 |
1.95e-34 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 131.71 E-value: 1.95e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1031 VTFNEVVFNYPTraNVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLN---VQWLRA 1107
Cdd:COG2884 2 IRFENVSKRYPG--GREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKrreIPYLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1108 QLGIVSQE-PILFDCSIAENIAY-----GdnsrvVPHDEIVRAAKEAnihpfIET--LPQKYNTRVGdkgtQLSGGQKQR 1179
Cdd:COG2884 80 RIGVVFQDfRLLPDRTVYENVALplrvtG-----KSRKEIRRRVREV-----LDLvgLSDKAKALPH----ELSGGEQQR 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 338817954 1180 IAIARALIRQPRVLLLDEATSALDTE-SEKVVqEALDKAREGRTCIVIA-HRLSTIQNADL-IVVIENGKVKEHG 1251
Cdd:COG2884 146 VAIARALVNRPELLLADEPTGNLDPEtSWEIM-ELLEEINRRGTTVLIAtHDLELVDRMPKrVLELEDGRLVRDE 219
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
391-609 |
4.72e-34 |
|
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: 130.45 E-value: 4.72e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 391 LEFSDVHFSYPSRaniKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDI-------RNfnvr 463
Cdd:cd03301 1 VELENVTKRFGNV---TALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVtdlppkdRD---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 464 clreiIGVVSQEPVLF-STTIAENIRYG--RGNVTMDEIEKAVKEANAydfIMKLpqkfDTLVGDRGAQLSGGQKQRIAI 540
Cdd:cd03301 74 -----IAMVFQNYALYpHMTVYDNIAFGlkLRKVPKDEIDERVREVAE---LLQI----EHLLDRKPKQLSGGQRQRVAL 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 338817954 541 ARALVRNPKILLLDEATSALDTESEAEVQAALDK--AREGRTTIVIAH-RLSTIRNADVIAGFEDGVIVEQG 609
Cdd:cd03301 142 GRAIVREPKVFLMDEPLSNLDAKLRVQMRAELKRlqQRLGTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
409-617 |
5.74e-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: 130.92 E-value: 5.74e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 409 LKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRclREIIGVVSQEPVLF-STTIAENI 487
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE--KRDISYVPQNYALFpHMTVYKNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 488 RYGRGNVTMD--EIEKAVKEanaydfIMKLpQKFDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESE 565
Cdd:cd03299 93 AYGLKKRKVDkkEIERKVLE------IAEM-LGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTK 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 338817954 566 AEVQAALDKARE--GRTTIVIAHRLSTIRN-ADVIAGFEDGVIVEQGSHSELMKK 617
Cdd:cd03299 166 EKLREELKKIRKefGVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEVFKK 220
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1047-1252 |
1.70e-33 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 133.92 E-value: 1.70e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1047 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQwlRAQLGIVSQEPILF-DCSIAE 1125
Cdd:PRK09452 28 EVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE--NRHVNTVFQSYALFpHMTVFE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1126 NIAYGDNSRVVPHDEIVRAAKEANIHPFIETLPQKyntrvgdKGTQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTE 1205
Cdd:PRK09452 106 NVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQR-------KPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYK 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 338817954 1206 SEKVVQEALdKA--RE-GRTCIVIAH-RLSTIQNADLIVVIENGKVKEHGT 1252
Cdd:PRK09452 179 LRKQMQNEL-KAlqRKlGITFVFVTHdQEEALTMSDRIVVMRDGRIEQDGT 228
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
1045-1256 |
1.73e-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: 129.28 E-value: 1.73e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1045 NVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAkkLNVQWLRAQLGIVSQEPILF-DCSI 1123
Cdd:cd03300 12 GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI--TNLPPHKRPVNTVFQNYALFpHLTV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1124 AENIAYGDNSRVVPHDEIVRAAKEANIHPFIETLPQKYNTrvgdkgtQLSGGQKQRIAIARALIRQPRVLLLDEATSALD 1203
Cdd:cd03300 90 FENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPS-------QLSGGQQQRVAIARALVNEPKVLLLDEPLGALD 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 338817954 1204 TESEKVVQEALDK--AREGRTCIVIAHRLS-TIQNADLIVVIENGKVKEHGTHQQL 1256
Cdd:cd03300 163 LKLRKDMQLELKRlqKELGITFVFVTHDQEeALTMSDRIAVMNKGKIQQIGTPEEI 218
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
1046-1259 |
2.41e-33 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 130.07 E-value: 2.41e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1046 VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQWLRA----QLGIVSQEPILF-D 1120
Cdd:cd03294 37 TVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRElrrkKISMVFQSFALLpH 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1121 CSIAENIAYGDNSRVVPHDEIVRAAKEA----NIHPFIETLPQkyntrvgdkgtQLSGGQKQRIAIARALIRQPRVLLLD 1196
Cdd:cd03294 117 RTVLENVAFGLEVQGVPRAEREERAAEAlelvGLEGWEHKYPD-----------ELSGGMQQRVGLARALAVDPDILLMD 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 338817954 1197 EATSALDTESEKVVQEALDK--AREGRTCIVIAHRLS-TIQNADLIVVIENGKVKEHGTHQQLLAQ 1259
Cdd:cd03294 186 EAFSALDPLIRREMQDELLRlqAELQKTIVFITHDLDeALRLGDRIAIMKDGRLVQVGTPEEILTN 251
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1031-1259 |
2.46e-33 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 129.44 E-value: 2.46e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1031 VTFNEVVFNYPTRanvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLnvqwlRAQLG 1110
Cdd:COG1121 7 IELENLTVSYGGR---PVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA-----RRRIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1111 IVSQE-------PIlfdcSIAENIAYGDNSRVVP-------HDEIVRAA-KEANIHPFIetlpqkyNTRVGdkgtQLSGG 1175
Cdd:COG1121 79 YVPQRaevdwdfPI----TVRDVVLMGRYGRRGLfrrpsraDREAVDEAlERVGLEDLA-------DRPIG----ELSGG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1176 QKQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEALDK-AREGRTCIVIAHRLSTI-QNADLIVVIeNGKVKEHGTH 1253
Cdd:COG1121 144 QQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRElRREGKTILVVTHDLGAVrEYFDRVLLL-NRGLVAHGPP 222
|
....*.
gi 338817954 1254 QQLLAQ 1259
Cdd:COG1121 223 EEVLTP 228
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
391-615 |
2.51e-33 |
|
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: 136.35 E-value: 2.51e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 391 LEFSDVHFSYPSRANI--------KILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLyDPTEGKISIDGQDIRNFN- 461
Cdd:COG4172 276 LEARDLKVWFPIKRGLfrrtvghvKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRL-IPSEGEIRFDGQDLDGLSr 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 462 --VRCLREIIGVVSQEPvlFST-----TIAENIRYG----RGNVTMDEIEKAVKEAnaydfimkLPQkfdtlVG-DRGA- 528
Cdd:COG4172 355 raLRPLRRRMQVVFQDP--FGSlsprmTVGQIIAEGlrvhGPGLSAAERRARVAEA--------LEE-----VGlDPAAr 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 529 -----QLSGGQKQRIAIARALVRNPKILLLDEATSALDteseAEVQAA-LD-----KAREGRTTIVIAHRLSTIRN-ADV 596
Cdd:COG4172 420 hryphEFSGGQRQRIAIARALILEPKLLVLDEPTSALD----VSVQAQiLDllrdlQREHGLAYLFISHDLAVVRAlAHR 495
|
250
....*....|....*....
gi 338817954 597 IAGFEDGVIVEQGSHSELM 615
Cdd:COG4172 496 VMVMKDGKVVEQGPTEQVF 514
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
391-615 |
2.82e-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: 128.32 E-value: 2.82e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 391 LEFSDVHFSYpsrANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNV-RCLREII 469
Cdd:cd03224 1 LEVENLNAGY---GKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPhERARAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 470 GVVSQEPVLFST-TIAENIRYGRGNVTMDEIEKAVKEAnaYDFIMKLPQKFDTLVGdrgaQLSGGQKQRIAIARALVRNP 548
Cdd:cd03224 78 GYVPEGRRIFPElTVEENLLLGAYARRRAKRKARLERV--YELFPRLKERRKQLAG----TLSGGEQQMLAIARALMSRP 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 338817954 549 KILLLDEATSALDTESEAEVQAALDKAREGRTTIVI----AHRLSTIrnADVIAGFEDGVIVEQGSHSELM 615
Cdd:cd03224 152 KLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLveqnARFALEI--ADRAYVLERGRVVLEGTAAELL 220
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
1045-1247 |
5.72e-33 |
|
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: 125.97 E-value: 5.72e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1045 NVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQwLRAQLGIVSQEPILF-DCSI 1123
Cdd:cd03230 12 KKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEE-VKRRIGYLPEEPSLYeNLTV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1124 AENIaygdnsrvvphdeivraakeanihpfietlpqkyntrvgdkgtQLSGGQKQRIAIARALIRQPRVLLLDEATSALD 1203
Cdd:cd03230 91 RENL-------------------------------------------KLSGGMKQRLALAQALLHDPELLILDEPTSGLD 127
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 338817954 1204 TESEKVVQEALDK-AREGRTCIVIAHRLSTIQN-ADLIVVIENGKV 1247
Cdd:cd03230 128 PESRREFWELLRElKKEGKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
408-614 |
1.23e-32 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 126.97 E-value: 1.23e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 408 ILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNfnVRCLREIIGVVSQEPVLFS-TTIAEN 486
Cdd:cd03300 15 ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITN--LPPHKRPVNTVFQNYALFPhLTVFEN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 487 IRYG--RGNVTMDEIEKAVKEAnaydfiMKLPQkFDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTES 564
Cdd:cd03300 93 IAFGlrLKKLPKAEIKERVAEA------LDLVQ-LEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 338817954 565 EAEVQAALDK--AREGRTTIVIAHRLS-TIRNADVIAGFEDGVIVEQGSHSEL 614
Cdd:cd03300 166 RKDMQLELKRlqKELGITFVFVTHDQEeALTMSDRIAVMNKGKIQQIGTPEEI 218
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1031-1259 |
1.40e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 128.31 E-value: 1.40e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1031 VTFNEVVFNYPTRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQWLRAQLG 1110
Cdd:PRK13650 5 IEVKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1111 IVSQEP--ILFDCSIAENIAYGDNSRVVPHDEIVRAAKEA----NIHPFIETLPQKyntrvgdkgtqLSGGQKQRIAIAR 1184
Cdd:PRK13650 85 MVFQNPdnQFVGATVEDDVAFGLENKGIPHEEMKERVNEAlelvGMQDFKEREPAR-----------LSGGQKQRVAIAG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 338817954 1185 ALIRQPRVLLLDEATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTIQNADLIVVIENGKVKEHGTHQQLLAQ 1259
Cdd:PRK13650 154 AVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDdyQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFSR 230
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1046-1247 |
1.73e-32 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 133.22 E-value: 1.73e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1046 VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQwlRAQ-LGI--VSQEPILF-DC 1121
Cdd:COG1129 17 VKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPR--DAQaAGIaiIHQELNLVpNL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1122 SIAENIAYGD---NSRVVPHDEIVRAAKEA------NIHPfietlpqkyNTRVGDkgtqLSGGQKQRIAIARALIRQPRV 1192
Cdd:COG1129 95 SVAENIFLGReprRGGLIDWRAMRRRARELlarlglDIDP---------DTPVGD----LSVAQQQLVEIARALSRDARV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1193 LLLDEATSAL-DTESE---KVVQEaLdkAREGRTCIVIAHRLSTIQN-ADLIVVIENGKV 1247
Cdd:COG1129 162 LILDEPTASLtEREVErlfRIIRR-L--KAQGVAIIYISHRLDEVFEiADRVTVLRDGRL 218
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
1048-1257 |
2.60e-32 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 126.30 E-value: 2.60e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1048 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQwlRAQLGIVSQEPILF-DCSIAEN 1126
Cdd:cd03299 14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE--KRDISYVPQNYALFpHMTVYKN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1127 IAYGDNSRVVPHDEIVRAAKEANIHPFIETLPQKYNTRvgdkgtqLSGGQKQRIAIARALIRQPRVLLLDEATSALDTES 1206
Cdd:cd03299 92 IAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPET-------LSGGEQQRVAIARALVVNPKILLLDEPFSALDVRT 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 338817954 1207 EKVVQEALDKARE--GRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHGTHQQLL 1257
Cdd:cd03299 165 KEKLREELKKIRKefGVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEVF 218
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
391-630 |
2.98e-32 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 130.07 E-value: 2.98e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 391 LEFSDVHFSYPSRaniKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNfnVRCLREIIG 470
Cdd:PRK09452 15 VELRGISKSFDGK---EVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITH--VPAENRHVN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 471 VVSQEPVLFS-TTIAENIRYG--RGNVTMDEIEKAVKEAnaydfiMKLPQkFDTLVGDRGAQLSGGQKQRIAIARALVRN 547
Cdd:PRK09452 90 TVFQSYALFPhMTVFENVAFGlrMQKTPAAEITPRVMEA------LRMVQ-LEEFAQRKPHQLSGGQQQRVAIARAVVNK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 548 PKILLLDEATSALDTESEAEVQAALdKA--RE-GRTTIVIAH-RLSTIRNADVIAGFEDGVIVEQGSHSElmkkegIYFR 623
Cdd:PRK09452 163 PKVLLLDESLSALDYKLRKQMQNEL-KAlqRKlGITFVFVTHdQEEALTMSDRIVVMRDGRIEQDGTPRE------IYEE 235
|
....*..
gi 338817954 624 LVNMQTA 630
Cdd:PRK09452 236 PKNLFVA 242
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1045-1256 |
3.00e-32 |
|
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: 126.30 E-value: 3.00e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1045 NVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQwlRAQLGIVSQEPILF-DCSI 1123
Cdd:cd03296 14 DFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQ--ERNVGFVFQHYALFrHMTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1124 AENIAYG----DNSRVVPHDEIVRAAKEANIHPFIETLPQKYNTrvgdkgtQLSGGQKQRIAIARALIRQPRVLLLDEAT 1199
Cdd:cd03296 92 FDNVAFGlrvkPRSERPPEAEIRAKVHELLKLVQLDWLADRYPA-------QLSGGQRQRVALARALAVEPKVLLLDEPF 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1200 SALDTESEKVVQEALDKARE--GRTCIVIAHRLS-TIQNADLIVVIENGKVKEHGTHQQL 1256
Cdd:cd03296 165 GALDAKVRKELRRWLRRLHDelHVTTVFVTHDQEeALEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1042-1256 |
3.06e-32 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 128.70 E-value: 3.06e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1042 TRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLN---VQWLRAQLGIVSQEPil 1118
Cdd:COG4608 27 TVGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSgreLRPLRRRMQMVFQDP-- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1119 FDC-----SIAENIAYG-DNSRVVPHDEIVRAAKEAnihpfIET--LPQKYNTRVGDkgtQLSGGQKQRIAIARALIRQP 1190
Cdd:COG4608 105 YASlnprmTVGDIIAEPlRIHGLASKAERRERVAEL-----LELvgLRPEHADRYPH---EFSGGQRQRIGIARALALNP 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 338817954 1191 RVLLLDEATSALDtesekV-VQ-------EALdKAREGRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHGTHQQL 1256
Cdd:COG4608 177 KLIVCDEPVSALD-----VsIQaqvlnllEDL-QDELGLTYLFISHDLSVVRHiSDRVAVMYLGKIVEIAPRDEL 245
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1040-1259 |
3.49e-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: 128.25 E-value: 3.49e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1040 YPTRAN-VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMA---GSVLLDGQEAKKLNVQWLRA----QLGI 1111
Cdd:COG0444 11 FPTRRGvVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPGitsGEILFDGEDLLKLSEKELRKirgrEIQM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1112 VSQEP---------ILFdcSIAENI-AYGDNSRVVPHDEIVRAAKEANIHPfietlPQKyntRVGDKGTQLSGGQKQRIA 1181
Cdd:COG0444 91 IFQDPmtslnpvmtVGD--QIAEPLrIHGGLSKAEARERAIELLERVGLPD-----PER---RLDRYPHELSGGMRQRVM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1182 IARALIRQPRVLLLDEATSALDTesekVVQ-EALD-----KAREGRTCIVIAHRLSTI-QNADLIVVIENGKVKEHGTHQ 1254
Cdd:COG0444 161 IARALALEPKLLIADEPTTALDV----TIQaQILNllkdlQRELGLAILFITHDLGVVaEIADRVAVMYAGRIVEEGPVE 236
|
....*
gi 338817954 1255 QLLAQ 1259
Cdd:COG0444 237 ELFEN 241
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
391-616 |
3.73e-32 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 127.05 E-value: 3.73e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 391 LEFSDVHFSYPSrANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLREIIG 470
Cdd:PRK13635 6 IRVEHISFRYPD-AATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 471 VVSQEP--VLFSTTIAENIRYGRGN--VTMDE----IEKAVKEANAYDFIMKLPqkfdtlvgdrgAQLSGGQKQRIAIAR 542
Cdd:PRK13635 85 MVFQNPdnQFVGATVQDDVAFGLENigVPREEmverVDQALRQVGMEDFLNREP-----------HRLSGGQKQRVAIAG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 338817954 543 ALVRNPKILLLDEATSALDTESEAEVQAALD--KAREGRTTIVIAHRLSTIRNADVIAGFEDGVIVEQGSHSELMK 616
Cdd:PRK13635 154 VLALQPDIIILDEATSMLDPRGRREVLETVRqlKEQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFK 229
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
1046-1258 |
6.69e-32 |
|
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: 124.47 E-value: 6.69e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1046 VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQwLRAQLGI--VSQEPILF-DCS 1122
Cdd:cd03224 13 SQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPH-ERARAGIgyVPEGRRIFpELT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1123 IAENIAYGDNSRVvphdeivRAAKEANIHPFIETLPQKYnTRVGDKGTQLSGGQKQRIAIARALIRQPRVLLLDEATSAL 1202
Cdd:cd03224 92 VEENLLLGAYARR-------RAKRKARLERVYELFPRLK-ERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 338817954 1203 dteSEKVVQE---ALDKAREGRTCIVIAHrlstiQNADLI-------VVIENGKVKEHGTHQQLLA 1258
Cdd:cd03224 164 ---APKIVEEifeAIRELRDEGVTILLVE-----QNARFAleiadraYVLERGRVVLEGTAAELLA 221
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
407-616 |
7.54e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 126.32 E-value: 7.54e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 407 KILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDI--RNFNVRCLREIIGVVSQEP--VLFSTT 482
Cdd:PRK13637 21 KALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdKKVKLSDIRKKVGLVFQYPeyQLFEET 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 483 IAENIRYGRGNVTM--DEIEKAVKEANAydfIMKLPqkFDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEATSAL 560
Cdd:PRK13637 101 IEKDIAFGPINLGLseEEIENRVKRAMN---IVGLD--YEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 338817954 561 DTESEAEVQAALDKARE--GRTTIVIAHRLSTI-RNADVIAGFEDGVIVEQGSHSELMK 616
Cdd:PRK13637 176 DPKGRDEILNKIKELHKeyNMTIILVSHSMEDVaKLADRIIVMNKGKCELQGTPREVFK 234
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
1032-1247 |
7.90e-32 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 124.99 E-value: 7.90e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1032 TFNEVVFNYPTraNVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQE---AKKLNVQWLRAQ 1108
Cdd:cd03256 2 EVENLSKTYPN--GKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDinkLKGKALRQLRRQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1109 LGIVSQEPILFD-CSIAENIAYGDNSRVVPHDEIVRAAKEANIHPFIETLPQ-----KYNTRVGdkgtQLSGGQKQRIAI 1182
Cdd:cd03256 80 IGMIFQQFNLIErLSVLENVLSGRLGRRSTWRSLFGLFPKEEKQRALAALERvglldKAYQRAD----QLSGGQQQRVAI 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 338817954 1183 ARALIRQPRVLLLDEATSALDTESEKVVQEAL-DKARE-GRTCIVIAHRLSTI-QNADLIVVIENGKV 1247
Cdd:cd03256 156 ARALMQQPKLILADEPVASLDPASSRQVMDLLkRINREeGITVIVSLHQVDLArEYADRIVGLKDGRI 223
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
391-615 |
1.02e-31 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 124.43 E-value: 1.02e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 391 LEFSDV--HFsypsrANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIR--NFNVRCLR 466
Cdd:PRK09493 2 IEFKNVskHF-----GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpKVDERLIR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 467 EIIGVVSQEPVLFSTTIA-ENIRYG----RGnvtmdeIEKAVKEANAYDFIMKlpqkfdtlVG--DRG----AQLSGGQK 535
Cdd:PRK09493 77 QEAGMVFQQFYLFPHLTAlENVMFGplrvRG------ASKEEAEKQARELLAK--------VGlaERAhhypSELSGGQQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 536 QRIAIARALVRNPKILLLDEATSALDTESEAEVQAAL-DKAREGRTTIVIAHRLSTIRN-ADVIAGFEDGVIVEQGSHSE 613
Cdd:PRK09493 143 QRVAIARALAVKPKLMLFDEPTSALDPELRHEVLKVMqDLAEEGMTMVIVTHEIGFAEKvASRLIFIDKGRIAEDGDPQV 222
|
..
gi 338817954 614 LM 615
Cdd:PRK09493 223 LI 224
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
391-614 |
1.15e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 125.58 E-value: 1.15e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 391 LEFSDVHFSYPSraNIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCL--REI 468
Cdd:PRK13639 2 LETRDLKYSYPD--GTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLevRKT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 469 IGVVSQEP--VLFSTTIAENIRYGRGNV--TMDEIEKAVKEA----NAYDFIMKLPQkfdtlvgdrgaQLSGGQKQRIAI 540
Cdd:PRK13639 80 VGIVFQNPddQLFAPTVEEDVAFGPLNLglSKEEVEKRVKEAlkavGMEGFENKPPH-----------HLSGGQKKRVAI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 338817954 541 ARALVRNPKILLLDEATSALDTESEAEVQAAL-DKAREGRTTIVIAHRLSTI-RNADVIAGFEDGVIVEQGSHSEL 614
Cdd:PRK13639 149 AGILAMKPEIIVLDEPTSGLDPMGASQIMKLLyDLNKEGITIIISTHDVDLVpVYADKVYVMSDGKIIKEGTPKEV 224
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1042-1259 |
1.28e-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: 131.35 E-value: 1.28e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1042 TRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFyDPMAGSVLLDGQEAKKLN---VQWLRAQLGIVSQEPil 1118
Cdd:COG4172 295 TVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRL-IPSEGEIRFDGQDLDGLSrraLRPLRRRMQVVFQDP-- 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1119 FDC-----SIAENIAYGdnsRVVPHDEIVRAAKEANIhpfIETLpqkynTRVG-DKGT------QLSGGQKQRIAIARAL 1186
Cdd:COG4172 372 FGSlsprmTVGQIIAEG---LRVHGPGLSAAERRARV---AEAL-----EEVGlDPAArhryphEFSGGQRQRIAIARAL 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1187 IRQPRVLLLDEATSALDteseKVVQ-EALD-----KAREGRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHGTHQQLLAQ 1259
Cdd:COG4172 441 ILEPKLLVLDEPTSALD----VSVQaQILDllrdlQREHGLAYLFISHDLAVVRAlAHRVMVMKDGKVVEQGPTEQVFDA 516
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
407-609 |
1.34e-31 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 123.56 E-value: 1.34e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 407 KILKGLNLKVK---SGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQ---DIR-NFNVRCLREIIGVVSQEPVLF 479
Cdd:cd03297 8 KRLPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlfDSRkKINLPPQQRKIGLVFQQYALF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 480 S-TTIAENIRYGRGNVTMDEIEKAVKEANAYdfiMKLpqkfDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEATS 558
Cdd:cd03297 88 PhLNVRENLAFGLKRKRNREDRISVDELLDL---LGL----DHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFS 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 338817954 559 ALDTESEAEVQAALDK--AREGRTTIVIAHRLSTI-RNADVIAGFEDGVIVEQG 609
Cdd:cd03297 161 ALDRALRLQLLPELKQikKNLNIPVIFVTHDLSEAeYLADRIVVMEDGRLQYIG 214
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
407-1268 |
1.55e-31 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 134.91 E-value: 1.55e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 407 KILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQdirnfnvrclreiIGVVSQEPVLFSTTIAEN 486
Cdd:PTZ00243 674 VLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAERS-------------IAYVPQQAWIMNATVRGN 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 487 IRYgrgnvtMDE-----IEKAVK----EANaydfIMKLPQKFDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEAT 557
Cdd:PTZ00243 741 ILF------FDEedaarLADAVRvsqlEAD----LAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPL 810
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 558 SALDTE-SEAEVQAALDKAREGRTTIVIAHRLSTIRNADVIAGFEDGVIVEQGSHSELMKKEgIYFRL-----VNMQTAG 631
Cdd:PTZ00243 811 SALDAHvGERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFMRTS-LYATLaaelkENKDSKE 889
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 632 SQILSEEFEVELSDEKAagdVAPNGwkarifrnstkkslKSPHQNRLDEETNELDANVPPVSFLKVLKLNKTEWPYFVVG 711
Cdd:PTZ00243 890 GDADAEVAEVDAAPGGA---VDHEP--------------PVAKQEGNAEGGDGAALDAAAGRLMTREEKASGSVPWSTYV 952
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 712 TVCAIANGALQPAFSII---LSEMIAI-------------FGPGDDAvkqqkcnmFSLVFLGLGVLSFFTFFLQGFTFGK 775
Cdd:PTZ00243 953 AYLRFCGGLHAAGFVLAtfaVTELVTVssgvwlsmwstrsFKLSAAT--------YLYVYLGIVLLGTFSVPLRFFLSYE 1024
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 776 AGEILTTRLRSMAFKAMLRQDMSWFDdhKNSTGALSTRLATDAAqvqgatgtrlalIAQNTANLGTGIIISFIYGWQLTL 855
Cdd:PTZ00243 1025 AMRRGSRNMHRDLLRSVSRGTMSFFD--TTPLGRILNRFSRDID------------ILDNTLPMSYLYLLQCLFSICSSI 1090
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 856 LLLSVV-PFIAVA----GIVEMK-MLAGNAkrdkkemeaagkiateAIENIRTVVSLTQERKFeSMYVEKLHGpyrnsvr 929
Cdd:PTZ00243 1091 LVTSASqPFVLVAlvpcGYLYYRlMQFYNS----------------ANREIRRIKSVAKSPVF-TLLEEALQG------- 1146
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 930 KAHI--YGITFSISQ-AFMYFSYAgcfrFGSYLIVNGHMRFKDVILVF-SAIVLGAVAL-------GHASSfaPDYAKAK 998
Cdd:PTZ00243 1147 SATItaYGKAHLVMQeALRRLDVV----YSCSYLENVANRWLGVRVEFlSNIVVTVIALigvigtmLRATS--QEIGLVS 1220
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 999 LSAAYLFSLFE------RQ------------------------------PLIDSYSGE-GLWPDKF-------------- 1027
Cdd:PTZ00243 1221 LSLTMAMQTTAtlnwlvRQvatveadmnsverllyytdevphedmpeldEEVDALERRtGMAADVTgtvviepasptsaa 1300
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1028 -----EGSVTFNEVVFNYptRANVP-VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLN 1101
Cdd:PTZ00243 1301 phpvqAGSLVFEGVQMRY--REGLPlVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYG 1378
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1102 VQWLRAQLGIVSQEPILFDCSIAENIaygDNSRVVPHDEIVRAAKEANIHPFIETLPQKYNTRVGDKGTQLSGGQKQRIA 1181
Cdd:PTZ00243 1379 LRELRRQFSMIPQDPVLFDGTVRQNV---DPFLEASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMC 1455
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1182 IARALI-RQPRVLLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIENGKVKEHGTHQQL-LAQ 1259
Cdd:PTZ00243 1456 MARALLkKGSGFILMDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELvMNR 1535
|
....*....
gi 338817954 1260 KGIYFSMVN 1268
Cdd:PTZ00243 1536 QSIFHSMVE 1544
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
391-614 |
1.88e-31 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 130.14 E-value: 1.88e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 391 LEFSDVHFSYPSranIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLREI-I 469
Cdd:COG1129 5 LEMRGISKSFGG---VKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQAAgI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 470 GVVSQEPVLFST-TIAENI---RYGRGNVTMD--EIEKAVKEANAYdfiMKLPQKFDTLVGDrgaqLSGGQKQRIAIARA 543
Cdd:COG1129 82 AIIHQELNLVPNlSVAENIflgREPRRGGLIDwrAMRRRARELLAR---LGLDIDPDTPVGD----LSVAQQQLVEIARA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 338817954 544 LVRNPKILLLDEATSALdteSEAEVQAALD-----KAReGRTTIVIAHRLSTIRN-ADVIAGFEDGVIVEQGSHSEL 614
Cdd:COG1129 155 LSRDARVLILDEPTASL---TEREVERLFRiirrlKAQ-GVAIIYISHRLDEVFEiADRVTVLRDGRLVGTGPVAEL 227
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
749-965 |
1.95e-31 |
|
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: 125.32 E-value: 1.95e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 749 NMFSLVFLGLGVLSFFTFFLQGFTFGKAGEILTTRLRSMAFKAMLRQDMSWFDDHKnsTGALSTRLATDAAQVQGATGTR 828
Cdd:cd18573 41 KTFALALLGVFVVGAAANFGRVYLLRIAGERIVARLRKRLFKSILRQDAAFFDKNK--TGELVSRLSSDTSVVGKSLTQN 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 829 LALIAQNTANLGTGIIISFIYGWQLTLLLLSVVPFIAVAGIVEMKMLAGNAKRDKKEMEAAGKIATEAIENIRTVVSLTQ 908
Cdd:cd18573 119 LSDGLRSLVSGVGGIGMMLYISPKLTLVMLLVVPPIAVGAVFYGRYVRKLSKQVQDALADATKVAEERLSNIRTVRAFAA 198
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 338817954 909 ERKFESMYVEKLHGPYRNSVRKAHIYGITFSISQAFMYFSYAGCFRFGSYLIVNGHM 965
Cdd:cd18573 199 ERKEVERYAKKVDEVFDLAKKEALASGLFFGSTGFSGNLSLLSVLYYGGSLVASGEL 255
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
391-597 |
2.01e-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: 122.59 E-value: 2.01e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 391 LEFSDVHFSYPSRAnikILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRcLREIIG 470
Cdd:COG4133 3 LEAENLSCRRGERL---LFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDARED-YRRRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 471 VVSQEPVLFST-TIAENIR-----YGRgNVTMDEIEKAVKEanaydfiMKLPQKFDTLVGdrgaQLSGGQKQRIAIARAL 544
Cdd:COG4133 79 YLGHADGLKPElTVRENLRfwaalYGL-RADREAIDEALEA-------VGLAGLADLPVR----QLSAGQKRRVALARLL 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 338817954 545 VRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIA-HRLSTIRNADVI 597
Cdd:COG4133 147 LSPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTtHQPLELAAARVL 200
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
391-614 |
2.75e-31 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 123.73 E-value: 2.75e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 391 LEFSDVHFSYPSRaniKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYD-----PTEGKISIDGQDI---RNFNV 462
Cdd:PRK14239 6 LQVSDLSVYYNKK---KALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnpevTITGSIVYNGHNIyspRTDTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 463 RcLREIIGVVSQEPVLFSTTIAENIRYG------RGNVTMDE-IEKAVKEANAYDFIMklpqkfDTLvGDRGAQLSGGQK 535
Cdd:PRK14239 83 D-LRKEIGMVFQQPNPFPMSIYENVVYGlrlkgiKDKQVLDEaVEKSLKGASIWDEVK------DRL-HDSALGLSGGQQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 536 QRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTI-RNADVIAGFEDGVIVEQGSHSEL 614
Cdd:PRK14239 155 QRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQAsRISDRTGFFLDGDLIEYNDTKQM 234
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1042-1241 |
2.78e-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: 2.78e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1042 TRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQWlRAQLGIVSQEPILF-D 1120
Cdd:COG4133 11 RRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDY-RRRLAYLGHADGLKpE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1121 CSIAENIA-----YGdnsRVVPHDEIVRAAKEANIHPFIETLPQkyntrvgdkgtQLSGGQKQRIAIARALIRQPRVLLL 1195
Cdd:COG4133 90 LTVRENLRfwaalYG---LRADREAIDEALEAVGLAGLADLPVR-----------QLSAGQKRRVALARLLLSPAPLWLL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 338817954 1196 DEATSALDTESEKVVQEALDKAREGRTCIVIA-HRLSTIQNADLIVV 1241
Cdd:COG4133 156 DEPFTALDAAGVALLAELIAAHLARGGAVLLTtHQPLELAAARVLDL 202
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1040-1252 |
3.12e-31 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 126.07 E-value: 3.12e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1040 YPTRAN-VPVLQGLSLEVKKGQTLALVGSSGCGKST---VVQLLERfydPMAGSVLLDGQEAKKLNVQWLRA---QLGIV 1112
Cdd:PRK11153 11 FPQGGRtIHALNNVSLHIPAGEIFGVIGASGAGKSTlirCINLLER---PTSGRVLVDGQDLTALSEKELRKarrQIGMI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1113 SQE-PILFDCSIAENIAY-----GdnsrvVPHDEIvraakEANIHPFIEtlpqkyntRVG--DKG----TQLSGGQKQRI 1180
Cdd:PRK11153 88 FQHfNLLSSRTVFDNVALplelaG-----TPKAEI-----KARVTELLE--------LVGlsDKAdrypAQLSGGQKQRV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 338817954 1181 AIARALIRQPRVLLLDEATSALDTESEKVVQEALDKA-RE-GRTCIVIAHRLSTI-QNADLIVVIENGKVKEHGT 1252
Cdd:PRK11153 150 AIARALASNPKVLLCDEATSALDPATTRSILELLKDInRElGLTIVLITHEMDVVkRICDRVAVIDAGRLVEQGT 224
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
1031-1247 |
3.62e-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: 122.13 E-value: 3.62e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1031 VTFNEVVFNYPtrANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLN---VQWLRA 1107
Cdd:cd03292 1 IEFINVTKTYP--NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRgraIPYLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1108 QLGIVSQE-PILFDCSIAENIAYGDNSRVVPHDEIVRAAKEAnihpfIETLPQKYNTRvgDKGTQLSGGQKQRIAIARAL 1186
Cdd:cd03292 79 KIGVVFQDfRLLPDRNVYENVAFALEVTGVPPREIRKRVPAA-----LELVGLSHKHR--ALPAELSGGEQQRVAIARAI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 338817954 1187 IRQPRVLLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNA--DLIVVIENGKV 1247
Cdd:cd03292 152 VNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTtrHRVIALERGKL 214
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
408-614 |
3.98e-31 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 123.32 E-value: 3.98e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 408 ILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKI-----SIDGQdiRNFN-----VRCLREIIGVVSQEPV 477
Cdd:PRK11264 18 VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIrvgdiTIDTA--RSLSqqkglIRQLRQHVGFVFQNFN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 478 LFS-TTIAENIRygRGNVTMDEIEKAVKEANAYDFIMKLpqkfdTLVGDRGA---QLSGGQKQRIAIARALVRNPKILLL 553
Cdd:PRK11264 96 LFPhRTVLENII--EGPVIVKGEPKEEATARARELLAKV-----GLAGKETSyprRLSGGQQQRVAIARALAMRPEVILF 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 338817954 554 DEATSALDTESEAEVQAALDK-AREGRTTIVIAHRLSTIRN-ADVIAGFEDGVIVEQGSHSEL 614
Cdd:PRK11264 169 DEPTSALDPELVGEVLNTIRQlAQEKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKAL 231
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
1033-1251 |
4.42e-31 |
|
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: 121.87 E-value: 4.42e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1033 FNEVVFNYPtraNVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLnvqwlRAQLGIV 1112
Cdd:cd03235 2 VEDLTVSYG---GHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE-----RKRIGYV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1113 SQEPIL---FDCSIAENIAYGDNSRVVPHDEIVRAAKEAnihpFIETLpqkynTRVGDKG------TQLSGGQKQRIAIA 1183
Cdd:cd03235 74 PQRRSIdrdFPISVRDVVLMGLYGHKGLFRRLSKADKAK----VDEAL-----ERVGLSEladrqiGELSGGQQQRVLLA 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1184 RALIRQPRVLLLDEATSALDTESEKVVQEALDK-AREGRTCIVIAHRLSTIQN-ADLIVVIeNGKVKEHG 1251
Cdd:cd03235 145 RALVQDPDLLLLDEPFAGVDPKTQEDIYELLRElRREGMTILVVTHDLGLVLEyFDRVLLL-NRTVVASG 213
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
1036-1251 |
5.83e-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: 120.23 E-value: 5.83e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1036 VVFNYPTRanvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQWLRAQLGIVSQe 1115
Cdd:cd03214 5 LSVGYGGR---TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1116 pilfdcsiaeniaygdnsrvvphdeivrAAKEANIHPFIEtlpQKYNTrvgdkgtqLSGGQKQRIAIARALIRQPRVLLL 1195
Cdd:cd03214 81 ----------------------------ALELLGLAHLAD---RPFNE--------LSGGERQRVLLARALAQEPPILLL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 338817954 1196 DEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLS-TIQNADLIVVIENGKVKEHG 1251
Cdd:cd03214 122 DEPTSHLDIAHQIELLELLRRlaRERGKTVVMVLHDLNlAARYADRVILLKDGRIVAQG 180
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
117-328 |
1.85e-30 |
|
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: 122.62 E-value: 1.85e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 117 YSGLGGGVLVAA---YIQVSFWTLAAGRQIKKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDDVSKISEGIGDKVGMFF 193
Cdd:cd18573 44 ALALLGVFVVGAaanFGRVYLLRIAGERIVARLRKRLFKSILRQDAAFFDKNKTGELVSRLSSDTSVVGKSLTQNLSDGL 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 194 QAIATFFAGFIVGFIRGWKLTLVIMAISPILGLSTAVWAKILSTFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKEL 273
Cdd:cd18573 124 RSLVSGVGGIGMMLYISPKLTLVMLLVVPPIAVGAVFYGRYVRKLSKQVQDALADATKVAEERLSNIRTVRAFAAERKEV 203
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 338817954 274 ERYQKHLENAKKIGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTIG 328
Cdd:cd18573 204 ERYAKKVDEVFDLAKKEALASGLFFGSTGFSGNLSLLSVLYYGGSLVASGELTVG 258
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1053-1259 |
2.36e-30 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 120.24 E-value: 2.36e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1053 SLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVqwlrAQ--LGIVSQEPILFD-CSIAENIAY 1129
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPP----AErpVSMLFQENNLFPhLTVAQNIGL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1130 GDNSR----VVPHDEIVRAAKEANIHPFIETLPQkyntrvgdkgtQLSGGQKQRIAIARALIRQPRVLLLDEATSALD-- 1203
Cdd:COG3840 95 GLRPGlkltAEQRAQVEQALERVGLAGLLDRLPG-----------QLSGGQRQRVALARCLVRKRPILLLDEPFSALDpa 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 338817954 1204 --TESEKVVQEALDkaREGRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHGTHQQLLAQ 1259
Cdd:COG3840 164 lrQEMLDLVDELCR--ERGLTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAALLDG 220
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
1048-1248 |
2.76e-30 |
|
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: 119.28 E-value: 2.76e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1048 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGqeaKKLNVQWLRAQLGIVSQEP--ILFDCSIAE 1125
Cdd:cd03226 15 ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNG---KPIKAKERRKSIGYVMQDVdyQLFTDSVRE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1126 NIAYGDNSrvvPHDEIVRAA---KEANIHPFIETLPQkyntrvgdkgtQLSGGQKQRIAIARALIRQPRVLLLDEATSAL 1202
Cdd:cd03226 92 ELLLGLKE---LDAGNEQAEtvlKDLDLYALKERHPL-----------SLSGGQKQRLAIAAALLSGKDLLIFDEPTSGL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 338817954 1203 DTESEKVVQEALDK-AREGRTCIVIAHRLSTIQN-ADLIVVIENGKVK 1248
Cdd:cd03226 158 DYKNMERVGELIRElAAQGKAVIVITHDYEFLAKvCDRVLLLANGAIV 205
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1031-1258 |
3.02e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 121.63 E-value: 3.02e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1031 VTFNEVVFNYPTraNVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLN-VQWLRAQL 1109
Cdd:PRK13644 2 IRLENVSYSYPD--GTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSkLQGIRKLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1110 GIVSQEP--ILFDCSIAENIAYGDNSRVVPHDEIVRAAKEAnihpFIETLPQKYNTRvgdKGTQLSGGQKQRIAIARALI 1187
Cdd:PRK13644 80 GIVFQNPetQFVGRTVEEDLAFGPENLCLPPIEIRKRVDRA----LAEIGLEKYRHR---SPKTLSGGQGQCVALAGILT 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 338817954 1188 RQPRVLLLDEATSALDTESEKVVQEALDKA-REGRTCIVIAHRLSTIQNADLIVVIENGKVKEHGTHQQLLA 1258
Cdd:PRK13644 153 MEPECLIFDEVTSMLDPDSGIAVLERIKKLhEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLS 224
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
391-614 |
3.23e-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: 119.53 E-value: 3.23e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 391 LEFSDVHFSYPSRANIkILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLREIiG 470
Cdd:cd03263 1 LQIRNLTKTYKKGTKP-AVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQSL-G 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 471 VVSQEPVLFST-TIAENIRY-----GRGNVTMDEiekavkEANAYDFIMKLPQKFDTLVGDrgaqLSGGQKQRIAIARAL 544
Cdd:cd03263 79 YCPQFDALFDElTVREHLRFyarlkGLPKSEIKE------EVELLLRVLGLTDKANKRART----LSGGMKRKLSLAIAL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 338817954 545 VRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTIRN-ADVIAGFEDGVIVEQGSHSEL 614
Cdd:cd03263 149 IGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEAlCDRIAIMSDGKLRCIGSPQEL 219
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
391-606 |
3.56e-30 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 117.53 E-value: 3.56e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 391 LEFSDVHFSYPsraNIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVR-CLREII 469
Cdd:cd03216 1 LELRGITKRFG---GVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRdARRAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 470 GVVSQepvlfsttiaenirygrgnvtmdeiekavkeanaydfimklpqkfdtlvgdrgaqLSGGQKQRIAIARALVRNPK 549
Cdd:cd03216 78 AMVYQ-------------------------------------------------------LSVGERQMVEIARALARNAR 102
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 338817954 550 ILLLDEATSALdteSEAEVQAALD----KAREGRTTIVIAHRLSTIRN-ADVIAGFEDGVIV 606
Cdd:cd03216 103 LLILDEPTAAL---TPAEVERLFKvirrLRAQGVAVIFISHRLDEVFEiADRVTVLRDGRVV 161
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1031-1257 |
4.02e-30 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 120.20 E-value: 4.02e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1031 VTFNEVVFNYptrANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAK--KLNVQWLRAQ 1108
Cdd:PRK09493 2 IEFKNVSKHF---GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpKVDERLIRQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1109 LGIVSQEPILFDCSIA-ENIAYGDNSrvvphdeiVRAAKEANIHPFIETLPQKYN--TRVGDKGTQLSGGQKQRIAIARA 1185
Cdd:PRK09493 79 AGMVFQQFYLFPHLTAlENVMFGPLR--------VRGASKEEAEKQARELLAKVGlaERAHHYPSELSGGQQQRVAIARA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 338817954 1186 LIRQPRVLLLDEATSALDTE-SEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHGTHQQLL 1257
Cdd:PRK09493 151 LAVKPKLMLFDEPTSALDPElRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKvASRLIFIDKGRIAEDGDPQVLI 224
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
409-614 |
4.12e-30 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 119.75 E-value: 4.12e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 409 LKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRclREIIGVVSQEPVLFS-TTIAENI 487
Cdd:cd03296 18 LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQ--ERNVGFVFQHYALFRhMTVFDNV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 488 RYG------RGNVTMDEIEKAVKEanaydfIMKLPQkFDTLvGDR-GAQLSGGQKQRIAIARALVRNPKILLLDEATSAL 560
Cdd:cd03296 96 AFGlrvkprSERPPEAEIRAKVHE------LLKLVQ-LDWL-ADRyPAQLSGGQRQRVALARALAVEPKVLLLDEPFGAL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 338817954 561 DTESEAEVQAALDKARE--GRTTIVIAHRLS-TIRNADVIAGFEDGVIVEQGSHSEL 614
Cdd:cd03296 168 DAKVRKELRRWLRRLHDelHVTTVFVTHDQEeALEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
753-965 |
8.35e-30 |
|
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: 120.82 E-value: 8.35e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 753 LVFLGLGVLSFFTFFLQGFTFGKAGEILTTRLRSMAFKAMLRQDMSWFDdhKNSTGALSTRLATDAAQVQGATGTRLALI 832
Cdd:cd18780 46 LILLGVVLIGSIATFLRSWLFTLAGERVVARLRKRLFSAIIAQEIAFFD--VTRTGELLNRLSSDTQVLQNAVTVNLSML 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 833 AQNTANLGTGIIISFIYGWQLTLLLLSVVPFIAVAGIVEMKMLAGNAKRDKKEMEAAGKIATEAIENIRTVVSLTQERKF 912
Cdd:cd18780 124 LRYLVQIIGGLVFMFTTSWKLTLVMLSVVPPLSIGAVIYGKYVRKLSKKFQDALAAASTVAEESISNIRTVRSFAKETKE 203
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 338817954 913 ESMYVEKLHGPYRNSVRKAHIYGITFSISQAFMYFSYAGCFRFGSYLIVNGHM 965
Cdd:cd18780 204 VSRYSEKINESYLLGKKLARASGGFNGFMGAAAQLAIVLVLWYGGRLVIDGEL 256
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
385-618 |
8.98e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 120.23 E-value: 8.98e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 385 DNIkgnLEFSDVHFSYPSraNIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRC 464
Cdd:PRK13647 2 DNI---IEVEDLHFRYKD--GTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKW 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 465 LREIIGVVSQEP--VLFSTTIAENIRYGRGN--VTMDEIEKAVKEA----NAYDFIMKLPQkfdtlvgdrgaQLSGGQKQ 536
Cdd:PRK13647 77 VRSKVGLVFQDPddQVFSSTVWDDVAFGPVNmgLDKDEVERRVEEAlkavRMWDFRDKPPY-----------HLSYGQKK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 537 RIAIARALVRNPKILLLDEATSALDTESEAEVQAALDK-AREGRTTIVIAHRLS-TIRNADVIAGFEDGVIVEQGSHSEL 614
Cdd:PRK13647 146 RVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRlHNQGKTVIVATHDVDlAAEWADQVIVLKEGRVLAEGDKSLL 225
|
....
gi 338817954 615 MKKE 618
Cdd:PRK13647 226 TDED 229
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
391-614 |
1.47e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 119.45 E-value: 1.47e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 391 LEFSDVHFSYPSRANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLREIIG 470
Cdd:PRK13650 5 IEVKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 471 VVSQEP--VLFSTTIAENIRYGRGN--VTMDEIEKAVKEA----NAYDFIMKLPqkfdtlvgdrgAQLSGGQKQRIAIAR 542
Cdd:PRK13650 85 MVFQNPdnQFVGATVEDDVAFGLENkgIPHEEMKERVNEAlelvGMQDFKEREP-----------ARLSGGQKQRVAIAG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 338817954 543 ALVRNPKILLLDEATSALDTESEAEVQAALDKARE--GRTTIVIAHRLSTIRNADVIAGFEDGVIVEQGSHSEL 614
Cdd:PRK13650 154 AVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDdyQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPREL 227
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
391-607 |
1.47e-29 |
|
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: 117.92 E-value: 1.47e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 391 LEFSDVHFSYPSRAN-IKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFN------VR 463
Cdd:COG4181 9 IELRGLTKTVGTGAGeLTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDedararLR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 464 clREIIGVVSQ-EPVLFSTTIAENI-----RYGRGNVTmdeiEKAVKEANAYDfimklpqkfdtlVGDRG----AQLSGG 533
Cdd:COG4181 89 --ARHVGFVFQsFQLLPTLTALENVmlpleLAGRRDAR----ARARALLERVG------------LGHRLdhypAQLSGG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 338817954 534 QKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAAL-DKAREGRTTIVIA-HRLSTIRNADVIAGFEDGVIVE 607
Cdd:COG4181 151 EQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLfELNRERGTTLVLVtHDPALAARCDRVLRLRAGRLVE 226
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
1049-1247 |
1.54e-29 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 117.40 E-value: 1.54e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1049 LQGLSLEVK---KGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQ----EAKKLNVQWLRAQLGIVSQEPILF-D 1120
Cdd:cd03297 10 LPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlfdSRKKINLPPQQRKIGLVFQQYALFpH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1121 CSIAENIAYG-----DNSRVVPHDEIVRAAkeaNIHPFIETLPQkyntrvgdkgtQLSGGQKQRIAIARALIRQPRVLLL 1195
Cdd:cd03297 90 LNVRENLAFGlkrkrNREDRISVDELLDLL---GLDHLLNRYPA-----------QLSGGEKQRVALARALAAQPELLLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 338817954 1196 DEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLSTIQN-ADLIVVIENGKV 1247
Cdd:cd03297 156 DEPFSALDRALRLQLLPELKQikKNLNIPVIFVTHDLSEAEYlADRIVVMEDGRL 210
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
391-601 |
2.23e-29 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 118.60 E-value: 2.23e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 391 LEFSDVHFSYPSRaniKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYD-----PTEGKISIDGQDI--RNFNVR 463
Cdd:PRK14258 8 IKVNNLSFYYDTQ---KILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNElesevRVEGRVEFFNQNIyeRRVNLN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 464 CLREIIGVVSQEPVLFSTTIAENIRYG------RGNVTMDEI-EKAVKEANAYDFIMKLPQKfdtlvgdRGAQLSGGQKQ 536
Cdd:PRK14258 85 RLRRQVSMVHPKPNLFPMSVYDNVAYGvkivgwRPKLEIDDIvESALKDADLWDEIKHKIHK-------SALDLSGGQQQ 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 338817954 537 RIAIARALVRNPKILLLDEATSALDTESEAEVQAALD--KAREGRTTIVIAHRLSTI-RNADVIAGFE 601
Cdd:PRK14258 158 RLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQslRLRSELTMVIVSHNLHQVsRLSDFTAFFK 225
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
391-614 |
2.55e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 119.04 E-value: 2.55e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 391 LEFSDVHFSYPSRANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLREIIG 470
Cdd:PRK13642 5 LEVENLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 471 VVSQEP--VLFSTTIAENIRYGRGN--VTMDEIEKAVKEA----NAYDFIMKLPqkfdtlvgdrgAQLSGGQKQRIAIAR 542
Cdd:PRK13642 85 MVFQNPdnQFVGATVEDDVAFGMENqgIPREEMIKRVDEAllavNMLDFKTREP-----------ARLSGGQKQRVAVAG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 338817954 543 ALVRNPKILLLDEATSALDTESEAEVQAALDKAREGR--TTIVIAHRLSTIRNADVIAGFEDGVIVEQGSHSEL 614
Cdd:PRK13642 154 IIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYqlTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSEL 227
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1045-1247 |
2.82e-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: 114.83 E-value: 2.82e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1045 NVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQwlRAQ-LGIvsqepilfdcsi 1123
Cdd:cd03216 12 GVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPR--DARrAGI------------ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1124 aeniaygdnsrvvphdeivraakeANIHpfietlpqkyntrvgdkgtQLSGGQKQRIAIARALIRQPRVLLLDEATSAL- 1202
Cdd:cd03216 78 ------------------------AMVY-------------------QLSVGERQMVEIARALARNARLLILDEPTAALt 114
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 338817954 1203 DTESEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVIENGKV 1247
Cdd:cd03216 115 PAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEiADRVTVLRDGRV 160
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
1045-1251 |
3.00e-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: 116.59 E-value: 3.00e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1045 NVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQ-----EAKKLNVqwlraqlGIVSQEPILF 1119
Cdd:cd03301 12 NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRdvtdlPPKDRDI-------AMVFQNYALY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1120 -DCSIAENIAYGDNSRVVPHDEIVRAAKEANIHPFIETLPQKyntrvgdKGTQLSGGQKQRIAIARALIRQPRVLLLDEA 1198
Cdd:cd03301 85 pHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDR-------KPKQLSGGQRQRVALGRAIVREPKVFLMDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 338817954 1199 TSALDTESEKVVQEALDK--AREGRTCIVIAH-RLSTIQNADLIVVIENGKVKEHG 1251
Cdd:cd03301 158 LSNLDAKLRVQMRAELKRlqQRLGTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
391-618 |
3.15e-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: 117.88 E-value: 3.15e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 391 LEFSDVHFSYPSRaniKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGK-ISIDGQDIRNFNVRCLREII 469
Cdd:COG1119 4 LELRNVTVRRGGK---TILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdVRLFGERRGGEDVWELRKRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 470 GVVSQEpvlfsttIAENIRygrGNVTmdeIEKAVKEAnAYDFIMkLPQKFD-----------TLVG-----DRG-AQLSG 532
Cdd:COG1119 81 GLVSPA-------LQLRFP---RDET---VLDVVLSG-FFDSIG-LYREPTdeqrerarellELLGlahlaDRPfGTLSQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 533 GQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDK-AREGRTTIV-IAHRLStirnaDVIAGF------EDGV 604
Cdd:COG1119 146 GEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKlAAEGAPTLVlVTHHVE-----EIPPGIthvlllKDGR 220
|
250
....*....|....
gi 338817954 605 IVEQGSHSELMKKE 618
Cdd:COG1119 221 VVAAGPKEEVLTSE 234
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1031-1256 |
3.66e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 118.32 E-value: 3.66e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1031 VTFNEVVFNYPTRANVpVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQWLRAQLG 1110
Cdd:PRK13648 8 IVFKNVSFQYQSDASF-TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1111 IVSQEPI-LFDCSIAE-NIAYGDNSRVVPHDEIVR----AAKEANIHPFIETLPQkyntrvgdkgtQLSGGQKQRIAIAR 1184
Cdd:PRK13648 87 IVFQNPDnQFVGSIVKyDVAFGLENHAVPYDEMHRrvseALKQVDMLERADYEPN-----------ALSGGQKQRVAIAG 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 338817954 1185 ALIRQPRVLLLDEATSALDTESEKVVQEALDKAREGR--TCIVIAHRLSTIQNADLIVVIENGKVKEHGTHQQL 1256
Cdd:PRK13648 156 VLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEI 229
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
708-965 |
5.30e-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: 118.41 E-value: 5.30e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 708 FVVGTVCAIANGALqPAFsiiLSEMI-AIFGPGDDAVKQQKCNMFSLVFLGLGVLSFftffLQGFTFGKAGEILTTRLRS 786
Cdd:cd18572 2 FVFLVVAALSELAI-PHY---TGAVIdAVVADGSREAFYRAVLLLLLLSVLSGLFSG----LRGGCFSYAGTRLVRRLRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 787 MAFKAMLRQDMSWFDDHKnsTGALSTRLATDAAQVQGATGTRLALIAQNTANLGTGIIISFIYGWQLTLLLLSVVPFIAV 866
Cdd:cd18572 74 DLFRSLLRQDIAFFDATK--TGELTSRLTSDCQKVSDPLSTNLNVFLRNLVQLVGGLAFMFSLSWRLTLLAFITVPVIAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 867 AGIVEMKMLAGNAKRDKKEMEAAGKIATEAIENIRTVVSLTQERKFESMYVEKLHGPYRNSVRKAHIYGITFSISQAFMY 946
Cdd:cd18572 152 ITKVYGRYYRKLSKEIQDALAEANQVAEEALSNIRTVRSFATEEREARRYERALDKALKLSVRQALAYAGYVAVNTLLQN 231
|
250
....*....|....*....
gi 338817954 947 FSYAGCFRFGSYLIVNGHM 965
Cdd:cd18572 232 GTQVLVLFYGGHLVLSGRM 250
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
1048-1252 |
5.48e-29 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 116.38 E-value: 5.48e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1048 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQwLRAQLGIVS--QEPILF-DCSIA 1124
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPH-EIARLGIGRtfQIPRLFpELTVL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1125 ENI----------AYGDNSRVVPHDEIVRAAKEAnihpfIET--LPQKYNTRVGDkgtqLSGGQKQRIAIARALIRQPRV 1192
Cdd:cd03219 94 ENVmvaaqartgsGLLLARARREEREARERAEEL-----LERvgLADLADRPAGE----LSYGQQRRLEIARALATDPKL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 338817954 1193 LLLDEATSAL-DTESEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHGT 1252
Cdd:cd03219 165 LLLDEPAAGLnPEETEELAELIRELRERGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGT 226
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1038-1267 |
5.55e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 117.91 E-value: 5.55e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1038 FNYP--TRAnvpvLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQWLRAQLGIVSQE 1115
Cdd:PRK13647 12 FRYKdgTKA----LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLVFQD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1116 P--ILFDCSIAENIAYGDNSRVVPHDEIVRAAKEA----NIHPFIETLPQkyntrvgdkgtQLSGGQKQRIAIARALIRQ 1189
Cdd:PRK13647 88 PddQVFSSTVWDDVAFGPVNMGLDKDEVERRVEEAlkavRMWDFRDKPPY-----------HLSYGQKKRVAIAGVLAMD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1190 PRVLLLDEATSALDTESEKVVQEALDK-AREGRTCIVIAHRLS-TIQNADLIVVIENGKVKEHG-----THQQLLAQKGI 1262
Cdd:PRK13647 157 PDVIVLDEPMAYLDPRGQETLMEILDRlHNQGKTVIVATHDVDlAAEWADQVIVLKEGRVLAEGdksllTDEDIVEQAGL 236
|
....*
gi 338817954 1263 YFSMV 1267
Cdd:PRK13647 237 RLPLV 241
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
385-618 |
5.85e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 117.54 E-value: 5.85e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 385 DNIkgnLEFSDVHFSYPSRANIKiLKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRC 464
Cdd:PRK13648 5 NSI---IVFKNVSFQYQSDASFT-LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 465 LREIIGVVSQEP--VLFSTTIAENIRYGRGN--VTMDEIEKAVKEA----NAYDFIMKLPQkfdtlvgdrgaQLSGGQKQ 536
Cdd:PRK13648 81 LRKHIGIVFQNPdnQFVGSIVKYDVAFGLENhaVPYDEMHRRVSEAlkqvDMLERADYEPN-----------ALSGGQKQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 537 RIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKAREGR--TTIVIAHRLSTIRNADVIAGFEDGVIVEQGSHSEL 614
Cdd:PRK13648 150 RVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEI 229
|
....
gi 338817954 615 MKKE 618
Cdd:PRK13648 230 FDHA 233
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
390-618 |
6.23e-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: 6.23e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 390 NLEFSDVHFSYPSRAnikilKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNV--Rclre 467
Cdd:COG3840 1 MLRLDDLTYRYGDFP-----LRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPaeR---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 468 IIGVVSQEPVLFS-TTIAENIRYG---RGNVTMDE---IEKAVKEANAYDFIMKLPqkfdtlvgdrgAQLSGGQKQRIAI 540
Cdd:COG3840 72 PVSMLFQENNLFPhLTVAQNIGLGlrpGLKLTAEQraqVEQALERVGLAGLLDRLP-----------GQLSGGQRQRVAL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 541 ARALVRNPKILLLDEATSALDTESEAEVQAALDK--AREGRTTIVIAHRLS-TIRNADVIAGFEDGVIVEQGSHSELMKK 617
Cdd:COG3840 141 ARCLVRKRPILLLDEPFSALDPALRQEMLDLVDElcRERGLTVLMVTHDPEdAARIADRVLLVADGRIAADGPTAALLDG 220
|
.
gi 338817954 618 E 618
Cdd:COG3840 221 E 221
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
391-608 |
9.52e-29 |
|
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: 116.83 E-value: 9.52e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 391 LEFSDVHFSYPS------RANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFN--- 461
Cdd:TIGR02769 3 LEVRDVTHTYRTgglfgaKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDrkq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 462 VRCLREIIGVVSQE-PVLFS--TTIAENIRYGRGNVT-MDEIEKAVKEANAYDfIMKLPqkfDTLVGDRGAQLSGGQKQR 537
Cdd:TIGR02769 83 RRAFRRDVQLVFQDsPSAVNprMTVRQIIGEPLRHLTsLDESEQKARIAELLD-MVGLR---SEDADKLPRQLSGGQLQR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 338817954 538 IAIARALVRNPKILLLDEATSALDTESEAEVQAALDK--AREGRTTIVIAHRLSTI-RNADVIAGFEDGVIVEQ 608
Cdd:TIGR02769 159 INIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKlqQAFGTAYLFITHDLRLVqSFCQRVAVMDKGQIVEE 232
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
385-618 |
1.11e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 117.21 E-value: 1.11e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 385 DNIkgnLEFSDVHFSYPSrANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDP---TEGKISIDGQDIRNFN 461
Cdd:PRK13640 3 DNI---VEFKHVSFTYPD-SKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDGITLTAKT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 462 VRCLREIIGVVSQEP--VLFSTTIAENIRYGRGN--VTMDEIEKAVKEANA----YDFIMKLPQkfdtlvgdrgaQLSGG 533
Cdd:PRK13640 79 VWDIREKVGIVFQNPdnQFVGATVGDDVAFGLENraVPRPEMIKIVRDVLAdvgmLDYIDSEPA-----------NLSGG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 534 QKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKARE--GRTTIVIAHRLSTIRNADVIAGFEDGVIVEQGSH 611
Cdd:PRK13640 148 QKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKknNLTVISITHDIDEANMADQVLVLDDGKLLAQGSP 227
|
....*..
gi 338817954 612 SELMKKE 618
Cdd:PRK13640 228 VEIFSKV 234
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1042-1244 |
1.37e-28 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 114.50 E-value: 1.37e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1042 TRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDP---MAGSVLLDGQEAKKLNVQwlRAQLGIVSQEPIL 1118
Cdd:COG4136 10 TLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALPAE--QRRIGILFQDDLL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1119 FD-CSIAENIAYG---DNSRVVPHDEIVRAAKEANIHPFIETLPqkyntrvgdkgTQLSGGQKQRIAIARALIRQPRVLL 1194
Cdd:COG4136 88 FPhLSVGENLAFAlppTIGRAQRRARVEQALEEAGLAGFADRDP-----------ATLSGGQRARVALLRALLAEPRALL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 338817954 1195 LDEATSALDTE-SEKVVQEALDKARE-GRTCIVIAHRLSTIQNADLIVVIEN 1244
Cdd:COG4136 157 LDEPFSKLDAAlRAQFREFVFEQIRQrGIPALLVTHDEEDAPAAGRVLDLGN 208
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
403-607 |
1.45e-28 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 116.32 E-value: 1.45e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 403 RANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFN---VRCLREIIGVVSQEP--- 476
Cdd:PRK10419 22 HQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNraqRKAFRRDIQMVFQDSisa 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 477 VLFSTTIAENIRYG-RGNVTMDEIEKAVKEANAYDfIMKLPqkfDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDE 555
Cdd:PRK10419 102 VNPRKTVREIIREPlRHLLSLDKAERLARASEMLR-AVDLD---DSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDE 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 338817954 556 ATSALDTESEAEVQAALDKAREGRTT--IVIAHRLSTI-RNADVIAGFEDGVIVE 607
Cdd:PRK10419 178 AVSNLDLVLQAGVIRLLKKLQQQFGTacLFITHDLRLVeRFCQRVMVMDNGQIVE 232
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
711-983 |
1.57e-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: 116.81 E-value: 1.57e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 711 GTVCAIANGALQPAFSIILSEMI-AIFGPGDDAVKQQkcnmFSLVFLGLGVL-SFFTFFlQGFTFGKAGEILTTRLRSMA 788
Cdd:cd18576 1 GLILLLLSSAIGLVFPLLAGQLIdAALGGGDTASLNQ----IALLLLGLFLLqAVFSFF-RIYLFARVGERVVADLRKDL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 789 FKAMLRQDMSWFDDHKnsTGALSTRLATDAAQVQGATGTRLALIAQNTANLGTGIIISFIYGWQLTLLLLSVVPFIAVAG 868
Cdd:cd18576 76 YRHLQRLPLSFFHERR--VGELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWKLTLLMLATVPVVVLVA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 869 IVEMKMLAGNAKRDKKEMEAAGKIATEAIENIRTVVSLTQERkFESM-YVEKLHGPYRNSVRKAHIYGITFSISQAFMYF 947
Cdd:cd18576 154 VLFGRRIRKLSKKVQDELAEANTIVEETLQGIRVVKAFTRED-YEIErYRKALERVVKLALKRARIRALFSSFIIFLLFG 232
|
250 260 270
....*....|....*....|....*....|....*...
gi 338817954 948 SYAGCFRFGSYLIVNGHMRFKDVI--LVFSAIVLGAVA 983
Cdd:cd18576 233 AIVAVLWYGGRLVLAGELTAGDLVafLLYTLFIAGSIG 270
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
384-628 |
1.61e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 116.87 E-value: 1.61e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 384 PDNIkgnLEFSDVHFSYPSraNIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQ--DIRNFN 461
Cdd:PRK13636 2 EDYI---LKVEELNYNYSD--GTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpiDYSRKG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 462 VRCLREIIGVVSQEP--VLFSTTIAENIRYGRGNVTM--DEIEKAVKEANAYDFIMKLPQKfdtlvgdRGAQLSGGQKQR 537
Cdd:PRK13636 77 LMKLRESVGMVFQDPdnQLFSASVYQDVSFGAVNLKLpeDEVRKRVDNALKRTGIEHLKDK-------PTHCLSFGQKKR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 538 IAIARALVRNPKILLLDEATSALDTESEAEV-QAALDKAREGRTTIVIA-HRLSTIR-NADVIAGFEDGVIVEQGSHSEL 614
Cdd:PRK13636 150 VAIAGVLVMEPKVLVLDEPTAGLDPMGVSEImKLLVEMQKELGLTIIIAtHDIDIVPlYCDNVFVMKEGRVILQGNPKEV 229
|
250
....*....|....*
gi 338817954 615 M-KKEGIyfRLVNMQ 628
Cdd:PRK13636 230 FaEKEML--RKVNLR 242
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
1018-1275 |
1.70e-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: 124.67 E-value: 1.70e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1018 SGEGLWPDKFE---------GSVTFNEVVFNYpTRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAG 1088
Cdd:TIGR00957 615 SHEELEPDSIErrtikpgegNSITVHNATFTW-ARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEG 693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1089 SVLLDGQEAkklnvqwlraqlgIVSQEPILFDCSIAENIAYGDNSRVVPHDEIVRAAKeanIHPFIETLPQKYNTRVGDK 1168
Cdd:TIGR00957 694 HVHMKGSVA-------------YVPQQAWIQNDSLRENILFGKALNEKYYQQVLEACA---LLPDLEILPSGDRTEIGEK 757
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1169 GTQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEAL---DKAREGRTCIVIAHRLSTIQNADLIVVIENG 1245
Cdd:TIGR00957 758 GVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVigpEGVLKNKTRILVTHGISYLPQVDVIIVMSGG 837
|
250 260 270
....*....|....*....|....*....|
gi 338817954 1246 KVKEHGTHQQLLAQKGIYFSMVNIQAGTQN 1275
Cdd:TIGR00957 838 KISEMGSYQELLQRDGAFAEFLRTYAPDEQ 867
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
412-617 |
1.85e-28 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 118.28 E-value: 1.85e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 412 LNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRcLREIIgVVSQEPVLFS-TTIAENIRYG 490
Cdd:PRK11432 25 LNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQ-QRDIC-MVFQSYALFPhMSLGENVGYG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 491 RG--NVTMDEIEKAVKEANAydfimklpqkfdtLV-----GDRGA-QLSGGQKQRIAIARALVRNPKILLLDEATSALDt 562
Cdd:PRK11432 103 LKmlGVPKEERKQRVKEALE-------------LVdlagfEDRYVdQISGGQQQRVALARALILKPKVLLFDEPLSNLD- 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 338817954 563 eseAEVQAAL-DKARE-----GRTTIVIAHRLS-TIRNADVIAGFEDGVIVEQGSHSELMKK 617
Cdd:PRK11432 169 ---ANLRRSMrEKIRElqqqfNITSLYVTHDQSeAFAVSDTVIVMNKGKIMQIGSPQELYRQ 227
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
391-620 |
2.09e-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: 114.69 E-value: 2.09e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 391 LEFSDVHFSYPsraNIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNV-RCLREII 469
Cdd:COG0410 4 LEVENLHAGYG---GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPhRIARLGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 470 GVVSQEPVLFST-TIAENIRYGRGNVTMDEIEKAVKEAnAYDFIMKLPQKFDTlvgdRGAQLSGGQKQRIAIARALVRNP 548
Cdd:COG0410 81 GYVPEGRRIFPSlTVEENLLLGAYARRDRAEVRADLER-VYELFPRLKERRRQ----RAGTLSGGEQQMLAIGRALMSRP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 549 KILLLDEATSALdteseA-----EVQAALDKAREGRTTIVI----AHRLSTIrnADVIAGFEDGVIVEQGSHSELMKKEG 619
Cdd:COG0410 156 KLLLLDEPSLGL-----ApliveEIFEIIRRLNREGVTILLveqnARFALEI--ADRAYVLERGRIVLEGTAAELLADPE 228
|
.
gi 338817954 620 I 620
Cdd:COG0410 229 V 229
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
391-617 |
3.45e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 115.65 E-value: 3.45e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 391 LEFSDVHFSYPSRA--NIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDI----RNFNVRC 464
Cdd:PRK13646 3 IRFDNVSYTYQKGTpyEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIthktKDKYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 465 LREIIGVVSQ--EPVLFSTTIAENIRYGRGNVTMDeIEKAvkEANAYDFIMKLPQKFDTLvGDRGAQLSGGQKQRIAIAR 542
Cdd:PRK13646 83 VRKRIGMVFQfpESQLFEDTVEREIIFGPKNFKMN-LDEV--KNYAHRLLMDLGFSRDVM-SQSPFQMSGGQMRKIAIVS 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 338817954 543 ALVRNPKILLLDEATSALDTESEAEVQAALDKAR--EGRTTIVIAHRLSTI-RNADVIAGFEDGVIVEQGSHSELMKK 617
Cdd:PRK13646 159 ILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtdENKTIILVSHDMNEVaRYADEVIVMKEGSIVSQTSPKELFKD 236
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1036-1258 |
4.16e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 115.19 E-value: 4.16e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1036 VVFNYPTRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQWLRAQLGIVSQE 1115
Cdd:PRK13642 10 LVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIGMVFQN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1116 P--ILFDCSIAENIAYGDNSRVVPHDEIVRAAKEAnihpFIETLPQKYNTRvgdKGTQLSGGQKQRIAIARALIRQPRVL 1193
Cdd:PRK13642 90 PdnQFVGATVEDDVAFGMENQGIPREEMIKRVDEA----LLAVNMLDFKTR---EPARLSGGQKQRVAVAGIIALRPEII 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 338817954 1194 LLDEATSALD----TESEKVVQEALDKARegRTCIVIAHRLSTIQNADLIVVIENGKVKEHGTHQQLLA 1258
Cdd:PRK13642 163 ILDESTSMLDptgrQEIMRVIHEIKEKYQ--LTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFA 229
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
391-615 |
5.68e-28 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 114.30 E-value: 5.68e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 391 LEFSDVHFSYPSRaniKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIR------------ 458
Cdd:PRK10619 6 LNVIDLHKRYGEH---EVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlkva 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 459 -NFNVRCLREIIGVVSQEPVLFS-TTIAENIRygRGNVTMDEIEKAVKEANAYDFIMKLPQKfDTLVGDRGAQLSGGQKQ 536
Cdd:PRK10619 83 dKNQLRLLRTRLTMVFQHFNLWShMTVLENVM--EAPIQVLGLSKQEARERAVKYLAKVGID-ERAQGKYPVHLSGGQQQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 537 RIAIARALVRNPKILLLDEATSALDTESEAEVQAALDK-AREGRTTIVIAHRLSTIRNADVIAGF-EDGVIVEQGSHSEL 614
Cdd:PRK10619 160 RVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQlAEEGKTMVVVTHEMGFARHVSSHVIFlHQGKIEEEGAPEQL 239
|
.
gi 338817954 615 M 615
Cdd:PRK10619 240 F 240
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1048-1259 |
6.95e-28 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 116.74 E-value: 6.95e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1048 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQwlRAQLGIVSQEPILF-DCSIAEN 1126
Cdd:PRK11432 21 VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQ--QRDICMVFQSYALFpHMSLGEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1127 IAYGDNSRVVPHDEIVRAAKEA----NIHPFIEtlpqkyntRVGDkgtQLSGGQKQRIAIARALIRQPRVLLLDEATSAL 1202
Cdd:PRK11432 99 VGYGLKMLGVPKEERKQRVKEAlelvDLAGFED--------RYVD---QISGGQQQRVALARALILKPKVLLFDEPLSNL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 338817954 1203 DTESEKVVQEaldKARE-----GRTCIVIAHRLS-TIQNADLIVVIENGKVKEHGTHQQLLAQ 1259
Cdd:PRK11432 168 DANLRRSMRE---KIRElqqqfNITSLYVTHDQSeAFAVSDTVIVMNKGKIMQIGSPQELYRQ 227
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1046-1259 |
1.34e-27 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 119.02 E-value: 1.34e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1046 VPVLQGLSLEVKKGQTLALVGSSGCGKS----TVVQLLERFYDPMAGSVLLDGQEAKKLNVQWLRA----QLGIVSQEPI 1117
Cdd:COG4172 23 VEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERELRRirgnRIAMIFQEPM 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1118 -----LFdcSIAENIAygdnSRVVPHDEIVRAAKEANIhpfIETLpqkynTRVG--DKGT-------QLSGGQKQRIAIA 1183
Cdd:COG4172 103 tslnpLH--TIGKQIA----EVLRLHRGLSGAAARARA---LELL-----ERVGipDPERrldayphQLSGGQRQRVMIA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1184 RALIRQPRVLLLDEATSALDTesekVVQ-EALD-----KAREGRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHGTHQQL 1256
Cdd:COG4172 169 MALANEPDLLIADEPTTALDV----TVQaQILDllkdlQRELGMALLLITHDLGVVRRfADRVAVMRQGEIVEQGPTAEL 244
|
...
gi 338817954 1257 LAQ 1259
Cdd:COG4172 245 FAA 247
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
126-361 |
1.47e-27 |
|
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: 114.12 E-value: 1.47e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 126 VAAYIQVSFWTLAAGRQIKKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDDVSKISEGIGDKVGMFFQAIATFFAGFIV 205
Cdd:cd18576 51 VFSFFRIYLFARVGERVVADLRKDLYRHLQRLPLSFFHERRVGELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 206 GFIRGWKLTLVIMAISPILGLSTAVWAKILSTFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKELERYQKHLENAKK 285
Cdd:cd18576 131 LFFISWKLTLLMLATVPVVVLVAVLFGRRIRKLSKKVQDELAEANTIVEETLQGIRVVKAFTREDYEIERYRKALERVVK 210
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 338817954 286 IGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTIGNAMT-VFFSILIGAfSVGQAAPCIDAFANARGAA 361
Cdd:cd18576 211 LALKRARIRALFSSFIIFLLFGAIVAVLWYGGRLVLAGELTAGDLVAfLLYTLFIAG-SIGSLADLYGQLQKALGAS 286
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
391-606 |
1.47e-27 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 120.21 E-value: 1.47e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 391 LEFSDVHFSYPS-RANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCL---- 465
Cdd:PRK10535 5 LELKDIRRSYPSgEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALaqlr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 466 REIIGVVSQEPVLFSTTIAENirygrgNVTMDEI----EKAVKEANAYDFIMKLpqKFDTLVGDRGAQLSGGQKQRIAIA 541
Cdd:PRK10535 85 REHFGFIFQRYHLLSHLTAAQ------NVEVPAVyaglERKQRLLRAQELLQRL--GLEDRVEYQPSQLSGGQQQRVSIA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 338817954 542 RALVRNPKILLLDEATSALDTESEAEVQAALDKARE-GRTTIVIAHRLSTIRNADVIAGFEDGVIV 606
Cdd:PRK10535 157 RALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDrGHTVIIVTHDPQVAAQAERVIEIRDGEIV 222
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
391-609 |
1.52e-27 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 111.10 E-value: 1.52e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 391 LEFSDVHF---SYPSRANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLL--QRLYDPTEGKISIDGQDIRNFNVRCl 465
Cdd:cd03213 4 LSFRNLTVtvkSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGRPLDKRSFRK- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 466 reIIGVVSQEPVLFST-TIAENIrygrgnvtmdeiekavkeanayDFIMKLpqkfdtlvgdRGaqLSGGQKQRIAIARAL 544
Cdd:cd03213 83 --IIGYVPQDDILHPTlTVRETL----------------------MFAAKL----------RG--LSGGERKRVSIALEL 126
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 338817954 545 VRNPKILLLDEATSALDTESEAEVQAALDK-AREGRTTIVIAHRLSTirnaDVIAGFEDGVIVEQG 609
Cdd:cd03213 127 VSNPSLLFLDEPTSGLDSSSALQVMSLLRRlADTGRTIICSIHQPSS----EIFELFDKLLLLSQG 188
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
1052-1260 |
1.56e-27 |
|
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: 115.59 E-value: 1.56e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1052 LSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQ----EAKKLNVQWLRAQLGIVSQEPILF-DCSIAEN 1126
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRtlfdSRKGIFLPPEKRRIGYVFQEARLFpHLSVRGN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1127 IAYGdNSRVVPHDEIVRAAKEA---NIHPFIETLPQKyntrvgdkgtqLSGGQKQRIAIARALIRQPRVLLLDEATSALD 1203
Cdd:TIGR02142 96 LRYG-MKRARPSERRISFERVIellGIGHLLGRLPGR-----------LSGGEKQRVAIGRALLSSPRLLLMDEPLAALD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1204 TESEKVVQEALDKARE--GRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHGTHQQLLAQK 1260
Cdd:TIGR02142 164 DPRKYEILPYLERLHAefGIPILYVSHSLQEVLRlADRVVVLEDGRVAAAGPIAEVWASP 223
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
264-587 |
1.63e-27 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 119.14 E-value: 1.63e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 264 IAF-GGQNKELERYQKHLENAKKIgIKKAISANISMGiAFLLIYASYALAFWY--GSTLVISKEYTIGNAMTV--FFSIL 338
Cdd:COG4178 234 IALyRGEAAERRRLRRRFDAVIAN-WRRLIRRQRNLT-FFTTGYGQLAVIFPIlvAAPRYFAGEITLGGLMQAasAFGQV 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 339 IGAFSVgqaapCIDAFAN-ARGAAYVI-----FDIIDNNPKIDSFSERGHKPDNikGNLEFSDVHFSYPSRAniKILKGL 412
Cdd:COG4178 312 QGALSW-----FVDNYQSlAEWRATVDrlagfEEALEAADALPEAASRIETSED--GALALEDLTLRTPDGR--PLLEDL 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 413 NLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISI-DGQDIrnfnvrcLreiigVVSQEPVLFSTTIAENIRY-- 489
Cdd:COG4178 383 SLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpAGARV-------L-----FLPQRPYLPLGTLREALLYpa 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 490 GRGNVTMDEIEKAVKEANaydfIMKLPQKFDTlVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQ 569
Cdd:COG4178 451 TAEAFSDAELREALEAVG----LGHLAERLDE-EADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALY 525
|
330
....*....|....*...
gi 338817954 570 AALDKAREGRTTIVIAHR 587
Cdd:COG4178 526 QLLREELPGTTVISVGHR 543
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
391-617 |
1.77e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 113.96 E-value: 1.77e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 391 LEFSDVHFSYPSRANI--KILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDI----RNFNVRC 464
Cdd:PRK13634 3 ITFQKVEHRYQYKTPFerRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVItagkKNKKLKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 465 LREIIGVVSQ--EPVLFSTTIAENIRYGRGNVTMDEiEKAVKEANAYDFIMKLPQKfdtlVGDRGA-QLSGGQKQRIAIA 541
Cdd:PRK13634 83 LRKKVGIVFQfpEHQLFEETVEKDICFGPMNFGVSE-EDAKQKAREMIELVGLPEE----LLARSPfELSGGQMRRVAIA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 542 RALVRNPKILLLDEATSALDTESEAEVQ---AALDKaREGRTTIVIAHRLSTIRN-ADVIAGFEDGVIVEQGSHSELMKK 617
Cdd:PRK13634 158 GVLAMEPEVLVLDEPTAGLDPKGRKEMMemfYKLHK-EKGLTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTPREIFAD 236
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
391-614 |
1.80e-27 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 118.63 E-value: 1.80e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 391 LEFSDVHFSYPSRANIK-ILKGLNLKVKSGQTVALVGNSGCGKSTT----VQLLQRLYDPTEGKISIDGQDIRNFNVRCL 465
Cdd:COG4172 7 LSVEDLSVAFGQGGGTVeAVKGVSFDIAAGETLALVGESGSGKSVTalsiLRLLPDPAAHPSGSILFDGQDLLGLSEREL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 466 REI----IGVVSQEPV-----LFS--TTIAENIRYGRGnVTMDEIEKAVKEAnaydfimkLpqkfdTLVGDRGA------ 528
Cdd:COG4172 87 RRIrgnrIAMIFQEPMtslnpLHTigKQIAEVLRLHRG-LSGAAARARALEL--------L-----ERVGIPDPerrlda 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 529 ---QLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALD--KAREGRTTIVIAHRLSTIRN-ADVIAGFED 602
Cdd:COG4172 153 yphQLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKdlQRELGMALLLITHDLGVVRRfADRVAVMRQ 232
|
250
....*....|..
gi 338817954 603 GVIVEQGSHSEL 614
Cdd:COG4172 233 GEIVEQGPTAEL 244
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
409-600 |
1.82e-27 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 112.95 E-value: 1.82e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 409 LKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYD--PT---EGKISIDGQDIRNFNVRC--LREIIGVVSQEPVLFST 481
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDliPGfrvEGKVTFHGKNLYAPDVDPveVRRRIGMVFQKPNPFPK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 482 TIAENIRYG------RGNvtMDE-IEKAVKEANAYDFIM-KLPQKfdtlvgdrGAQLSGGQKQRIAIARALVRNPKILLL 553
Cdd:PRK14243 106 SIYDNIAYGaringyKGD--MDElVERSLRQAALWDEVKdKLKQS--------GLSLSGGQQQRLCIARAIAVQPEVILM 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 338817954 554 DEATSALDTESEAEVQAALDKAREGRTTIVIAHRL-STIRNADVIAGF 600
Cdd:PRK14243 176 DEPCSALDPISTLRIEELMHELKEQYTIIIVTHNMqQAARVSDMTAFF 223
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
1029-1263 |
2.13e-27 |
|
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: 113.03 E-value: 2.13e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1029 GSVTFNEVVFNYpTRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDpMAGSVLLDGQEAKKLNVQWLRAQ 1108
Cdd:cd03289 1 GQMTVKDLTAKY-TEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1109 LGIVSQEPILFDCSIAENI-AYGDNSrvvpHDEIVRAAKEANIHPFIETLPQKYNTRVGDKGTQLSGGQKQRIAIARALI 1187
Cdd:cd03289 79 FGVIPQKVFIFSGTFRKNLdPYGKWS----DEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 338817954 1188 RQPRVLLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIENGKVKEHGTHQQLLAQKGIY 1263
Cdd:cd03289 155 SKAKILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHF 230
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1045-1258 |
2.25e-27 |
|
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: 112.00 E-value: 2.25e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1045 NVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVqWLRAQLGI--VSQEPILF-DC 1121
Cdd:COG0410 15 GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPP-HRIARLGIgyVPEGRRIFpSL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1122 SIAENIAYGdnSRVVPHDEIVRAAKEA--NIHPFIETlpqkyntRVGDKGTQLSGGQKQRIAIARALIRQPRVLLLDEAT 1199
Cdd:COG0410 94 TVEENLLLG--AYARRDRAEVRADLERvyELFPRLKE-------RRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPS 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 338817954 1200 SALdteSEKVVQEALDK----AREGRTCIVI---AHRLSTIqnADLIVVIENGKVKEHGTHQQLLA 1258
Cdd:COG0410 165 LGL---APLIVEEIFEIirrlNREGVTILLVeqnARFALEI--ADRAYVLERGRIVLEGTAAELLA 225
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
1049-1230 |
2.96e-27 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 112.57 E-value: 2.96e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1049 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMA-----GSVLLDGQE--AKKLNVQWLRAQLGIVSQEPILFDC 1121
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLIPgfrveGKVTFHGKNlyAPDVDPVEVRRRIGMVFQKPNPFPK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1122 SIAENIAYGD--NSRVVPHDEIV-RAAKEAnihpfieTLPQKYNTRVGDKGTQLSGGQKQRIAIARALIRQPRVLLLDEA 1198
Cdd:PRK14243 106 SIYDNIAYGAriNGYKGDMDELVeRSLRQA-------ALWDEVKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEP 178
|
170 180 190
....*....|....*....|....*....|..
gi 338817954 1199 TSALDTESEKVVQEALDKAREGRTCIVIAHRL 1230
Cdd:PRK14243 179 CSALDPISTLRIEELMHELKEQYTIIIVTHNM 210
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
405-614 |
3.31e-27 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 111.93 E-value: 3.31e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 405 NIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYD-----PTEGKISIDGQDIRNFNVRCLREIIGVVSQEPVLF 479
Cdd:PRK14247 15 QVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDIFKMDVIELRRRVQMVFQIPNPI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 480 ST-TIAENIRYG----RGNVTMDEIEKAVKEAnaydfiMKLPQKFDTlVGDR----GAQLSGGQKQRIAIARALVRNPKI 550
Cdd:PRK14247 95 PNlSIFENVALGlklnRLVKSKKELQERVRWA------LEKAQLWDE-VKDRldapAGKLSGGQQQRLCIARALAFQPEV 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 338817954 551 LLLDEATSALDTESEAEVQAALDKAREGRTTIVIAH-RLSTIRNADVIAGFEDGVIVEQGSHSEL 614
Cdd:PRK14247 168 LLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHfPQQAARISDYVAFLYKGQIVEWGPTREV 232
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
390-612 |
3.76e-27 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 111.64 E-value: 3.76e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 390 NLEFSDVHFSYpsrANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIrNFN-------V 462
Cdd:COG4161 2 SIQLKNINCFY---GSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQF-DFSqkpsekaI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 463 RCLREIIGVVSQE----PVLfstTIAENIRYGRGNVTMDEIEKAVKEANAYDFIMKLPQKFDTLvgdrGAQLSGGQKQRI 538
Cdd:COG4161 78 RLLRQKVGMVFQQynlwPHL---TVMENLIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRF----PLHLSGGQQQRV 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 338817954 539 AIARALVRNPKILLLDEATSALDTESEAE-VQAALDKAREGRTTIVIAHRLSTIRN-ADVIAGFEDGVIVEQGSHS 612
Cdd:COG4161 151 AIARALMMEPQVLLFDEPTAALDPEITAQvVEIIRELSQTGITQVIVTHEVEFARKvASQVVYMEKGRIIEQGDAS 226
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
404-618 |
3.79e-27 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 112.03 E-value: 3.79e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 404 ANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLREIIGVVSQEPVL-FSTT 482
Cdd:PRK11231 13 GTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHHLTpEGIT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 483 IAENIRYGR-------GNVTMDEiEKAVKEAnaydfiMKLPQkFDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDE 555
Cdd:PRK11231 93 VRELVAYGRspwlslwGRLSAED-NARVNQA------MEQTR-INHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 338817954 556 ATSALDTESEAEVQAALDKAR-EGRTTIVIAHRLS-TIRNADVIAGFEDGVIVEQGSHSELMKKE 618
Cdd:PRK11231 165 PTTYLDINHQVELMRLMRELNtQGKTVVTVLHDLNqASRYCDHLVVLANGHVMAQGTPEEVMTPG 229
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1031-1252 |
4.45e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 112.59 E-value: 4.45e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1031 VTFNEVVFNYPTrANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGS---VLLDGQEAKKLNVQWLRA 1107
Cdd:PRK13640 6 VEFKHVSFTYPD-SKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnskITVDGITLTAKTVWDIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1108 QLGIVSQEP--ILFDCSIAENIAYGDNSRVVPHDEIVR----AAKEANIHPFIETLPQkyntrvgdkgtQLSGGQKQRIA 1181
Cdd:PRK13640 85 KVGIVFQNPdnQFVGATVGDDVAFGLENRAVPRPEMIKivrdVLADVGMLDYIDSEPA-----------NLSGGQKQRVA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 338817954 1182 IARALIRQPRVLLLDEATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTIQNADLIVVIENGKVKEHGT 1252
Cdd:PRK13640 154 IAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKknNLTVISITHDIDEANMADQVLVLDDGKLLAQGS 226
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1032-1228 |
5.68e-27 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 111.49 E-value: 5.68e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1032 TFNEVVFNYP-TRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEakklnVQWLRAQLG 1110
Cdd:COG4525 5 TVRHVSVRYPgGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVP-----VTGPGADRG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1111 IVSQEPILFD-CSIAENIAYGDNSRVVPHDEIVRAAKEanihpfietlpqkYNTRVGDKGT------QLSGGQKQRIAIA 1183
Cdd:COG4525 80 VVFQKDALLPwLNVLDNVAFGLRLRGVPKAERRARAEE-------------LLALVGLADFarrriwQLSGGMRQRVGIA 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 338817954 1184 RALIRQPRVLLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAH 1228
Cdd:COG4525 147 RALAADPRFLLMDEPFGALDALTREQMQELLLDvwQRTGKGVFLITH 193
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
395-620 |
9.03e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 111.33 E-value: 9.03e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 395 DVHFSYPSRANIK---ILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNF-NVRCLREIIG 470
Cdd:PRK13633 9 NVSYKYESNEESTeklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEeNLWDIRNKAG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 471 VVSQEP--VLFSTTIAENIRYGRGN--VTMDEIEKAVKEA----NAYDFIMKLPQkfdtlvgdrgaQLSGGQKQRIAIAR 542
Cdd:PRK13633 89 MVFQNPdnQIVATIVEEDVAFGPENlgIPPEEIRERVDESlkkvGMYEYRRHAPH-----------LLSGGQKQRVAIAG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 543 ALVRNPKILLLDEATSALDTESEAEVQAALDK--AREGRTTIVIAHRLSTIRNADVIAGFEDGVIVEQG------SHSEL 614
Cdd:PRK13633 158 ILAMRPECIIFDEPTAMLDPSGRREVVNTIKElnKKYGITIILITHYMEEAVEADRIIVMDSGKVVMEGtpkeifKEVEM 237
|
....*.
gi 338817954 615 MKKEGI 620
Cdd:PRK13633 238 MKKIGL 243
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
1049-1259 |
9.81e-27 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 113.27 E-value: 9.81e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1049 LQGLSLEVK-----KGQTlALVGSSGCGKSTVVQL---LERfydPMAGSVLLDGQ----EAKKLNVQWLRAQLGIVSQEP 1116
Cdd:COG4148 11 RGGFTLDVDftlpgRGVT-ALFGPSGSGKTTLLRAiagLER---PDSGRIRLGGEvlqdSARGIFLPPHRRRIGYVFQEA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1117 ILFD-CSIAENIAYG-----DNSRVVPHDEIVRAakeANIHPFIETLPQkyntrvgdkgtQLSGGQKQRIAIARALIRQP 1190
Cdd:COG4148 87 RLFPhLSVRGNLLYGrkrapRAERRISFDEVVEL---LGIGHLLDRRPA-----------TLSGGERQRVAIGRALLSSP 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 338817954 1191 RVLLLDEATSALDTESeKvvQEALDK----AREGRTCIV-IAHRLSTIQN-ADLIVVIENGKVKEHGTHQQLLAQ 1259
Cdd:COG4148 153 RLLLMDEPLAALDLAR-K--AEILPYlerlRDELDIPILyVSHSLDEVARlADHVVLLEQGRVVASGPLAEVLSR 224
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1044-1259 |
1.05e-26 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 112.37 E-value: 1.05e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1044 ANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLN---VQWLRAQLGIVSQEPilfd 1120
Cdd:PRK11308 26 RLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADpeaQKLLRQKIQIVFQNP---- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1121 csiaeniaYGD-NSR----------VVPHDEIVRAAKEANIHPFIEtlpqkyntRVGDKGTQ-------LSGGQKQRIAI 1182
Cdd:PRK11308 102 --------YGSlNPRkkvgqileepLLINTSLSAAERREKALAMMA--------KVGLRPEHydryphmFSGGQRQRIAI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1183 ARALIRQPRVLLLDEATSALDTESE-KVVQEALDKAREGRTCIV-IAHRLSTIQN-ADLIVVIENGKVKEHGTHQQLLAQ 1259
Cdd:PRK11308 166 ARALMLDPDVVVADEPVSALDVSVQaQVLNLMMDLQQELGLSYVfISHDLSVVEHiADEVMVMYLGRCVEKGTKEQIFNN 245
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
405-609 |
1.10e-26 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 108.84 E-value: 1.10e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 405 NIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNfNVRCLREIiGVVSQEPVLFST-TI 483
Cdd:cd03268 12 KKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQK-NIEALRRI-GALIEAPGFYPNlTA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 484 AENIR-----YGRGNVTMDEIEKAVKEANAYDfimklpqkfdtlvgDRGAQLSGGQKQRIAIARALVRNPKILLLDEATS 558
Cdd:cd03268 90 RENLRllarlLGIRKKRIDEVLDVVGLKDSAK--------------KKVKGFSLGMKQRLGIALALLGNPDLLILDEPTN 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 338817954 559 ALDTESEAEVQAAL-DKAREGRTTIVIAHRLSTIRN-ADVIAGFEDGVIVEQG 609
Cdd:cd03268 156 GLDPDGIKELRELIlSLRDQGITVLISSHLLSEIQKvADRIGIINKGKLIEEG 208
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1035-1260 |
1.29e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 111.09 E-value: 1.29e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1035 EVVFNYP--TRAnvpvLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQ--EAKKLNVQWLRAQLG 1110
Cdd:PRK13636 10 ELNYNYSdgTHA----LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpiDYSRKGLMKLRESVG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1111 IVSQEP--ILFDCSIAENIAYGDNSRVVPHDEIVRAAKEANIHPFIETLPqkyntrvgDKGTQ-LSGGQKQRIAIARALI 1187
Cdd:PRK13636 86 MVFQDPdnQLFSASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLK--------DKPTHcLSFGQKKRVAIAGVLV 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 338817954 1188 RQPRVLLLDEATSALD----TESEKVVQEALDKAreGRTCIVIAHRLSTIQ-NADLIVVIENGKVKEHGTHQQLLAQK 1260
Cdd:PRK13636 158 MEPKVLVLDEPTAGLDpmgvSEIMKLLVEMQKEL--GLTIIIATHDIDIVPlYCDNVFVMKEGRVILQGNPKEVFAEK 233
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1047-1245 |
1.66e-26 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 116.06 E-value: 1.66e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1047 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLL-----------ERfydPMAGSVLLdgqeakklnvqwlraqlgiVSQE 1115
Cdd:COG4178 377 PLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIaglwpygsgriAR---PAGARVLF-------------------LPQR 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1116 PILFDCSIAENIAYGDNSRVVPHDEIVRAAKEANIHPFIETLpqkynTRVGDKGTQLSGGQKQRIAIARALIRQPRVLLL 1195
Cdd:COG4178 435 PYLPLGTLREALLYPATAEAFSDAELREALEAVGLGHLAERL-----DEEADWDQVLSLGEQQRLAFARLLLHKPDWLFL 509
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 338817954 1196 DEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIENG 1245
Cdd:COG4178 510 DEATSALDEENEAALYQLLREELPGTTVISVGHRSTLAAFHDRVLELTGD 559
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
391-616 |
1.72e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 111.07 E-value: 1.72e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 391 LEFSDVHFSYP--SRANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIR----NFNVRC 464
Cdd:PRK13641 3 IKFENVDYIYSpgTPMEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgNKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 465 LREIIGVVSQ--EPVLFSTTIAENIRYGRGNVTMDEIEKAVKeanAYDFIMKLPQKfDTLVGDRGAQLSGGQKQRIAIAR 542
Cdd:PRK13641 83 LRKKVSLVFQfpEAQLFENTVLKDVEFGPKNFGFSEDEAKEK---ALKWLKKVGLS-EDLISKSPFELSGGQMRRVAIAG 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 338817954 543 ALVRNPKILLLDEATSALDTESEAEV-QAALDKAREGRTTIVIAHrlstirNADVIAGFEDGVIVEQgsHSELMK 616
Cdd:PRK13641 159 VMAYEPEILCLDEPAAGLDPEGRKEMmQLFKDYQKAGHTVILVTH------NMDDVAEYADDVLVLE--HGKLIK 225
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
391-617 |
2.50e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 110.22 E-value: 2.50e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 391 LEFSDVHFSYPS------RAnikiLKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIR----NF 460
Cdd:PRK13649 3 INLQNVSYTYQAgtpfegRA----LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITstskNK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 461 NVRCLREIIGVVSQ--EPVLFSTTIAENIRYGRGN--VTMDEIEKAVKEanaydfimKLpqkfdTLVG------DRGA-Q 529
Cdd:PRK13649 79 DIKQIRKKVGLVFQfpESQLFEETVLKDVAFGPQNfgVSQEEAEALARE--------KL-----ALVGiseslfEKNPfE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 530 LSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIV-IAHRLSTIRN-ADVIAGFEDGVIVE 607
Cdd:PRK13649 146 LSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVlVTHLMDDVANyADFVYVLEKGKLVL 225
|
250
....*....|
gi 338817954 608 QGSHSELMKK 617
Cdd:PRK13649 226 SGKPKDIFQD 235
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1047-1265 |
3.07e-26 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 112.24 E-value: 3.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1047 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKklNVQWLRAQLGIVSQEPILF-DCSIAE 1125
Cdd:PRK11607 33 HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLS--HVPPYQRPINMMFQSYALFpHMTVEQ 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1126 NIAYGDNSRVVPHDEIVRAAKE--ANIHpfietlPQKYNTRvgdKGTQLSGGQKQRIAIARALIRQPRVLLLDEATSALD 1203
Cdd:PRK11607 111 NIAFGLKQDKLPKAEIASRVNEmlGLVH------MQEFAKR---KPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALD 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 338817954 1204 TESEKVVQ-EALD-KAREGRTCIVIAH-RLSTIQNADLIVVIENGKVKEHGTHQQLLAQKGIYFS 1265
Cdd:PRK11607 182 KKLRDRMQlEVVDiLERVGVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYS 246
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1049-1252 |
3.08e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 110.14 E-value: 3.08e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1049 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQE--AKKLNVQWLRAQLGIVSQEP--ILFDCSIA 1124
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDitDKKVKLSDIRKKVGLVFQYPeyQLFEETIE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1125 ENIAYGDNSRVVPHDEIVRAAKEAnihpfIETLPQKYNTrVGDKGT-QLSGGQKQRIAIARALIRQPRVLLLDEATSALD 1203
Cdd:PRK13637 103 KDIAFGPINLGLSEEEIENRVKRA-----MNIVGLDYED-YKDKSPfELSGGQKRRVAIAGVVAMEPKILILDEPTAGLD 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 338817954 1204 TeseKVVQEALDKARE-----GRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHGT 1252
Cdd:PRK13637 177 P---KGRDEILNKIKElhkeyNMTIILVSHSMEDVAKlADRIIVMNKGKCELQGT 228
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
391-623 |
3.60e-26 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 110.82 E-value: 3.60e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 391 LEFSDVHFSYPSR-------ANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFN-- 461
Cdd:PRK11308 6 LQAIDLKKHYPVKrglfkpeRLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADpe 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 462 -VRCLREIIGVVSQ-----------------EPVLFSTTIAENIRYGRGNVTMDEIEKAVKEANAYdfimklPQKFdtlv 523
Cdd:PRK11308 86 aQKLLRQKIQIVFQnpygslnprkkvgqileEPLLINTSLSAAERREKALAMMAKVGLRPEHYDRY------PHMF---- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 524 gdrgaqlSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAAL-DKAREGRTTIV-IAHRLSTIRN-ADVIAGF 600
Cdd:PRK11308 156 -------SGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMmDLQQELGLSYVfISHDLSVVEHiADEVMVM 228
|
250 260
....*....|....*....|...
gi 338817954 601 EDGVIVEQGShselmkKEGIYFR 623
Cdd:PRK11308 229 YLGRCVEKGT------KEQIFNN 245
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
1049-1245 |
4.55e-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: 107.94 E-value: 4.55e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1049 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQWLraqlgIVSQEPILFD-CSIAENI 1127
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM-----VVFQNYSLLPwLTVRENI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1128 AYGDNsRVVPHdeIVRAAKEANIHPFIETLPQkynTRVGDKG-TQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTES 1206
Cdd:TIGR01184 76 ALAVD-RVLPD--LSKSERRAIVEEHIALVGL---TEAADKRpGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALT 149
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 338817954 1207 EKVVQEALDKARE--GRTCIVIAHRL-STIQNADLIVVIENG 1245
Cdd:TIGR01184 150 RGNLQEELMQIWEehRVTVLMVTHDVdEALLLSDRVVMLTNG 191
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
391-612 |
4.92e-26 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 108.18 E-value: 4.92e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 391 LEFSDVHFSYPSRaniKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQdirNFN--------- 461
Cdd:PRK11124 3 IQLNGINCFYGAH---QALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGN---HFDfsktpsdka 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 462 VRCLREIIGVVSQEPVLFS-TTIAENIRYGRGNVT-MDEiEKAVKEAnaydfiMKLPQKFD-TLVGDR-GAQLSGGQKQR 537
Cdd:PRK11124 77 IRELRRNVGMVFQQYNLWPhLTVQQNLIEAPCRVLgLSK-DQALARA------EKLLERLRlKPYADRfPLHLSGGQQQR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 338817954 538 IAIARALVRNPKILLLDEATSALDTESEAEVQAALDKARE-GRTTIVIAHRLSTIRN-ADVIAGFEDGVIVEQGSHS 612
Cdd:PRK11124 150 VAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAEtGITQVIVTHEVEVARKtASRVVYMENGHIVEQGDAS 226
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
1040-1256 |
4.94e-26 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 107.59 E-value: 4.94e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1040 YPTRANvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKlNVQWLRAQLGIVSQEPILF 1119
Cdd:cd03263 10 YKKGTK-PAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLGYCPQFDALF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1120 D-CSIAENIAYgdNSRV--VPHDEIvraakEANIHPFIET--LPQKYNTRVGDkgtqLSGGQKQRIAIARALIRQPRVLL 1194
Cdd:cd03263 88 DeLTVREHLRF--YARLkgLPKSEI-----KEEVELLLRVlgLTDKANKRART----LSGGMKRKLSLAIALIGGPSVLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 338817954 1195 LDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHGTHQQL 1256
Cdd:cd03263 157 LDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEAlCDRIAIMSDGKLRCIGSPQEL 219
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
391-614 |
5.64e-26 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 110.57 E-value: 5.64e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 391 LEFSD--VHFSYPSR--------ANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNF 460
Cdd:PRK15079 9 LEVADlkVHFDIKDGkqwfwqppKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGM 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 461 NVRCLREI---IGVVSQEPvLFSTT--------IAENIRYGRGNVTMDEIEKAVKEanaydFIMK---LPQkfdtLVGDR 526
Cdd:PRK15079 89 KDDEWRAVrsdIQMIFQDP-LASLNprmtigeiIAEPLRTYHPKLSRQEVKDRVKA-----MMLKvglLPN----LINRY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 527 GAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDK-ARE-GRTTIVIAHRLSTIRN-ADVIAGFEDG 603
Cdd:PRK15079 159 PHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQlQREmGLSLIFIAHDLAVVKHiSDRVLVMYLG 238
|
250
....*....|.
gi 338817954 604 VIVEQGSHSEL 614
Cdd:PRK15079 239 HAVELGTYDEV 249
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
391-609 |
7.12e-26 |
|
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: 106.81 E-value: 7.12e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 391 LEFSDVHFSYpSRANIKilkgLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRclREIIG 470
Cdd:cd03298 1 VRLDKIRFSY-GEQPMH----FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA--DRPVS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 471 VVSQEPVLFS-TTIAENIRYGRG------NVTMDEIEKAVKEANAYDFIMKLPQkfdtlvgdrgaQLSGGQKQRIAIARA 543
Cdd:cd03298 74 MLFQENNLFAhLTVEQNVGLGLSpglkltAEDRQAIEVALARVGLAGLEKRLPG-----------ELSGGERQRVALARV 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 338817954 544 LVRNPKILLLDEATSALDTESEAEVQAALDK--AREGRTTIVIAHRLSTIRN-ADVIAGFEDGVIVEQG 609
Cdd:cd03298 143 LVRDKPVLLLDEPFAALDPALRAEMLDLVLDlhAETKMTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
1044-1245 |
7.23e-26 |
|
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: 107.03 E-value: 7.23e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1044 ANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVL----LDGQEAKKLNVQWLRAQLGIVSQEPILF 1119
Cdd:cd03290 12 SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHwsnkNESEPSFEATRSRNRYSVAYAAQKPWLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1120 DCSIAENIAYGDNSRVVPHDEIVRAAkeaNIHPFIETLPQKYNTRVGDKGTQLSGGQKQRIAIARALIRQPRVLLLDEAT 1199
Cdd:cd03290 92 NATVEENITFGSPFNKQRYKAVTDAC---SLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPF 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 338817954 1200 SALDTE-SEKVVQEALDK--AREGRTCIVIAHRLSTIQNADLIVVIENG 1245
Cdd:cd03290 169 SALDIHlSDHLMQEGILKflQDDKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1030-1233 |
7.80e-26 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 108.20 E-value: 7.80e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1030 SVTFNEVVFNYPTRAnvpVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDpMAGSVLLDGQ--------EAKKLN 1101
Cdd:PRK14258 7 AIKVNNLSFYYDTQK---ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNE-LESEVRVEGRveffnqniYERRVN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1102 VQWLRAQLGIVSQEPILFDCSIAENIAYGDN----SRVVPHDEIVRAA-KEANihpfietLPQKYNTRVGDKGTQLSGGQ 1176
Cdd:PRK14258 83 LNRLRRQVSMVHPKPNLFPMSVYDNVAYGVKivgwRPKLEIDDIVESAlKDAD-------LWDEIKHKIHKSALDLSGGQ 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 338817954 1177 KQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEALD--KAREGRTCIVIAHRLSTI 1233
Cdd:PRK14258 156 QQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQslRLRSELTMVIVSHNLHQV 214
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1042-1257 |
8.10e-26 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 111.47 E-value: 8.10e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1042 TRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQWLRAQLGIVSQEPIL-FD 1120
Cdd:PRK09536 12 EFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLsFE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1121 CSIAENIAYGDN---SRVVPHDEIVRAAKEanihpfiETLPQKYNTRVGDKG-TQLSGGQKQRIAIARALIRQPRVLLLD 1196
Cdd:PRK09536 92 FDVRQVVEMGRTphrSRFDTWTETDRAAVE-------RAMERTGVAQFADRPvTSLSGGERQRVLLARALAQATPVLLLD 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 338817954 1197 EATSALDTESE----KVVQEALDkarEGRTCIVIAHRLS-TIQNADLIVVIENGKVKEHGTHQQLL 1257
Cdd:PRK09536 165 EPTASLDINHQvrtlELVRRLVD---DGKTAVAAIHDLDlAARYCDELVLLADGRVRAAGPPADVL 227
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1048-1258 |
8.26e-26 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 107.91 E-value: 8.26e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1048 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSV-----LLDGQE---AKKLNVQWLRAQLGIVSQEPILF 1119
Cdd:PRK11264 18 VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIrvgdiTIDTARslsQQKGLIRQLRQHVGFVFQNFNLF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1120 DC-SIAENIAYGdnSRVV---PHDEIVRAAKEanihpfietlpqkYNTRVGDKGTQ------LSGGQKQRIAIARALIRQ 1189
Cdd:PRK11264 98 PHrTVLENIIEG--PVIVkgePKEEATARARE-------------LLAKVGLAGKEtsyprrLSGGQQQRVAIARALAMR 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 338817954 1190 PRVLLLDEATSALDTEsekVVQEALDK----AREGRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHGTHQQLLA 1258
Cdd:PRK11264 163 PEVILFDEPTSALDPE---LVGEVLNTirqlAQEKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKALFA 233
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1034-1260 |
8.36e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 108.63 E-value: 8.36e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1034 NEVVFNYPTraNVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQWL--RAQLGI 1111
Cdd:PRK13639 5 RDLKYSYPD--GTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLevRKTVGI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1112 VSQEP--ILFDCSIAENIAYGDNSRVVPHDEIVRAAKEA----NIHPFIETLPQkyntrvgdkgtQLSGGQKQRIAIARA 1185
Cdd:PRK13639 83 VFQNPddQLFAPTVEEDVAFGPLNLGLSKEEVEKRVKEAlkavGMEGFENKPPH-----------HLSGGQKKRVAIAGI 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 338817954 1186 LIRQPRVLLLDEATSALDTE-SEKVVQEALDKAREGRTCIVIAHRLSTIQ-NADLIVVIENGKVKEHGTHQQLLAQK 1260
Cdd:PRK13639 152 LAMKPEIIVLDEPTSGLDPMgASQIMKLLYDLNKEGITIIISTHDVDLVPvYADKVYVMSDGKIIKEGTPKEVFSDI 228
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
391-609 |
8.76e-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: 106.51 E-value: 8.76e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 391 LEFSDVHFSYPSRaniKILKGLNLKVKSGQTvALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNfNVRCLREIIG 470
Cdd:cd03264 1 LQLENLTKRYGKK---RALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLRRRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 471 VVSQEPVLFST-TIAENIRY-GRGNVTMD-----EIEKAVKEANAYDFimklpqkfdtlVGDRGAQLSGGQKQRIAIARA 543
Cdd:cd03264 76 YLPQEFGVYPNfTVREFLDYiAWLKGIPSkevkaRVDEVLELVNLGDR-----------AKKKIGSLSGGMRRRVGIAQA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 338817954 544 LVRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTIRN-ADVIAGFEDGVIVEQG 609
Cdd:cd03264 145 LVGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1031-1259 |
8.92e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 108.64 E-value: 8.92e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1031 VTFNEVVFNY---PTRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQW-LR 1106
Cdd:PRK13633 5 IKCKNVSYKYesnEESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLWdIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1107 AQLGIVSQEPilfDCSIA-----ENIAYGDNSRVVPHDEIVR----AAKEANIHPFIETLPQkyntrvgdkgtQLSGGQK 1177
Cdd:PRK13633 85 NKAGMVFQNP---DNQIVativeEDVAFGPENLGIPPEEIRErvdeSLKKVGMYEYRRHAPH-----------LLSGGQK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1178 QRIAIARALIRQPRVLLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLSTIQNADLIVVIENGKVKEHGTHQQ 1255
Cdd:PRK13633 151 QRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKElnKKYGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKE 230
|
....
gi 338817954 1256 LLAQ 1259
Cdd:PRK13633 231 IFKE 234
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
391-618 |
9.42e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 108.35 E-value: 9.42e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 391 LEFSDVHFSYpsRANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLREIIG 470
Cdd:PRK13652 4 IETRDLCYSY--SGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 471 VVSQEP--VLFSTTIAENIRYGRGNVTMDE------IEKAVKEANAYDFIMKLPQkfdtlvgdrgaQLSGGQKQRIAIAR 542
Cdd:PRK13652 82 LVFQNPddQIFSPTVEQDIAFGPINLGLDEetvahrVSSALHMLGLEELRDRVPH-----------HLSGGEKKRVAIAG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 338817954 543 ALVRNPKILLLDEATSALDTESEAEVQAALDKARE--GRTTIVIAHRLSTIRN-ADVIAGFEDGVIVEQGSHSELMKKE 618
Cdd:PRK13652 151 VIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPEtyGMTVIFSTHQLDLVPEmADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
391-606 |
9.73e-26 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 107.14 E-value: 9.73e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 391 LEFSDVHFSYpsrANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRclrEI-- 468
Cdd:cd03219 1 LEVRGLTKRF---GGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPH---EIar 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 469 --IGVVSQEPVLFST-TIAENIRYG-----RGNVTMDEIEKAVKEANAYDF----IMKLPQKFDTLVGDrgaqLSGGQKQ 536
Cdd:cd03219 75 lgIGRTFQIPRLFPElTVLENVMVAaqartGSGLLLARARREEREARERAEelleRVGLADLADRPAGE----LSYGQQR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 338817954 537 RIAIARALVRNPKILLLDEATSALdteSEAEVQAALDK----AREGRTTIVIAHRLstirnaDVIAGFEDGVIV 606
Cdd:cd03219 151 RLEIARALATDPKLLLLDEPAAGL---NPEETEELAELirelRERGITVLLVEHDM------DVVMSLADRVTV 215
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
1048-1251 |
1.04e-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: 106.12 E-value: 1.04e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1048 VLQGLSLEVKKGQTlALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKlNVQWLRAQLGIVSQEPILFD-CSIAEN 1126
Cdd:cd03264 15 ALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLRRRIGYLPQEFGVYPnFTVREF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1127 IAY-----GDNSRVVPHdEIVRAAKEANIHPFietlpqkYNTRVGdkgtQLSGGQKQRIAIARALIRQPRVLLLDEATSA 1201
Cdd:cd03264 93 LDYiawlkGIPSKEVKA-RVDEVLELVNLGDR-------AKKKIG----SLSGGMRRRVGIAQALVGDPSILIVDEPTAG 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 338817954 1202 LDTESEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHG 1251
Cdd:cd03264 161 LDPEERIRFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
390-561 |
1.50e-25 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 109.93 E-value: 1.50e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 390 NLEFSDVHFSYPsrANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDI-------RNfnv 462
Cdd:PRK11650 3 GLKLQAVRKSYD--GKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVnelepadRD--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 463 rclreiIGVVSQEPVLFS-TTIAENIRYG---RGnVTMDEIEKAVKEANAydfIMKLpqkfDTLVGDRGAQLSGGQKQRI 538
Cdd:PRK11650 78 ------IAMVFQNYALYPhMSVRENMAYGlkiRG-MPKAEIEERVAEAAR---ILEL----EPLLDRKPRELSGGQRQRV 143
|
170 180
....*....|....*....|...
gi 338817954 539 AIARALVRNPKILLLDEATSALD 561
Cdd:PRK11650 144 AMGRAIVREPAVFLFDEPLSNLD 166
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
1043-1260 |
1.61e-25 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 107.58 E-value: 1.61e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1043 RANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQWLRA---QLGIVSQepilf 1119
Cdd:TIGR02769 21 KQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQRRAfrrDVQLVFQ----- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1120 DC--------SIAENIA-----YGDNSRVVPHDEIVRAAKEANIHPFI-ETLPQkyntrvgdkgtQLSGGQKQRIAIARA 1185
Cdd:TIGR02769 96 DSpsavnprmTVRQIIGeplrhLTSLDESEQKARIAELLDMVGLRSEDaDKLPR-----------QLSGGQLQRINIARA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 338817954 1186 LIRQPRVLLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHGTHQQLLAQK 1260
Cdd:TIGR02769 165 LAVKPKLIVLDEAVSNLDMVLQAVILELLRKlqQAFGTAYLFITHDLRLVQSfCQRVAVMDKGQIVEECDVAQLLSFK 242
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
391-588 |
1.90e-25 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 112.04 E-value: 1.90e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 391 LEFSDVHFSYPS-RANikilKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQ--DIRNFNVrCLRE 467
Cdd:COG3845 6 LELRGITKRFGGvVAN----DDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKpvRIRSPRD-AIAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 468 IIGVVSQEPVLFST-TIAENIRYGR-----GNVTMDEIEKAVKE-ANAYDFIMKLpqkfDTLVGDrgaqLSGGQKQRIAI 540
Cdd:COG3845 81 GIGMVHQHFMLVPNlTVAENIVLGLeptkgGRLDRKAARARIRElSERYGLDVDP----DAKVED----LSVGEQQRVEI 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 338817954 541 ARALVRNPKILLLDEATSALdTESEA-EVQAALDK-AREGRTTIVIAHRL 588
Cdd:COG3845 153 LKALYRGARILILDEPTAVL-TPQEAdELFEILRRlAAEGKSIIFITHKL 201
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
423-615 |
1.94e-25 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 109.42 E-value: 1.94e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 423 ALVGNSGCGKSTTVQLLQRLYDPTEGKISIDG---QDI-RNFNVRCLREIIGVVSQEPVLFST-TIAENIRYGRgnvtmd 497
Cdd:COG4148 29 ALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGevlQDSaRGIFLPPHRRRIGYVFQEARLFPHlSVRGNLLYGR------ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 498 eieKAVKEANAydfimklPQKFDTLVG--------DRG-AQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEV 568
Cdd:COG4148 103 ---KRAPRAER-------RISFDEVVEllgighllDRRpATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEI 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 338817954 569 QAALDK-AREGRTTIV-IAHRLSTI-RNADVIAGFEDGVIVEQGSHSELM 615
Cdd:COG4148 173 LPYLERlRDELDIPILyVSHSLDEVaRLADHVVLLEQGRVVASGPLAEVL 222
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1043-1257 |
2.12e-25 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 106.78 E-value: 2.12e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1043 RANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQWLRAQLGIVSQEPIL-FDC 1121
Cdd:PRK13548 12 LGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQHSSLsFPF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1122 SIAENIAYGdnsrVVPHDEIVRAAKEanihpfietLPQKYNTRVGDKG------TQLSGGQKQRIAIARALIR------Q 1189
Cdd:PRK13548 92 TVEEVVAMG----RAPHGLSRAEDDA---------LVAAALAQVDLAHlagrdyPQLSGGEQQRVQLARVLAQlwepdgP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 338817954 1190 PRVLLLDEATSALD-TESEKVVQEALDKARE-GRTCIVIAHRLS-TIQNADLIVVIENGKVKEHGTHQQLL 1257
Cdd:PRK13548 159 PRWLLLDEPTSALDlAHQHHVLRLARQLAHErGLAVIVVLHDLNlAARYADRIVLLHQGRLVADGTPAEVL 229
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1046-1249 |
2.62e-25 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 105.98 E-value: 2.62e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1046 VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQL---LERfydPMAGSVLLDGQEAKKLN----VQWLRAQLGIVSQE--- 1115
Cdd:COG4181 25 LTILKGISLEVEAGESVAIVGASGSGKSTLLGLlagLDR---PTSGTVRLAGQDLFALDedarARLRARHVGFVFQSfql 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1116 -PILfdcSIAENIAygdnsrvVP-----HDEIVRAAKEAnihpfietLpqkynTRVGDKG------TQLSGGQKQRIAIA 1183
Cdd:COG4181 102 lPTL---TALENVM-------LPlelagRRDARARARAL--------L-----ERVGLGHrldhypAQLSGGEQQRVALA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 338817954 1184 RALIRQPRVLLLDEATSALDTESEKVVQEAL-DKARE-GRTCIVIAHRLSTIQNADLIVVIENGKVKE 1249
Cdd:COG4181 159 RAFATEPAILFADEPTGNLDAATGEQIIDLLfELNRErGTTLVLVTHDPALAARCDRVLRLRAGRLVE 226
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
1052-1251 |
2.78e-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: 105.27 E-value: 2.78e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1052 LSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQwlRAQLGIVSQEPILF-DCSIAENIAYG 1130
Cdd:cd03298 17 FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA--DRPVSMLFQENNLFaHLTVEQNVGLG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1131 DNSRV----VPHDEIVRAAKEANIHPFIETLPQkyntrvgdkgtQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTES 1206
Cdd:cd03298 95 LSPGLkltaEDRQAIEVALARVGLAGLEKRLPG-----------ELSGGERQRVALARVLVRDKPVLLLDEPFAALDPAL 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 338817954 1207 EKVVQEALDK--AREGRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHG 1251
Cdd:cd03298 164 RAEMLDLVLDlhAETKMTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
409-614 |
3.03e-25 |
|
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: 105.14 E-value: 3.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 409 LKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNfNVRCLREIIGVVSQEPvlfsttIAENIR 488
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREVRRRIGIVFQDL------SVDDEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 489 YGRGNVTM---------DEIEKAVKEANAYdfiMKLPQKFDTLVGdrgaQLSGGQKQRIAIARALVRNPKILLLDEATSA 559
Cdd:cd03265 89 TGWENLYIharlygvpgAERRERIDELLDF---VGLLEAADRLVK----TYSGGMRRRLEIARSLVHRPEVLFLDEPTIG 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 338817954 560 LDTESEAEVQAALDK--AREGRTTIVIAHRLSTIRN-ADVIAGFEDGVIVEQGSHSEL 614
Cdd:cd03265 162 LDPQTRAHVWEYIEKlkEEFGMTILLTTHYMEEAEQlCDRVAIIDHGRIIAEGTPEEL 219
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
1031-1258 |
3.19e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 107.41 E-value: 3.19e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1031 VTFNEVVFNYptRANVP----VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLL------DGQEAKKL 1100
Cdd:PRK13634 3 ITFQKVEHRY--QYKTPferrALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIgervitAGKKNKKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1101 NVqwLRAQLGIVSQ--EPILFDCSIAENIAYGDNSRVVPHDEIVRAAKEAnihpfIET--LPQKYNTRvgdKGTQLSGGQ 1176
Cdd:PRK13634 81 KP--LRKKVGIVFQfpEHQLFEETVEKDICFGPMNFGVSEEDAKQKAREM-----IELvgLPEELLAR---SPFELSGGQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1177 KQRIAIARALIRQPRVLLLDEATSALDTESEKVVQE---ALDKaREGRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHGT 1252
Cdd:PRK13634 151 MRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEmfyKLHK-EKGLTTVLVTHSMEDAARyADQIVVMHKGTVFLQGT 229
|
....*.
gi 338817954 1253 HQQLLA 1258
Cdd:PRK13634 230 PREIFA 235
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
405-577 |
3.25e-25 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 108.63 E-value: 3.25e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 405 NIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLReiIGVVSQEPVLFS-TTI 483
Cdd:PRK10851 14 RTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRK--VGFVFQHYALFRhMTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 484 AENIRYG------RGNVTMDEIEKAVkeanaydfiMKLPQ--KFDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDE 555
Cdd:PRK10851 92 FDNIAFGltvlprRERPNAAAIKAKV---------TQLLEmvQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDE 162
|
170 180
....*....|....*....|..
gi 338817954 556 ATSALDTESEAEVQAALDKARE 577
Cdd:PRK10851 163 PFGALDAQVRKELRRWLRQLHE 184
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1049-1239 |
3.52e-25 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 106.01 E-value: 3.52e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1049 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYD-----PMAGSVLLDGQE--AKKLNVQWLRAQLGIVSQEPILFDC 1121
Cdd:PRK14239 21 LNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnpevTITGSIVYNGHNiySPRTDTVDLRKEIGMVFQQPNPFPM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1122 SIAENIAYG-------DNSRVvphDEIV-RAAKEANIHpfietlpQKYNTRVGDKGTQLSGGQKQRIAIARALIRQPRVL 1193
Cdd:PRK14239 101 SIYENVVYGlrlkgikDKQVL---DEAVeKSLKGASIW-------DEVKDRLHDSALGLSGGQQQRVCIARVLATSPKII 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 338817954 1194 LLDEATSALDTESEKVVQEALDKAREGRTCIVIAHrlsTIQNADLI 1239
Cdd:PRK14239 171 LLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTR---SMQQASRI 213
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
389-626 |
3.79e-25 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 113.72 E-value: 3.79e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 389 GNLEFSDVHFSYpsRANIK-ILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLRE 467
Cdd:PTZ00243 1307 GSLVFEGVQMRY--REGLPlVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRR 1384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 468 IIGVVSQEPVLFSTTIAENIRyGRGNVTMDEIEKAVKEANAYDFIMKLPQKFDTLVGDRGAQLSGGQKQRIAIARALV-R 546
Cdd:PTZ00243 1385 QFSMIPQDPVLFDGTVRQNVD-PFLEASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLkK 1463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 547 NPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTIRNADVIAGFEDGVIVEQGSHSEL-MKKEGIYFRLV 625
Cdd:PTZ00243 1464 GSGFILMDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELvMNRQSIFHSMV 1543
|
.
gi 338817954 626 N 626
Cdd:PTZ00243 1544 E 1544
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1045-1251 |
4.48e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 105.77 E-value: 4.48e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1045 NVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYD-----PMAGSVLLDGQEAKKLNVQWLRAQLGIVSQEP-IL 1118
Cdd:PRK14247 15 QVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDIFKMDVIELRRRVQMVFQIPnPI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1119 FDCSIAENIAYGDN-SRVVPH----DEIVRAAKEAnihpfiETLPQKYNTRVGDKGTQLSGGQKQRIAIARALIRQPRVL 1193
Cdd:PRK14247 95 PNLSIFENVALGLKlNRLVKSkkelQERVRWALEK------AQLWDEVKDRLDAPAGKLSGGQQQRLCIARALAFQPEVL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 338817954 1194 LLDEATSALDTESEKVVQEALDKAREGRTCIVIAH------RLStiqnaDLIVVIENGKVKEHG 1251
Cdd:PRK14247 169 LADEPTANLDPENTAKIESLFLELKKDMTIVLVTHfpqqaaRIS-----DYVAFLYKGQIVEWG 227
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1041-1251 |
5.59e-25 |
|
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: 103.78 E-value: 5.59e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1041 PTRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLL--ERFYDPMAGSVLLDGqeaKKLNVQWLRAQLGIVSQEPIL 1118
Cdd:cd03213 17 PSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLING---RPLDKRSFRKIIGYVPQDDIL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1119 FDC-SIAENIAYgdnsrvvphdeivrAAKeanihpfietLpqkyntrvgdKGtqLSGGQKQRIAIARALIRQPRVLLLDE 1197
Cdd:cd03213 94 HPTlTVRETLMF--------------AAK----------L----------RG--LSGGERKRVSIALELVSNPSLLFLDE 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 338817954 1198 ATSALDTESEKVVQEALDK-AREGRTCIVIAHRLST--IQNADLIVVIENGKVKEHG 1251
Cdd:cd03213 138 PTSGLDSSSALQVMSLLRRlADTGRTIICSIHQPSSeiFELFDKLLLLSQGRVIYFG 194
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1046-1247 |
6.07e-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: 105.51 E-value: 6.07e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1046 VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVqWLRAQLGIVS--QEPILF-DCS 1122
Cdd:COG0411 17 LVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPP-HRIARLGIARtfQNPRLFpELT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1123 IAENIA----YGDNSRVVPH-----------DEIVRAAKEAnihpfIET--LPQKYNTRVGDkgtqLSGGQKQRIAIARA 1185
Cdd:COG0411 96 VLENVLvaahARLGRGLLAAllrlprarreeREARERAEEL-----LERvgLADRADEPAGN----LSYGQQRRLEIARA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 338817954 1186 LIRQPRVLLLDEATSAL-DTESEKVVqEALDKARE--GRTCIVIAHRLSTIQN-ADLIVVIENGKV 1247
Cdd:COG0411 167 LATEPKLLLLDEPAAGLnPEETEELA-ELIRRLRDerGITILLIEHDMDLVMGlADRIVVLDFGRV 231
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
1030-1253 |
6.50e-25 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 105.09 E-value: 6.50e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1030 SVTFNEVVFNYptrANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQE---AKKLN---VQ 1103
Cdd:COG4161 2 SIQLKNINCFY---GSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQfdfSQKPSekaIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1104 WLRAQLGIVSQEPILFdcsiaeniaygdnsrvvPH----DEIVRA-------AKEANIHPFIETLPQkynTRVGDKGT-- 1170
Cdd:COG4161 79 LLRQKVGMVFQQYNLW-----------------PHltvmENLIEApckvlglSKEQAREKAMKLLAR---LRLTDKADrf 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1171 --QLSGGQKQRIAIARALIRQPRVLLLDEATSALDTE-SEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVIENGK 1246
Cdd:COG4161 139 plHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEiTAQVVEIIRELSQTGITQVIVTHEVEFARKvASQVVYMEKGR 218
|
....*..
gi 338817954 1247 VKEHGTH 1253
Cdd:COG4161 219 IIEQGDA 225
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
408-614 |
7.09e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 105.51 E-value: 7.09e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 408 ILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQ------DIRNFNVRCLREIIGVVSQEPVLFS- 480
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkDIFQIDAIKLRKEVGMVFQQPNPFPh 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 481 TTIAENIRY---GRGNVTMDEIEKAVKEANAYDFIMKlpQKFDTLvGDRGAQLSGGQKQRIAIARALVRNPKILLLDEAT 557
Cdd:PRK14246 105 LSIYDNIAYplkSHGIKEKREIKKIVEECLRKVGLWK--EVYDRL-NSPASQLSGGQQQRLTIARALALKPKVLLMDEPT 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 338817954 558 SALDTESEAEVQAALDKAREGRTTIVIAHRLSTI-RNADVIAGFEDGVIVEQGSHSEL 614
Cdd:PRK14246 182 SMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVaRVADYVAFLYNGELVEWGSSNEI 239
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
391-586 |
7.39e-25 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 105.33 E-value: 7.39e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 391 LEFSDVHFSYP-SRANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRclReii 469
Cdd:COG4525 4 LTVRHVSVRYPgGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGAD--R--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 470 GVVSQEPVLFS-TTIAENIRYG---RGnvtmdeIEKAVKEANAYDFImklpqkfdTLVGDRGA------QLSGGQKQRIA 539
Cdd:COG4525 79 GVVFQKDALLPwLNVLDNVAFGlrlRG------VPKAERRARAEELL--------ALVGLADFarrriwQLSGGMRQRVG 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 338817954 540 IARALVRNPKILLLDEATSALDTESEAEVQAALDK--AREGRTTIVIAH 586
Cdd:COG4525 145 IARALAADPRFLLMDEPFGALDALTREQMQELLLDvwQRTGKGVFLITH 193
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
408-609 |
7.82e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 104.92 E-value: 7.82e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 408 ILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYD-----PTEGKISIDGQDIRNFNVRCL--REIIGVVSQEPVLFS 480
Cdd:PRK14267 19 VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGRNIYSPDVDPIevRREVGMVFQYPNPFP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 481 -TTIAENIRYG-------RGNVTMDE-IEKAVKEANAYDfimklpqKFDTLVGDRGAQLSGGQKQRIAIARALVRNPKIL 551
Cdd:PRK14267 99 hLTIYDNVAIGvklnglvKSKKELDErVEWALKKAALWD-------EVKDRLNDYPSNLSGGQRQRLVIARALAMKPKIL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 338817954 552 LLDEATSALDTESEAEVQAALDKAREGRTTIVIAHR-LSTIRNADVIAGFEDGVIVEQG 609
Cdd:PRK14267 172 LMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSpAQAARVSDYVAFLYLGKLIEVG 230
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
407-609 |
8.59e-25 |
|
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: 104.28 E-value: 8.59e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 407 KILKGLNLKVKSGQTVALVGNSGCGKSTTVQLL-QRLYDP--TEGKISIDGQDIRNFNVRclrEIIGVVSQEPVLFST-T 482
Cdd:cd03234 21 RILNDVSLHVESGQVMAILGSSGSGKTTLLDAIsGRVEGGgtTSGQILFNGQPRKPDQFQ---KCVAYVRQDDILLPGlT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 483 IAENIRYGRGNVTMDEIEKAVKEANAYDFIMKlpQKFDTLVGD-RGAQLSGGQKQRIAIARALVRNPKILLLDEATSALD 561
Cdd:cd03234 98 VRETLTYTAILRLPRKSSDAIRKKRVEDVLLR--DLALTRIGGnLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLD 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 338817954 562 TESEAEVQAAL-DKAREGRTTIVIAH--RLSTIRNADVIAGFEDGVIVEQG 609
Cdd:cd03234 176 SFTALNLVSTLsQLARRNRIVILTIHqpRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
391-610 |
9.23e-25 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 110.18 E-value: 9.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 391 LEFSDVHFSYPSRANIK--------ILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYdPTEGKISIDGQDIRNFNV 462
Cdd:PRK15134 276 LDVEQLQVAFPIRKGILkrtvdhnvVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLHNLNR 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 463 RCL---REIIGVVSQEP---------VLfsTTIAENIRYGRGNVTMDEIEKAVKEAnaydfiMKlPQKFDTLVGDR-GAQ 529
Cdd:PRK15134 355 RQLlpvRHRIQVVFQDPnsslnprlnVL--QIIEEGLRVHQPTLSAAQREQQVIAV------ME-EVGLDPETRHRyPAE 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 530 LSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKAREGR--TTIVIAHRLSTIRNA--DVIAgFEDGVI 605
Cdd:PRK15134 426 FSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHqlAYLFISHDLHVVRALchQVIV-LRQGEV 504
|
....*
gi 338817954 606 VEQGS 610
Cdd:PRK15134 505 VEQGD 509
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1041-1251 |
9.75e-25 |
|
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: 103.60 E-value: 9.75e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1041 PTRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKlNVQWLRAQLGIVSQEPILFD 1120
Cdd:cd03266 13 DVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-EPAEARRRLGFVSDSTGLYD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1121 -CSIAENIAY-GDNSRVVPHDEIVRAAKEANIHPFIETLpqkyNTRVGDkgtqLSGGQKQRIAIARALIRQPRVLLLDEA 1198
Cdd:cd03266 92 rLTARENLEYfAGLYGLKGDELTARLEELADRLGMEELL----DRRVGG----FSTGMRQKVAIARALVHDPPVLLLDEP 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 338817954 1199 TSALDTESEKVVQEALDKAREGRTCIVIA-HRLSTIQN-ADLIVVIENGKVKEHG 1251
Cdd:cd03266 164 TTGLDVMATRALREFIRQLRALGKCILFStHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
391-561 |
9.97e-25 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 104.03 E-value: 9.97e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 391 LEFSDVHFSYPSRaniKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLREIIG 470
Cdd:PRK10247 8 LQLQNVGYLAGDA---KILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 471 VVSQEPVLFSTTIAENIRYGRgnvtmdEIEKAVKEANAY-DFIMK--LPqkfDTLVGDRGAQLSGGQKQRIAIARALVRN 547
Cdd:PRK10247 85 YCAQTPTLFGDTVYDNLIFPW------QIRNQQPDPAIFlDDLERfaLP---DTILTKNIAELSGGEKQRISLIRNLQFM 155
|
170
....*....|....
gi 338817954 548 PKILLLDEATSALD 561
Cdd:PRK10247 156 PKVLLLDEITSALD 169
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
412-615 |
1.19e-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: 107.12 E-value: 1.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 412 LNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGqdirnfnvRCL------------REIIGVVSQEPVLF 479
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNG--------RTLfdsrkgiflppeKRRIGYVFQEARLF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 480 S-TTIAENIRYGRGNVTMDEieKAVKEANAYDFImklpqKFDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEATS 558
Cdd:TIGR02142 88 PhLSVRGNLRYGMKRARPSE--RRISFERVIELL-----GIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 559 ALDTESEAEVQAALDK-AREGRTTIV-IAHRLSTI-RNADVIAGFEDGVIVEQGSHSELM 615
Cdd:TIGR02142 161 ALDDPRKYEILPYLERlHAEFGIPILyVSHSLQEVlRLADRVVVLEDGRVAAAGPIAEVW 220
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
126-344 |
1.59e-24 |
|
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; The bacterial lipid flippase MsbA is found in Gram-negative bacteria and transports lipid A and lipopolysaccharide (LPS) from the cytoplasmic leaflet to the periplasmic leaflet of the inner membrane. MsbA is also a polyspecific transporter capable of transporting a broad spectrum of drug molecules. Additionally, MsbA exhibits significant sequence similarity to mammalian multidrug resistance (MDR) proteins such as human MDR protein 1 (MDR1) and LmrA from Lactococcus lactis. This subgroup also contains a putative transporter Brevibacillus brevis TycD; the location of the tycD gene within the Tyc (tyrocidine) biosynthesis operon suggests that TycD may play a role in the secretion of the cyclic decapeptide antibiotic tyrocidine. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349996 [Multi-domain] Cd Length: 292 Bit Score: 105.20 E-value: 1.59e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 126 VAAYIQVSFWTLAAGRQIKKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDDVSKISEGIGDKVGMFFQAIATFFAGFIV 205
Cdd:cd18552 54 LASYLQTYLMAYVGQRVVRDLRNDLFDKLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGV 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 206 GFIRGWKLTLVIMAISPILGLSTAVWAKILSTFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKELERYQKHLENAKK 285
Cdd:cd18552 134 LFYLDWKLTLIALVVLPLAALPIRRIGKRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRR 213
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 338817954 286 IGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTIGNamtvFFSILIGAFSV 344
Cdd:cd18552 214 LSMKIARARALSSPLMELLGAIAIALVLWYGGYQVISGELTPGE----FISFITALLLL 268
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
406-621 |
2.50e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 105.32 E-value: 2.50e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 406 IKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISID----GQD--------------IRNFnvRCLRE 467
Cdd:PRK13631 39 LVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGdiyiGDKknnhelitnpyskkIKNF--KELRR 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 468 IIGVVSQEP--VLFSTTIAENIRYGRGNVTMDEIEkAVKEANAYDFIMKLpqKFDTLvgDRGA-QLSGGQKQRIAIARAL 544
Cdd:PRK13631 117 RVSMVFQFPeyQLFKDTIEKDIMFGPVALGVKKSE-AKKLAKFYLNKMGL--DDSYL--ERSPfGLSGGQKRRVAIAGIL 191
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 338817954 545 VRNPKILLLDEATSALDTESEAE-VQAALDKAREGRTTIVIAHRLSTIRN-ADVIAGFEDGVIVEQGSHSELMKKEGIY 621
Cdd:PRK13631 192 AIQPEILIFDEPTAGLDPKGEHEmMQLILDAKANNKTVFVITHTMEHVLEvADEVIVMDKGKILKTGTPYEIFTDQHII 270
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
409-636 |
2.59e-24 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 107.04 E-value: 2.59e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 409 LKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLREI----IGVVSQEPVLFS-TTI 483
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVrrkkIAMVFQSFALMPhMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 484 AENIRYGrgnVTMDEIEKAVKEANAYDFIMKLpqKFDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTE 563
Cdd:PRK10070 124 LDNTAFG---MELAGINAEERREKALDALRQV--GLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPL 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 564 SEAEVQAALDK--AREGRTTIVIAHRL-STIRNADVIAGFEDGVIVEQGSHSELMKKEG-----IYFRLVNMqtagSQIL 635
Cdd:PRK10070 199 IRTEMQDELVKlqAKHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEILNNPAndyvrTFFRGVDI----SQVF 274
|
.
gi 338817954 636 S 636
Cdd:PRK10070 275 S 275
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1048-1259 |
2.89e-24 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 103.51 E-value: 2.89e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1048 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQE-------------AKKLNVQWLRAQLGIVSQ 1114
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTinlvrdkdgqlkvADKNQLRLLRTRLTMVFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1115 EPILFD-CSIAENI--AYGDNSRVVPHDEIVRAAKEANIHPFIETLPQKYNTrvgdkgtQLSGGQKQRIAIARALIRQPR 1191
Cdd:PRK10619 100 HFNLWShMTVLENVmeAPIQVLGLSKQEARERAVKYLAKVGIDERAQGKYPV-------HLSGGQQQRVSIARALAMEPE 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1192 VLLLDEATSALDTESEKVVQEALDK-AREGRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHGTHQQLLAQ 1259
Cdd:PRK10619 173 VLLFDEPTSALDPELVGEVLRIMQQlAEEGKTMVVVTHEMGFARHvSSHVIFLHQGKIEEEGAPEQLFGN 242
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
391-610 |
4.43e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 103.53 E-value: 4.43e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 391 LEFSDVHFSYPSraNIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFN-VRCLREII 469
Cdd:PRK13644 2 IRLENVSYSYPD--GTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSkLQGIRKLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 470 GVVSQEP--VLFSTTIAENIRYGRGNVTMD--EIEKAVKEANAYDFIMKLPQKfdtlvgdRGAQLSGGQKQRIAIARALV 545
Cdd:PRK13644 80 GIVFQNPetQFVGRTVEEDLAFGPENLCLPpiEIRKRVDRALAEIGLEKYRHR-------SPKTLSGGQGQCVALAGILT 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 338817954 546 RNPKILLLDEATSALDTESEAEVQAALDKA-REGRTTIVIAHRLSTIRNADVIAGFEDGVIVEQGS 610
Cdd:PRK13644 153 MEPECLIFDEVTSMLDPDSGIAVLERIKKLhEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGE 218
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1046-1245 |
4.53e-24 |
|
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: 102.13 E-value: 4.53e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1046 VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQE-----AKKLNVQWL---RAQLGIVSQ--- 1114
Cdd:COG4778 24 LPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGgwvdlAQASPREILalrRRTIGYVSQflr 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1115 ------------EPILfdcsiaeniaygdnSRVVPHDEIVRAAKEA----NIHPFIETLPQkyNTrvgdkgtqLSGGQKQ 1178
Cdd:COG4778 104 viprvsaldvvaEPLL--------------ERGVDREEARARARELlarlNLPERLWDLPP--AT--------FSGGEQQ 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 338817954 1179 RIAIARALIRQPRVLLLDEATSALDTESEKVVQEALDKAREGRTCIV-IAHRLSTIQN-ADLIVVIENG 1245
Cdd:COG4778 160 RVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIgIFHDEEVREAvADRVVDVTPF 228
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
407-588 |
4.70e-24 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 103.24 E-value: 4.70e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 407 KILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNfnvrcLRE-----IIGVVSQEPVL--- 478
Cdd:COG1101 20 RALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTK-----LPEykrakYIGRVFQDPMMgta 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 479 FSTTIAEN--IRYGRGN-------VTMDEIE---KAVKEANaydfiMKLPQKFDTLVGdrgaQLSGGQKQRIAIARALVR 546
Cdd:COG1101 95 PSMTIEENlaLAYRRGKrrglrrgLTKKRRElfrELLATLG-----LGLENRLDTKVG----LLSGGQRQALSLLMATLT 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 338817954 547 NPKILLLDEATSALDTESEAEVQAALDK--AREGRTTIVIAHRL 588
Cdd:COG1101 166 KPKLLLLDEHTAALDPKTAALVLELTEKivEENNLTTLMVTHNM 209
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
391-603 |
4.78e-24 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 101.64 E-value: 4.78e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 391 LEFSDVHFSYPSraNIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKI----------SIDGQDIRNf 460
Cdd:cd03290 1 VQVTNGYFSWGS--GLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsnknesepSFEATRSRN- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 461 nvrclREIIGVVSQEPVLFSTTIAENIRYGrgNVTMDEIEKAVKEANAYD-FIMKLPQKFDTLVGDRGAQLSGGQKQRIA 539
Cdd:cd03290 78 -----RYSVAYAAQKPWLLNATVEENITFG--SPFNKQRYKAVTDACSLQpDIDLLPFGDQTEIGERGINLSGGQRQRIC 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 338817954 540 IARALVRNPKILLLDEATSALDTE-SEAEVQAALDK--AREGRTTIVIAHRLSTIRNADVIAGFEDG 603
Cdd:cd03290 151 VARALYQNTNIVFLDDPFSALDIHlSDHLMQEGILKflQDDKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
1030-1252 |
5.12e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 103.29 E-value: 5.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1030 SVTFNEVVFNYP--TRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQE----AKKLNVQ 1103
Cdd:PRK13649 2 GINLQNVSYTYQagTPFEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLitstSKNKDIK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1104 WLRAQLGIVSQ--EPILFDCSIAENIAYGDNSRVVPHDEIVRAAKEA-NIHPFIETLPQKyntrvgdKGTQLSGGQKQRI 1180
Cdd:PRK13649 82 QIRKKVGLVFQfpESQLFEETVLKDVAFGPQNFGVSQEEAEALAREKlALVGISESLFEK-------NPFELSGGQMRRV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 338817954 1181 AIARALIRQPRVLLLDEATSALDTESEKVVQEALDKARE-GRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHGT 1252
Cdd:PRK13649 155 AIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQsGMTIVLVTHLMDDVANyADFVYVLEKGKLVLSGK 228
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
1031-1251 |
6.19e-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: 101.14 E-value: 6.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1031 VTFNEVVFNYPTRanvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQWlrAQLG 1110
Cdd:cd03268 1 LKTNDLTKTYGKK---RVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEAL--RRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1111 IVSQEPILFD-CSIAENIAYGDNSRVVPHDEIVRAAKEANIHpfietlpqkynTRVGDKGTQLSGGQKQRIAIARALIRQ 1189
Cdd:cd03268 76 ALIEAPGFYPnLTARENLRLLARLLGIRKKRIDEVLDVVGLK-----------DSAKKKVKGFSLGMKQRLGIALALLGN 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 338817954 1190 PRVLLLDEATSALDTESEKVVQEAL-DKAREGRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHG 1251
Cdd:cd03268 145 PDLLILDEPTNGLDPDGIKELRELIlSLRDQGITVLISSHLLSEIQKvADRIGIINKGKLIEEG 208
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
393-586 |
7.21e-24 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 107.46 E-value: 7.21e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 393 FSDVHFSYPSRaniKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGqdirnfNVRclreiIGVV 472
Cdd:COG0488 1 LENLSKSFGGR---PLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK------GLR-----IGYL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 473 SQEPVLFST-TIAENIRYGRGNVT-----MDEIEKAVK-----------------EANAYDF------IMK---LPQK-F 519
Cdd:COG0488 67 PQEPPLDDDlTVLDTVLDGDAELRaleaeLEELEAKLAepdedlerlaelqeefeALGGWEAearaeeILSglgFPEEdL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 338817954 520 DTLVGDrgaqLSGGQKQRIAIARALVRNPKILLLDEATSALDTES----EAEVqaaldKAREGrTTIVIAH 586
Cdd:COG0488 147 DRPVSE----LSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESiewlEEFL-----KNYPG-TVLVVSH 207
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
401-609 |
9.11e-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: 100.91 E-value: 9.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 401 PSRANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIrNFNVRCLREIIGVVSQEPVLFS 480
Cdd:cd03266 13 DVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDV-VKEPAEARRRLGFVSDSTGLYD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 481 -TTIAENIRY--GRGNVTMDEIEKAVKEanaydfimkLPQKFDT--LVGDRGAQLSGGQKQRIAIARALVRNPKILLLDE 555
Cdd:cd03266 92 rLTARENLEYfaGLYGLKGDELTARLEE---------LADRLGMeeLLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDE 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 338817954 556 ATSALDTESEAEVQAALDKAREGRTTIVIA-HRLSTI-RNADVIAGFEDGVIVEQG 609
Cdd:cd03266 163 PTTGLDVMATRALREFIRQLRALGKCILFStHIMQEVeRLCDRVVVLHRGRVVYEG 218
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
391-618 |
9.31e-24 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 102.16 E-value: 9.31e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 391 LEFSDVHFSYPSRAnikILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLREIIG 470
Cdd:PRK13548 3 LEARNLSVRLGGRT---LLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 471 VVSQEPVL-FSTTIAENIRYGRGnvTMDEIEKAVKEanaydfimkLPQKFDTLVG-----DRG-AQLSGGQKQRIAIARA 543
Cdd:PRK13548 80 VLPQHSSLsFPFTVEEVVAMGRA--PHGLSRAEDDA---------LVAAALAQVDlahlaGRDyPQLSGGEQQRVQLARV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 544 LVR------NPKILLLDEATSALDTESEAEV-QAALDKARE-GRTTIVIAHRLS-TIRNADVIAGFEDGVIVEQGSHSEL 614
Cdd:PRK13548 149 LAQlwepdgPPRWLLLDEPTSALDLAHQHHVlRLARQLAHErGLAVIVVLHDLNlAARYADRIVLLHQGRLVADGTPAEV 228
|
....
gi 338817954 615 MKKE 618
Cdd:PRK13548 229 LTPE 232
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1030-1203 |
1.46e-23 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 103.77 E-value: 1.46e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1030 SVTFNEVVFNYPtrANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQL---LERFydpMAGSVLLDGQeakklnvqwlr 1106
Cdd:PRK11650 3 GLKLQAVRKSYD--GKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMvagLERI---TSGEIWIGGR----------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1107 aqlgIVSQ-EPILFDC-------------SIAENIAYGDNSRVVPHDEIVR----AAKEANIHPFIETLPQkyntrvgdk 1168
Cdd:PRK11650 67 ----VVNElEPADRDIamvfqnyalyphmSVRENMAYGLKIRGMPKAEIEErvaeAARILELEPLLDRKPR--------- 133
|
170 180 190
....*....|....*....|....*....|....*
gi 338817954 1169 gtQLSGGQKQRIAIARALIRQPRVLLLDEATSALD 1203
Cdd:PRK11650 134 --ELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLD 166
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1049-1247 |
1.79e-23 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 105.88 E-value: 1.79e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1049 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEakklnVQW------LRAQLGIVSQEPILFDC- 1121
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKP-----VRIrsprdaIALGIGMVHQHFMLVPNl 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1122 SIAENIAYGDNSRVVPHDEIVRAAKEanihpfIETLPQKY------NTRVGDkgtqLSGGQKQRIAIARALIRQPRVLLL 1195
Cdd:COG3845 96 TVAENIVLGLEPTKGGRLDRKAARAR------IRELSERYgldvdpDAKVED----LSVGEQQRVEILKALYRGARILIL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 338817954 1196 DEATSAL-DTESEKVVqEALDK-AREGRTCIVIAHRLSTI-QNADLIVVIENGKV 1247
Cdd:COG3845 166 DEPTAVLtPQEADELF-EILRRlAAEGKSIIFITHKLREVmAIADRVTVLRRGKV 219
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
391-618 |
1.81e-23 |
|
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: 100.31 E-value: 1.81e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 391 LEFSDVHFSYPSRaniKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNV-RCLREII 469
Cdd:cd03218 1 LRAENLSKRYGKR---KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMhKRARLGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 470 GVVSQEPVLF-STTIAENIRygrgnVTMDEIEKAVKEANaydfimklpQKFDTLVGD---------RGAQLSGGQKQRIA 539
Cdd:cd03218 78 GYLPQEASIFrKLTVEENIL-----AVLEIRGLSKKERE---------EKLEELLEEfhithlrksKASSLSGGERRRVE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 540 IARALVRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIA-HR----LSTIRNADVIAgfeDGVIVEQGSHSEL 614
Cdd:cd03218 144 IARALATNPKFLLLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITdHNvretLSITDRAYIIY---EGKVLAEGTPEEI 220
|
....
gi 338817954 615 MKKE 618
Cdd:cd03218 221 AANE 224
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1047-1258 |
1.93e-23 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 101.62 E-value: 1.93e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1047 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQ--EAKKLNVQWLRAQLGIVSQEP--ILFDCS 1122
Cdd:PRK13638 15 PVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKplDYSKRGLLALRQQVATVFQDPeqQIFYTD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1123 IAENIAYGDNSRVVPHDEIVRAAKEAnihpfiETLPQKYNTRvgDKGTQ-LSGGQKQRIAIARALIRQPRVLLLDEATSA 1201
Cdd:PRK13638 95 IDSDIAFSLRNLGVPEAEITRRVDEA------LTLVDAQHFR--HQPIQcLSHGQKKRVAIAGALVLQARYLLLDEPTAG 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 338817954 1202 LDTESEKVVQEALDK-AREGRTCIVIAHRLSTI-QNADLIVVIENGKVKEHGTHQQLLA 1258
Cdd:PRK13638 167 LDPAGRTQMIAIIRRiVAQGNHVIISSHDIDLIyEISDAVYVLRQGQILTHGAPGEVFA 225
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1047-1228 |
2.16e-23 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 100.93 E-value: 2.16e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1047 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEakklnVQWLRAQLGIVSQ-EPILFDCSIAE 1125
Cdd:PRK11248 15 PALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKP-----VEGPGAERGVVFQnEGLLPWRNVQD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1126 NIAYGDNSRVVPHDEIVRAAKEANIHPFIETLPQKYNTrvgdkgtQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTE 1205
Cdd:PRK11248 90 NVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIW-------QLSGGQRQRVGIARALAANPQLLLLDEPFGALDAF 162
|
170 180
....*....|....*....|....*
gi 338817954 1206 SEKVVQEALDK--AREGRTCIVIAH 1228
Cdd:PRK11248 163 TREQMQTLLLKlwQETGKQVLLITH 187
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1043-1257 |
2.59e-23 |
|
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: 100.54 E-value: 2.59e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1043 RANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAG-SVLLDGQEAKKLNVQWLRAQLGIVS---QEPIL 1118
Cdd:COG1119 13 RGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGEDVWELRKRIGLVSpalQLRFP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1119 FDCSIAENIAYG--DNSRVVPH--DEIVRAAKEAnihpfIETLpqkyntRVGDKG----TQLSGGQKQRIAIARALIRQP 1190
Cdd:COG1119 93 RDETVLDVVLSGffDSIGLYREptDEQRERAREL-----LELL------GLAHLAdrpfGTLSQGEQRRVLIARALVKDP 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 338817954 1191 RVLLLDEATSALDTESEKVVQEALDK-AREGRTCIV-IAHRL----STIQNAdliVVIENGKVKEHGTHQQLL 1257
Cdd:COG1119 162 ELLILDEPTAGLDLGARELLLALLDKlAAEGAPTLVlVTHHVeeipPGITHV---LLLKDGRVVAAGPKEEVL 231
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
409-586 |
2.72e-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: 99.85 E-value: 2.72e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 409 LKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLreiigVVSQEPVLFS-TTIAENI 487
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM-----VVFQNYSLLPwLTVRENI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 488 RYGRGNVtMDEIEKAVKEANAYDFImklpqkfdTLVGDRGA------QLSGGQKQRIAIARALVRNPKILLLDEATSALD 561
Cdd:TIGR01184 76 ALAVDRV-LPDLSKSERRAIVEEHI--------ALVGLTEAadkrpgQLSGGMKQRVAIARALSIRPKVLLLDEPFGALD 146
|
170 180
....*....|....*....|....*..
gi 338817954 562 TESEAEVQAALDKARE--GRTTIVIAH 586
Cdd:TIGR01184 147 ALTRGNLQEELMQIWEehRVTVLMVTH 173
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
391-615 |
2.79e-23 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 100.68 E-value: 2.79e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 391 LEFSDVHFSYPSRAN------IKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQ--DIRNFNV 462
Cdd:COG4167 5 LEVRNLSKTFKYRTGlfrrqqFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHklEYGDYKY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 463 RCLReiIGVVSQEPvlfSTTIAENIRYG-------RGNVTMDEIEKAVKeanaydfImklpqkFDTL--VGDRGAQ---- 529
Cdd:COG4167 85 RCKH--IRMIFQDP---NTSLNPRLNIGqileeplRLNTDLTAEEREER-------I------FATLrlVGLLPEHanfy 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 530 ---LSGGQKQRIAIARALVRNPKILLLDEATSALDTESEA-------EVQaaldkAREGRTTIVIAHRLSTIRN-ADVIA 598
Cdd:COG4167 147 phmLSSGQKQRVALARALILQPKIIIADEALAALDMSVRSqiinlmlELQ-----EKLGISYIYVSQHLGIVKHiSDKVL 221
|
250
....*....|....*..
gi 338817954 599 GFEDGVIVEQGSHSELM 615
Cdd:COG4167 222 VMHQGEVVEYGKTAEVF 238
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
1048-1247 |
3.20e-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: 99.65 E-value: 3.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1048 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMA---GSVLLDGQEAKKlnVQWLRaQLGIVSQEPILFDC-SI 1123
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFNGQPRKP--DQFQK-CVAYVRQDDILLPGlTV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1124 AENIAYGDNSRV-VPHDEIVRAAKEAnihpfIETLPQKYNTRVGDKG-TQLSGGQKQRIAIARALIRQPRVLLLDEATSA 1201
Cdd:cd03234 99 RETLTYTAILRLpRKSSDAIRKKRVE-----DVLLRDLALTRIGGNLvKGISGGERRRVSIAVQLLWDPKVLILDEPTSG 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 338817954 1202 LDTESE-KVVQEALDKAREGRTCIVIAH--RLSTIQNADLIVVIENGKV 1247
Cdd:cd03234 174 LDSFTAlNLVSTLSQLARRNRIVILTIHqpRSDLFRLFDRILLLSSGEI 222
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1044-1260 |
3.31e-23 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 100.47 E-value: 3.31e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1044 ANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQWLRAQLGIVSQEPIL-FDCS 1122
Cdd:PRK11231 13 GTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHHLTpEGIT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1123 IAENIAYGDN------SRVVPHDE-IVRAAKEANihpFIETLPQKyntRVgdkgTQLSGGQKQRIAIARALIRQPRVLLL 1195
Cdd:PRK11231 93 VRELVAYGRSpwlslwGRLSAEDNaRVNQAMEQT---RINHLADR---RL----TDLSGGQRQRAFLAMVLAQDTPVVLL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1196 DEATSALD----TESEKVVQEAldkAREGRTCIVIAHRLS-TIQNADLIVVIENGKVKEHGTHQQLLAQK 1260
Cdd:PRK11231 163 DEPTTYLDinhqVELMRLMREL---NTQGKTVVTVLHDLNqASRYCDHLVVLANGHVMAQGTPEEVMTPG 229
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1048-1257 |
3.86e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 100.12 E-value: 3.86e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1048 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERF---YDP---MAGSVLLDGQEAKKLNVQWLRAQLGIVSQEPILF-D 1120
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLieiYDSkikVDGKVLYFGKDIFQIDAIKLRKEVGMVFQQPNPFpH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1121 CSIAENIAYGDNSRVVPHDEIVRAAKEANIHPFieTLPQKYNTRVGDKGTQLSGGQKQRIAIARALIRQPRVLLLDEATS 1200
Cdd:PRK14246 105 LSIYDNIAYPLKSHGIKEKREIKKIVEECLRKV--GLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTS 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 338817954 1201 ALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHGTHQQLL 1257
Cdd:PRK14246 183 MIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARvADYVAFLYNGELVEWGSSNEIF 240
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
392-618 |
4.20e-23 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 100.16 E-value: 4.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 392 EFSDVHFSYpsrANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLREIIGV 471
Cdd:COG4604 3 EIKNVSKRY---GGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 472 VSQEPVLFST-TIAENIRYGR-----GNVTmDEIEKAVKEANAYDFIMKLPQKF-DtlvgdrgaQLSGGQKQRIAIARAL 544
Cdd:COG4604 80 LRQENHINSRlTVRELVAFGRfpyskGRLT-AEDREIIDEAIAYLDLEDLADRYlD--------ELSGGQRQRAFIAMVL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 545 VRNPKILLLDEATSALDTESEAEVQAALDK-ARE-GRTTIVIAHRLstirN-----ADVIAGFEDGVIVEQGSHSELMKK 617
Cdd:COG4604 151 AQDTDYVLLDEPLNNLDMKHSVQMMKLLRRlADElGKTVVIVLHDI----NfascyADHIVAMKDGRVVAQGTPEEIITP 226
|
.
gi 338817954 618 E 618
Cdd:COG4604 227 E 227
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
389-647 |
4.31e-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: 100.70 E-value: 4.31e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 389 GNLEFSDVHFSYPSRANiKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDpTEGKISIDGQDIRNFNVRCLREI 468
Cdd:cd03289 1 GQMTVKDLTAKYTEGGN-AVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 469 IGVVSQEPVLFSTTIAENIR-YGRGNvtMDEIEKAVKEANAYDFIMKLPQKFDTLVGDRGAQLSGGQKQRIAIARALVRN 547
Cdd:cd03289 79 FGVIPQKVFIFSGTFRKNLDpYGKWS--DEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 548 PKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRL--------------STIRNADVIAGF--EDGVIVEQGSH 611
Cdd:cd03289 157 AKILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIeamlecqrflvieeNKVRQYDSIQKLlnEKSHFKQAISP 236
|
250 260 270
....*....|....*....|....*....|....*...
gi 338817954 612 SELMKKEGIYFRLVNMQTAGSQI--LSEEFEVELSDEK 647
Cdd:cd03289 237 SDRLKLFPRRNSSKSKRKPRPQIqaLQEETEEEVQDTR 274
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
391-617 |
4.69e-23 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 99.76 E-value: 4.69e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 391 LEFSDVHFSYPSRaniKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLL--QRLYDPTEGKISIDGQDIRNFNV--RClR 466
Cdd:COG0396 1 LEIKNLHVSVEGK---EILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLmgHPKYEVTSGSILLDGEDILELSPdeRA-R 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 467 EIIGVVSQEPV--------LFSTTIAENIRygRGNVTMDEIEKAVKEANAydfIMKLPQKFdtlvGDRG--AQLSGGQKQ 536
Cdd:COG0396 77 AGIFLAFQYPVeipgvsvsNFLRTALNARR--GEELSAREFLKLLKEKMK---ELGLDEDF----LDRYvnEGFSGGEKK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 537 RIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKAR-EGRTTIVIAH--RLSTIRNADVIAGFEDGVIVEQGShSE 613
Cdd:COG0396 148 RNEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRsPDRGILIITHyqRILDYIKPDFVHVLVDGRIVKSGG-KE 226
|
....
gi 338817954 614 LMKK 617
Cdd:COG0396 227 LALE 230
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
391-614 |
5.00e-23 |
|
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: 99.14 E-value: 5.00e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 391 LEFSDVHFSYpsrANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDI-------Rnfnvr 463
Cdd:TIGR03410 1 LEVSNLNVYY---GQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDItklppheR----- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 464 cLREIIGVVSQEPVLFST-TIAENIRYGRGnvTMDEIEKAVKeanayDFIMKL-PQKFDTLvGDRGAQLSGGQKQRIAIA 541
Cdd:TIGR03410 73 -ARAGIAYVPQGREIFPRlTVEENLLTGLA--ALPRRSRKIP-----DEIYELfPVLKEML-GRRGGDLSGGQQQQLAIA 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 338817954 542 RALVRNPKILLLDEATSALDTESEAEVQAALDK--AREGRTTIVIAHRLSTIRN-ADVIAGFEDGVIVEQGSHSEL 614
Cdd:TIGR03410 144 RALVTRPKLLLLDEPTEGIQPSIIKDIGRVIRRlrAEGGMAILLVEQYLDFARElADRYYVMERGRVVASGAGDEL 219
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
1048-1252 |
7.98e-23 |
|
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: 98.37 E-value: 7.98e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1048 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQWlRAQLGI--VSQEPILF-DCSIA 1124
Cdd:TIGR03410 15 ILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHE-RARAGIayVPQGREIFpRLTVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1125 ENIAYGDNsrvvphdeiVRAAKEANIHPFIETL-P---QKYNTRVGDkgtqLSGGQKQRIAIARALIRQPRVLLLDEATS 1200
Cdd:TIGR03410 94 ENLLTGLA---------ALPRRSRKIPDEIYELfPvlkEMLGRRGGD----LSGGQQQQLAIARALVTRPKLLLLDEPTE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 338817954 1201 ALDTESEKVVQEALDK--AREGRTCIVIAHRLS-TIQNADLIVVIENGKVKEHGT 1252
Cdd:TIGR03410 161 GIQPSIIKDIGRVIRRlrAEGGMAILLVEQYLDfARELADRYYVMERGRVVASGA 215
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
400-614 |
8.37e-23 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 102.03 E-value: 8.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 400 YPSRANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQdiRNFNVRCLREIIGVVSQEPVLF 479
Cdd:PRK11000 10 TKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEK--RMNDVPPAERGVGMVFQSYALY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 480 S-TTIAENIRYGR--GNVTMDEIEKAVKEANAydfIMKLpqkfDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEA 556
Cdd:PRK11000 88 PhLSVAENMSFGLklAGAKKEEINQRVNQVAE---VLQL----AHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 338817954 557 TSALDTESEAEVQAALDK--AREGRTTIVIAH-RLSTIRNADVIAGFEDGVIVEQGSHSEL 614
Cdd:PRK11000 161 LSNLDAALRVQMRIEISRlhKRLGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
391-617 |
9.32e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 100.19 E-value: 9.32e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 391 LEFSDVHFSYPSRANI--KILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDgqDI------RNFNV 462
Cdd:PRK13643 2 IKFEKVNYTYQPNSPFasRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVG--DIvvsstsKQKEI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 463 RCLREIIGVVSQEP--VLFSTTIAENIRYGRGN--VTMDEIEKAVKE-----ANAYDFIMKLPqkfdtlvgdrgAQLSGG 533
Cdd:PRK13643 80 KPVRKKVGVVFQFPesQLFEETVLKDVAFGPQNfgIPKEKAEKIAAEklemvGLADEFWEKSP-----------FELSGG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 534 QKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKARE-GRTTIVIAHRLSTIRN-ADVIAGFEDGVIVEQGSH 611
Cdd:PRK13643 149 QMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQsGQTVVLVTHLMDDVADyADYVYLLEKGHIISCGTP 228
|
....*.
gi 338817954 612 SELMKK 617
Cdd:PRK13643 229 SDVFQE 234
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1037-1263 |
9.63e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 100.70 E-value: 9.63e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1037 VFNYPTRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSV---------------LLDGQEAKKL- 1100
Cdd:PRK13631 30 VFDEKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdiyigdkknnheLITNPYSKKIk 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1101 NVQWLRAQLGIVSQEP--ILFDCSIAENIAYGDNSRVVPHDEivrAAKEANIH--------PFIETLPqkyntrvgdkgT 1170
Cdd:PRK13631 110 NFKELRRRVSMVFQFPeyQLFKDTIEKDIMFGPVALGVKKSE---AKKLAKFYlnkmglddSYLERSP-----------F 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1171 QLSGGQKQRIAIARALIRQPRVLLLDEATSALDTESEK-VVQEALDKAREGRTCIVIAHRLSTI-QNADLIVVIENGKVK 1248
Cdd:PRK13631 176 GLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHeMMQLILDAKANNKTVFVITHTMEHVlEVADEVIVMDKGKIL 255
|
250
....*....|....*
gi 338817954 1249 EHGTHQQLLAQKGIY 1263
Cdd:PRK13631 256 KTGTPYEIFTDQHII 270
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1053-1260 |
9.77e-23 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 98.50 E-value: 9.77e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1053 SLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQwlRAQLGIVSQEPILFD-CSIAENIAYGD 1131
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS--RRPVSMLFQENNLFShLTVAQNIGLGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1132 NS----RVVPHDEIVRAAKEANIHPFIETLPqkyntrvgdkgTQLSGGQKQRIAIARALIRQPRVLLLDEATSALD---- 1203
Cdd:PRK10771 97 NPglklNAAQREKLHAIARQMGIEDLLARLP-----------GQLSGGQRQRVALARCLVREQPILLLDEPFSALDpalr 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 338817954 1204 TESEKVVQEALDkaREGRTCIVIAHRLS-TIQNADLIVVIENGKVKEHGTHQQLLAQK 1260
Cdd:PRK10771 166 QEMLTLVSQVCQ--ERQLTLLMVSHSLEdAARIAPRSLVVADGRIAWDGPTDELLSGK 221
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
1044-1251 |
1.11e-22 |
|
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: 97.35 E-value: 1.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1044 ANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGqeaKKLNVQwLRAQLGIVSQEPILF-DCS 1122
Cdd:cd03269 11 GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDG---KPLDIA-ARNRIGYLPEERGLYpKMK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1123 IAENIAYGDNSRVVPHDEIVRAAKEanihpFIET--LPQKYNTRVgdkgTQLSGGQKQRIAIARALIRQPRVLLLDEATS 1200
Cdd:cd03269 87 VIDQLVYLAQLKGLKKEEARRRIDE-----WLERleLSEYANKRV----EELSKGNQQKVQFIAAVIHDPELLILDEPFS 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 338817954 1201 ALDTESEKVVQEAL-DKAREGRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHG 1251
Cdd:cd03269 158 GLDPVNVELLKDVIrELARAGKTVILSTHQMELVEElCDRVLLLNKGRAVLYG 210
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
396-614 |
1.13e-22 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 99.55 E-value: 1.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 396 VHFSYPSRANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQdirnfnvrclreiIGVVSQE 475
Cdd:cd03291 40 LFFSNLCLVGAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-------------ISFSSQF 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 476 PVLFSTTIAENIRYGrgnVTMDEI--EKAVKEANAYDFIMKLPQKFDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLL 553
Cdd:cd03291 107 SWIMPGTIKENIIFG---VSYDEYryKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLL 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 338817954 554 DEATSALDTESEAEV-QAALDKAREGRTTIVIAHRLSTIRNADVIAGFEDGVIVEQGSHSEL 614
Cdd:cd03291 184 DSPFGYLDVFTEKEIfESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSEL 245
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
412-614 |
1.43e-22 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 101.45 E-value: 1.43e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 412 LNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNfnVRCLREIIGVVSQEPVLFS-TTIAENIRYG 490
Cdd:PRK11607 38 VSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSH--VPPYQRPINMMFQSYALFPhMTVEQNIAFG 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 491 --RGNVTMDEIEKAVKE----ANAYDFIMKLPQkfdtlvgdrgaQLSGGQKQRIAIARALVRNPKILLLDEATSALDTE- 563
Cdd:PRK11607 116 lkQDKLPKAEIASRVNEmlglVHMQEFAKRKPH-----------QLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKl 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 338817954 564 ---SEAEVQAALDkaREGRTTIVIAH-RLSTIRNADVIAGFEDGVIVEQGSHSEL 614
Cdd:PRK11607 185 rdrMQLEVVDILE--RVGVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1048-1256 |
1.50e-22 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 100.93 E-value: 1.50e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1048 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQwlRAQLGIVSQEPILF-DCSIAEN 1126
Cdd:PRK10851 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHAR--DRKVGFVFQHYALFrHMTVFDN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1127 IAYGdnSRVVP-HDEIVRAAKEANIHPFIET-----LPQKYNTrvgdkgtQLSGGQKQRIAIARALIRQPRVLLLDEATS 1200
Cdd:PRK10851 95 IAFG--LTVLPrRERPNAAAIKAKVTQLLEMvqlahLADRYPA-------QLSGGQKQRVALARALAVEPQILLLDEPFG 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 338817954 1201 ALDTESEKVVQEALDKARE--GRTCIVIAH-RLSTIQNADLIVVIENGKVKEHGTHQQL 1256
Cdd:PRK10851 166 ALDAQVRKELRRWLRQLHEelKFTSVFVTHdQEEAMEVADRVVVMSQGNIEQAGTPDQV 224
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
402-577 |
1.67e-22 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 97.17 E-value: 1.67e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 402 SRANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDP---TEGKISIDGQDIRNFNVRcLREIiGVVSQEPVL 478
Cdd:COG4136 10 TLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALPAE-QRRI-GILFQDDLL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 479 FS-TTIAENIRYG-----RGNVTMDEIEKAVKEANAYDFimklpqkfdtlvGDRG-AQLSGGQKQRIAIARALVRNPKIL 551
Cdd:COG4136 88 FPhLSVGENLAFAlpptiGRAQRRARVEQALEEAGLAGF------------ADRDpATLSGGQRARVALLRALLAEPRAL 155
|
170 180
....*....|....*....|....*..
gi 338817954 552 LLDEATSALDTESEAEVQA-ALDKARE 577
Cdd:COG4136 156 LLDEPFSKLDAALRAQFREfVFEQIRQ 182
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1048-1249 |
1.78e-22 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 98.61 E-value: 1.78e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1048 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLN----------VQWL----------RA 1107
Cdd:PRK10419 27 VLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNraqrkafrrdIQMVfqdsisavnpRK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1108 QLGIVSQEPI--LFDCSIAENIAygdnsRVvphDEIVRAAKEANIHpfIETLPQkyntrvgdkgtQLSGGQKQRIAIARA 1185
Cdd:PRK10419 107 TVREIIREPLrhLLSLDKAERLA-----RA---SEMLRAVDLDDSV--LDKRPP-----------QLSGGQLQRVCLARA 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 338817954 1186 LIRQPRVLLLDEATSALDteseKVVQ-EALD-----KAREGRTCIVIAHRLSTIQN-ADLIVVIENGKVKE 1249
Cdd:PRK10419 166 LAVEPKLLILDEAVSNLD----LVLQaGVIRllkklQQQFGTACLFITHDLRLVERfCQRVMVMDNGQIVE 232
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
108-361 |
2.34e-22 |
|
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: 98.71 E-value: 2.34e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 108 EEMTRYAYYYSGLGGGVLVAAYIQVSFWTLAAGRQIKKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDDVSKISEGIGD 187
Cdd:cd18575 33 ALLNRAFLLLLAVALVLALASALRFYLVSWLGERVVADLRKAVFAHLLRLSPSFFETTRTGEVLSRLTTDTTLIQTVVGS 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 188 KVGMFFQAIATFFAGFIVGFIRGWKLTLVIMAISPILGLSTAVWAKILSTFSDKELAAYAKAGAVAEEALGAIRTVIAFG 267
Cdd:cd18575 113 SLSIALRNLLLLIGGLVMLFITSPKLTLLVLLVIPLVVLPIILFGRRVRRLSRASQDRLADLSAFAEETLSAIKTVQAFT 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 268 GQNKELERYQKHLENAKKIGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTIGN-AMTVFFSILIgAFSVGQ 346
Cdd:cd18575 193 REDAERQRFATAVEAAFAAALRRIRARALLTALVIFLVFGAIVFVLWLGAHDVLAGRMSAGElSQFVFYAVLA-AGSVGA 271
|
250
....*....|....*
gi 338817954 347 AAPCIDAFANARGAA 361
Cdd:cd18575 272 LSEVWGDLQRAAGAA 286
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
1047-1258 |
2.39e-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: 97.23 E-value: 2.39e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1047 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVqWLRAQLGI--VSQEPILF-DCSI 1123
Cdd:cd03218 14 KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPM-HKRARLGIgyLPQEASIFrKLTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1124 AENIAYGDNSRVVPHDEIVRAAkEANIHPF-IETLPQKyntrvgdKGTQLSGGQKQRIAIARALIRQPRVLLLDEATSAL 1202
Cdd:cd03218 93 EENILAVLEIRGLSKKEREEKL-EELLEEFhITHLRKS-------KASSLSGGERRRVEIARALATNPKFLLLDEPFAGV 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 338817954 1203 DTESEKVVQEALDKAREGRTCIVIA-HRLS-TIQNADLIVVIENGKVKEHGTHQQLLA 1258
Cdd:cd03218 165 DPIAVQDIQKIIKILKDRGIGVLITdHNVReTLSITDRAYIIYEGKVLAEGTPEEIAA 222
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
413-615 |
2.52e-22 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 97.35 E-value: 2.52e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 413 NLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRclREIIGVVSQEPVLFS-TTIAENIRYG- 490
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS--RRPVSMLFQENNLFShLTVAQNIGLGl 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 491 RGNVTMDEIEKAVKEANAY-----DFIMKLPqkfdtlvgdrgAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESE 565
Cdd:PRK10771 97 NPGLKLNAAQREKLHAIARqmgieDLLARLP-----------GQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALR 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 338817954 566 AEVQAALDKAREGR--TTIVIAHRLS-TIRNAD---VIAgfeDGVIVEQGSHSELM 615
Cdd:PRK10771 166 QEMLTLVSQVCQERqlTLLMVSHSLEdAARIAPrslVVA---DGRIAWDGPTDELL 218
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1046-1246 |
2.88e-22 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 102.31 E-value: 2.88e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1046 VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYdPMA---GSVLLDGQEAKKLNVQWL-RAQLGIVSQEPILF-D 1120
Cdd:PRK13549 18 VKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHGtyeGEIIFEGEELQASNIRDTeRAGIAIIHQELALVkE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1121 CSIAENIAYGdnSRVVPH-----DEIVRAAKE------ANIHPfietlpqkyNTRVGDkgtqLSGGQKQRIAIARALIRQ 1189
Cdd:PRK13549 97 LSVLENIFLG--NEITPGgimdyDAMYLRAQKllaqlkLDINP---------ATPVGN----LGLGQQQLVEIAKALNKQ 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1190 PRVLLLDEATSALdTESEKVVQEAL--DKAREGRTCIVIAHRLSTIQN-ADLIVVIENGK 1246
Cdd:PRK13549 162 ARLLILDEPTASL-TESETAVLLDIirDLKAHGIACIYISHKLNEVKAiSDTICVIRDGR 220
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1048-1251 |
2.89e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 97.61 E-value: 2.89e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1048 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYD-----PMAGSVLLDGQE--AKKLNVQWLRAQLGIVSQEPILF- 1119
Cdd:PRK14267 19 VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGRNiySPDVDPIEVRREVGMVFQYPNPFp 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1120 DCSIAENIAYGD--NSRVVPH---DEIVR-AAKEAnihpfieTLPQKYNTRVGDKGTQLSGGQKQRIAIARALIRQPRVL 1193
Cdd:PRK14267 99 HLTIYDNVAIGVklNGLVKSKkelDERVEwALKKA-------ALWDEVKDRLNDYPSNLSGGQRQRLVIARALAMKPKIL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 338817954 1194 LLDEATSALDTESEKVVQEALDKAREGRTCIVIAHrlSTIQNA---DLIVVIENGKVKEHG 1251
Cdd:PRK14267 172 LMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTH--SPAQAArvsDYVAFLYLGKLIEVG 230
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1049-1260 |
3.37e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 98.36 E-value: 3.37e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1049 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQ----EAKKLNVQWLRAQLGIVSQ--EPILFDCS 1122
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYhitpETGNKNLKKLRKKVSLVFQfpEAQLFENT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1123 IAENIAYGDNSRVVPHDEivraAKEANIhpfietlpqKYNTRVG------DKGT-QLSGGQKQRIAIARALIRQPRVLLL 1195
Cdd:PRK13641 103 VLKDVEFGPKNFGFSEDE----AKEKAL---------KWLKKVGlsedliSKSPfELSGGQMRRVAIAGVMAYEPEILCL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 338817954 1196 DEATSALDTESEK-VVQEALDKAREGRTCIVIAHRLSTI-QNADLIVVIENGKVKEHGTHQQLLAQK 1260
Cdd:PRK13641 170 DEPAAGLDPEGRKeMMQLFKDYQKAGHTVILVTHNMDDVaEYADDVLVLEHGKLIKHASPKEIFSDK 236
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1048-1254 |
4.36e-22 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 96.62 E-value: 4.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1048 VLQGLSLEVKKGQTLALVGSSGCGKST---VVQLLErfydpMAGSVLLD--------GQEAKKLNVQWLRAQLGIVSQE- 1115
Cdd:PRK11124 17 ALFDITLDCPQGETLVLLGPSGAGKSSllrVLNLLE-----MPRSGTLNiagnhfdfSKTPSDKAIRELRRNVGMVFQQy 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1116 ---PILfdcSIAENIAYGDnSRV--VPHDEIVRAAKEanihpFIETLpqkyntRVGDKGT----QLSGGQKQRIAIARAL 1186
Cdd:PRK11124 92 nlwPHL---TVQQNLIEAP-CRVlgLSKDQALARAEK-----LLERL------RLKPYADrfplHLSGGQQQRVAIARAL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1187 IRQPRVLLLDEATSALDTE-SEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHGTHQ 1254
Cdd:PRK11124 157 MMEPQVLLFDEPTAALDPEiTAQIVSIIRELAETGITQVIVTHEVEVARKtASRVVYMENGHIVEQGDAS 226
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1047-1240 |
4.52e-22 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 96.32 E-value: 4.52e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1047 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQWLRAQLGIVSQEPILFDCSIAEN 1126
Cdd:PRK10247 21 KILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTLFGDTVYDN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1127 IAYGDNSRvvpHDEIVRAAKEANIHPFieTLPQKyntrVGDKG-TQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTE 1205
Cdd:PRK10247 101 LIFPWQIR---NQQPDPAIFLDDLERF--ALPDT----ILTKNiAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDES 171
|
170 180 190
....*....|....*....|....*....|....*..
gi 338817954 1206 SEKVVQEALDK-AREGRTCIV-IAHRLSTIQNADLIV 1240
Cdd:PRK10247 172 NKHNVNEIIHRyVREQNIAVLwVTHDKDEINHADKVI 208
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
708-965 |
4.97e-22 |
|
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: 97.89 E-value: 4.97e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 708 FVVGTVCAIANGALQPAFSIILSEMIaifgpgDDAVKQQKCN---MFSLVFLGLGVLSFFTFFLQGFTFGKAGEILTTRL 784
Cdd:cd18542 1 YLLAILALLLATALNLLIPLLIRRII------DSVIGGGLREllwLLALLILGVALLRGVFRYLQGYLAEKASQKVAYDL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 785 RSMAFKAMLRQDMSWFDdhKNSTGALSTRLATDAAQVQGATGTRLALIAQNTANLGTGIIISFIYGWQLTLLLLSVVPFI 864
Cdd:cd18542 75 RNDLYDHLQRLSFSFHD--KARTGDLMSRCTSDVDTIRRFLAFGLVELVRAVLLFIGALIIMFSINWKLTLISLAIIPFI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 865 AVAGIVEMKMLaGNAKRDKKEMEAA-GKIATEAIENIRTVVSLTQErKFESMYVEKLHGPYRN-SVRKAHIYGITFSISQ 942
Cdd:cd18542 153 ALFSYVFFKKV-RPAFEEIREQEGElNTVLQENLTGVRVVKAFARE-DYEIEKFDKENEEYRDlNIKLAKLLAKYWPLMD 230
|
250 260
....*....|....*....|...
gi 338817954 943 AFMYFSYAGCFRFGSYLIVNGHM 965
Cdd:cd18542 231 FLSGLQIVLVLWVGGYLVINGEI 253
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
391-587 |
5.72e-22 |
|
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: 94.14 E-value: 5.72e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 391 LEFSDVhfSYPSRANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISidgqdirnfnvRCLREIIG 470
Cdd:cd03223 1 IELENL--SLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIG-----------MPEGEDLL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 471 VVSQEPVLFSTTIAENIRYGRGNVtmdeiekavkeanaydfimklpqkfdtlvgdrgaqLSGGQKQRIAIARALVRNPKI 550
Cdd:cd03223 68 FLPQRPYLPLGTLREQLIYPWDDV-----------------------------------LSGGEQQRLAFARLLLHKPKF 112
|
170 180 190
....*....|....*....|....*....|....*...
gi 338817954 551 LLLDEATSALDTESEAEVqaaLDKAREGRTTIV-IAHR 587
Cdd:cd03223 113 VFLDEATSALDEESEDRL---YQLLKELGITVIsVGHR 147
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1036-1230 |
7.21e-22 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 96.69 E-value: 7.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1036 VVFNYPTRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVqWLRAQL-GIVSQ 1114
Cdd:COG1101 9 KTFNPGTVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPE-YKRAKYiGRVFQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1115 EPILFDC---SIAEN--IAYGDNSRVvphdEIVRAAKEANIHPFIET-------LPQKYNTRVGdkgtQLSGGQKQRIAI 1182
Cdd:COG1101 88 DPMMGTApsmTIEENlaLAYRRGKRR----GLRRGLTKKRRELFRELlatlglgLENRLDTKVG----LLSGGQRQALSL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 338817954 1183 ARALIRQPRVLLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRL 1230
Cdd:COG1101 160 LMATLTKPKLLLLDEHTAALDPKTAALVLELTEKivEENNLTTLMVTHNM 209
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
1053-1257 |
8.64e-22 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 99.34 E-value: 8.64e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1053 SLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQWL----RAQLGIVSQE-PILFDCSIAENI 1127
Cdd:PRK10070 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELrevrRKKIAMVFQSfALMPHMTVLDNT 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1128 AYGDNSRVVPHDEIVRAAKEANIHPFIETLPQKYNtrvgdkgTQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTESE 1207
Cdd:PRK10070 128 AFGMELAGINAEERREKALDALRQVGLENYAHSYP-------DELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIR 200
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 338817954 1208 KVVQEALDK--AREGRTCIVIAHRL-STIQNADLIVVIENGKVKEHGTHQQLL 1257
Cdd:PRK10070 201 TEMQDELVKlqAKHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
97-336 |
9.09e-22 |
|
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: 97.12 E-value: 9.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 97 LSMLNPG-------RILEEEMTRYAYYYSG--LGGGVL--VAAYIQVSFWTLAAGRQIKKIRQKFFHAILRQEMGWFDIK 165
Cdd:cd18542 14 LNLLIPLlirriidSVIGGGLRELLWLLALliLGVALLrgVFRYLQGYLAEKASQKVAYDLRNDLYDHLQRLSFSFHDKA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 166 GTTELNTRLTDDVSKISEGIGDKVGMFFQAIATFFAGFIVGFIRGWKLTLVIMAISPILGLST--------AVWAKI--- 234
Cdd:cd18542 94 RTGDLMSRCTSDVDTIRRFLAFGLVELVRAVLLFIGALIIMFSINWKLTLISLAIIPFIALFSyvffkkvrPAFEEIreq 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 235 ---LSTFsdkelaayakagavAEEALGAIRTVIAFGGQNKELERYQKHLENAKKIGIKKAISANISMGIAFLLIYASYAL 311
Cdd:cd18542 174 egeLNTV--------------LQENLTGVRVVKAFAREDYEIEKFDKENEEYRDLNIKLAKLLAKYWPLMDFLSGLQIVL 239
|
250 260
....*....|....*....|....*
gi 338817954 312 AFWYGSTLVISKEYTIGNaMTVFFS 336
Cdd:cd18542 240 VLWVGGYLVINGEITLGE-LVAFIS 263
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1040-1259 |
9.80e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 96.80 E-value: 9.80e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1040 YPTRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQWLRAQLGIVSQEP--I 1117
Cdd:PRK13652 11 YSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQNPddQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1118 LFDCSIAENIAYGDNSRVVPHDEIVRAAKEAnihpfIETLP-QKYNTRVGDkgtQLSGGQKQRIAIARALIRQPRVLLLD 1196
Cdd:PRK13652 91 IFSPTVEQDIAFGPINLGLDEETVAHRVSSA-----LHMLGlEELRDRVPH---HLSGGEKKRVAIAGVIAMEPQVLVLD 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 338817954 1197 EATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTI-QNADLIVVIENGKVKEHGTHQQLLAQ 1259
Cdd:PRK13652 163 EPTAGLDPQGVKELIDFLNDLPEtyGMTVIFSTHQLDLVpEMADYIYVMDKGRIVAYGTVEEIFLQ 228
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
408-605 |
1.03e-21 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 96.29 E-value: 1.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 408 ILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKIsIDGqdirNFNVRCLREIIGVVSQEPVLFS-TTIAEN 486
Cdd:PRK11247 27 VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAG----TAPLAEAREDTRLMFQDARLLPwKKVIDN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 487 IRYG-RGNVTMDEIE--KAVKEANAydfimklpqkfdtlVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTE 563
Cdd:PRK11247 102 VGLGlKGQWRDAALQalAAVGLADR--------------ANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDAL 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 338817954 564 SEAEVQAALDK--AREGRTTIVIAHRLS-TIRNADVIAGFEDGVI 605
Cdd:PRK11247 168 TRIEMQDLIESlwQQHGFTVLLVTHDVSeAVAMADRVLLIEEGKI 212
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
705-1260 |
1.06e-21 |
|
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: 102.68 E-value: 1.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 705 WPYFVVGTVCAI--ANGALQPafsIILSEMIAIFGPGDDAVKQQKcnmfslVFLGLGVLSFF---TFFLQGFTFG--KAG 777
Cdd:TIGR01271 80 WRFVFYGILLYFgeATKAVQP---LLLGRIIASYDPFNAPEREIA------YYLALGLCLLFivrTLLLHPAIFGlhHLG 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 778 EILTTRLRSMAFKAMLRQDMSWFDdhKNSTGALSTRLATDAAQV-QGATGTRLALIAQNTANLGTGIIISFIYGWQLTLL 856
Cdd:TIGR01271 151 MQMRIALFSLIYKKTLKLSSRVLD--KISTGQLVSLLSNNLNKFdEGLALAHFVWIAPLQVILLMGLIWELLEVNGFCGL 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 857 LLSVVPFIAVAGIVEMKMlagnAKRDKKemeaAGKIA------TEAIENIRTVVSLTQERKFESMyVEKLHGPYRNSVRK 930
Cdd:TIGR01271 229 GFLILLALFQACLGQKMM----PYRDKR----AGKISerlaitSEIIENIQSVKAYCWEEAMEKI-IKNIRQDELKLTRK 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 931 AhiygitfsisqAFMYFSYAGCFRFGSYLIVNG----HMRFKDVIL--VFSA----IVL---------GAVALGHASSFA 991
Cdd:TIGR01271 300 I-----------AYLRYFYSSAFFFSGFFVVFLsvvpYALIKGIILrrIFTTisycIVLrmtvtrqfpGAIQTWYDSLGA 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 992 ----PDYAKAK------------------LSAAY---LFSLFERQPLIDSYSG-----EGLWPDKFEGSVTfnevvfnyp 1041
Cdd:TIGR01271 369 itkiQDFLCKEeyktleynltttevemvnVTASWdegIGELFEKIKQNNKARKqpngdDGLFFSNFSLYVT--------- 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1042 tranvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQeakklnvqwlraqLGIVSQEPILFDC 1121
Cdd:TIGR01271 440 -----PVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR-------------ISFSPQTSWIMPG 501
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1122 SIAENIAYGdnsrvVPHDEI--VRAAKEANIHPFIETLPQKYNTRVGDKGTQLSGGQKQRIAIARALIRQPRVLLLDEAT 1199
Cdd:TIGR01271 502 TIKDNIIFG-----LSYDEYryTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPF 576
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 338817954 1200 SALDTESEKVVQEA-LDKAREGRTCIVIAHRLSTIQNADLIVVIENGKVKEHGTHQQLLAQK 1260
Cdd:TIGR01271 577 THLDVVTEKEIFEScLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAKR 638
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
406-606 |
1.69e-21 |
|
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: 95.49 E-value: 1.69e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 406 IKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRclrEII--GVVS--QEPVLFST 481
Cdd:COG0411 17 LVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPH---RIArlGIARtfQNPRLFPE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 482 -TIAENIRYGRGNVTMDEIEKAV--------KEANAYDFIM------KLPQKFDTLVGDrgaqLSGGQKQRIAIARALVR 546
Cdd:COG0411 94 lTVLENVLVAAHARLGRGLLAALlrlprarrEEREARERAEellervGLADRADEPAGN----LSYGQQRRLEIARALAT 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 338817954 547 NPKILLLDEATSALdteSEAEVQAALD-----KAREGRTTIVIAHRLstirnaDVIAGFEDGVIV 606
Cdd:COG0411 170 EPKLLLLDEPAAGL---NPEETEELAElirrlRDERGITILLIEHDM------DLVMGLADRIVV 225
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
1045-1252 |
2.00e-21 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 94.75 E-value: 2.00e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1045 NVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLL---ERfYDPMAGSVLLDGQEAKKLNVQwLRAQLGI-VS-QEPI-- 1117
Cdd:COG0396 12 GKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLmghPK-YEVTSGSILLDGEDILELSPD-ERARAGIfLAfQYPVei 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1118 --------LfdcSIAENIAYGDNSRVVP-HDEIVRAAKEANihpfietLPQKYNTR---VGdkgtqLSGGQKQRIAIARA 1185
Cdd:COG0396 90 pgvsvsnfL---RTALNARRGEELSAREfLKLLKEKMKELG-------LDEDFLDRyvnEG-----FSGGEKKRNEILQM 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1186 LIRQPRVLLLDEATSALDTESEKVVQEALDKAR-EGRTCIVIAH--RLSTIQNADLIVVIENGKVKEHGT 1252
Cdd:COG0396 155 LLLEPKLAILDETDSGLDIDALRIVAEGVNKLRsPDRGILIITHyqRILDYIKPDFVHVLVDGRIVKSGG 224
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
1048-1247 |
2.41e-21 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 95.13 E-value: 2.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1048 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDP-----MAGSVLL-DGQEAKKLNVQWLRaqlgivsqepILFDC 1121
Cdd:PRK11247 27 VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPsagelLAGTAPLaEAREDTRLMFQDAR----------LLPWK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1122 SIAENIAYG--DNSRVVPHD--EIVRAAKEANIHPfietlpqkyntrvgdkgTQLSGGQKQRIAIARALIRQPRVLLLDE 1197
Cdd:PRK11247 97 KVIDNVGLGlkGQWRDAALQalAAVGLADRANEWP-----------------AALSGGQKQRVALARALIHRPGLLLLDE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 338817954 1198 ATSALDTESEKVVQEALDK--AREGRTCIVIAHRLS-TIQNADLIVVIENGKV 1247
Cdd:PRK11247 160 PLGALDALTRIEMQDLIESlwQQHGFTVLLVTHDVSeAVAMADRVLLIEEGKI 212
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
700-1272 |
2.43e-21 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 101.59 E-value: 2.43e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 700 LNKTEWPYFVVGTVCAIANGALQPAFSIILSEMIAIFGPGDDAvkqqkcnmfslvFLGLgVLSFFTFFlqGFTFGKAGEI 779
Cdd:PLN03232 295 LNNSLGGRFWLGGIFKIGHDLSQFVGPVILSHLLQSMQEGDPA------------WVGY-VYAFLIFF--GVTFGVLCES 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 780 --------LTTRLRSMAFKAMLRQDMSWFDD-HKN-STGALSTRLATDAAQVQgatgtrlaLIAQNTANLGTG---IIIS 846
Cdd:PLN03232 360 qyfqnvgrVGFRLRSTLVAAIFHKSLRLTHEaRKNfASGKVTNMITTDANALQ--------QIAEQLHGLWSApfrIIVS 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 847 FIYGWQL--------TLLLLSVVPFIAVAgIVEMKMLA--GNAKRDKKEmeaagKIATEAIENIRTVVSLTQERKFESMy 916
Cdd:PLN03232 432 MVLLYQQlgvaslfgSLILFLLIPLQTLI-VRKMRKLTkeGLQWTDKRV-----GIINEILASMDTVKCYAWEKSFESR- 504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 917 VEKLHGPYRNSVRKAHIygitFSISQAFMYFS---YAGCFRFGSYLIVNGHMRFKDVILVFSAIVLGAVALGHASSFAPD 993
Cdd:PLN03232 505 IQGIRNEELSWFRKAQL----LSAFNSFILNSipvVVTLVSFGVFVLLGGDLTPARAFTSLSLFAVLRSPLNMLPNLLSQ 580
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 994 YAKAKLSAAYLFSLF--ERQPLIDSYSGEGLWPdkfegSVTFNEVVFNYPTRANVPVLQGLSLEVKKGQTLALVGSSGCG 1071
Cdd:PLN03232 581 VVNANVSLQRIEELLlsEERILAQNPPLQPGAP-----AISIKNGYFSWDSKTSKPTLSDINLEIPVGSLVAIVGGTGEG 655
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1072 KSTVVQLLERFYDPMAGSVLLdgqeakklnvqwLRAQLGIVSQEPILFDCSIAENIAYGDNsrvVPHDEIVRAAKEANIH 1151
Cdd:PLN03232 656 KTSLISAMLGELSHAETSSVV------------IRGSVAYVPQVSWIFNATVRENILFGSD---FESERYWRAIDVTALQ 720
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1152 PFIETLPQKYNTRVGDKGTQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTE-SEKVVQEALDKAREGRTCIVIAHRL 1230
Cdd:PLN03232 721 HDLDLLPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHvAHQVFDSCMKDELKGKTRVLVTNQL 800
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 338817954 1231 STIQNADLIVVIENGKVKEHGTHQQlLAQKGIYFSMVNIQAG 1272
Cdd:PLN03232 801 HFLPLMDRIILVSEGMIKEEGTFAE-LSKSGSLFKKLMENAG 841
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
395-618 |
2.59e-21 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 95.24 E-value: 2.59e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 395 DVHFSYPSRAnikILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCL-REIIGVVS 473
Cdd:PRK10575 16 NVSFRVPGRT---LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFaRKVAYLPQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 474 QEPVLFSTTIAENIRYGR-------GNVTMDEIEKaVKEANAYDFIMKLPQKfdtLVGdrgaQLSGGQKQRIAIARALVR 546
Cdd:PRK10575 93 QLPAAEGMTVRELVAIGRypwhgalGRFGAADREK-VEEAISLVGLKPLAHR---LVD----SLSGGERQRAWIAMLVAQ 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 338817954 547 NPKILLLDEATSALDTESEAEVQAALDK-ARE-GRTTIVIAHRLS-TIRNADVIAGFEDGVIVEQGSHSELMKKE 618
Cdd:PRK10575 165 DSRCLLLDEPTSALDIAHQVDVLALVHRlSQErGLTVIAVLHDINmAARYCDYLVALRGGEMIAQGTPAELMRGE 239
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
364-588 |
3.33e-21 |
|
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: 101.14 E-value: 3.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 364 IFDIIDNnPKIDSFSERGHKPDNIKGNLEFSDVHFS--YPSRANI--------------KILKGLNLKVKSGQTVALVGN 427
Cdd:TIGR01271 1175 VFKFIDL-PQEEPRPSGGGGKYQLSTVLVIENPHAQkcWPSGGQMdvqgltakyteagrAVLQDLSFSVEGGQRVGLLGR 1253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 428 SGCGKSTTVQLLQRLYDpTEGKISIDGQDIRNFNVRCLREIIGVVSQEPVLFSTTIAENIR-YGRgnVTMDEIEKAVKEA 506
Cdd:TIGR01271 1254 TGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNLDpYEQ--WSDEEIWKVAEEV 1330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 507 NAYDFIMKLPQKFDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAH 586
Cdd:TIGR01271 1331 GLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEH 1410
|
..
gi 338817954 587 RL 588
Cdd:TIGR01271 1411 RV 1412
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
1040-1242 |
3.76e-21 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 92.68 E-value: 3.76e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1040 YPTRanvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQwlraqlgiVSQEPILF 1119
Cdd:NF040873 2 YGGR---PVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQ--------RSEVPDSL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1120 DCSIAENIAYGDNSRVVPHDEIVRAAKEANIHPFietlpqkynTRVGDKG------TQLSGGQKQRIAIARALIRQPRVL 1193
Cdd:NF040873 71 PLTVRDLVAMGRWARRGLWRRLTRDDRAAVDDAL---------ERVGLADlagrqlGELSGGQRQRALLAQGLAQEADLL 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 338817954 1194 LLDEATSALDTESEKVVQEAL-DKAREGRTCIVIAHRLSTIQNADLIVVI 1242
Cdd:NF040873 142 LLDEPTTGLDAESRERIIALLaEEHARGATVVVVTHDLELVRRADPCVLL 191
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
1039-1260 |
4.17e-21 |
|
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: 94.92 E-value: 4.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1039 NYPTRANvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQWLRAQlgivsqepil 1118
Cdd:cd03291 44 NLCLVGA-PVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRISFSSQFSWIMPG---------- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1119 fdcSIAENIAYGdnsrvVPHDE-----IVRAAK-EANIHPFietlPQKYNTRVGDKGTQLSGGQKQRIAIARALIRQPRV 1192
Cdd:cd03291 113 ---TIKENIIFG-----VSYDEyryksVVKACQlEEDITKF----PEKDNTVLGEGGITLSGGQRARISLARAVYKDADL 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 338817954 1193 LLLDEATSALDTESEKVVQEA-LDKAREGRTCIVIAHRLSTIQNADLIVVIENGKVKEHGTHQQLLAQK 1260
Cdd:cd03291 181 YLLDSPFGYLDVFTEKEIFEScVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSLR 249
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
391-620 |
4.18e-21 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 94.69 E-value: 4.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 391 LEFSDVHFSYPSRaniKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIrNFNVR---CLRE 467
Cdd:PRK13638 2 LATSDLWFRYQDE---PVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPL-DYSKRgllALRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 468 IIGVVSQEP--VLFSTTIAENIRYGRGN--VTMDEIEKAVKEANaydfimklpqkfdTLVGDRGAQ------LSGGQKQR 537
Cdd:PRK13638 78 QVATVFQDPeqQIFYTDIDSDIAFSLRNlgVPEAEITRRVDEAL-------------TLVDAQHFRhqpiqcLSHGQKKR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 538 IAIARALVRNPKILLLDEATSALDTESEAEVQAALDK-AREGRTTIVIAHRLSTIRN-ADVIAGFEDGVIVEQG------ 609
Cdd:PRK13638 145 VAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRiVAQGNHVIISSHDIDLIYEiSDAVYVLRQGQILTHGapgevf 224
|
250
....*....|.
gi 338817954 610 SHSELMKKEGI 620
Cdd:PRK13638 225 ACTEAMEQAGL 235
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
406-618 |
4.66e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 95.54 E-value: 4.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 406 IKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNF------------------------N 461
Cdd:PRK13651 20 LKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKkktkekekvleklviqktrfkkikK 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 462 VRCLREIIGVVSQ--EPVLFSTTIAENIRYGRGNVTMDEiEKAVKEANAYDFIMKLPQKFDtlvgDRGA-QLSGGQKQRI 538
Cdd:PRK13651 100 IKEIRRRVGVVFQfaEYQLFEQTIEKDIIFGPVSMGVSK-EEAKKRAAKYIELVGLDESYL----QRSPfELSGGQKRRV 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 539 AIARALVRNPKILLLDEATSALDTESEAEVQAALDKA-REGRTTIVIAHRLSTI--RNADVIAgFEDGVIVEQGSHSELM 615
Cdd:PRK13651 175 ALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLnKQGKTIILVTHDLDNVleWTKRTIF-FKDGKIIKDGDTYDIL 253
|
...
gi 338817954 616 KKE 618
Cdd:PRK13651 254 SDN 256
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
708-979 |
4.84e-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: 94.80 E-value: 4.84e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 708 FVVGTVCAIANGALQPAFSIILSEMI-AIFGPGDdavkQQKCNMFSLVFLGLGVLSFFTFFLQGFTFGKAGEILTTRLRS 786
Cdd:cd18552 1 LALAILGMILVAATTAALAWLLKPLLdDIFVEKD----LEALLLVPLAIIGLFLLRGLASYLQTYLMAYVGQRVVRDLRN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 787 MAFKAMLRQDMSWFDdhKNSTGALSTRLATDAAQVQGATGTRLALIAQNTANLGTGIIISFIYGWQLTLLLLSVVPFIAV 866
Cdd:cd18552 77 DLFDKLLRLPLSFFD--RNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKLTLIALVVLPLAAL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 867 AgiveMKMLAGNAKRD-KKEMEAAGKIAT---EAIENIRTVVSLTQERKFESMYVEKLHGPYRNSVRKAHIYGITFSISQ 942
Cdd:cd18552 155 P----IRRIGKRLRKIsRRSQESMGDLTSvlqETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIARARALSSPLME 230
|
250 260 270
....*....|....*....|....*....|....*..
gi 338817954 943 AFMYFSYAGCFRFGSYLIVNGHMRFKDVILVFSAIVL 979
Cdd:cd18552 231 LLGAIAIALVLWYGGYQVISGELTPGEFISFITALLL 267
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1031-1252 |
4.94e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 94.80 E-value: 4.94e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1031 VTFNEVvfNYPTRANVP----VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSV----LLDGQEAKKLNV 1102
Cdd:PRK13643 2 IKFEKV--NYTYQPNSPfasrALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVtvgdIVVSSTSKQKEI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1103 QWLRAQLGIVSQEP--ILFDCSIAENIAYGDNSRVVPHDEIVRAAKE-----ANIHPFIETLPqkyntrvgdkgTQLSGG 1175
Cdd:PRK13643 80 KPVRKKVGVVFQFPesQLFEETVLKDVAFGPQNFGIPKEKAEKIAAEklemvGLADEFWEKSP-----------FELSGG 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 338817954 1176 QKQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEALDKARE-GRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHGT 1252
Cdd:PRK13643 149 QMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQsGQTVVLVTHLMDDVADyADYVYLLEKGHIISCGT 227
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1048-1258 |
5.50e-21 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 98.62 E-value: 5.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1048 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYdPMAGSVLLDGQEAKKLNVQWL---RAQLGIVSQEP---ILFDC 1121
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLHNLNRRQLlpvRHRIQVVFQDPnssLNPRL 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1122 SIAENIAYGDNsrvVPHDEIVRAAKEANIhpfIETLpqkynTRVG-DKGT------QLSGGQKQRIAIARALIRQPRVLL 1194
Cdd:PRK15134 380 NVLQIIEEGLR---VHQPTLSAAQREQQV---IAVM-----EEVGlDPETrhrypaEFSGGQRQRIAIARALILKPSLII 448
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 338817954 1195 LDEATSALDteseKVVQE---ALDKAREGR---TCIVIAHRLSTIQN-ADLIVVIENGKVKEHGTHQQLLA 1258
Cdd:PRK15134 449 LDEPTSSLD----KTVQAqilALLKSLQQKhqlAYLFISHDLHVVRAlCHQVIVLRQGEVVEQGDCERVFA 515
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
126-347 |
5.95e-21 |
|
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: 94.69 E-value: 5.95e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 126 VAAYIQVSFWTLAAGRQIKKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDDVSKISEGIGDKVGMFFQAIATFFAGFIV 205
Cdd:cd18784 51 VAAGIRGGLFTLAMARLNIRIRNLLFRSIVSQEIGFFDTVKTGDITSRLTSDTTTMSDTVSLNLNIFLRSLVKAIGVIVF 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 206 GFIRGWKLTLVIMAISPILGLSTAVWAKILSTFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKELERYQKHLENAKK 285
Cdd:cd18784 131 MFKLSWQLSLVTLIGLPLIAIVSKVYGDYYKKLSKAVQDSLAKANEVAEETISSIRTVRSFANEDGEANRYSEKLKDTYK 210
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 338817954 286 IGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTIGNamtvFFSILIGAFSVGQA 347
Cdd:cd18784 211 LKIKEALAYGGYVWSNELTELALTVSTLYYGGHLVITGQISGGN----LISFILYQLELGSC 268
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
399-595 |
9.73e-21 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 91.14 E-value: 9.73e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 399 SYPSRAnikILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISidgqdirnfnVRCLREIIGVV--SQEP 476
Cdd:NF040873 1 GYGGRP---VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVR----------RAGGARVAYVPqrSEVP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 477 VLFSTTIAENIRYGR-------GNVTMDEiEKAVKEAnaydfIMKLpqKFDTLVGDRGAQLSGGQKQRIAIARALVRNPK 549
Cdd:NF040873 68 DSLPLTVRDLVAMGRwarrglwRRLTRDD-RAAVDDA-----LERV--GLADLAGRQLGELSGGQRQRALLAQGLAQEAD 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 338817954 550 ILLLDEATSALDTESEAEVQAAL-DKAREGRTTIVIAHRLSTIRNAD 595
Cdd:NF040873 140 LLLLDEPTTGLDAESRERIIALLaEEHARGATVVVVTHDLELVRRAD 186
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
141-361 |
1.24e-20 |
|
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: 93.65 E-value: 1.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 141 RQIKKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDDVSKISEGIGDKVGMFFQAIATFFAGFIVGFIRGWKLTLVIMAI 220
Cdd:cd18551 66 RVVLDLRRRLWRRLLRLPVSFFDRRRSGDLVSRVTNDTTLLRELITSGLPQLVTGVLTVVGAVVLMFLLDWVLTLVTLAV 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 221 SPILGLSTAVWAKILSTFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKELERYQKHLENAKKIGIKKAISANISMGI 300
Cdd:cd18551 146 VPLAFLIILPLGRRIRKASKRAQDALGELSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAKIEALIGPL 225
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 338817954 301 AFLLIYASYALAFWYGSTLVISKEYTIGNAMTVFFSILIGAFSVGQAAPCIDAFANARGAA 361
Cdd:cd18551 226 MGLAVQLALLVVLGVGGARVASGALTVGTLVAFLLYLFQLITPLSQLSSFFTQLQKALGAL 286
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
402-609 |
1.58e-20 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 95.68 E-value: 1.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 402 SRANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLREIIGVVSQEPVL-FS 480
Cdd:PRK09536 12 EFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLsFE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 481 TTIAENIRYGRGN-----VTMDE-----IEKAVKEANAYDFImklPQKFDTlvgdrgaqLSGGQKQRIAIARALVRNPKI 550
Cdd:PRK09536 92 FDVRQVVEMGRTPhrsrfDTWTEtdraaVERAMERTGVAQFA---DRPVTS--------LSGGERQRVLLARALAQATPV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 338817954 551 LLLDEATSALDTESEAE-VQAALDKAREGRTTIVIAHRLS-TIRNADVIAGFEDGVIVEQG 609
Cdd:PRK09536 161 LLLDEPTASLDINHQVRtLELVRRLVDDGKTAVAAIHDLDlAARYCDELVLLADGRVRAAG 221
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
406-605 |
1.90e-20 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 91.73 E-value: 1.90e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 406 IKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQD----------IRNFNVRclREIIGVVSQe 475
Cdd:COG4778 24 LPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGgwvdlaqaspREILALR--RRTIGYVSQ- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 476 pvlFSTTI----AENIrygrgnVTMDEIEKAVKEANAYDFIMKLPQKFDtlVGDRGAQL-----SGGQKQRIAIARALVR 546
Cdd:COG4778 101 ---FLRVIprvsALDV------VAEPLLERGVDREEARARARELLARLN--LPERLWDLppatfSGGEQQRVNIARGFIA 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 547 NPKILLLDEATSALDTESEAEVQAALDKAREGRTTIV-IAHrlstirNADVIAGFEDGVI 605
Cdd:COG4778 170 DPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIgIFH------DEEVREAVADRVV 223
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1048-1258 |
2.05e-20 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 93.33 E-value: 2.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1048 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGqEAKKLNVQWLRAQLGIVSQ----EPilfDCSI 1123
Cdd:PRK13537 22 VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCG-EPVPSRARHARQRVGVVPQfdnlDP---DFTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1124 AENIA-----YGDNSrvvphdeivrAAKEANIHPFIE--TLPQKYNTRVGDkgtqLSGGQKQRIAIARALIRQPRVLLLD 1196
Cdd:PRK13537 98 RENLLvfgryFGLSA----------AAARALVPPLLEfaKLENKADAKVGE----LSGGMKRRLTLARALVNDPDVLVLD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 338817954 1197 EATSALDTESEKVVQEALDK--AReGRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHGTHQQLLA 1258
Cdd:PRK13537 164 EPTTGLDPQARHLMWERLRSllAR-GKTILLTTHFMEEAERlCDRLCVIEEGRKIAEGAPHALIE 227
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1046-1246 |
2.21e-20 |
|
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: 96.43 E-value: 2.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1046 VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFY--DPMAGSVLLDGQEAKKLNVQWL-RAQLGIVSQEPILF-DC 1121
Cdd:TIGR02633 14 VKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYphGTWDGEIYWSGSPLKASNIRDTeRAGIVIIHQELTLVpEL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1122 SIAENIAYGD----NSRVVPHDEIVRAAKEANIHPFIETLPqkyNTR-VGDKGtqlsGGQKQRIAIARALIRQPRVLLLD 1196
Cdd:TIGR02633 94 SVAENIFLGNeitlPGGRMAYNAMYLRAKNLLRELQLDADN---VTRpVGDYG----GGQQQLVEIAKALNKQARLLILD 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 338817954 1197 EATSAL-DTESEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVIENGK 1246
Cdd:TIGR02633 167 EPSSSLtEKETEILLDIIRDLKAHGVACVYISHKLNEVKAvCDTICVIRDGQ 218
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
1037-1256 |
2.47e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 93.23 E-value: 2.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1037 VFNYPTRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSV-----------------------LLD 1093
Cdd:PRK13651 11 IFNKKLPTELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknkkktkekekvleklVIQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1094 GQEAKKL-NVQWLRAQLGIVSQ--EPILFDCSIAENIAYGDNSRVVPHDEIVRAAKEanihpFIET--LPQKYNTRvgdK 1168
Cdd:PRK13651 91 KTRFKKIkKIKEIRRRVGVVFQfaEYQLFEQTIEKDIIFGPVSMGVSKEEAKKRAAK-----YIELvgLDESYLQR---S 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1169 GTQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEALDKA-REGRTCIVIAHRL-STIQNADLIVVIENGK 1246
Cdd:PRK13651 163 PFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLnKQGKTIILVTHDLdNVLEWTKRTIFFKDGK 242
|
250
....*....|.
gi 338817954 1247 -VKEHGTHQQL 1256
Cdd:PRK13651 243 iIKDGDTYDIL 253
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
406-603 |
2.54e-20 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 96.15 E-value: 2.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 406 IKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYdPT---EGKISIDGQDIRNFNVR-CLREIIGVVSQEPVLFST 481
Cdd:PRK13549 18 VKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHgtyEGEIIFEGEELQASNIRdTERAGIAIIHQELALVKE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 482 -TIAENIRYGRGNVTMDEIEKAVKEANAYDFIMKLpqKFDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEATSAL 560
Cdd:PRK13549 97 lSVLENIFLGNEITPGGIMDYDAMYLRAQKLLAQL--KLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDEPTASL 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 338817954 561 dTESEAEVQAAL--DKAREGRTTIVIAHRLSTIRN-ADVIAGFEDG 603
Cdd:PRK13549 175 -TESETAVLLDIirDLKAHGIACIYISHKLNEVKAiSDTICVIRDG 219
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
408-620 |
3.47e-20 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 91.97 E-value: 3.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 408 ILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLREIIGVVSQEPVL-FSTTIAEN 486
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTpGDITVQEL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 487 IRYGRG------NVTMDEIEKAVKEANAYDFIMKLP-QKFDTlvgdrgaqLSGGQKQRIAIARALVRNPKILLLDEATSA 559
Cdd:PRK10253 102 VARGRYphqplfTRWRKEDEEAVTKAMQATGITHLAdQSVDT--------LSGGQRQRAWIAMVLAQETAIMLLDEPTTW 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 338817954 560 LDTESEAEVQAALDK--AREGRTTIVIAHRLS-TIRNADVIAGFEDGVIVEQGSHSELMKKEGI 620
Cdd:PRK10253 174 LDISHQIDLLELLSElnREKGYTLAAVLHDLNqACRYASHLIALREGKIVAQGAPKEIVTAELI 237
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
399-555 |
4.02e-20 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 90.86 E-value: 4.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 399 SYPSRaniKILKGLNLKVKSGQTVALVGNSGCGKSTT----VQLLQrlydPTEGKISIDGQDIRNF--NVRClREIIGVV 472
Cdd:COG1137 12 SYGKR---TVVKDVSLEVNQGEIVGLLGPNGAGKTTTfymiVGLVK----PDSGRIFLDGEDITHLpmHKRA-RLGIGYL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 473 SQEPVLF-STTIAENIRygrgnvtmdeiekAVKEanaydfIMKLP-----QKFDTLVGD---------RGAQLSGGQKQR 537
Cdd:COG1137 84 PQEASIFrKLTVEDNIL-------------AVLE------LRKLSkkereERLEELLEEfgithlrksKAYSLSGGERRR 144
|
170
....*....|....*...
gi 338817954 538 IAIARALVRNPKILLLDE 555
Cdd:COG1137 145 VEIARALATNPKFILLDE 162
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
391-617 |
4.06e-20 |
|
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: 89.89 E-value: 4.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 391 LEFSDVHFSypsRANIKILKGLNLKVKSGQTVALVGNSGCGKSTtvqLLQRL-----YDPTEGKISIDGQDIRNFNV--R 463
Cdd:cd03217 1 LEIKDLHVS---VGGKEILKGVNLTIKKGEVHALMGPNGSGKST---LAKTImghpkYEVTEGEILFKGEDITDLPPeeR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 464 ClREIIGVVSQEPVLFS-TTIAENIRYgrgnvtmdeiekaVKEAnaydfimklpqkfdtlvgdrgaqLSGGQKQRIAIAR 542
Cdd:cd03217 75 A-RLGIFLAFQYPPEIPgVKNADFLRY-------------VNEG-----------------------FSGGEKKRNEILQ 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 543 ALVRNPKILLLDEATSALDTESEAEVQAALDKAR-EGRTTIVIAH--RLSTIRNADVIAGFEDGVIVEQGSHS---ELMK 616
Cdd:cd03217 118 LLLLEPDLAILDEPDSGLDIDALRLVAEVINKLReEGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVKSGDKElalEIEK 197
|
.
gi 338817954 617 K 617
Cdd:cd03217 198 K 198
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
708-965 |
4.60e-20 |
|
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: 92.11 E-value: 4.60e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 708 FVVGTVCAIANGALQPAFSIILSEMIaifgpgdDAVKQQKCNMFSLVFL-GLGVLSFFTFFLQGFTFGKAGEILTTRLRS 786
Cdd:cd18551 1 LILALLLSLLGTAASLAQPLLVKNLI-------DALSAGGSSGGLLALLvALFLLQAVLSALSSYLLGRTGERVVLDLRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 787 MAFKAMLRQDMSWFDdhKNSTGALSTRLATDAAQVQgatgtrlALIAQNTANLGTGII-------ISFIYGWQLTLLLLS 859
Cdd:cd18551 74 RLWRRLLRLPVSFFD--RRRSGDLVSRVTNDTTLLR-------ELITSGLPQLVTGVLtvvgavvLMFLLDWVLTLVTLA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 860 VVPFIAVAGIVEMKMLAGNAKRDKKEMEAAGKIATEAIENIRTVVSLTQERKFESMYVEKLHGPYRNSVRKAHIYGITFS 939
Cdd:cd18551 145 VVPLAFLIILPLGRRIRKASKRAQDALGELSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAKIEALIGP 224
|
250 260
....*....|....*....|....*.
gi 338817954 940 ISQAFMYFSYAGCFRFGSYLIVNGHM 965
Cdd:cd18551 225 LMGLAVQLALLVVLGVGGARVASGAL 250
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
1030-1260 |
4.68e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 92.15 E-value: 4.68e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1030 SVTFNEVVFNYP--TRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDG----QEAKKLNVQ 1103
Cdd:PRK13646 2 TIRFDNVSYTYQkgTPYEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDititHKTKDKYIR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1104 WLRAQLGIVSQ--EPILFDCSIAENIAYG--------DNSRVVPHDEIVRAAKEANI---HPFietlpqkyntrvgdkgt 1170
Cdd:PRK13646 82 PVRKRIGMVFQfpESQLFEDTVEREIIFGpknfkmnlDEVKNYAHRLLMDLGFSRDVmsqSPF----------------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1171 QLSGGQKQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEALDKAR--EGRTCIVIAHRLSTI-QNADLIVVIENGKV 1247
Cdd:PRK13646 145 QMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtdENKTIILVSHDMNEVaRYADEVIVMKEGSI 224
|
250
....*....|...
gi 338817954 1248 KEHGTHQQLLAQK 1260
Cdd:PRK13646 225 VSQTSPKELFKDK 237
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
1027-1258 |
5.00e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 91.70 E-value: 5.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1027 FEGSVTFNEVVFNYPTRAnvpvlqglslevkkgqTLALVGSSGCGKSTVVQLLERFYDPMAG-----SVLLDGQEA-KKL 1100
Cdd:PRK14271 31 FAGKTVLDQVSMGFPARA----------------VTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIfNYR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1101 NVQWLRAQLGIVSQEPILFDCSIAENIAYGDNS-RVVPHDEIvRAAKEANIHPFieTLPQKYNTRVGDKGTQLSGGQKQR 1179
Cdd:PRK14271 95 DVLEFRRRVGMLFQRPNPFPMSIMDNVLAGVRAhKLVPRKEF-RGVAQARLTEV--GLWDAVKDRLSDSPFRLSGGQQQL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1180 IAIARALIRQPRVLLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHGTHQQLLA 1258
Cdd:PRK14271 172 LCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARiSDRAALFFDGRLVEEGPTEQLFS 251
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
391-620 |
5.17e-20 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 95.12 E-value: 5.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 391 LEFSDVHFSYpsrANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLREI-I 469
Cdd:PRK15439 12 LCARSISKQY---SGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLgI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 470 GVVSQEPVLF-STTIAENIRYG--RGNVTMDEIEKAVKEANAYdfiMKLPQKFDTL-VGDRgaqlsggqkQRIAIARALV 545
Cdd:PRK15439 89 YLVPQEPLLFpNLSVKENILFGlpKRQASMQKMKQLLAALGCQ---LDLDSSAGSLeVADR---------QIVEILRGLM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 546 RNPKILLLDEATSALdTESEAE-----VQAALDKareGRTTIVIAHRLSTIRN-ADVIAGFEDGVIVEQGSHSELMKKEG 619
Cdd:PRK15439 157 RDSRILILDEPTASL-TPAETErlfsrIRELLAQ---GVGIVFISHKLPEIRQlADRISVMRDGTIALSGKTADLSTDDI 232
|
.
gi 338817954 620 I 620
Cdd:PRK15439 233 I 233
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
1031-1229 |
6.35e-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: 87.98 E-value: 6.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1031 VTFNEVVFNypTRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGqeakklnvqwlRAQLG 1110
Cdd:cd03223 1 IELENLSLA--TPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPE-----------GEDLL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1111 IVSQEPILFDCSIAENIAYgdnsrvvPHDEIvraakeanihpfietlpqkyntrvgdkgtqLSGGQKQRIAIARALIRQP 1190
Cdd:cd03223 68 FLPQRPYLPLGTLREQLIY-------PWDDV------------------------------LSGGEQQRLAFARLLLHKP 110
|
170 180 190
....*....|....*....|....*....|....*....
gi 338817954 1191 RVLLLDEATSALDTESEKVVQEALDKarEGRTCIVIAHR 1229
Cdd:cd03223 111 KFVFLDEATSALDEESEDRLYQLLKE--LGITVISVGHR 147
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1047-1259 |
7.39e-20 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 94.77 E-value: 7.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1047 PVLQGLSLEVKKGQTLALVGSSGCGKS-TVVQLLERFYDP----MAGSVLLDGQEAKKLNVQWLRA----QLGIVSQEPI 1117
Cdd:PRK15134 23 TVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFHGESLLHASEQTLRGvrgnKIAMIFQEPM 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1118 L-------FDCSIAENIAYGDNSRVVP-HDEIVRAAKEANIHpfietlpqKYNTRVGDKGTQLSGGQKQRIAIARALIRQ 1189
Cdd:PRK15134 103 VslnplhtLEKQLYEVLSLHRGMRREAaRGEILNCLDRVGIR--------QAAKRLTDYPHQLSGGERQRVMIAMALLTR 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 338817954 1190 PRVLLLDEATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTI-QNADLIVVIENGKVKEHGTHQQLLAQ 1259
Cdd:PRK15134 175 PELLIADEPTTALDVSVQAQILQLLRELQQelNMGLLFITHNLSIVrKLADRVAVMQNGRCVEQNRAATLFSA 247
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
391-618 |
7.51e-20 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 92.59 E-value: 7.51e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 391 LEFSDVHFSYPSRAnikILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNfNVRCLREIIG 470
Cdd:PRK13536 42 IDLAGVSKSYGDKA---VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA-RARLARARIG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 471 VVSQEPVL-FSTTIAEN-IRYGR-GNVTMDEIEKAVkeANAYDFiMKLPQKFDTLVgdrgAQLSGGQKQRIAIARALVRN 547
Cdd:PRK13536 118 VVPQFDNLdLEFTVRENlLVFGRyFGMSTREIEAVI--PSLLEF-ARLESKADARV----SDLSGGMKRRLTLARALIND 190
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 338817954 548 PKILLLDEATSALDTESEAEVQAALDK--AReGRTTIVIAHRLSTI-RNADVIAGFEDGVIVEQGSHSELMKKE 618
Cdd:PRK13536 191 PQLLILDEPTTGLDPHARHLIWERLRSllAR-GKTILLTTHFMEEAeRLCDRLCVLEAGRKIAEGRPHALIDEH 263
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1048-1231 |
7.79e-20 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 89.87 E-value: 7.79e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1048 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQW---LRAQ-LGIVSQ-EPILFDCS 1122
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAkaeLRNQkLGFIYQfHHLLPDFT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1123 IAENIAYGDNSRVVPHDEIVRAAKEANIHPFIETlpqkyntRVGDKGTQLSGGQKQRIAIARALIRQPRVLLLDEATSAL 1202
Cdd:PRK11629 104 ALENVAMPLLIGKKKPAEINSRALEMLAAVGLEH-------RANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNL 176
|
170 180 190
....*....|....*....|....*....|.
gi 338817954 1203 DTESEKVVQEALDK--AREGRTCIVIAHRLS 1231
Cdd:PRK11629 177 DARNADSIFQLLGElnRLQGTAFLVVTHDLQ 207
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
1052-1259 |
1.14e-19 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 90.28 E-value: 1.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1052 LSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQWlRAQLgI--VSQEPilfdcsiaeNIAY 1129
Cdd:COG4167 32 VSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDYKY-RCKH-IrmIFQDP---------NTSL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1130 GDNSRV-----VP---HDEIVRAAKEANIhpfIETLpqkynTRVG-------DKGTQLSGGQKQRIAIARALIRQPRVLL 1194
Cdd:COG4167 101 NPRLNIgqileEPlrlNTDLTAEEREERI---FATL-----RLVGllpehanFYPHMLSSGQKQRVALARALILQPKIII 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 338817954 1195 LDEATSALD--TESEKV-----VQEaldkaREGRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHGTHQQLLAQ 1259
Cdd:COG4167 173 ADEALAALDmsVRSQIInlmleLQE-----KLGISYIYVSQHLGIVKHiSDKVLVMHQGEVVEYGKTAEVFAN 240
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
391-586 |
1.16e-19 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 90.14 E-value: 1.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 391 LEFSDVHFSYPSRaniKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRclReiiG 470
Cdd:PRK11248 2 LQISHLYADYGGK---PALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAE--R---G 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 471 VVSQ-EPVLFSTTIAENIRYGrgnVTMDEIEKAVKEANAYDFIMKlpqkfdtlVGDRGA------QLSGGQKQRIAIARA 543
Cdd:PRK11248 74 VVFQnEGLLPWRNVQDNVAFG---LQLAGVEKMQRLEIAHQMLKK--------VGLEGAekryiwQLSGGQRQRVGIARA 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 338817954 544 LVRNPKILLLDEATSALDTESEAEVQAALDK--AREGRTTIVIAH 586
Cdd:PRK11248 143 LAANPQLLLLDEPFGALDAFTREQMQTLLLKlwQETGKQVLLITH 187
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
391-607 |
1.18e-19 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 94.36 E-value: 1.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 391 LEFSDVHFSYPSRaniKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIdGQdirnfNVRclreiIG 470
Cdd:COG0488 316 LELEGLSKSYGDK---TLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GE-----TVK-----IG 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 471 VVSQEPVLF--STTIAENIRYGRGNVTmdeiekavkEANAYDFIMKL---PQKFDTLVGDrgaqLSGGQKQRIAIARALV 545
Cdd:COG0488 382 YFDQHQEELdpDKTVLDELRDGAPGGT---------EQEVRGYLGRFlfsGDDAFKPVGV----LSGGEKARLALAKLLL 448
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 338817954 546 RNPKILLLDEATSALDTESEAEVQAALDkAREGrTTIVIAH-R--LSTIrnADVIAGFEDGVIVE 607
Cdd:COG0488 449 SPPNVLLLDEPTNHLDIETLEALEEALD-DFPG-TVLLVSHdRyfLDRV--ATRILEFEDGGVRE 509
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1031-1250 |
1.75e-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: 1.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1031 VTFNEVVFNYPTRanvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLdGQeakklNVQwlraqLG 1110
Cdd:COG0488 316 LELEGLSKSYGDK---TLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GE-----TVK-----IG 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1111 IVSQEPILFDcsiaeniaygDNSRVVphDEIVRAA---KEANIHPFIETL---PQKYNTRVGDkgtqLSGGQKQRIAIAR 1184
Cdd:COG0488 382 YFDQHQEELD----------PDKTVL--DELRDGApggTEQEVRGYLGRFlfsGDDAFKPVGV----LSGGEKARLALAK 445
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 338817954 1185 ALIRQPRVLLLDEATSALDTESEKVVQEALDkAREGrTCIVIAH-R--LSTIqnADLIVVIENGKVKEH 1250
Cdd:COG0488 446 LLLSPPNVLLLDEPTNHLDIETLEALEEALD-DFPG-TVLLVSHdRyfLDRV--ATRILEFEDGGVREY 510
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1046-1247 |
1.84e-19 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 94.41 E-value: 1.84e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1046 VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQWL----RAQLGIVSQE-PILFD 1120
Cdd:PRK10535 21 VEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALaqlrREHFGFIFQRyHLLSH 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1121 CSIAENIAygdnsrvVP--HDEIVRAAKEANIHPFIETLpqKYNTRVGDKGTQLSGGQKQRIAIARALIRQPRVLLLDEA 1198
Cdd:PRK10535 101 LTAAQNVE-------VPavYAGLERKQRLLRAQELLQRL--GLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEP 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 338817954 1199 TSALDTESEKVVQEALDKARE-GRTCIVIAHRLSTIQNADLIVVIENGKV 1247
Cdd:PRK10535 172 TGALDSHSGEEVMAILHQLRDrGHTVIIVTHDPQVAAQAERVIEIRDGEI 221
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
391-591 |
1.86e-19 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 93.53 E-value: 1.86e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 391 LEFSDVHFSYPSranIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDiRNFN-VRCLREI- 468
Cdd:PRK10762 5 LQLKGIDKAFPG---VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKE-VTFNgPKSSQEAg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 469 IGVVSQEPVLFST-TIAENIRYGRGNVT-MDEIE--KAVKEANAYDFIMKLPQKFDTLVGDrgaqLSGGQKQRIAIARAL 544
Cdd:PRK10762 81 IGIIHQELNLIPQlTIAENIFLGREFVNrFGRIDwkKMYAEADKLLARLNLRFSSDKLVGE----LSIGEQQMVEIAKVL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 338817954 545 VRNPKILLLDEATSAL-DTESEA------EVQAaldkarEGRTTIVIAHRLSTI 591
Cdd:PRK10762 157 SFESKVIIMDEPTDALtDTETESlfrvirELKS------QGRGIVYISHRLKEI 204
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1030-1251 |
2.14e-19 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 91.63 E-value: 2.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1030 SVTFNEVVFNYptrANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQ-----EAKKLNVqw 1104
Cdd:PRK11000 3 SVTLRNVTKAY---GDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKrmndvPPAERGV-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1105 lraqlGIVSQEPILF-DCSIAENIAYG----------DNSRVVPHDEIVRAAKeanihpFIETLPQkyntrvgdkgtQLS 1173
Cdd:PRK11000 78 -----GMVFQSYALYpHLSVAENMSFGlklagakkeeINQRVNQVAEVLQLAH------LLDRKPK-----------ALS 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1174 GGQKQRIAIARALIRQPRVLLLDEATSALDTESEkvVQEALDKA----REGRTCIVIAH-RLSTIQNADLIVVIENGKVK 1248
Cdd:PRK11000 136 GGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALR--VQMRIEISrlhkRLGRTMIYVTHdQVEAMTLADKIVVLDAGRVA 213
|
...
gi 338817954 1249 EHG 1251
Cdd:PRK11000 214 QVG 216
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1044-1259 |
2.50e-19 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 90.17 E-value: 2.50e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1044 ANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNvqwlRAQLGIVSQEPILF-DCS 1122
Cdd:COG4152 12 GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPED----RRRIGYLPEERGLYpKMK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1123 IAENIAY-----GdnsrvVPHDEIVRAAKEanihpFIET--LPQKYNTRVGDkgtqLSGGQKQRIAIARALIRQPRVLLL 1195
Cdd:COG4152 88 VGEQLVYlarlkG-----LSKAEAKRRADE-----WLERlgLGDRANKKVEE----LSKGNQQKVQLIAALLHDPELLIL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 338817954 1196 DEATSALDTES-EKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHGTHQQLLAQ 1259
Cdd:COG4152 154 DEPFSGLDPVNvELLKDVIRELAAKGTTVIFSSHQMELVEElCDRIVIINKGRKVLSGSVDEIRRQ 219
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1048-1247 |
3.16e-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: 86.72 E-value: 3.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1048 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNV-QWLRAQLGIVSQEP----ILFDCS 1122
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPrDAIRAGIAYVPEDRkregLVLDLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1123 IAENIAygdnsrvvphdeivraakeanihpfietLPQkyntrvgdkgtQLSGGQKQRIAIARALIRQPRVLLLDEATSAL 1202
Cdd:cd03215 95 VAENIA----------------------------LSS-----------LLSGGNQQKVVLARWLARDPRVLILDEPTRGV 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 338817954 1203 DTES-EKVVQEALDKAREGRTCIVIahrlST-----IQNADLIVVIENGKV 1247
Cdd:cd03215 136 DVGAkAEIYRLIRELADAGKAVLLI----SSeldelLGLCDRILVMYEGRI 182
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1047-1253 |
4.69e-19 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 90.28 E-value: 4.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1047 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSV-LLDGQEAKKlnVQWLRAQLGIVSQepilFD----- 1120
Cdd:PRK13536 55 AVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKItVLGVPVPAR--ARLARARIGVVPQ----FDnldle 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1121 CSIAEN-IAYGDNSRVVPHDeivraaKEANIHPFIE--TLPQKYNTRVGDkgtqLSGGQKQRIAIARALIRQPRVLLLDE 1197
Cdd:PRK13536 129 FTVRENlLVFGRYFGMSTRE------IEAVIPSLLEfaRLESKADARVSD----LSGGMKRRLTLARALINDPQLLILDE 198
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1198 ATSALDTESEKVVQEALDK--AReGRTCIVIAHRLSTIQN-ADLIVVIENG-KVKEHGTH 1253
Cdd:PRK13536 199 PTTGLDPHARHLIWERLRSllAR-GKTILLTTHFMEEAERlCDRLCVLEAGrKIAEGRPH 257
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
1049-1256 |
5.39e-19 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 87.04 E-value: 5.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1049 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKlNVQWLRAQLGIVSQEPILFDCSIA-ENI 1127
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREVRRRIGIVFQDLSVDDELTGwENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1128 A-----YGdnsrvVPHDEivRAAKEANIHPFIEtLPQKYNTRVGdkgtQLSGGQKQRIAIARALIRQPRVLLLDEATSAL 1202
Cdd:cd03265 95 YiharlYG-----VPGAE--RRERIDELLDFVG-LLEAADRLVK----TYSGGMRRRLEIARSLVHRPEVLFLDEPTIGL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 338817954 1203 DTESEKVVQEALDK--AREGRTCIVIAHRLSTI-QNADLIVVIENGKVKEHGTHQQL 1256
Cdd:cd03265 163 DPQTRAHVWEYIEKlkEEFGMTILLTTHYMEEAeQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1046-1259 |
5.54e-19 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 91.90 E-value: 5.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1046 VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQ-WLRAQLGIVSQEPILF-DCSI 1123
Cdd:PRK11288 17 VKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTaALAAGVAIIYQELHLVpEMTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1124 AENIAYGD--NSR-VVPHDEIVRAAKEANIHPFIETLPqkyNTRVGDkgtqLSGGQKQRIAIARALIRQPRVLLLDEATS 1200
Cdd:PRK11288 97 AENLYLGQlpHKGgIVNRRLLNYEAREQLEHLGVDIDP---DTPLKY----LSIGQRQMVEIAKALARNARVIAFDEPTS 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1201 ALDT-ESE---KVVQEALDkarEGRTCIVIAHRLSTI-QNADLIVVIENG-KVKEHG-----THQQLLAQ 1259
Cdd:PRK11288 170 SLSArEIEqlfRVIRELRA---EGRVILYVSHRMEEIfALCDAITVFKDGrYVATFDdmaqvDRDQLVQA 236
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
403-615 |
5.61e-19 |
|
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: 92.17 E-value: 5.61e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 403 RANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKIS-------IDGQDIRNFNVRCLREIIGVVSQE 475
Cdd:TIGR03269 294 RGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNvrvgdewVDMTKPGPDGRGRAKRYIGILHQE 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 476 PVLFS-TTIAENIRYGRGNVTMDEI--EKAV--------KEANAYDFIMKLPQkfdtlvgdrgaQLSGGQKQRIAIARAL 544
Cdd:TIGR03269 374 YDLYPhRTVLDNLTEAIGLELPDELarMKAVitlkmvgfDEEKAEEILDKYPD-----------ELSEGERHRVALAQVL 442
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 338817954 545 VRNPKILLLDEATSALDTESEAEVQAALDKARE--GRTTIVIAHRLSTIRN-ADVIAGFEDGVIVEQGSHSELM 615
Cdd:TIGR03269 443 IKEPRIVILDEPTGTMDPITKVDVTHSILKAREemEQTFIIVSHDMDFVLDvCDRAALMRDGKIVKIGDPEEIV 516
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
406-561 |
5.94e-19 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 87.14 E-value: 5.94e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 406 IKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVR---CLR-EIIGVVSQEPVLFST 481
Cdd:PRK10584 23 LSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEaraKLRaKHVGFVFQSFMLIPT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 482 TIA-ENIRYG---RGNVTMDEIEKAVKEANAydfiMKLPQKFDTLvgdrGAQLSGGQKQRIAIARALVRNPKILLLDEAT 557
Cdd:PRK10584 103 LNAlENVELPallRGESSRQSRNGAKALLEQ----LGLGKRLDHL----PAQLSGGEQQRVALARAFNGRPDVLFADEPT 174
|
....
gi 338817954 558 SALD 561
Cdd:PRK10584 175 GNLD 178
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
391-607 |
1.00e-18 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 91.13 E-value: 1.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 391 LEFSDVHFSYPSranIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVR-CLREII 469
Cdd:PRK11288 5 LSFDGIGKTFPG---VKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTaALAAGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 470 GVVSQE----PVLfstTIAENIRYGRGNVTMDEIEKAVKEANAYDFIMKLPQKFD--TLVGDrgaqLSGGQKQRIAIARA 543
Cdd:PRK11288 82 AIIYQElhlvPEM---TVAENLYLGQLPHKGGIVNRRLLNYEAREQLEHLGVDIDpdTPLKY----LSIGQRQMVEIAKA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 338817954 544 LVRNPKILLLDEATSALdTESEAEVQAALDKA--REGRTTIVIAHRLSTI-RNADVIAGFEDGVIVE 607
Cdd:PRK11288 155 LARNARVIAFDEPTSSL-SAREIEQLFRVIRElrAEGRVILYVSHRMEEIfALCDAITVFKDGRYVA 220
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
391-618 |
1.11e-18 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 88.32 E-value: 1.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 391 LEFSDVHFSYPSRAnikILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNfNVRCLREIIG 470
Cdd:PRK13537 8 IDFRNVEKRYGDKL---VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPS-RARHARQRVG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 471 VVSQ----EPvlfSTTIAENIR-YGRG-NVTMDEIEKAVkeANAYDFiMKLPQKFDTLVGDrgaqLSGGQKQRIAIARAL 544
Cdd:PRK13537 84 VVPQfdnlDP---DFTVRENLLvFGRYfGLSAAAARALV--PPLLEF-AKLENKADAKVGE----LSGGMKRRLTLARAL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 338817954 545 VRNPKILLLDEATSALDTESEAEVQAALDK--AReGRTTIVIAHRLSTI-RNADVIAGFEDGVIVEQGSHSELMKKE 618
Cdd:PRK13537 154 VNDPDVLVLDEPTTGLDPQARHLMWERLRSllAR-GKTILLTTHFMEEAeRLCDRLCVIEEGRKIAEGAPHALIESE 229
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
389-645 |
1.19e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 87.76 E-value: 1.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 389 GNLEFSDVHFSYPSRA--NIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEG-------KISIDGQDIRN 459
Cdd:PRK13645 5 KDIILDNVSYTYAKKTpfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGqtivgdyAIPANLKKIKE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 460 fnVRCLREIIGVVSQEP--VLFSTTIAENIRYGRGNVTMDEiEKAVKEANAYDFIMKLPQKFdtlVGDRGAQLSGGQKQR 537
Cdd:PRK13645 85 --VKRLRKEIGLVFQFPeyQLFQETIEKDIAFGPVNLGENK-QEAYKKVPELLKLVQLPEDY---VKRSPFELSGGQKRR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 538 IAIARALVRNPKILLLDEATSALDTESEAEVQAALDK--AREGRTTIVIAHRLSTI-RNADVIAGFEDGVIVEQG----- 609
Cdd:PRK13645 159 VALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERlnKEYKKRIIMVTHNMDQVlRIADEVIVMHEGKVISIGspfei 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 338817954 610 -SHSELMKKEGI-----YFRLVNMQTAGSQILS------EEFEVELSD 645
Cdd:PRK13645 239 fSNQELLTKIEIdppklYQLMYKLKNKGIDLLNknirtiEEFAKELAK 286
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1049-1253 |
1.23e-18 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 86.08 E-value: 1.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1049 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLN---VQWLRAQLGIVSQEP-ILFDCSIA 1124
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKnreVPFLRRQIGMIFQDHhLLMDRTVY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1125 ENIAygdnsrvVPHdeIVRAAKEANIHPFIETLPQKyntrVG--DKG----TQLSGGQKQRIAIARALIRQPRVLLLDEA 1198
Cdd:PRK10908 98 DNVA-------IPL--IIAGASGDDIRRRVSAALDK----VGllDKAknfpIQLSGGEQQRVGIARAVVNKPAVLLADEP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 338817954 1199 TSALDTE-SEKVVQEALDKAREGRTCIVIAHRLSTIQNADL-IVVIENGKVkeHGTH 1253
Cdd:PRK10908 165 TGNLDDAlSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYrMLTLSDGHL--HGGV 219
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
391-609 |
1.54e-18 |
|
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: 85.41 E-value: 1.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 391 LEFSDVHFSYpsrANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNvrclREIIG 470
Cdd:cd03269 1 LEVENVTKRF---GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA----RNRIG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 471 VVSQEPVLF-STTIAENIRY-GRgnvtmdeiEKAVKEANAYDFIMKLPQKFDtlVGD----RGAQLSGGQKQRIAIARAL 544
Cdd:cd03269 74 YLPEERGLYpKMKVIDQLVYlAQ--------LKGLKKEEARRRIDEWLERLE--LSEyankRVEELSKGNQQKVQFIAAV 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 338817954 545 VRNPKILLLDEATSALDTESeAEV--QAALDKAREGRTTIVIAHRLSTI-RNADVIAGFEDGVIVEQG 609
Cdd:cd03269 144 IHDPELLILDEPFSGLDPVN-VELlkDVIRELARAGKTVILSTHQMELVeELCDRVLLLNKGRAVLYG 210
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
1046-1249 |
1.63e-18 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 90.62 E-value: 1.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1046 VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYdP---MAGSVLLDGQEAKKLNvqwLRA--QLGIV--SQE--- 1115
Cdd:NF040905 14 VKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PhgsYEGEILFDGEVCRFKD---IRDseALGIViiHQElal 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1116 -PILfdcSIAENIAYGdNSR----VVPHDEIVRAAKE------ANIHPfietlpqkyNTRVGDKGTqlsgGQKQRIAIAR 1184
Cdd:NF040905 90 iPYL---SIAENIFLG-NERakrgVIDWNETNRRAREllakvgLDESP---------DTLVTDIGV----GKQQLVEIAK 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 338817954 1185 ALIRQPRVLLLDEATSAL-DTESEKVVQEALDKAREGRTCIVIAHRLSTI-QNADLIVVIENGKVKE 1249
Cdd:NF040905 153 ALSKDVKLLILDEPTAALnEEDSAALLDLLLELKAQGITSIIISHKLNEIrRVADSITVLRDGRTIE 219
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
391-652 |
1.64e-18 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 87.47 E-value: 1.64e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 391 LEFSDVHFSYpsrANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRnfnvRCLREIIG 470
Cdd:COG4152 2 LELKGLTKRF---GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLD----PEDRRRIG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 471 VVSQEPVLF-STTIAENIRY-GR--GnVTMDEIEKAVKEanaydfimkLPQKFDtlVGDRGA----QLSGGQKQRIAIAR 542
Cdd:COG4152 75 YLPEERGLYpKMKVGEQLVYlARlkG-LSKAEAKRRADE---------WLERLG--LGDRANkkveELSKGNQQKVQLIA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 543 ALVRNPKILLLDEATSALDTESeAEV--QAALDKAREGRTTIVIAHRLSTI-RNADVIAGFEDGVIVEQGSHSELMKKEG 619
Cdd:COG4152 143 ALLHDPELLILDEPFSGLDPVN-VELlkDVIRELAAKGTTVIFSSHQMELVeELCDRIVIINKGRKVLSGSVDEIRRQFG 221
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 338817954 620 IYFRLVNMQTAGSQILS-----------EEFEVELSDEKAAGDV 652
Cdd:COG4152 222 RNTLRLEADGDAGWLRAlpgvtvveedgDGAELKLEDGADAQEL 265
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
394-614 |
1.82e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 87.07 E-value: 1.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 394 SDVHFSYPSRANIKILKGLNLKVKSGQT---------VALVGNSGCGKSTTVQLLQRLYDPTEG-----KISIDGQDIRN 459
Cdd:PRK14271 13 ADVDAAAPAMAAVNLTLGFAGKTVLDQVsmgfparavTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 460 F-NVRCLREIIGVVSQEPVLFSTTIAENIRYG-RGNVTMDEIE-KAVKEANAYDfiMKLPQKFDTLVGDRGAQLSGGQKQ 536
Cdd:PRK14271 93 YrDVLEFRRRVGMLFQRPNPFPMSIMDNVLAGvRAHKLVPRKEfRGVAQARLTE--VGLWDAVKDRLSDSPFRLSGGQQQ 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 338817954 537 RIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLS-TIRNADVIAGFEDGVIVEQGSHSEL 614
Cdd:PRK14271 171 LLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAqAARISDRAALFFDGRLVEEGPTEQL 249
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
100-339 |
1.93e-18 |
|
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: 87.47 E-value: 1.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 100 LNPGRILEEEMTRYAYYYSGLGGGVLVAAYIQvSFWTLAAGRQI-KKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDDV 178
Cdd:cd18541 29 LTAGTLTASQLLRYALLILLLALLIGIFRFLW-RYLIFGASRRIeYDLRNDLFAHLLTLSPSFYQKNRTGDLMARATNDL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 179 SKISEGIGDKVGMFFQAIATFFAGFIVGFIRGWKLTLVIMAISPILGLSTAVWAKI-----------LSTFSDKelaaya 247
Cdd:cd18541 108 NAVRMALGPGILYLVDALFLGVLVLVMMFTISPKLTLIALLPLPLLALLVYRLGKKihkrfrkvqeaFSDLSDR------ 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 248 kagavAEEALGAIRTVIAFGGQNKELERYQKHLENAKKIGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTI 327
Cdd:cd18541 182 -----VQESFSGIRVIKAFVQEEAEIERFDKLNEEYVEKNLRLARVDALFFPLIGLLIGLSFLIVLWYGGRLVIRGTITL 256
|
250
....*....|....
gi 338817954 328 GN--AMTVFFSILI 339
Cdd:cd18541 257 GDlvAFNSYLGMLI 270
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
391-620 |
3.16e-18 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 85.32 E-value: 3.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 391 LEFSDVHFSYpsrANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNF-NVRCLREII 469
Cdd:PRK11614 6 LSFDKVSAHY---GKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWqTAKIMREAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 470 GVVSQEPVLFS-TTIAENIRYGRGNVTMDEIEKAVKEAnaYDFIMKLPQKfdtlVGDRGAQLSGGQKQRIAIARALVRNP 548
Cdd:PRK11614 83 AIVPEGRRVFSrMTVEENLAMGGFFAERDQFQERIKWV--YELFPRLHER----RIQRAGTMSGGEQQMLAIGRALMSQP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 338817954 549 KILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLS--TIRNADVIAGFEDGVIVEQGSHSELMKKEGI 620
Cdd:PRK11614 157 RLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNAnqALKLADRGYVLENGHVVLEDTGDALLANEAV 230
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
1051-1256 |
3.20e-18 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 87.45 E-value: 3.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1051 GLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLN-VQWL--RAQLGIVSQEPILF---DCSIA 1124
Cdd:PRK15079 39 GVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKdDEWRavRSDIQMIFQDPLASlnpRMTIG 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1125 ENIA------YGDNSRVVPHDEIVRAAKEANIHP-FIETLPQKYntrvgdkgtqlSGGQKQRIAIARALIRQPRVLLLDE 1197
Cdd:PRK15079 119 EIIAeplrtyHPKLSRQEVKDRVKAMMLKVGLLPnLINRYPHEF-----------SGGQCQRIGIARALILEPKLIICDE 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 338817954 1198 ATSALDTESE-KVVQEALDKARE-GRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHGTHQQL 1256
Cdd:PRK15079 188 PVSALDVSIQaQVVNLLQQLQREmGLSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEV 249
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1047-1197 |
4.40e-18 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 85.08 E-value: 4.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1047 PVLQGLSLEVKKGQTLALVGSSGCGKSTVvqllerFY------DPMAGSVLLDGQEAKKLNVqWLRAQLGI--VSQEPIL 1118
Cdd:COG1137 17 TVVKDVSLEVNQGEIVGLLGPNGAGKTTT------FYmivglvKPDSGRIFLDGEDITHLPM-HKRARLGIgyLPQEASI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1119 F-DCSIAENIaygdnsRVVPhdEIVRAAKEAnIHPFIETLPQKYN-TRVGD-KGTQLSGGQKQRIAIARALIRQPRVLLL 1195
Cdd:COG1137 90 FrKLTVEDNI------LAVL--ELRKLSKKE-REERLEELLEEFGiTHLRKsKAYSLSGGERRRVEIARALATNPKFILL 160
|
..
gi 338817954 1196 DE 1197
Cdd:COG1137 161 DE 162
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1048-1249 |
4.87e-18 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 84.45 E-value: 4.87e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1048 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQW---LRAQ-LGIVSQEPILFDCSI 1123
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEArakLRAKhVGFVFQSFMLIPTLN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1124 A-ENIAY-----GDNSRvVPHDEIVRAAKEANIHPFIETLPqkyntrvgdkgTQLSGGQKQRIAIARALIRQPRVLLLDE 1197
Cdd:PRK10584 105 AlENVELpallrGESSR-QSRNGAKALLEQLGLGKRLDHLP-----------AQLSGGEQQRVALARAFNGRPDVLFADE 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 338817954 1198 ATSALDTES-EKVVQEALDKARE-GRTCIVIAHRLSTIQNADLIVVIENGKVKE 1249
Cdd:PRK10584 173 PTGNLDRQTgDKIADLLFSLNREhGTTLILVTHDLQLAARCDRRLRLVNGQLQE 226
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
409-641 |
5.32e-18 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 89.07 E-value: 5.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 409 LKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLREI-IGVVSQE-PVLFSTTIAEN 486
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLgIGIIYQElSVIDELTVLEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 487 IRYGR------GNVTMDEIEKAVKEANAYDFIMKLPQKFDTLVGDrgaqLSGGQKQRIAIARALVRNPKILLLDEATSAL 560
Cdd:PRK09700 101 LYIGRhltkkvCGVNIIDWREMRVRAAMMLLRVGLKVDLDEKVAN----LSISHKQMLEIAKTLMLDAKVIIMDEPTSSL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 561 DTESEAEVQAALDKAR-EGRTTIVIAHRLSTIRN-ADVIAGFEDGVIVEQGSHSE--------LMKKEGIYFRLVNMQTA 630
Cdd:PRK09700 177 TNKEVDYLFLIMNQLRkEGTAIVYISHKLAEIRRiCDRYTVMKDGSSVCSGMVSDvsnddivrLMVGRELQNRFNAMKEN 256
|
250
....*....|..
gi 338817954 631 GSQILSEE-FEV 641
Cdd:PRK09700 257 VSNLAHETvFEV 268
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
419-609 |
7.44e-18 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 89.14 E-value: 7.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 419 GQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFN---VRCLREIIGVVSQEPV-------LFSTTIAENIR 488
Cdd:PRK10261 350 GETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSpgkLQALRRDIQFIFQDPYasldprqTVGDSIMEPLR 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 489 YgRGNVTMDEIEKAV---------KEANAYDFimklPQKFdtlvgdrgaqlSGGQKQRIAIARALVRNPKILLLDEATSA 559
Cdd:PRK10261 430 V-HGLLPGKAAAARVawllervglLPEHAWRY----PHEF-----------SGGQRQRICIARALALNPKVIIADEAVSA 493
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 338817954 560 LDTESEAE-VQAALDKARE-GRTTIVIAHRLSTI-RNADVIAGFEDGVIVEQG 609
Cdd:PRK10261 494 LDVSIRGQiINLLLDLQRDfGIAYLFISHDMAVVeRISHRVAVMYLGQIVEIG 546
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1049-1256 |
9.12e-18 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 84.68 E-value: 9.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1049 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFY--DPMAGS-VLLDG---QEAKKL--NVQWLRAQLGIVSQEPILFD 1120
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgDKSAGShIELLGrtvQREGRLarDIRKSRANTGYIFQQFNLVN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1121 -CSIAENIAYGDNSRVVPHDEIVRAAKEANIHPFIETLpqkynTRVG------DKGTQLSGGQKQRIAIARALIRQPRVL 1193
Cdd:PRK09984 100 rLSVLENVLIGALGSTPFWRTCFSWFTREQKQRALQAL-----TRVGmvhfahQRVSTLSGGQQQRVAIARALMQQAKVI 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 338817954 1194 LLDEATSALDTESEKVVQEALD--KAREGRTCIVIAHRLS-TIQNADLIVVIENGKVKEHGTHQQL 1256
Cdd:PRK09984 175 LADEPIASLDPESARIVMDTLRdiNQNDGITVVVTLHQVDyALRYCERIVALRQGHVFYDGSSQQF 240
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
403-585 |
9.93e-18 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 83.00 E-value: 9.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 403 RANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLREIIGvvSQEPVLFSTT 482
Cdd:PRK13539 12 RGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHYLG--HRNAMKPALT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 483 IAENIR-----YGRGNVTMDEIEKAVKEANAYDfimkLPQKFdtlvgdrgaqLSGGQKQRIAIARALVRNPKILLLDEAT 557
Cdd:PRK13539 90 VAENLEfwaafLGGEELDIAAALEAVGLAPLAH----LPFGY----------LSAGQKRRVALARLLVSNRPIWILDEPT 155
|
170 180
....*....|....*....|....*...
gi 338817954 558 SALDTESEAEVqAALDKAREGRTTIVIA 585
Cdd:PRK13539 156 AALDAAAVALF-AELIRAHLAQGGIVIA 182
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
408-614 |
1.02e-17 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 88.22 E-value: 1.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 408 ILKGLNLKVKSGQTVALVGNSGCGKS-TTVQLLQRLYDP----TEGKISIDGQDIRNFNVRCLREI----IGVVSQEPVL 478
Cdd:PRK15134 24 VVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFHGESLLHASEQTLRGVrgnkIAMIFQEPMV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 479 -------FSTTIAENIRYGRGnvtMDeiekavKEANAYDFIMKLPQkfdtlVGDRGA---------QLSGGQKQRIAIAR 542
Cdd:PRK15134 104 slnplhtLEKQLYEVLSLHRG---MR------REAARGEILNCLDR-----VGIRQAakrltdyphQLSGGERQRVMIAM 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 338817954 543 ALVRNPKILLLDEATSALDTESEAEVQAALDKARE--GRTTIVIAHRLSTIRN-ADVIAGFEDGVIVEQGSHSEL 614
Cdd:PRK15134 170 ALLTRPELLIADEPTTALDVSVQAQILQLLRELQQelNMGLLFITHNLSIVRKlADRVAVMQNGRCVEQNRAATL 244
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
412-615 |
1.12e-17 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 86.08 E-value: 1.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 412 LNLKVK-----SGQTvALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQ---DIRN-FNVRCLREIIGVVSQEPVLFS-T 481
Cdd:PRK11144 13 LCLTVNltlpaQGIT-AIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRvlfDAEKgICLPPEKRRIGYVFQDARLFPhY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 482 TIAENIRYGrgnvtMDEiekavkeanaydfimKLPQKFDTLVG--------DR-GAQLSGGQKQRIAIARALVRNPKILL 552
Cdd:PRK11144 92 KVRGNLRYG-----MAK---------------SMVAQFDKIVAllgiepllDRyPGSLSGGEKQRVAIGRALLTAPELLL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 338817954 553 LDEATSALDTESEAEVQAALDK-AREGRTTIV-IAHRLSTI-RNADVIAGFEDGVIVEQGS-----HSELM 615
Cdd:PRK11144 152 MDEPLASLDLPRKRELLPYLERlAREINIPILyVSHSLDEIlRLADRVVVLEQGKVKAFGPleevwASSAM 222
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
1048-1251 |
1.14e-17 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 82.57 E-value: 1.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1048 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERF--YDPMAGSVLLDGQEAKKLNVQwLRAQLGI--VSQEPIlfdcsi 1123
Cdd:cd03217 15 ILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPE-ERARLGIflAFQYPP------ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1124 aeniaygdnsrvvphdEI--VRAAKeanihpFIetlpqkyntRVGDKGtqLSGGQKQRIAIARALIRQPRVLLLDEATSA 1201
Cdd:cd03217 88 ----------------EIpgVKNAD------FL---------RYVNEG--FSGGEKKRNEILQLLLLEPDLAILDEPDSG 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 338817954 1202 LDTESEKVVQEALDKAR-EGRTCIVIAH--RLSTIQNADLIVVIENGKVKEHG 1251
Cdd:cd03217 135 LDIDALRLVAEVINKLReEGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVKSG 187
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
1046-1251 |
1.16e-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: 83.35 E-value: 1.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1046 VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQeakklnVQW-LRAQLGIVSQ----EPILFD 1120
Cdd:cd03220 35 FWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGR------VSSlLGLGGGFNPEltgrENIYLN 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1121 CSIaeniaYGdnsrvVPHDEIvrAAKEANIHPFIEtLPQKYNTRVGdkgtQLSGGQKQRIAIARALIRQPRVLLLDEATS 1200
Cdd:cd03220 109 GRL-----LG-----LSRKEI--DEKIDEIIEFSE-LGDFIDLPVK----TYSSGMKARLAFAIATALEPDILLIDEVLA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 338817954 1201 ALDTE-SEKVVQEALDKAREGRTCIVIAHRLSTI-QNADLIVVIENGKVKEHG 1251
Cdd:cd03220 172 VGDAAfQEKCQRRLRELLKQGKTVILVSHDPSSIkRLCDRALVLEKGKIRFDG 224
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
397-609 |
1.24e-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: 83.35 E-value: 1.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 397 HFSYPSRANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQdirnfnVRCLREI-IGVvsqE 475
Cdd:cd03220 26 LGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGR------VSSLLGLgGGF---N 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 476 PVLfstTIAENIRYgRG---NVTMDEIEKavKEANAYDFiMKLPQKFDTLVGdrgaQLSGGQKQRIAIARALVRNPKILL 552
Cdd:cd03220 97 PEL---TGRENIYL-NGrllGLSRKEIDE--KIDEIIEF-SELGDFIDLPVK----TYSSGMKARLAFAIATALEPDILL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 338817954 553 LDEATSALDTESEAEVQAALDKAREGRTTIVIA-HRLSTIRN-ADVIAGFEDGVIVEQG 609
Cdd:cd03220 166 IDEVLAVGDAAFQEKCQRRLRELLKQGKTVILVsHDPSSIKRlCDRALVLEKGKIRFDG 224
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
412-633 |
1.29e-17 |
|
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: 89.30 E-value: 1.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 412 LNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNfNVRCLREIIGVVSQEPVLFS-TTIAENIRYg 490
Cdd:TIGR01257 949 LNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET-NLDAVRQSLGMCPQHNILFHhLTVAEHILF- 1026
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 491 RGNVTMDEIEKAVKEANAYDFIMKLPQKFDtlvgDRGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQA 570
Cdd:TIGR01257 1027 YAQLKGRSWEEAQLEMEAMLEDTGLHHKRN----EEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWD 1102
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 338817954 571 ALDKAREGRTTIVIAHRLStirNADVIAgfEDGVIVEQG----SHSELMKKE----GIYFRLV-NMQTAGSQ 633
Cdd:TIGR01257 1103 LLLKYRSGRTIIMSTHHMD---EADLLG--DRIAIISQGrlycSGTPLFLKNcfgtGFYLTLVrKMKNIQSQ 1169
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1051-1256 |
1.31e-17 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 83.89 E-value: 1.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1051 GLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQWLrAQLGIVS--QEPILF-DCSIAENI 1127
Cdd:PRK11300 23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQI-ARMGVVRtfQHVRLFrEMTVIENL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1128 AygdnsrVVPHDEI--------------VRAAKEA--NIHPFIET--LPQKYNTRVGDkgtqLSGGQKQRIAIARALIRQ 1189
Cdd:PRK11300 102 L------VAQHQQLktglfsgllktpafRRAESEAldRAATWLERvgLLEHANRQAGN----LAYGQQRRLEIARCMVTQ 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1190 PRVLLLDEATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHGTHQQL 1256
Cdd:PRK11300 172 PEILMLDEPAAGLNPKETKELDELIAELRNehNVTVLLIEHDMKLVMGiSDRIYVVNQGTPLANGTPEEI 241
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
408-589 |
2.25e-17 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 82.94 E-value: 2.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 408 ILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLREI----IGVVSQ-EPVLFSTT 482
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELrnqkLGFIYQfHHLLPDFT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 483 IAENirygrgnVTMDEI--EKAVKEANAYDFIMKLPQKFDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEATSAL 560
Cdd:PRK11629 104 ALEN-------VAMPLLigKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNL 176
|
170 180 190
....*....|....*....|....*....|.
gi 338817954 561 DTESEAEVQAALDK--AREGRTTIVIAHRLS 589
Cdd:PRK11629 177 DARNADSIFQLLGElnRLQGTAFLVVTHDLQ 207
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
407-609 |
2.39e-17 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 83.02 E-value: 2.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 407 KILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIR--NFNVRCLREIiGVVSQEPVLFST-TI 483
Cdd:PRK10895 17 RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISllPLHARARRGI-GYLPQEASIFRRlSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 484 AENIrygrgnVTMDEIEKAVKEANAYDFIMKLPQKFDT--LVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEATSALD 561
Cdd:PRK10895 96 YDNL------MAVLQIRDDLSAEQREDRANELMEEFHIehLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVD 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 338817954 562 TESEAEVQAALDKARE-GRTTIVIAHRLStirnaDVIAGFEDGVIVEQG 609
Cdd:PRK10895 170 PISVIDIKRIIEHLRDsGLGVLITDHNVR-----ETLAVCERAYIVSQG 213
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1033-1260 |
2.76e-17 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 86.66 E-value: 2.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1033 FNEVVFNYPTRanvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQeakklnvqwlrAQLGIV 1112
Cdd:COG0488 1 LENLSKSFGGR---PLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKG-----------LRIGYL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1113 SQEPILFD-CSIAENIAYGDNSRVVPHDEIVRA-----------AKEANIHPFIETL-------------------PQKY 1161
Cdd:COG0488 67 PQEPPLDDdLTVLDTVLDGDAELRALEAELEELeaklaepdedlERLAELQEEFEALggweaearaeeilsglgfpEEDL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1162 NTRVGDkgtqLSGGQKQRIAIARALIRQPRVLLLDEATSALDTESekvVQ--EALDKAREGrTCIVIAH-R--LSTIqnA 1236
Cdd:COG0488 147 DRPVSE----LSGGWRRRVALARALLSEPDLLLLDEPTNHLDLES---IEwlEEFLKNYPG-TVLVVSHdRyfLDRV--A 216
|
250 260
....*....|....*....|....*
gi 338817954 1237 DLIVVIENGKVKEH-GTHQQLLAQK 1260
Cdd:COG0488 217 TRILELDRGKLTLYpGNYSAYLEQR 241
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
1027-1259 |
3.37e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 83.52 E-value: 3.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1027 FEGSVTFNEVVFNYPTRA--NVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLdGQEA-----KK 1099
Cdd:PRK13645 3 FSKDIILDNVSYTYAKKTpfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIV-GDYAipanlKK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1100 LN-VQWLRAQLGIVSQEP--ILFDCSIAENIAYGDNSRVVPHDEIVRAAKEAnihPFIETLPQKYNTRvgdKGTQLSGGQ 1176
Cdd:PRK13645 82 IKeVKRLRKEIGLVFQFPeyQLFQETIEKDIAFGPVNLGENKQEAYKKVPEL---LKLVQLPEDYVKR---SPFELSGGQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1177 KQRIAIARALIRQPRVLLLDEATSALDTESEK---VVQEALDKaREGRTCIVIAHRLSTI-QNADLIVVIENGKVKEHG- 1251
Cdd:PRK13645 156 KRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEdfiNLFERLNK-EYKKRIIMVTHNMDQVlRIADEVIVMHEGKVISIGs 234
|
250
....*....|...
gi 338817954 1252 -----THQQLLAQ 1259
Cdd:PRK13645 235 pfeifSNQELLTK 247
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
383-606 |
5.11e-17 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 82.00 E-value: 5.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 383 KPDNIKGNLEfsdvHFSYPSRANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNV 462
Cdd:cd03267 15 KEPGLIGSLK----SLFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 463 RCLREIIGVVSQE-------PVLFSTTIAENIrYgrgNVTMDEIEKAVKEANAydfIMKLPQKFDTLVgdrgAQLSGGQK 535
Cdd:cd03267 91 KFLRRIGVVFGQKtqlwwdlPVIDSFYLLAAI-Y---DLPPARFKKRLDELSE---LLDLEELLDTPV----RQLSLGQR 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 338817954 536 QRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKA-REGRTTIVIahrlsTIRNADVIAGFEDGVIV 606
Cdd:cd03267 160 MRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYnRERGTTVLL-----TSHYMKDIEALARRVLV 226
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1042-1227 |
5.29e-17 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 81.07 E-value: 5.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1042 TRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQWLRAQLGIVSQ-EPILfd 1120
Cdd:PRK13539 11 VRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHYLGHRNAmKPAL-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1121 cSIAENIA-----YGDnsrvvpHDEIVRAAKEA-NIHPfIETLPQKYntrvgdkgtqLSGGQKQRIAIARALIRQPRVLL 1194
Cdd:PRK13539 89 -TVAENLEfwaafLGG------EELDIAAALEAvGLAP-LAHLPFGY----------LSAGQKRRVALARLLVSNRPIWI 150
|
170 180 190
....*....|....*....|....*....|...
gi 338817954 1195 LDEATSALDTESEKVVQEALdKAREGRTCIVIA 1227
Cdd:PRK13539 151 LDEPTAALDAAAVALFAELI-RAHLAQGGIVIA 182
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
391-586 |
5.49e-17 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 79.03 E-value: 5.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 391 LEFSDVHFSYPSRaniKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIdGQDIRnfnvrclreiIG 470
Cdd:cd03221 1 IELENLSKTYGGK---LLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTW-GSTVK----------IG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 471 VVsqepvlfsttiaenirygrgnvtmdeiekavkeanaydfimklpqkfdtlvgdrgAQLSGGQKQRIAIARALVRNPKI 550
Cdd:cd03221 67 YF-------------------------------------------------------EQLSGGEKMRLALAKLLLENPNL 91
|
170 180 190
....*....|....*....|....*....|....*.
gi 338817954 551 LLLDEATSALDTESEAEVQAALdKAREGrTTIVIAH 586
Cdd:cd03221 92 LLLDEPTNHLDLESIEALEEAL-KEYPG-TVILVSH 125
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
406-607 |
5.69e-17 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 85.61 E-value: 5.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 406 IKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYdPT---EGKISIDGQdIRNFnvRCLR--EIIGVV--SQE--- 475
Cdd:NF040905 14 VKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PHgsyEGEILFDGE-VCRF--KDIRdsEALGIViiHQElal 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 476 -PVLfstTIAENIRYG-----RGNVTMDEIEKAVKEanaydfIMK---LPQKFDTLVGDRGAqlsgGQKQRIAIARALVR 546
Cdd:NF040905 90 iPYL---SIAENIFLGnerakRGVIDWNETNRRARE------LLAkvgLDESPDTLVTDIGV----GKQQLVEIAKALSK 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 338817954 547 NPKILLLDEATSAL-DTESEAEVQAALDKAREGRTTIVIAHRLSTIRN-ADVIAGFEDGVIVE 607
Cdd:NF040905 157 DVKLLILDEPTAALnEEDSAALLDLLLELKAQGITSIIISHKLNEIRRvADSITVLRDGRTIE 219
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
1048-1214 |
7.07e-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: 7.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1048 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQWLRAQLGIVSQEPILFDCSIAENI 1127
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSVLENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1128 AY--GDNSRvvphDEIVRAAKEANIHPFiETLPqkyntrvgdkGTQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTE 1205
Cdd:cd03231 95 RFwhADHSD----EQVEEALARVGLNGF-EDRP----------VAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKA 159
|
....*....
gi 338817954 1206 SEKVVQEAL 1214
Cdd:cd03231 160 GVARFAEAM 168
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1038-1258 |
8.25e-17 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 82.14 E-value: 8.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1038 FNYPT----RANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQWLRAQLGIVS 1113
Cdd:PRK15112 14 FRYRTgwfrRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIRMIF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1114 QEPilfdcSIAENiaygDNSRV-----VP---HDEIVRAAKEANIhpfIETLPQkyntrVG---DKGT----QLSGGQKQ 1178
Cdd:PRK15112 94 QDP-----STSLN----PRQRIsqildFPlrlNTDLEPEQREKQI---IETLRQ-----VGllpDHASyyphMLAPGQKQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1179 RIAIARALIRQPRVLLLDEATSALD-TESEKVVQEALD-KAREGRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHGTHQQ 1255
Cdd:PRK15112 157 RLGLARALILRPKVIIADEALASLDmSMRSQLINLMLElQEKQGISYIYVTQHLGMMKHiSDQVLVMHQGEVVERGSTAD 236
|
...
gi 338817954 1256 LLA 1258
Cdd:PRK15112 237 VLA 239
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
409-603 |
9.52e-17 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 79.40 E-value: 9.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 409 LKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLREI-IGVVSQEP----VLFSTTI 483
Cdd:cd03215 16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAgIAYVPEDRkregLVLDLSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 484 AENIrygrgnvtmdeiekavkeanaydfimklpqkfdTLvgdrGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTE 563
Cdd:cd03215 96 AENI---------------------------------AL----SSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVG 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 338817954 564 SEAEVQAALDK-AREGRTTIVIahrlST-----IRNADVIAGFEDG 603
Cdd:cd03215 139 AKAEIYRLIRElADAGKAVLLI----SSeldelLGLCDRILVMYEG 180
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
396-591 |
1.01e-16 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 80.69 E-value: 1.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 396 VHFSYPSRANI---KILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDI---RNFNVRCLREII 469
Cdd:PRK10908 2 IRFEHVSKAYLggrQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDItrlKNREVPFLRRQI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 470 GVVSQEP-VLFSTTIAENIRYGR--GNVTMDEIEKAVKEANAYDFIMKLPQKFDTlvgdrgaQLSGGQKQRIAIARALVR 546
Cdd:PRK10908 82 GMIFQDHhLLMDRTVYDNVAIPLiiAGASGDDIRRRVSAALDKVGLLDKAKNFPI-------QLSGGEQQRVGIARAVVN 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 338817954 547 NPKILLLDEATSALDTE-SEAEVQAALDKAREGRTTIVIAHRLSTI 591
Cdd:PRK10908 155 KPAVLLADEPTGNLDDAlSEGILRLFEEFNRVGVTVLMATHDIGLI 200
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
408-616 |
1.07e-16 |
|
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: 1.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 408 ILKGLNLKVKSGQTVALVGNSGCGKSTtvqLLQRL--YDPT----EGKISIDGQDIrnfNVRCLREIIGVVSQEPVLFST 481
Cdd:TIGR00955 40 LLKNVSGVAKPGELLAVMGSSGAGKTT---LMNALafRSPKgvkgSGSVLLNGMPI---DAKEMRAISAYVQQDDLFIPT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 482 -TIAENI------RYGRgNVTMDEIEKAVKEanaydFI--MKLPQKFDTLVGDRGAQ--LSGGQKQRIAIARALVRNPKI 550
Cdd:TIGR00955 114 lTVREHLmfqahlRMPR-RVTKKEKRERVDE-----VLqaLGLRKCANTRIGVPGRVkgLSGGERKRLAFASELLTDPPL 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 338817954 551 LLLDEATSALDTESEAEVQAALDK-AREGRTTIVIAHRLST--IRNADVIAGFEDGVIVEQGSHSELMK 616
Cdd:TIGR00955 188 LFCDEPTSGLDSFMAYSVVQVLKGlAQKGKTIICTIHQPSSelFELFDKIILMAEGRVAYLGSPDQAVP 256
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
740-965 |
1.19e-16 |
|
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: 81.97 E-value: 1.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 740 DDAVKQQKCNMFSLVFLGLGVLSFFTFFLQG-----FTFGKAGeiLTTRLRSMAFKAMLRQDMSWFDdhKNSTGALSTRL 814
Cdd:cd18784 24 DGIVIEKSQDKFSRAIIIMGLLAIASSVAAGirgglFTLAMAR--LNIRIRNLLFRSIVSQEIGFFD--TVKTGDITSRL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 815 ATDAAQVQGATGTRLALIAQNTANLGTGIIISFIYGWQLTLLLLSVVPFIAVAGIVEMKMLAGNAKRDKKEMEAAGKIAT 894
Cdd:cd18784 100 TSDTTTMSDTVSLNLNIFLRSLVKAIGVIVFMFKLSWQLSLVTLIGLPLIAIVSKVYGDYYKKLSKAVQDSLAKANEVAE 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 338817954 895 EAIENIRTVVSLTQERKFESMYVEKLHGPYRNSVRKAHIYGITFSISQAFMYFSYAGCFRFGSYLIVNGHM 965
Cdd:cd18784 180 ETISSIRTVRSFANEDGEANRYSEKLKDTYKLKIKEALAYGGYVWSNELTELALTVSTLYYGGHLVITGQI 250
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1046-1252 |
1.54e-16 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 80.51 E-value: 1.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1046 VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGqeakklNVQWLraqLGI-VSQEPILfdcSIA 1124
Cdd:COG1134 39 FWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG------RVSAL---LELgAGFHPEL---TGR 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1125 ENI-----AYGdnsrvVPHDEIVRAAKE----ANIHPFIETlPQKYntrvgdkgtqLSGGQKQRIAIARALIRQPRVLLL 1195
Cdd:COG1134 107 ENIylngrLLG-----LSRKEIDEKFDEivefAELGDFIDQ-PVKT----------YSSGMRARLAFAVATAVDPDILLV 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 338817954 1196 DEATSALDTE-SEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHGT 1252
Cdd:COG1134 171 DEVLAVGDAAfQKKCLARIRELRESGRTVIFVSHSMGAVRRlCDRAIWLEKGRLVMDGD 229
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1043-1259 |
2.35e-16 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 83.70 E-value: 2.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1043 RANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSV-------LLDGQEAKKLNVQWLRAQLGIVSQE 1115
Cdd:TIGR03269 294 RGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnvrvgdeWVDMTKPGPDGRGRAKRYIGILHQE 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1116 PILF-DCSIAENIAygDNSRVVPHDEIvrAAKEANIHPFIETLPQKYNTRVGDKGT-QLSGGQKQRIAIARALIRQPRVL 1193
Cdd:TIGR03269 374 YDLYpHRTVLDNLT--EAIGLELPDEL--ARMKAVITLKMVGFDEEKAEEILDKYPdELSEGERHRVALAQVLIKEPRIV 449
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 338817954 1194 LLDEATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHGTHQQLLAQ 1259
Cdd:TIGR03269 450 ILDEPTGTMDPITKVDVTHSILKAREemEQTFIIVSHDMDFVLDvCDRAALMRDGKIVKIGDPEEIVEE 518
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1031-1262 |
2.62e-16 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 79.92 E-value: 2.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1031 VTFNEVVFNYptrANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLerFYDPMA--GSVLLDGQEAkklnVQW---- 1104
Cdd:PRK11614 6 LSFDKVSAHY---GKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTL--CGDPRAtsGRIVFDGKDI----TDWqtak 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1105 -LRAQLGIVSQEPILFD-CSIAENIAYGD--NSRVVPHDEIVRAakeanihpfIETLPQKYNTRVGDKGTqLSGGQKQRI 1180
Cdd:PRK11614 77 iMREAVAIVPEGRRVFSrMTVEENLAMGGffAERDQFQERIKWV---------YELFPRLHERRIQRAGT-MSGGEQQML 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1181 AIARALIRQPRVLLLDEATSALdteSEKVVQEALDKAR----EGRTCIVIAHRLS-TIQNADLIVVIENGKVKEHGTHQQ 1255
Cdd:PRK11614 147 AIGRALMSQPRLLLLDEPSLGL---APIIIQQIFDTIEqlreQGMTIFLVEQNANqALKLADRGYVLENGHVVLEDTGDA 223
|
....*..
gi 338817954 1256 LLAQKGI 1262
Cdd:PRK11614 224 LLANEAV 230
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1047-1247 |
2.65e-16 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 83.53 E-value: 2.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1047 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNV-QWLRAQLGIVS----QEPILFDC 1121
Cdd:COG1129 266 GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPrDAIRAGIAYVPedrkGEGLVLDL 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1122 SIAENI---AYGDNSR--VVPHDEIVRAAKEanihpFIETLpqkyNTRVGDKGT---QLSGGQKQRIAIARALIRQPRVL 1193
Cdd:COG1129 346 SIRENItlaSLDRLSRggLLDRRRERALAEE-----YIKRL----RIKTPSPEQpvgNLSGGNQQKVVLAKWLATDPKVL 416
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 338817954 1194 LLDEATSALD--TESE--KVVQEAldkAREGRTCIVIahrlST-----IQNADLIVVIENGKV 1247
Cdd:COG1129 417 ILDEPTRGIDvgAKAEiyRLIREL---AAEGKAVIVI----SSelpelLGLSDRILVMREGRI 472
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1037-1251 |
2.66e-16 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 84.14 E-value: 2.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1037 VFNYPTRaNVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLN---VQWLRAQLGIVS 1113
Cdd:PRK10261 329 LLNRVTR-EVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSpgkLQALRRDIQFIF 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1114 QEPIlfdCSIAENIAYGDnSRVVP---HDEIVRAAKEANIHPFIEtlpqkyntRVGDKGT-------QLSGGQKQRIAIA 1183
Cdd:PRK10261 408 QDPY---ASLDPRQTVGD-SIMEPlrvHGLLPGKAAAARVAWLLE--------RVGLLPEhawryphEFSGGQRQRICIA 475
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 338817954 1184 RALIRQPRVLLLDEATSALDTE-SEKVVQEALDKARE-GRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHG 1251
Cdd:PRK10261 476 RALALNPKVIIADEAVSALDVSiRGQIINLLLDLQRDfGIAYLFISHDMAVVERiSHRVAVMYLGQIVEIG 546
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
1048-1257 |
2.74e-16 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 80.42 E-value: 2.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1048 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQWLRAQLGIVSQEPIL-FDCSIAEN 1126
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTpGDITVQEL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1127 IAYGDnsrvVPHDEIV---RAAKEANIHPFIETlpqkynTRVGDKGTQ----LSGGQKQRIAIARALIRQPRVLLLDEAT 1199
Cdd:PRK10253 102 VARGR----YPHQPLFtrwRKEDEEAVTKAMQA------TGITHLADQsvdtLSGGQRQRAWIAMVLAQETAIMLLDEPT 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 338817954 1200 SALDTESEKVVQEALDK--AREGRTCIVIAHRLS-TIQNADLIVVIENGKVKEHGTHQQLL 1257
Cdd:PRK10253 172 TWLDISHQIDLLELLSElnREKGYTLAAVLHDLNqACRYASHLIALREGKIVAQGAPKEIV 232
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1047-1271 |
2.76e-16 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 85.07 E-value: 2.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1047 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKlNVQWLRAQLGIVSQEPILFD-CSIAE 1125
Cdd:TIGR01257 944 PAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET-NLDAVRQSLGMCPQHNILFHhLTVAE 1022
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1126 NIAYGDNSRVVPHDEiVRAAKEANIHPfiETLPQKYNTRVGDkgtqLSGGQKQRIAIARALIRQPRVLLLDEATSALDTE 1205
Cdd:TIGR01257 1023 HILFYAQLKGRSWEE-AQLEMEAMLED--TGLHHKRNEEAQD----LSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPY 1095
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 338817954 1206 SEKVVQEALDKAREGRTCIVIAHRLStiqNADL----IVVIENGKVKEHGTHQQL--LAQKGIYFSMV----NIQA 1271
Cdd:TIGR01257 1096 SRRSIWDLLLKYRSGRTIIMSTHHMD---EADLlgdrIAIISQGRLYCSGTPLFLknCFGTGFYLTLVrkmkNIQS 1168
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
126-343 |
2.90e-16 |
|
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: 81.02 E-value: 2.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 126 VAAYIQVSFWTLAAGRQIKKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDDVSKISEGIGDKVGMFFQAIATFFAGFIV 205
Cdd:cd18564 69 LASYAGTYLTALVGQRVVLDLRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGAIQDLLVSGVLPLLTNLLTLVGMLGV 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 206 GFIRGWKLTLVIMAISPILGLSTAVWAKILSTFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKELERYQKHLENAKK 285
Cdd:cd18564 149 MFWLDWQLALIALAVAPLLLLAARRFSRRIKEASREQRRREGALASVAQESLSAIRVVQAFGREEHEERRFARENRKSLR 228
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 338817954 286 IGIK-KAISANISMGIAfLLIYASYALAFWYGSTLVISKEYTIGnAMTVFFSILIGAFS 343
Cdd:cd18564 229 AGLRaARLQALLSPVVD-VLVAVGTALVLWFGAWLVLAGRLTPG-DLLVFLAYLKNLYK 285
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
391-622 |
3.14e-16 |
|
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: 78.44 E-value: 3.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 391 LEFSDVHFSYPSRANIK-ILKGLNLKVKSGQTVALVGNSGCGKSTTVQLL-QRLYDPT-EGKISIDGQDIRnfnvRCLRE 467
Cdd:cd03232 4 LTWKNLNYTVPVKGGKRqLLNNISGYVKPGTLTALMGESGAGKTTLLDVLaGRKTAGViTGEILINGRPLD----KNFQR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 468 IIGVVSQEPVLFST-TIAENIRygrgnvtmdeiekavkeanaydFIMKLpqkfdtlvgdRGaqLSGGQKQRIAIARALVR 546
Cdd:cd03232 80 STGYVEQQDVHSPNlTVREALR----------------------FSALL----------RG--LSVEQRKRLTIGVELAA 125
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 338817954 547 NPKILLLDEATSALDTESEAEVQAALDK-AREGRTTIVIAHRLStirnADVIAGFeDGVIveqgshseLMKKEG--IYF 622
Cdd:cd03232 126 KPSILFLDEPTSGLDSQAAYNIVRFLKKlADSGQAILCTIHQPS----ASIFEKF-DRLL--------LLKRGGktVYF 191
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
391-606 |
3.57e-16 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 83.15 E-value: 3.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 391 LEFSDVhfSYPSRANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLREI-I 469
Cdd:COG3845 258 LEVENL--SVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLgV 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 470 GVVSQEP-----VLfSTTIAENI---RYGRGNVT------MDEIEKAVKEanaydfIMKlpqKFDTLVGDRGA---QLSG 532
Cdd:COG3845 336 AYIPEDRlgrglVP-DMSVAENLilgRYRRPPFSrggfldRKAIRAFAEE------LIE---EFDVRTPGPDTparSLSG 405
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 338817954 533 GQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKAR-EGRTTIVIAHRLSTIRN-ADVIAGFEDGVIV 606
Cdd:COG3845 406 GNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRdAGAAVLLISEDLDEILAlSDRIAVMYEGRIV 481
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1042-1256 |
3.86e-16 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 80.19 E-value: 3.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1042 TRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQWL---RAQLGIVSQEPIL 1118
Cdd:PRK11831 16 TRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLytvRKRMSMLFQSGAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1119 F-DCSIAENIAYgdnsrvvPHDEIVRAAkEANIHpfiETLPQKYNTrVGDKG------TQLSGGQKQRIAIARALIRQPR 1191
Cdd:PRK11831 96 FtDMNVFDNVAY-------PLREHTQLP-APLLH---STVMMKLEA-VGLRGaaklmpSELSGGMARRAALARAIALEPD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 338817954 1192 VLLLDEATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHGTHQQL 1256
Cdd:PRK11831 164 LIMFDEPFVGQDPITMGVLVKLISELNSalGVTCVVVSHDVPEVLSiADHAYIVADKKIVAHGSAQAL 231
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
406-603 |
3.89e-16 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 82.95 E-value: 3.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 406 IKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLY--DPTEGKISIDGQDIRNFNVR-CLREIIGVVSQEPVLF-ST 481
Cdd:TIGR02633 14 VKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYphGTWDGEIYWSGSPLKASNIRdTERAGIVIIHQELTLVpEL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 482 TIAENIRYG-----RGNVTMDEieKAVKEANAYDFIMKLPQKFDTL-VGDRGaqlsGGQKQRIAIARALVRNPKILLLDE 555
Cdd:TIGR02633 94 SVAENIFLGneitlPGGRMAYN--AMYLRAKNLLRELQLDADNVTRpVGDYG----GGQQQLVEIAKALNKQARLLILDE 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 338817954 556 ATSALdTESEAEVQAAL--DKAREGRTTIVIAHRLSTIRN-ADVIAGFEDG 603
Cdd:TIGR02633 168 PSSSL-TEKETEILLDIirDLKAHGVACVYISHKLNEVKAvCDTICVIRDG 217
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1048-1258 |
4.12e-16 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 82.93 E-value: 4.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1048 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERF--YDPMAGSVL----------------LDGQEAKKLNVQwlraql 1109
Cdd:TIGR03269 15 VLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIyhvalcekcgyverpsKVGEPCPVCGGT------ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1110 gIVSQEPILFDCS------IAENIA---------YGDNsRVVphDEIVRAAKEAN------IHPFIETLPQ-KYNTRVGD 1167
Cdd:TIGR03269 89 -LEPEEVDFWNLSdklrrrIRKRIAimlqrtfalYGDD-TVL--DNVLEALEEIGyegkeaVGRAVDLIEMvQLSHRITH 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1168 KGTQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEALDKA--REGRTCIVIAHRLSTIQN-ADLIVVIEN 1244
Cdd:TIGR03269 165 IARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAvkASGISMVLTSHWPEVIEDlSDKAIWLEN 244
|
250
....*....|....
gi 338817954 1245 GKVKEHGTHQQLLA 1258
Cdd:TIGR03269 245 GEIKEEGTPDEVVA 258
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
402-572 |
4.30e-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: 78.30 E-value: 4.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 402 SRANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLREIIGVVSQEPVLFST 481
Cdd:cd03231 9 ERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 482 TIAENIRYGRGNVTMDEIEKAVKEANAydfimklpqkfdTLVGDRG-AQLSGGQKQRIAIARALVRNPKILLLDEATSAL 560
Cdd:cd03231 89 SVLENLRFWHADHSDEQVEEALARVGL------------NGFEDRPvAQLSAGQQRRVALARLLLSGRPLWILDEPTTAL 156
|
170
....*....|..
gi 338817954 561 DTESEAEVQAAL 572
Cdd:cd03231 157 DKAGVARFAEAM 168
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
408-610 |
6.07e-16 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 78.97 E-value: 6.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 408 ILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGqdirnfNVRCLREIIGVVSQEpvlfsTTIAENI 487
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG------RVSALLELGAGFHPE-----LTGRENI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 488 R-----YGrgnVTMDEIEKAVKEANAY----DFImklpqkfDTLVGdrgaQLSGGQKQRIAIARALVRNPKILLLDEATS 558
Cdd:COG1134 110 YlngrlLG---LSRKEIDEKFDEIVEFaelgDFI-------DQPVK----TYSSGMRARLAFAVATAVDPDILLVDEVLA 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 338817954 559 ALDTE----SEAEVQaalDKAREGRTTIVIAHRLSTIRN-ADVIAGFEDGVIVEQGS 610
Cdd:COG1134 176 VGDAAfqkkCLARIR---ELRESGRTVIFVSHSMGAVRRlCDRAIWLEKGRLVMDGD 229
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1046-1246 |
1.09e-15 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 81.59 E-value: 1.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1046 VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAK----KLNVQwlrAQLGIVSQEPILFD- 1120
Cdd:PRK10762 17 VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfngpKSSQE---AGIGIIHQELNLIPq 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1121 CSIAENIAYG----------DNSRVvpHDEIVRAAKEANihpfietLPQKYNTRVGDkgtqLSGGQKQRIAIARALIRQP 1190
Cdd:PRK10762 94 LTIAENIFLGrefvnrfgriDWKKM--YAEADKLLARLN-------LRFSSDKLVGE----LSIGEQQMVEIAKVLSFES 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 338817954 1191 RVLLLDEATSAL-DTESE---KVVQEALDkarEGRTCIVIAHRLSTI-QNADLIVVIENGK 1246
Cdd:PRK10762 161 KVIIMDEPTDALtDTETEslfRVIRELKS---QGRGIVYISHRLKEIfEICDDVTVFRDGQ 218
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
403-615 |
1.14e-15 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 78.68 E-value: 1.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 403 RANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDI-------RNFNVRCL---------- 465
Cdd:PRK15112 23 RQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLhfgdysyRSQRIRMIfqdpstslnp 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 466 REIIGVVSQEPVLFSTTIAENIRYGRGNVTMDEIEKAVKEANAYDFImklpqkfdtlvgdrgaqLSGGQKQRIAIARALV 545
Cdd:PRK15112 103 RQRISQILDFPLRLNTDLEPEQREKQIIETLRQVGLLPDHASYYPHM-----------------LAPGQKQRLGLARALI 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 338817954 546 RNPKILLLDEATSALDTESEAE-VQAALD-KAREGRTTIVIAHRLSTIRN-ADVIAGFEDGVIVEQGSHSELM 615
Cdd:PRK15112 166 LRPKVIIADEALASLDMSMRSQlINLMLElQEKQGISYIYVTQHLGMMKHiSDQVLVMHQGEVVERGSTADVL 238
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
403-610 |
1.16e-15 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 82.21 E-value: 1.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 403 RANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDI--RNFNVRCLREI------------ 468
Cdd:PRK10261 26 QQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLrrRSRQVIELSEQsaaqmrhvrgad 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 469 IGVVSQEPV-----LFST--TIAENIRYGRGNVTmdeiEKAVKEANAYDFIMKLPQKfDTLVGDRGAQLSGGQKQRIAIA 541
Cdd:PRK10261 106 MAMIFQEPMtslnpVFTVgeQIAESIRLHQGASR----EEAMVEAKRMLDQVRIPEA-QTILSRYPHQLSGGMRQRVMIA 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 338817954 542 RALVRNPKILLLDEATSALDTESEAEVQAALDKAREGRT--TIVIAHRLSTIRN-ADVIAGFEDGVIVEQGS 610
Cdd:PRK10261 181 MALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSmgVIFITHDMGVVAEiADRVLVMYQGEAVETGS 252
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
750-983 |
1.18e-15 |
|
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: 79.07 E-value: 1.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 750 MFSLVFLGLGVLSFFTFFLqgftFGKAGEILTTRLRSMAFKAMLRQDMSWFDdhKNSTGALSTRLATDAAQVQGATGTRL 829
Cdd:cd18575 41 LLLAVALVLALASALRFYL----VSWLGERVVADLRKAVFAHLLRLSPSFFE--TTRTGEVLSRLTTDTTLIQTVVGSSL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 830 ALIAQNTANLGTGIIISFIYGWQLTLLLLSVVPFIAVAGIVEMKMLAGNAKRDKKEMEAAGKIATEAIENIRTVVSLTQE 909
Cdd:cd18575 115 SIALRNLLLLIGGLVMLFITSPKLTLLVLLVIPLVVLPIILFGRRVRRLSRASQDRLADLSAFAEETLSAIKTVQAFTRE 194
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 338817954 910 RKFESMYVEKLHGPYRNSVRKAHIYGITFSISQAFMYFSYAGCFRFGSYLIVNGHMRFKDVI--LVFSAIVLGAVA 983
Cdd:cd18575 195 DAERQRFATAVEAAFAAALRRIRARALLTALVIFLVFGAIVFVLWLGAHDVLAGRMSAGELSqfVFYAVLAAGSVG 270
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
52-342 |
1.22e-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: 78.98 E-value: 1.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 52 LFMFLGTLMAIAhgsgLPLMMivfGEMTDKFVdNTGNFSLPVNFSLSMLnpgrileeemtryayyysGLGGGVLVAAYIQ 131
Cdd:cd18548 6 LFKLLEVLLELL----LPTLM---ADIIDEGI-ANGDLSYILRTGLLML------------------LLALLGLIAGILA 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 132 VSFWTLAAGRQIKKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDDVSKISEGIGDKVGMFFQAIATFFAGFIVGFIRGW 211
Cdd:cd18548 60 GYFAAKASQGFGRDLRKDLFEKIQSFSFAEIDKFGTSSLITRLTNDVTQVQNFVMMLLRMLVRAPIMLIGAIIMAFRINP 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 212 KLTLVIMAISPILGLSTAVWAKILSTFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKELERYQKHLENAKKIGIKKA 291
Cdd:cd18548 140 KLALILLVAIPILALVVFLIMKKAIPLFKKVQKKLDRLNRVVRENLTGIRVIRAFNREDYEEERFDKANDDLTDTSLKAG 219
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 338817954 292 ISANISMGIAFLLIYASYALAFWYGSTLVISKEYTIGN-------AMTVFFSILIGAF 342
Cdd:cd18548 220 RLMALLNPLMMLIMNLAIVAILWFGGHLINAGSLQVGDlvafinyLMQILMSLMMLSM 277
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
1043-1227 |
1.46e-15 |
|
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: 76.63 E-value: 1.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1043 RANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQWLRAQLGIVSQEPILFDCS 1122
Cdd:TIGR01189 10 RGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLPGLKPELS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1123 IAENI----AYGDNSRVVPHDeivrAAKEANIHPFiETLPqkyntrvgdkGTQLSGGQKQRIAIARALIRQPRVLLLDEA 1198
Cdd:TIGR01189 90 ALENLhfwaAIHGGAQRTIED----ALAAVGLTGF-EDLP----------AAQLSAGQQRRLALARLWLSRRPLWILDEP 154
|
170 180
....*....|....*....|....*....
gi 338817954 1199 TSALDTESEKVVQEALDkAREGRTCIVIA 1227
Cdd:TIGR01189 155 TTALDKAGVALLAGLLR-AHLARGGIVLL 182
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1046-1245 |
1.59e-15 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 80.98 E-value: 1.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1046 VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQwLRAQLG--IVSQEPILFD-CS 1122
Cdd:PRK09700 18 VHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHK-LAAQLGigIIYQELSVIDeLT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1123 IAENIAYGDN-SRVVPHDEIVRAAK---EANIHPFIETLPQKYNTRVGDkgtqLSGGQKQRIAIARALIRQPRVLLLDEA 1198
Cdd:PRK09700 97 VLENLYIGRHlTKKVCGVNIIDWREmrvRAAMMLLRVGLKVDLDEKVAN----LSISHKQMLEIAKTLMLDAKVIIMDEP 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 338817954 1199 TSAL-DTESEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVIENG 1245
Cdd:PRK09700 173 TSSLtNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRiCDRYTVMKDG 221
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1046-1247 |
1.69e-15 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 80.87 E-value: 1.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1046 VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQwLRAQLGI--VSQEPILF-DCS 1122
Cdd:PRK15439 24 VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPA-KAHQLGIylVPQEPLLFpNLS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1123 IAENIAYGDNSRVVPHDEIVRAAKEANIHPFIETlpqkyntrvgdKGTQLSGGQKQRIAIARALIRQPRVLLLDEATSAL 1202
Cdd:PRK15439 103 VKENILFGLPKRQASMQKMKQLLAALGCQLDLDS-----------SAGSLEVADRQIVEILRGLMRDSRILILDEPTASL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 338817954 1203 D-TESEKV---VQEALDKareGRTCIVIAHRLSTI-QNADLIVVIENGKV 1247
Cdd:PRK15439 172 TpAETERLfsrIRELLAQ---GVGIVFISHKLPEIrQLADRISVMRDGTI 218
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
708-965 |
1.99e-15 |
|
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: 78.22 E-value: 1.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 708 FVVGTVCAIANGALQPAFSIILSEMIaifgpgdDAVKQQKCNM-----FSLVFLGLGVLSFFTFFLQGFTFGKAGEILTT 782
Cdd:cd18541 1 YLLGILFLILVDLLQLLIPRIIGRAI-------DALTAGTLTAsqllrYALLILLLALLIGIFRFLWRYLIFGASRRIEY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 783 RLRSMAFKAMLRQDMSWFddHKNSTGALSTRLATDAAQVQGATGTRLALIAQNTANLGTGIIISFIYGWQLTLLLLSVVP 862
Cdd:cd18541 74 DLRNDLFAHLLTLSPSFY--QKNRTGDLMARATNDLNAVRMALGPGILYLVDALFLGVLVLVMMFTISPKLTLIALLPLP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 863 FIAVAGIVEMKMLagnAKRDKKEMEAAGKIATEAIEN---IRTVVSLTQERKFESMYVEKLHGPYRNSVRKAHIYGITFS 939
Cdd:cd18541 152 LLALLVYRLGKKI---HKRFRKVQEAFSDLSDRVQESfsgIRVIKAFVQEEAEIERFDKLNEEYVEKNLRLARVDALFFP 228
|
250 260
....*....|....*....|....*.
gi 338817954 940 ISQAFMYFSYAGCFRFGSYLIVNGHM 965
Cdd:cd18541 229 LIGLLIGLSFLIVLWYGGRLVIRGTI 254
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
1031-1246 |
2.06e-15 |
|
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: 74.41 E-value: 2.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1031 VTFNEVVFNYPTRanvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLerfydpmagsvlldgqeakklnvqwlraqlg 1110
Cdd:cd03221 1 IELENLSKTYGGK---LLLKDISLTINPGDRIGLVGRNGAGKSTLLKLI------------------------------- 46
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1111 ivsqepilfdcsiaeniaygdNSRVVPHDEIVRAAKEANIHPFietlpqkyntrvgdkgTQLSGGQKQRIAIARALIRQP 1190
Cdd:cd03221 47 ---------------------AGELEPDEGIVTWGSTVKIGYF----------------EQLSGGEKMRLALAKLLLENP 89
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 338817954 1191 RVLLLDEATSALDTESEKVVQEALdKAREGrTCIVIAHRLSTIQN-ADLIVVIENGK 1246
Cdd:cd03221 90 NLLLLDEPTNHLDLESIEALEEAL-KEYPG-TVILVSHDRYFLDQvATKIIELEDGK 144
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
407-646 |
2.11e-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: 80.62 E-value: 2.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 407 KILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRL--YDPTEGKI--------SIDGQDIRNFNVRCLREIIGVVSQEP 476
Cdd:TIGR03269 14 EVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIiyhvalceKCGYVERPSKVGEPCPVCGGTLEPEE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 477 VLF---STTIAENIR-------------YGRGNV------TMDEIEKAVKEA--NAYDFI--MKLPQKFDTLVGDrgaqL 530
Cdd:TIGR03269 94 VDFwnlSDKLRRRIRkriaimlqrtfalYGDDTVldnvleALEEIGYEGKEAvgRAVDLIemVQLSHRITHIARD----L 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 531 SGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKA--REGRTTIVIAHRLSTIRN-ADVIAGFEDGVIVE 607
Cdd:TIGR03269 170 SGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAvkASGISMVLTSHWPEVIEDlSDKAIWLENGEIKE 249
|
250 260 270
....*....|....*....|....*....|....*....
gi 338817954 608 QGSHSELMKKegiYFRLVNMqtagsqiLSEEFEVELSDE 646
Cdd:TIGR03269 250 EGTPDEVVAV---FMEGVSE-------VEKECEVEVGEP 278
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
708-963 |
2.76e-15 |
|
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: 77.81 E-value: 2.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 708 FVVGTVCAIANGALQPAFSIILSEMIaifgpgDDAVKQQKCNM-----FSLVFLGLGVLSFFTFFLQGFTFGKAGEILTT 782
Cdd:cd18544 1 FILALLLLLLATALELLGPLLIKRAI------DDYIVPGQGDLqglllLALLYLGLLLLSFLLQYLQTYLLQKLGQRIIY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 783 RLRSMAFKAMLRQDMSWFDdhKNSTGALSTRLATDAAQVQGATGTRLALIAQNTANLGTGIIISFIYGWQLTLLLLSVVP 862
Cdd:cd18544 75 DLRRDLFSHIQRLPLSFFD--RTPVGRLVTRVTNDTEALNELFTSGLVTLIGDLLLLIGILIAMFLLNWRLALISLLVLP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 863 FIAVAgIVEMKMLAGNAKRDKKEMEAA--GKIAtEAIENIRTVVSLTQERKFESMYvEKLHGPYRNSVRKA-HIYGITFS 939
Cdd:cd18544 153 LLLLA-TYLFRKKSRKAYREVREKLSRlnAFLQ-ESISGMSVIQLFNREKREFEEF-DEINQEYRKANLKSiKLFALFRP 229
|
250 260
....*....|....*....|....
gi 338817954 940 ISQAFMYFSYAGCFRFGSYLIVNG 963
Cdd:cd18544 230 LVELLSSLALALVLWYGGGQVLSG 253
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
397-620 |
3.51e-15 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 77.17 E-value: 3.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 397 HFSYPSRANIkILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQ-RLYDPTE-------GKISIDGQDIRNFNVR---CL 465
Cdd:PRK13547 6 HLHVARRHRA-ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAgDLTGGGAprgarvtGDVTLNGEPLAAIDAPrlaRL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 466 REIIGVVSQEPVLFSttIAENIRYGR----------GNVTMDEIEKAVKEANAydfimklpqkfDTLVGDRGAQLSGGQK 535
Cdd:PRK13547 85 RAVLPQAAQPAFAFS--AREIVLLGRypharragalTHRDGEIAWQALALAGA-----------TALVGRDVTTLSGGEL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 536 QRIAIARAL---------VRNPKILLLDEATSALDTESEAEVQAAL-DKARE---GRTTIVIAHRLSTiRNADVIAGFED 602
Cdd:PRK13547 152 ARVQFARVLaqlwpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVrRLARDwnlGVLAIVHDPNLAA-RHADRIAMLAD 230
|
250
....*....|....*...
gi 338817954 603 GVIVEQGSHSELMKKEGI 620
Cdd:PRK13547 231 GAIVAHGAPADVLTPAHI 248
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
1028-1257 |
3.77e-15 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 77.14 E-value: 3.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1028 EGSVTFNEVVFNYPTRAnvpVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQWLRA 1107
Cdd:PRK10575 9 DTTFALRNVSFRVPGRT---LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFAR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1108 QLGIVSQE-PILFDCSIAENIAYGdnsRVVPHDEIVR--AAKEANIHPFIETLPQK-YNTRVGDkgtQLSGGQKQRIAIA 1183
Cdd:PRK10575 86 KVAYLPQQlPAAEGMTVRELVAIG---RYPWHGALGRfgAADREKVEEAISLVGLKpLAHRLVD---SLSGGERQRAWIA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 338817954 1184 RALIRQPRVLLLDEATSALDTESEKVVQEALDKAREGRTCIVIAhRLSTIQNA----DLIVVIENGKVKEHGTHQQLL 1257
Cdd:PRK10575 160 MLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIA-VLHDINMAarycDYLVALRGGEMIAQGTPAELM 236
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
118-329 |
3.87e-15 |
|
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: 77.38 E-value: 3.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 118 SGLGGGvlvaayiqvsFWTLAAGRQIKKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDDVSKISEGIGDKVGMFFQAIA 197
Cdd:cd18590 53 AGLRGG----------LFMCTLSRLNLRLRHQLFSSLVQQDIGFFEKTKTGDLTSRLSTDTTLMSRSVALNANVLLRSLV 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 198 TFFAGFIVGFIRGWKLTLVIMAISPILGLSTAVWAKILSTFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKELERYQ 277
Cdd:cd18590 123 KTLGMLGFMLSLSWQLTLLTLIEMPLTAIAQKVYNTYHQKLSQAVQDSIAKAGELAREAVSSIRTVRSFKAEEEEACRYS 202
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 338817954 278 KHLENAKKIGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTIGN 329
Cdd:cd18590 203 EALERTYNLKDRRDTVRAVYLLVRRVLQLGVQVLMLYCGRQLIQSGHLTTGS 254
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
395-606 |
3.90e-15 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 78.23 E-value: 3.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 395 DVHFSYPSrANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDP---TEGKISIDGQDIRNFNVRCLREI--- 468
Cdd:PRK09473 19 RVTFSTPD-GDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAngrIGGSATFNGREILNLPEKELNKLrae 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 469 -IGVVSQEPVlfsTTIAENIRYGRGNVTMDEIEKAVKEANAYDFIMKL----------------PQKFdtlvgdrgaqlS 531
Cdd:PRK09473 98 qISMIFQDPM---TSLNPYMRVGEQLMEVLMLHKGMSKAEAFEESVRMldavkmpearkrmkmyPHEF-----------S 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 338817954 532 GGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDK-AREGRTTIV-IAHRLStirnadVIAGFEDGVIV 606
Cdd:PRK09473 164 GGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNElKREFNTAIImITHDLG------VVAGICDKVLV 234
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1043-1256 |
4.34e-15 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 80.28 E-value: 4.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1043 RANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQWLR--------------AQ 1108
Cdd:PRK10261 26 QQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRSRQVIElseqsaaqmrhvrgAD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1109 LGIVSQEPI-----LFDC--SIAENIAYGDNsrvVPHDEIVRAAK----EANIhPFIETLPQKYNTrvgdkgtQLSGGQK 1177
Cdd:PRK10261 106 MAMIFQEPMtslnpVFTVgeQIAESIRLHQG---ASREEAMVEAKrmldQVRI-PEAQTILSRYPH-------QLSGGMR 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1178 QRIAIARALIRQPRVLLLDEATSALDTESE-------KVVQEALDKAregrtCIVIAHRLSTIQN-ADLIVVIENGKVKE 1249
Cdd:PRK10261 175 QRVMIAMALSCRPAVLIADEPTTALDVTIQaqilqliKVLQKEMSMG-----VIFITHDMGVVAEiADRVLVMYQGEAVE 249
|
....*..
gi 338817954 1250 HGTHQQL 1256
Cdd:PRK10261 250 TGSVEQI 256
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1049-1257 |
5.13e-15 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 76.50 E-value: 5.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1049 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQWL---------RAQLGIVSQEP--- 1116
Cdd:PRK11701 22 CRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALseaerrrllRTEWGFVHQHPrdg 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1117 ILFDCSIAENI-----AYGDNsrvvpHDEIVRAA-----KEANIHPfietlpqkynTRVGDKGTQLSGGQKQRIAIARAL 1186
Cdd:PRK11701 102 LRMQVSAGGNIgerlmAVGAR-----HYGDIRATagdwlERVEIDA----------ARIDDLPTTFSGGMQQRLQIARNL 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 338817954 1187 IRQPRVLLLDEATSALDTEsekvVQ-EALDKARE-----GRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHGTHQQLL 1257
Cdd:PRK11701 167 VTHPRLVFMDEPTGGLDVS----VQaRLLDLLRGlvrelGLAVVIVTHDLAVARLlAHRLLVMKQGRVVESGLTDQVL 240
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1039-1247 |
6.30e-15 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 79.30 E-value: 6.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1039 NYPTRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLL--ERfyDPMAGSVLLDGQEAKKLNV-QWLRAQLGIVSQE 1115
Cdd:COG3845 264 SVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALagLR--PPASGSIRLDGEDITGLSPrERRRLGVAYIPED 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1116 P-----ILfDCSIAENIA--YGDNSRVVPH-----DEIVRAAKEAnihpfIEtlpqKYNTRVGDKGT---QLSGGQKQRI 1180
Cdd:COG3845 342 RlgrglVP-DMSVAENLIlgRYRRPPFSRGgfldrKAIRAFAEEL-----IE----EFDVRTPGPDTparSLSGGNQQKV 411
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 338817954 1181 AIARALIRQPRVLLLDEATSALDTESEKVVQEALDKAR-EGRTCIVIAHRLSTIQN-ADLIVVIENGKV 1247
Cdd:COG3845 412 ILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRdAGAAVLLISEDLDEILAlSDRIAVMYEGRI 480
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
1049-1257 |
7.09e-15 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 79.32 E-value: 7.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1049 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLErFYDP----MAGSVLLDGqeaKKLNVQWLRAQLGIVSQEPILFDCSIA 1124
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALA-FRSPkgvkGSGSVLLNG---MPIDAKEMRAISAYVQQDDLFIPTLTV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1125 -ENIAYgdNSRVVPHDEIVRAAKEANIHPFIETLPQK--YNTRVGDKGTQ--LSGGQKQRIAIARALIRQPRVLLLDEAT 1199
Cdd:TIGR00955 117 rEHLMF--QAHLRMPRRVTKKEKRERVDEVLQALGLRkcANTRIGVPGRVkgLSGGERKRLAFASELLTDPPLLFCDEPT 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 338817954 1200 SALDTES-EKVVQEALDKAREGRTCIVIAHRLST--IQNADLIVVIENGKVKEHGTHQQLL 1257
Cdd:TIGR00955 195 SGLDSFMaYSVVQVLKGLAQKGKTIICTIHQPSSelFELFDKIILMAEGRVAYLGSPDQAV 255
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
100-328 |
9.95e-15 |
|
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: 76.27 E-value: 9.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 100 LNPGRILEEEMTRYAYYYSGLGGGVLVAAYIQVSFWTLAAGRQIKKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDDVS 179
Cdd:cd18544 30 IVPGQGDLQGLLLLALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRDLFSHIQRLPLSFFDRTPVGRLVTRVTNDTE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 180 KISEGIGDKVGMFFQAIATFFAGFIVGFIRGWKLTLVIMAISPILGLSTAVWAKILSTFSDKELAAYAKAGAVAEEALGA 259
Cdd:cd18544 110 ALNELFTSGLVTLIGDLLLLIGILIAMFLLNWRLALISLLVLPLLLLATYLFRKKSRKAYREVREKLSRLNAFLQESISG 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 338817954 260 IRTVIAFGGQNKELERYQKHLENAKKIGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTIG 328
Cdd:cd18544 190 MSVIQLFNREKREFEEFDEINQEYRKANLKSIKLFALFRPLVELLSSLALALVLWYGGGQVLSGAVTLG 258
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
401-585 |
1.19e-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: 74.22 E-value: 1.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 401 PSRANIKILKGLNLKVKSGQTVALVGNSGCGKSTtvqLLQRL------YDPTEGKISIDGQDIRNFNVRCLREIIgVVSQ 474
Cdd:cd03233 15 KGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCST---LLKALanrtegNVSVEGDIHYNGIPYKEFAEKYPGEII-YVSE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 475 EPVLFST-TIAEnirygrgnvTMDeiekAVKEANAYDFImklpqkfdtlvgdRGaqLSGGQKQRIAIARALVRNPKILLL 553
Cdd:cd03233 91 EDVHFPTlTVRE---------TLD----FALRCKGNEFV-------------RG--ISGGERKRVSIAEALVSRASVLCW 142
|
170 180 190
....*....|....*....|....*....|...
gi 338817954 554 DEATSALDTESEAE-VQAALDKAREGRTTIVIA 585
Cdd:cd03233 143 DNSTRGLDSSTALEiLKCIRTMADVLKTTTFVS 175
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
1041-1247 |
1.40e-14 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 74.68 E-value: 1.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1041 PTRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGqeakklNVQW-----LRAQLGIV--S 1113
Cdd:cd03267 29 RKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAG------LVPWkrrkkFLRRIGVVfgQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1114 QEPILFDCSIAENIAYgdnsrvvpHDEIVR---AAKEANIHPFIETLPQkynTRVGDKGT-QLSGGQKQRIAIARALIRQ 1189
Cdd:cd03267 103 KTQLWWDLPVIDSFYL--------LAAIYDlppARFKKRLDELSELLDL---EELLDTPVrQLSLGQRMRAEIAAALLHE 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 338817954 1190 PRVLLLDEATSALDTESEKVVQEALDKAREGR--TCIVIAHRLSTIQN-ADLIVVIENGKV 1247
Cdd:cd03267 172 PEILFLDEPTIGLDVVAQENIRNFLKEYNRERgtTVLLTSHYMKDIEAlARRVLVIDKGRL 232
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1045-1252 |
1.41e-14 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 75.12 E-value: 1.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1045 NVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQWLRAQLGIVSQEP-ILFDCSI 1123
Cdd:COG4604 13 GKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAILRQENhINSRLTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1124 AENIAYG----DNSRVVPHD-EIVRAAkeanIHPF-IETLPQKYNTrvgdkgtQLSGGQKQRIAIARALIRQPRVLLLDE 1197
Cdd:COG4604 93 RELVAFGrfpySKGRLTAEDrEIIDEA----IAYLdLEDLADRYLD-------ELSGGQRQRAFIAMVLAQDTDYVLLDE 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 338817954 1198 ATSALD----TESEKVVQEAldkARE-GRTCIVIAHRLstiqN-----ADLIVVIENGKVKEHGT 1252
Cdd:COG4604 162 PLNNLDmkhsVQMMKLLRRL---ADElGKTVVIVLHDI----NfascyADHIVAMKDGRVVAQGT 219
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
123-332 |
1.81e-14 |
|
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: 75.66 E-value: 1.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 123 GVLVAAYIqvSFWTLAAGRQIKKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDDVSK--------ISEGIgdkvgmffQ 194
Cdd:cd18574 56 SLLTFAYI--SLLSVVGERVAARLRNDLFSSLLRQDIAFFDTHRTGELVNRLTADVQEfkssfkqcVSQGL--------R 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 195 AIATFFAGFIVGFIRGWKLTLVIMAISPILGLSTAVWAKILSTFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKELE 274
Cdd:cd18574 126 SVTQTVGCVVSLYLISPKLTLLLLVIVPVVVLVGTLYGSFLRKLSRRAQAQVAKATGVADEALGNIRTVRAFAMEDRELE 205
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 338817954 275 RYQKHLENAKK--------IGIKKAISaNISMGIAFLLIYasyalafWYGSTLVISKEYTIGNAMT 332
Cdd:cd18574 206 LYEEEVEKAAKlneklglgIGIFQGLS-NLALNGIVLGVL-------YYGGSLVSRGELTAGDLMS 263
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
763-965 |
2.16e-14 |
|
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: 75.27 E-value: 2.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 763 FFTFFLQG-FTF------GKAGEILTTRLRSMAFKAMLRQDMSWFDDHKnsTGALSTRLATDaaqVQGATGTRLALIAQN 835
Cdd:cd18574 49 LGLYLLQSlLTFayisllSVVGERVAARLRNDLFSSLLRQDIAFFDTHR--TGELVNRLTAD---VQEFKSSFKQCVSQG 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 836 TANLG--TGIIISFIY-GWQLTLLLLSVVPFIAVAGIVEMKMLAGNAKRDKKEMEAAGKIATEAIENIRTVVSLTQERKF 912
Cdd:cd18574 124 LRSVTqtVGCVVSLYLiSPKLTLLLLVIVPVVVLVGTLYGSFLRKLSRRAQAQVAKATGVADEALGNIRTVRAFAMEDRE 203
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 338817954 913 ESMYVEKLhgpyrNSVRKAHIY-GITFSISQAFMYFSYAG----CFRFGSYLIVNGHM 965
Cdd:cd18574 204 LELYEEEV-----EKAAKLNEKlGLGIGIFQGLSNLALNGivlgVLYYGGSLVSRGEL 256
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
52-329 |
2.31e-14 |
|
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: 75.13 E-value: 2.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 52 LFMFLGTLMAIAhgsgLPLMMivfGEMTDKFVDNTGNfSLPVNFSlsmlnpgrileeEMTRYAYYYSGLGGGVLVAAYIQ 131
Cdd:cd18547 6 ILAIISTLLSVL----GPYLL---GKAIDLIIEGLGG-GGGVDFS------------GLLRILLLLLGLYLLSALFSYLQ 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 132 VSFWTLAAGRQIKKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDDVSKISEGIGDKVGMFFQAIATFFAGFIVGFIRGW 211
Cdd:cd18547 66 NRLMARVSQRTVYDLRKDLFEKLQRLPLSYFDTHSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISP 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 212 KLTLVIMAISPILGLSTAVWAKILSTFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKELERYQKHLENAKKIGIKKA 291
Cdd:cd18547 146 LLTLIVLVTVPLSLLVTKFIAKRSQKYFRKQQKALGELNGYIEEMISGQKVVKAFNREEEAIEEFDEINEELYKASFKAQ 225
|
250 260 270
....*....|....*....|....*....|....*...
gi 338817954 292 ISANISMGIAFLLIYASYALAFWYGSTLVISKEYTIGN 329
Cdd:cd18547 226 FYSGLLMPIMNFINNLGYVLVAVVGGLLVINGALTVGV 263
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
409-614 |
2.39e-14 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 77.37 E-value: 2.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 409 LKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVR-CLREIIGVVS----QEPVLFSTTI 483
Cdd:COG1129 268 VRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRdAIRAGIAYVPedrkGEGLVLDLSI 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 484 AENI------RYGRGNVtmdeIEKAVKEANAYDFIMKL---PQKFDTLVGdrgaQLSGGQKQRIAIARALVRNPKILLLD 554
Cdd:COG1129 348 RENItlasldRLSRGGL----LDRRRERALAEEYIKRLrikTPSPEQPVG----NLSGGNQQKVVLAKWLATDPKVLILD 419
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 338817954 555 EATSALDTESEAEVQAALDK-AREGRTTIVIahrlST-----IRNADVIAGFEDGVIVEQGSHSEL 614
Cdd:COG1129 420 EPTRGIDVGAKAEIYRLIRElAAEGKAVIVI----SSelpelLGLSDRILVMREGRIVGELDREEA 481
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
693-1249 |
3.09e-14 |
|
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: 77.15 E-value: 3.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 693 SFLKVLKlnKTEWPYFVVGTVCAIANGALqpafSIILSEMI--AIFGPGDDAVkqqkcnMFSLVFLGLGVLSFFTFFLQG 770
Cdd:COG4615 2 NLLRLLL--RESRWLLLLALLLGLLSGLA----NAGLIALInqALNATGAALA------RLLLLFAGLLVLLLLSRLASQ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 771 FTFGKAGEILTTRLRSMAFKAMLRQDMSWFDDHknSTGALSTRLATDAAQVQGATGtRLALIAQNTANlgtgIIISFIY- 849
Cdd:COG4615 70 LLLTRLGQHAVARLRLRLSRRILAAPLERLERI--GAARLLAALTEDVRTISQAFV-RLPELLQSVAL----VLGCLAYl 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 850 GWQLTLLLLSVVPFIAVAGIVEMKMLagnaKRDKKEMEAAGKIATEAIENIRTVVS------LTQERKfESMYVEKLHGP 923
Cdd:COG4615 143 AWLSPPLFLLTLVLLGLGVAGYRLLV----RRARRHLRRAREAEDRLFKHFRALLEgfkelkLNRRRR-RAFFDEDLQPT 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 924 ---YRNSVRKAH-IYGITFSISQAFMYFsyagcfrfgsyLIVnghmrfkdvILVFSAIVLGAVALGHASSFA-------- 991
Cdd:COG4615 218 aerYRDLRIRADtIFALANNWGNLLFFA-----------LIG---------LILFLLPALGWADPAVLSGFVlvllflrg 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 992 ---------PDYAKAKLSAAYLFSL---FERQPLIDSYSGEGLWPDKFEgSVTFNEVVFNYPTRANVP--VLQGLSLEVK 1057
Cdd:COG4615 278 plsqlvgalPTLSRANVALRKIEELelaLAAAEPAAADAAAPPAPADFQ-TLELRGVTYRYPGEDGDEgfTLGPIDLTIR 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1058 KGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQWLRAQLGIVSQEPILFDcsiaeniaygdnsRVVP 1137
Cdd:COG4615 357 RGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQLFSAVFSDFHLFD-------------RLLG 423
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1138 HDEIVRAAKeanIHPFIETLPQKYNTRVGDKG---TQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEAL 1214
Cdd:COG4615 424 LDGEADPAR---ARELLERLELDHKVSVEDGRfstTDLSQGQRKRLALLVALLEDRPILVFDEWAADQDPEFRRVFYTEL 500
|
570 580 590
....*....|....*....|....*....|....*...
gi 338817954 1215 ---DKAReGRTCIVIAHRLSTIQNADLIVVIENGKVKE 1249
Cdd:COG4615 501 lpeLKAR-GKTVIAISHDDRYFDLADRVLKMDYGKLVE 537
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
412-626 |
3.18e-14 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 73.81 E-value: 3.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 412 LNLKVKSGQTVALVGNSGCGKSTtvqLLQRLYD--PTEGKISIDGQDIRNFNVRCLREIIGVVSQE-PVLFSTTIAENI- 487
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKST---LLARMAGllPGSGSIQFAGQPLEAWSAAELARHRAYLSQQqTPPFAMPVFQYLt 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 488 RYGRGNVTMDEIEKAVKE-ANAYDFIMKLPqkfdTLVGdrgaQLSGGQKQRIAIARALVR-----NP--KILLLDEATSA 559
Cdd:PRK03695 92 LHQPDKTRTEAVASALNEvAEALGLDDKLG----RSVN----QLSGGEWQRVRLAAVVLQvwpdiNPagQLLLLDEPMNS 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 338817954 560 LDTESeaevQAALDK-----AREGRTTIVIAHRLS-TIRNADVIAGFEDGVIVEQGSHSELMKKE------GIYFRLVN 626
Cdd:PRK03695 164 LDVAQ----QAALDRllselCQQGIAVVMSSHDLNhTLRHADRVWLLKQGKLLASGRRDEVLTPEnlaqvfGVNFRRLD 238
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
1052-1251 |
3.64e-14 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 75.68 E-value: 3.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1052 LSLEVK-----KGQTlALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQ----EAKKLNVQWLRAQLGIVSQEPILF-DC 1121
Cdd:PRK11144 13 LCLTVNltlpaQGIT-AIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRvlfdAEKGICLPPEKRRIGYVFQDARLFpHY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1122 SIAENIAYG-DNSRVVPHDEIVRAAkeaNIHPFIETLPqkyntrvgdkgTQLSGGQKQRIAIARALIRQPRVLLLDEATS 1200
Cdd:PRK11144 92 KVRGNLRYGmAKSMVAQFDKIVALL---GIEPLLDRYP-----------GSLSGGEKQRVAIGRALLTAPELLLMDEPLA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 338817954 1201 ALDTESEKVVQEALDK-AREGRTCIV-IAHRLSTI-QNADLIVVIENGKVKEHG 1251
Cdd:PRK11144 158 SLDLPRKRELLPYLERlAREINIPILyVSHSLDEIlRLADRVVVLEQGKVKAFG 211
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
402-585 |
4.58e-14 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 72.39 E-value: 4.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 402 SRANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLREIIGVVSQEPVLFST 481
Cdd:TIGR01189 9 SRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLPGLKPEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 482 TIAENIRYGR--GNVTMDEIEKAVKEANAYDFImklpqkfDTLVgdrgAQLSGGQKQRIAIARALVRNPKILLLDEATSA 559
Cdd:TIGR01189 89 SALENLHFWAaiHGGAQRTIEDALAAVGLTGFE-------DLPA----AQLSAGQQRRLALARLWLSRRPLWILDEPTTA 157
|
170 180
....*....|....*....|....*.
gi 338817954 560 LDTESEAEVQAALDkAREGRTTIVIA 585
Cdd:TIGR01189 158 LDKAGVALLAGLLR-AHLARGGIVLL 182
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
397-587 |
6.91e-14 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 72.30 E-value: 6.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 397 HFSYPSRANIK-ILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIrNFNVRClreiigvvsqe 475
Cdd:COG2401 33 AFGVELRVVERyVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDVPDN-QFGREA----------- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 476 pvlfstTIAENIrYGRGNVTMD-EIEKAVKEANAYDFImklpQKFDtlvgdrgaQLSGGQKQRIAIARALVRNPKILLLD 554
Cdd:COG2401 101 ------SLIDAI-GRKGDFKDAvELLNAVGLSDAVLWL----RRFK--------ELSTGQKFRFRLALLLAERPKLLVID 161
|
170 180 190
....*....|....*....|....*....|....*
gi 338817954 555 EATSALDTESEAEVQAALDK-AREGRTTIVIA-HR 587
Cdd:COG2401 162 EFCSHLDRQTAKRVARNLQKlARRAGITLVVAtHH 196
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
418-609 |
7.20e-14 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 70.09 E-value: 7.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 418 SGQTVALVGNSGCGKSTTVQLLQRLYDPTEGK-ISIDGQDIRNFNVRCLREIIgvvsqepvlfsttiaenirygrgnvtm 496
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGvIYIDGEDILEEVLDQLLLII--------------------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 497 deiekavkeanaydfimklpqkfdtlVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALD--- 573
Cdd:smart00382 54 --------------------------VGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElrl 107
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 338817954 574 ----KAREGRTTIVIAHRLSTIRNADVIAGFEDGVIVEQG 609
Cdd:smart00382 108 llllKSEKNLTVILTTNDEKDLGPALLRRRFDRRIVLLLI 147
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
1033-1259 |
7.68e-14 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 75.78 E-value: 7.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1033 FNEVVFNYPTR--ANVPVlqglSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQWLRAQLG 1110
Cdd:PRK10522 325 LRNVTFAYQDNgfSVGPI----NLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFS 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1111 IVSQEPILFDcsiaeniaygdnsRVVPHDEivRAAKEANIHPFIETLPQKYNTRVGD---KGTQLSGGQKQRIAIARALI 1187
Cdd:PRK10522 401 AVFTDFHLFD-------------QLLGPEG--KPANPALVEKWLERLKMAHKLELEDgriSNLKLSKGQKKRLALLLALA 465
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 338817954 1188 RQPRVLLLDEATSALDTESEKVV-QEALDKARE-GRTCIVIAHRLSTIQNADLIVVIENGKVKE-HGTHQQLLAQ 1259
Cdd:PRK10522 466 EERDILLLDEWAADQDPHFRREFyQVLLPLLQEmGKTIFAISHDDHYFIHADRLLEMRNGQLSElTGEERDAASR 540
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
407-561 |
8.06e-14 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 72.84 E-value: 8.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 407 KILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQdirnfnvrcLReiIGVVSQEPVLFST---TI 483
Cdd:PRK09544 18 RVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGK---------LR--IGYVPQKLYLDTTlplTV 86
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 338817954 484 AENIRYgRGNVTMDEIEKAVKEANAYDFIMKLPQKfdtlvgdrgaqLSGGQKQRIAIARALVRNPKILLLDEATSALD 561
Cdd:PRK09544 87 NRFLRL-RPGTKKEDILPALKRVQAGHLIDAPMQK-----------LSGGETQRVLLARALLNRPQLLVLDEPTQGVD 152
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
708-965 |
1.03e-13 |
|
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: 73.29 E-value: 1.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 708 FVVGTVCAIANGALQPAFSIILSEMI--AIFGPGDDAVKqqkcnMFSLVFLGLGVLSFFTFFLQGFTFGKAGEILTTRLR 785
Cdd:cd18543 1 LILALLAALLATLAGLAIPLLTRRAIdgPIAHGDRSALW-----PLVLLLLALGVAEAVLSFLRRYLAGRLSLGVEHDLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 786 SMAFKAMLRQDMSWFDdhKNSTGALSTRLATDAAQVQGATGtRLALIAQNTANLGTGIIISFIYGWQLTLLLLSVVPFIA 865
Cdd:cd18543 76 TDLFAHLQRLDGAFHD--RWQSGQLLSRATSDLSLVQRFLA-FGPFLLGNLLTLVVGLVVMLVLSPPLALVALASLPPLV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 866 VAGIVEMKMLAGNAKRDKkemEAAGKIATEAIEN---IRTVVSLTQERKFESMYVEKLHGPYRNSVRKAHIYGITFSISQ 942
Cdd:cd18543 153 LVARRFRRRYFPASRRAQ---DQAGDLATVVEESvtgIRVVKAFGRERRELDRFEAAARRLRATRLRAARLRARFWPLLE 229
|
250 260
....*....|....*....|...
gi 338817954 943 AFMYFSYAGCFRFGSYLIVNGHM 965
Cdd:cd18543 230 ALPELGLAAVLALGGWLVANGSL 252
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
708-967 |
1.09e-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: 350009 [Multi-domain] Cd Length: 313 Bit Score: 73.37 E-value: 1.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 708 FVVGTVCAIANGALQPAFSIILSemIAIfgpgdDAVKQQKCNMFSLV------------FLGLGVLSFFTF-------FL 768
Cdd:cd18565 1 LVLGLLASILNRLFDLAPPLLIG--VAI-----DAVFNGEASFLPLVpaslgpadprgqLWLLGGLTVAAFlleslfqYL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 769 QGFTFGKAGEILTTRLRSMAFKAMLRQDMSWFDDHknSTGALSTRLATDAAQVQGATGTRLALIAQNTANLGTGIIISFI 848
Cdd:cd18565 74 SGVLWRRFAQRVQHDLRTDTYDHVQRLDMAFFEDR--QTGDLMSVLNNDVNQLERFLDDGANSIIRVVVTVLGIGAILFY 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 849 YGWQLTLLLLSVVPFIAVAGIVEMKMLagnAKRDKKEMEAAGKIAT---EAIENIRTVVSLTQERkFESMYVEKLHGPYR 925
Cdd:cd18565 152 LNWQLALVALLPVPLIIAGTYWFQRRI---EPRYRAVREAVGDLNArleNNLSGIAVIKAFTAED-FERERVADASEEYR 227
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 338817954 926 NSVRKAHIYGITFsisQAFMYF----SYAGCFRFGSYLIVNGHMRF 967
Cdd:cd18565 228 DANWRAIRLRAAF---FPVIRLvagaGFVATFVVGGYWVLDGPPLF 270
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
708-965 |
1.46e-13 |
|
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: 72.82 E-value: 1.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 708 FVVGTVCAIANGALQPAFSIILSEMI-AIFGP--GDDAVKQQKCNMFSLVFLGLGVLSFFTFFLQGFTFGKAGEILTTRL 784
Cdd:cd18547 1 LILVIILAIISTLLSVLGPYLLGKAIdLIIEGlgGGGGVDFSGLLRILLLLLGLYLLSALFSYLQNRLMARVSQRTVYDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 785 RSMAFKAMLRQDMSWFDdhKNSTGALSTRLATDAAQVQGATGTRLALIAQNTANLGTGIIISFIYGWQLTLLLLSVVPFI 864
Cdd:cd18547 81 RKDLFEKLQRLPLSYFD--THSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPLLTLIVLVTVPLS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 865 AVAgiveMKMLAGNAKRD-KKEMEAAGKI---ATEAIENIRTVVSLTQERKFESMYvEKLHGPYRNSVRKAHIY-GITFS 939
Cdd:cd18547 159 LLV----TKFIAKRSQKYfRKQQKALGELngyIEEMISGQKVVKAFNREEEAIEEF-DEINEELYKASFKAQFYsGLLMP 233
|
250 260
....*....|....*....|....*.
gi 338817954 940 ISQAFMYFSYAGCFRFGSYLIVNGHM 965
Cdd:cd18547 234 IMNFINNLGYVLVAVVGGLLVINGAL 259
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
408-614 |
1.50e-13 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 72.04 E-value: 1.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 408 ILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDP----TEGKISIDGQDIRNFNVRclREIIGVVSQ------EPV 477
Cdd:PRK10418 18 LVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGKPVAPCALR--GRKIATIMQnprsafNPL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 478 LFSTTIAENIRYGRGNVTMDEIEKAVKEANAYDFIMKLPQKFdtlvgdrGAQLSGGQKQRIAIARALVRNPKILLLDEAT 557
Cdd:PRK10418 96 HTMHTHARETCLALGKPADDATLTAALEAVGLENAARVLKLY-------PFEMSGGMLQRMMIALALLCEAPFIIADEPT 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 558 SALDTESEAEVQAALDK--AREGRTTIVIAHRLSTI-RNADVIAGFEDGVIVEQGSHSEL 614
Cdd:PRK10418 169 TDLDVVAQARILDLLESivQKRALGMLLVTHDMGVVaRLADDVAVMSHGRIVEQGDVETL 228
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
390-616 |
2.02e-13 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 72.85 E-value: 2.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 390 NLEFSDVHF---SYPSRANIKIlkglNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYD-P---TEGKISIDGQDIRNFNV 462
Cdd:PRK11022 5 NVDKLSVHFgdeSAPFRAVDRI----SYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDyPgrvMAEKLEFNGQDLQRISE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 463 RCLREIIG----VVSQEPVlfsTTIaeNIRYGRGNVTMDEIE------KAVKEANAYDFImklpqkfdTLVG--DRGA-- 528
Cdd:PRK11022 81 KERRNLVGaevaMIFQDPM---TSL--NPCYTVGFQIMEAIKvhqggnKKTRRQRAIDLL--------NQVGipDPASrl 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 529 -----QLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALD--KAREGRTTIVIAHRLSTI-RNADVIAGF 600
Cdd:PRK11022 148 dvyphQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLelQQKENMALVLITHDLALVaEAAHKIIVM 227
|
250
....*....|....*.
gi 338817954 601 EDGVIVEQGSHSELMK 616
Cdd:PRK11022 228 YAGQVVETGKAHDIFR 243
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
108-555 |
2.32e-13 |
|
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: 74.45 E-value: 2.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 108 EEMTRYAYYYSGLGGGVLVAAYI-QVSFWTLAAgRQIKKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDDVSKISEgig 186
Cdd:COG4615 45 AALARLLLLFAGLLVLLLLSRLAsQLLLTRLGQ-HAVARLRLRLSRRILAAPLERLERIGAARLLAALTEDVRTISQ--- 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 187 dkvgmFFQAIATFFAGFIVGFirgwkLTLVIMA-ISPILGLSTAVWAKILSTF---SDKELAAYAKAGAVAEEAL-GAIR 261
Cdd:COG4615 121 -----AFVRLPELLQSVALVL-----GCLAYLAwLSPPLFLLTLVLLGLGVAGyrlLVRRARRHLRRAREAEDRLfKHFR 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 262 TVIafGGqNKEL------------ERYQKHLENAKKIGIKKAISANISMGIAFLLIYASYALAFWYGSTLV-ISKEYTIG 328
Cdd:COG4615 191 ALL--EG-FKELklnrrrrraffdEDLQPTAERYRDLRIRADTIFALANNWGNLLFFALIGLILFLLPALGwADPAVLSG 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 329 NAMTVFFsiLIGAfsVGQAAPCIDAFANARGAAyvifdiidnnPKIDSFSERGHKPDNIKGN------------LEFSDV 396
Cdd:COG4615 268 FVLVLLF--LRGP--LSQLVGALPTLSRANVAL----------RKIEELELALAAAEPAAADaaappapadfqtLELRGV 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 397 HFSYPSRANIK--ILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLREIIGVVSQ 474
Cdd:COG4615 334 TYRYPGEDGDEgfTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQLFSAVFS 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 475 EPVLFSTTiaenirYGRGNVTMDEiekavkEANAYDFIMKLPQK-------FDTLvgdrgaQLSGGQKQRIAIARALVRN 547
Cdd:COG4615 414 DFHLFDRL------LGLDGEADPA------RARELLERLELDHKvsvedgrFSTT------DLSQGQRKRLALLVALLED 475
|
....*...
gi 338817954 548 PKILLLDE 555
Cdd:COG4615 476 RPILVFDE 483
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
1044-1251 |
2.53e-13 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 71.27 E-value: 2.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1044 ANVPVLQGLSLEVKKGQTLALVGSSGCGKS----TVVQLLERFYDPMAGSVLLDGQ--EAKKLN---------------- 1101
Cdd:PRK10418 14 AAQPLVHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDGKpvAPCALRgrkiatimqnprsafn 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1102 -VQWLRA-------QLGIVSQEPILFDCsiAENIAYGDNSRVvphdeivraakeANIHPFietlpqkyntrvgdkgtQLS 1173
Cdd:PRK10418 94 pLHTMHTharetclALGKPADDATLTAA--LEAVGLENAARV------------LKLYPF-----------------EMS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1174 GGQKQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLSTIQN-ADLIVVIENGKVKEH 1250
Cdd:PRK10418 143 GGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESivQKRALGMLLVTHDMGVVARlADDVAVMSHGRIVEQ 222
|
.
gi 338817954 1251 G 1251
Cdd:PRK10418 223 G 223
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
409-591 |
3.16e-13 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 71.45 E-value: 3.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 409 LKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRnfnvRCLRE-IIGVVSQEPVL---FSTTIA 484
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTR----QALQKnLVAYVPQSEEVdwsFPVLVE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 485 ENIRYGR-GNVTMDEIEKA-----VKEANAYDFIMKLPQKfdtlvgdRGAQLSGGQKQRIAIARALVRNPKILLLDEATS 558
Cdd:PRK15056 99 DVVMMGRyGHMGWLRRAKKrdrqiVTAALARVDMVEFRHR-------QIGELSGGQKKRVFLARAIAQQGQVILLDEPFT 171
|
170 180 190
....*....|....*....|....*....|....
gi 338817954 559 ALDTESEAEVQAALDKAR-EGRTTIVIAHRLSTI 591
Cdd:PRK15056 172 GVDVKTEARIISLLRELRdEGKTMLVSTHNLGSV 205
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
123-328 |
4.95e-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: 350007 [Multi-domain] Cd Length: 296 Bit Score: 71.39 E-value: 4.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 123 GVLVAAYIQVSF--W------TLAAGRQIKKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDDVSKISEGIGDKVGMFFQ 194
Cdd:cd18563 47 LGLAGAYVLSALlgIlrgrllARLGERITADLRRDLYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDFLSDGLPDFLT 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 195 AIATFFAGFIVGFIRGWKLTLVIMAISPILGLSTAVWAKILSTFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKELE 274
Cdd:cd18563 127 NILMIIGIGVVLFSLNWKLALLVLIPVPLVVWGSYFFWKKIRRLFHRQWRRWSRLNSVLNDTLPGIRVVKAFGQEKREIK 206
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 338817954 275 RYQKHLENAKKIGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTIG 328
Cdd:cd18563 207 RFDEANQELLDANIRAEKLWATFFPLLTFLTSLGTLIVWYFGGRQVLSGTMTLG 260
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
411-609 |
5.34e-13 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 70.40 E-value: 5.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 411 GLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDI--------------RNF-NVRCLREIIGV---- 471
Cdd:PRK11300 23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIeglpghqiarmgvvRTFqHVRLFREMTVIenll 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 472 VSQEPVLFSTTIAenirygrGNVTMDEIEKAvkEANAYDFIMKLPQKFDTL-VGDRGA-QLSGGQKQRIAIARALVRNPK 549
Cdd:PRK11300 103 VAQHQQLKTGLFS-------GLLKTPAFRRA--ESEALDRAATWLERVGLLeHANRQAgNLAYGQQRRLEIARCMVTQPE 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 338817954 550 ILLLDEATSALDTESEAEVQAALDKARE--GRTTIVIAHRLStirnadVIAGFEDGVIV-EQG 609
Cdd:PRK11300 174 ILMLDEPAAGLNPKETKELDELIAELRNehNVTVLLIEHDMK------LVMGISDRIYVvNQG 230
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
391-617 |
6.34e-13 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 70.21 E-value: 6.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 391 LEFSDVHFSYPSRAnikILKGLNLKVKSGQTVALVGNSGCGKSTTVQLL--QRLYDPTEGKISIDGQDIRNFN------- 461
Cdd:PRK09580 2 LSIKDLHVSVEDKA---ILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLagREDYEVTGGTVEFKGKDLLELSpedrage 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 462 -----VRCLREIIGVVSQepvLFSTTIAENIRYGRGNVTMDEIEKAvkeanayDFI------MKLPQkfDTLVGDRGAQL 530
Cdd:PRK09580 79 gifmaFQYPVEIPGVSNQ---FFLQTALNAVRSYRGQEPLDRFDFQ-------DLMeekialLKMPE--DLLTRSVNVGF 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 531 SGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKAREG-RTTIVIAH--RLSTIRNADVIAGFEDGVIVE 607
Cdd:PRK09580 147 SGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGkRSFIIVTHyqRILDYIKPDYVHVLYQGRIVK 226
|
250
....*....|
gi 338817954 608 QGSHSeLMKK 617
Cdd:PRK09580 227 SGDFT-LVKQ 235
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
1047-1229 |
6.88e-13 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 69.22 E-value: 6.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1047 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERfydpmagsVLLDGQEAKKLNVQWLraqlgivsqePILFDCSIAEN 1126
Cdd:COG2401 44 YVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAG--------ALKGTPVAGCVDVPDN----------QFGREASLIDA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1127 IA-YGDNSRVVphdEIVRAAKEANihpfietlPQKYNTRVgdkgTQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTE 1205
Cdd:COG2401 106 IGrKGDFKDAV---ELLNAVGLSD--------AVLWLRRF----KELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQ 170
|
170 180
....*....|....*....|....*.
gi 338817954 1206 SEKVVQEALDKA--REGRTCIVIAHR 1229
Cdd:COG2401 171 TAKRVARNLQKLarRAGITLVVATHH 196
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
394-591 |
7.02e-13 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 72.45 E-value: 7.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 394 SDVHFSYPSranIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIrNFNV--RCLREIIGV 471
Cdd:PRK10982 2 SNISKSFPG---VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEI-DFKSskEALENGISM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 472 VSQE-PVLFSTTIAENI---RYGRGNVTMDEiEKAVKEANAYdfimklpqkFDTL-----VGDRGAQLSGGQKQRIAIAR 542
Cdd:PRK10982 78 VHQElNLVLQRSVMDNMwlgRYPTKGMFVDQ-DKMYRDTKAI---------FDELdididPRAKVATLSVSQMQMIEIAK 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 338817954 543 ALVRNPKILLLDEATSALdteSEAEVQ---AALDKARE-GRTTIVIAHRLSTI 591
Cdd:PRK10982 148 AFSYNAKIVIMDEPTSSL---TEKEVNhlfTIIRKLKErGCGIVYISHKMEEI 197
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
408-591 |
9.60e-13 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 73.22 E-value: 9.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 408 ILKGLNLKVKSGQTVALVGNSGCGKSTtvqLLQRLYDPTEGKISIDGQDIRNFNVR--CLREIIGVVSQEPV-LFSTTIA 484
Cdd:TIGR00956 778 ILNNVDGWVKPGTLTALMGASGAGKTT---LLNVLAERVTTGVITGGDRLVNGRPLdsSFQRSIGYVQQQDLhLPTSTVR 854
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 485 ENIRYGRGNVTMDEIEKavKEANAY-DFIMKL---PQKFDTLVGDRGAQLSGGQKQRIAIARALVRNPKILL-LDEATSA 559
Cdd:TIGR00956 855 ESLRFSAYLRQPKSVSK--SEKMEYvEEVIKLlemESYADAVVGVPGEGLNVEQRKRLTIGVELVAKPKLLLfLDEPTSG 932
|
170 180 190
....*....|....*....|....*....|...
gi 338817954 560 LDTESEAEVQAALDK-AREGRTTIVIAHRLSTI 591
Cdd:TIGR00956 933 LDSQTAWSICKLMRKlADHGQAILCTIHQPSAI 965
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
708-971 |
1.04e-12 |
|
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: 70.17 E-value: 1.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 708 FVVGTVCAIANGALQPAFSIILSEMIaifgpgDDAVKQQKCNMFSLVFLGLGVLSFFTFFLQgFTFGKAGEILTTR---- 783
Cdd:cd18549 4 FFLDLFCAVLIAALDLVFPLIVRYII------DDLLPSKNLRLILIIGAILLALYILRTLLN-YFVTYWGHVMGARietd 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 784 LRSMAFKAMLRQDMSWFDDHKnsTGALSTRLATDAAQVqgatgTRLA-------LIAqnTANLGTGIIISFIYGWQLTLL 856
Cdd:cd18549 77 MRRDLFEHLQKLSFSFFDNNK--TGQLMSRITNDLFDI-----SELAhhgpedlFIS--IITIIGSFIILLTINVPLTLI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 857 LLSVVPFIAVAGIVEMKMLAGNAKRDKKEMeaaGKI---ATEAIENIRTVVSLTQE----RKFESMYVEklhgpYRNSVR 929
Cdd:cd18549 148 VFALLPLMIIFTIYFNKKMKKAFRRVREKI---GEInaqLEDSLSGIRVVKAFANEeyeiEKFDEGNDR-----FLESKK 219
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 338817954 930 KAHIY-GITFSISQAFMYFSYAGCFRFGSYLIVNGHMRFKDVI 971
Cdd:cd18549 220 KAYKAmAYFFSGMNFFTNLLNLVVLVAGGYFIIKGEITLGDLV 262
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
407-610 |
1.32e-12 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 69.27 E-value: 1.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 407 KILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLY--DPT-EGKISIDGQDIRNF-----NVRCLREIIGVVSQEPVL 478
Cdd:PRK09984 18 QALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgDKSaGSHIELLGRTVQREgrlarDIRKSRANTGYIFQQFNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 479 FST-TIAENIRYGRGNVT------MDEIEKAVKEaNAYDFIMKLPQKFdtLVGDRGAQLSGGQKQRIAIARALVRNPKIL 551
Cdd:PRK09984 98 VNRlSVLENVLIGALGSTpfwrtcFSWFTREQKQ-RALQALTRVGMVH--FAHQRVSTLSGGQQQRVAIARALMQQAKVI 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 338817954 552 LLDEATSALDTESEAEVQAALD--KAREGRTTIVIAHRLS-TIRNADVIAGFEDGVIVEQGS 610
Cdd:PRK09984 175 LADEPIASLDPESARIVMDTLRdiNQNDGITVVVTLHQVDyALRYCERIVALRQGHVFYDGS 236
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
404-592 |
2.18e-12 |
|
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: 71.70 E-value: 2.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 404 ANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQ--------RLYDPTEGKISIDGQDiRNFNVRCLREiigvvsqe 475
Cdd:TIGR00954 463 NGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGelwpvyggRLTKPAKGKLFYVPQR-PYMTLGTLRD-------- 533
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 476 PVLFSTTIAENIRYGRGNVTMDEIEKAVKeanaYDFIMKLPQKFDTlVGDRGAQLSGGQKQRIAIARALVRNPKILLLDE 555
Cdd:TIGR00954 534 QIIYPDSSEDMKRRGLSDKDLEQILDNVQ----LTHILEREGGWSA-VQDWMDVLSGGEKQRIAMARLFYHKPQFAILDE 608
|
170 180 190
....*....|....*....|....*....|....*...
gi 338817954 556 ATSALDTESEaevQAALDKARE-GRTTIVIAHRLSTIR 592
Cdd:TIGR00954 609 CTSAVSVDVE---GYMYRLCREfGITLFSVSHRKSLWK 643
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
419-609 |
2.37e-12 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 68.41 E-value: 2.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 419 GQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLREII---------GVVSQEP-------VLFSTT 482
Cdd:PRK11701 32 GEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALSEAErrrllrtewGFVHQHPrdglrmqVSAGGN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 483 IAENI------RYGRGNVT----MDEIEKAVkeanayDFIMKLPQKFdtlvgdrgaqlSGGQKQRIAIARALVRNPKILL 552
Cdd:PRK11701 112 IGERLmavgarHYGDIRATagdwLERVEIDA------ARIDDLPTTF-----------SGGMQQRLQIARNLVTHPRLVF 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 338817954 553 LDEATSALDTeseaEVQAA-LDKARE-----GRTTIVIAHRLSTIRN-ADVIAGFEDGVIVEQG 609
Cdd:PRK11701 175 MDEPTGGLDV----SVQARlLDLLRGlvrelGLAVVIVTHDLAVARLlAHRLLVMKQGRVVESG 234
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
406-583 |
2.57e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 69.35 E-value: 2.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 406 IKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDI---RNFNVRclreIIGVV----SQ---- 474
Cdd:COG4586 35 VEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPfkrRKEFAR----RIGVVfgqrSQlwwd 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 475 EPVLFSTTIAENIrYGrgnVTMDEIEKAVKEanaYDFIMKLPQKFDTLVgdRgaQLSGGQKQRIAIARALVRNPKILLLD 554
Cdd:COG4586 111 LPAIDSFRLLKAI-YR---IPDAEYKKRLDE---LVELLDLGELLDTPV--R--QLSLGQRMRCELAAALLHRPKILFLD 179
|
170 180 190
....*....|....*....|....*....|
gi 338817954 555 EATSALDTESEAEVQAALDK-AREGRTTIV 583
Cdd:COG4586 180 EPTIGLDVVSKEAIREFLKEyNRERGTTIL 209
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
411-586 |
2.73e-12 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 67.14 E-value: 2.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 411 GLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRnfnvRClREII-----------GVvsqEPVLf 479
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIR----RQ-RDEYhqdllylghqpGI---KTEL- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 480 stTIAENIRY---GRGNVTMDEIEKAvkeanaydfimkLPQkfdtlVGDRG------AQLSGGQKQRIAIARALVRNPKI 550
Cdd:PRK13538 90 --TALENLRFyqrLHGPGDDEALWEA------------LAQ-----VGLAGfedvpvRQLSAGQQRRVALARLWLTRAPL 150
|
170 180 190
....*....|....*....|....*....|....*..
gi 338817954 551 LLLDEATSALDTESEAEVQAALDK-AREGRTTIVIAH 586
Cdd:PRK13538 151 WILDEPFTAIDKQGVARLEALLAQhAEQGGMVILTTH 187
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
1058-1239 |
3.13e-12 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 65.47 E-value: 3.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1058 KGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVlldgqeakklnvqwlraqlgivsqepILFDCSIAeniaygdnsrvvp 1137
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGV--------------------------IYIDGEDI------------- 41
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1138 hdeivraakeanihpFIETLPQKYNTRVGDKGTQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEALD-- 1215
Cdd:smart00382 42 ---------------LEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElr 106
|
170 180
....*....|....*....|....*....
gi 338817954 1216 -----KAREGRTCIVIAHRLSTIQNADLI 1239
Cdd:smart00382 107 lllllKSEKNLTVILTTNDEKDLGPALLR 135
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1031-1230 |
5.52e-12 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 67.45 E-value: 5.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1031 VTFNEVVFNYPTRAnvpVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQeakklnvqwLRaqLG 1110
Cdd:PRK09544 5 VSLENVSVSFGQRR---VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGK---------LR--IG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1111 IVSQEpILFDCSIAENIaygdnSRV------VPHDEIVRAAKEANIHPFIETLPQKyntrvgdkgtqLSGGQKQRIAIAR 1184
Cdd:PRK09544 71 YVPQK-LYLDTTLPLTV-----NRFlrlrpgTKKEDILPALKRVQAGHLIDAPMQK-----------LSGGETQRVLLAR 133
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 338817954 1185 ALIRQPRVLLLDEATSALDTESEKVVQEALDKAREGRTCIV--IAHRL 1230
Cdd:PRK09544 134 ALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVlmVSHDL 181
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
753-914 |
5.88e-12 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350008 [Multi-domain] Cd Length: 307 Bit Score: 68.31 E-value: 5.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 753 LVFLGLGVLSFFTFFLQGFTFGKAGEILTTRLRSMAFKAMLRQDMSWFDDHKnsTGALSTRLATDAAQVQGATGTRLALI 832
Cdd:cd18564 58 AALVGIALLRGLASYAGTYLTALVGQRVVLDLRRDLFAHLQRLSLSFHDRRR--TGDLLSRLTGDVGAIQDLLVSGVLPL 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 833 AQNTANLGTGIIISFIYGWQLTLLLLSVVPFIAVAGIV---EMKMLAGNAKRDKKEMEAagkIATEAIENIRTVVSLTQE 909
Cdd:cd18564 136 LTNLLTLVGMLGVMFWLDWQLALIALAVAPLLLLAARRfsrRIKEASREQRRREGALAS---VAQESLSAIRVVQAFGRE 212
|
....*
gi 338817954 910 RKFES 914
Cdd:cd18564 213 EHEER 217
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1045-1252 |
6.54e-12 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 66.97 E-value: 6.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1045 NVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERF--YDPMAGSVLLDGQEAKKLNVQwLRAQLGI----------- 1111
Cdd:CHL00131 19 ENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHpaYKILEGDILFKGESILDLEPE-ERAHLGIflafqypieip 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1112 -VSQEPILfdcsiaeNIAYgdNSRvvphdEIVRAAKEANIHPFIETLPQKYNTrVGDKGTQL--------SGGQKQRIAI 1182
Cdd:CHL00131 98 gVSNADFL-------RLAY--NSK-----RKFQGLPELDPLEFLEIINEKLKL-VGMDPSFLsrnvnegfSGGEKKRNEI 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 338817954 1183 ARALIRQPRVLLLDEATSALDTESEKVVQEALDKAREGRTCIV-IAH--RLSTIQNADLIVVIENGKVKEHGT 1252
Cdd:CHL00131 163 LQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIIlITHyqRLLDYIKPDYVHVMQNGKIIKTGD 235
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
391-555 |
6.70e-12 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 69.62 E-value: 6.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 391 LEFSDVHFSYPSRANIkiLKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLREIIG 470
Cdd:PRK10522 323 LELRNVTFAYQDNGFS--VGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFS 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 471 VVSQEPVLFSTTIAEnirygrgnvtmdeiEKAVKEANAYDF---IMKLPQKFdTLVGDRGA--QLSGGQKQRIAIARALV 545
Cdd:PRK10522 401 AVFTDFHLFDQLLGP--------------EGKPANPALVEKwleRLKMAHKL-ELEDGRISnlKLSKGQKKRLALLLALA 465
|
170
....*....|
gi 338817954 546 RNPKILLLDE 555
Cdd:PRK10522 466 EERDILLLDE 475
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1048-1262 |
6.75e-12 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 66.84 E-value: 6.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1048 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQwLRAQLGI--VSQEPILFD-CSIA 1124
Cdd:PRK10895 18 VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLH-ARARRGIgyLPQEASIFRrLSVY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1125 ENIA-----YGDNSRVVPHDEIVRAAKEANIHPFIETLpqkyntrvgdkGTQLSGGQKQRIAIARALIRQPRVLLLDEAT 1199
Cdd:PRK10895 97 DNLMavlqiRDDLSAEQREDRANELMEEFHIEHLRDSM-----------GQSLSGGERRRVEIARALAANPKFILLDEPF 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 338817954 1200 SALDTESEKVVQEALDKARE-GRTCIVIAHRL-STIQNADLIVVIENGKVKEHGTHQQLLAQKGI 1262
Cdd:PRK10895 166 AGVDPISVIDIKRIIEHLRDsGLGVLITDHNVrETLAVCERAYIVSQGHLIAHGTPTEILQDEHV 230
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
381-614 |
7.09e-12 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 67.48 E-value: 7.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 381 GHKPDNIkgnLEFSDVHFSypsRANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNF 460
Cdd:PRK11831 1 EQSVANL---VDMRGVSFT---RGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAM 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 461 NVRCL---REIIGVVSQEPVLFS-TTIAENIRYG-RGNVTMDE--IEKAVkeanaydfIMKLPQkfdtlVGDRGA----- 528
Cdd:PRK11831 75 SRSRLytvRKRMSMLFQSGALFTdMNVFDNVAYPlREHTQLPAplLHSTV--------MMKLEA-----VGLRGAaklmp 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 529 -QLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEA-------EVQAALdkareGRTTIVIAHR----LSTIRNADV 596
Cdd:PRK11831 142 sELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGvlvklisELNSAL-----GVTCVVVSHDvpevLSIADHAYI 216
|
250
....*....|....*...
gi 338817954 597 IAgfeDGVIVEQGSHSEL 614
Cdd:PRK11831 217 VA---DKKIVAHGSAQAL 231
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
391-617 |
7.66e-12 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 66.97 E-value: 7.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 391 LEFSDVHFSYpsrANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLL--QRLYDPTEGKISIDGQDIRNFN--VRCLR 466
Cdd:CHL00131 8 LEIKNLHASV---NENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIagHPAYKILEGDILFKGESILDLEpeERAHL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 467 ----------EIIGVVSQEpvlFSTTIAENIRYGRGNVTMDEIEkavkeanAYDFIM------KLPQKFDTLVGDRGaqL 530
Cdd:CHL00131 85 giflafqypiEIPGVSNAD---FLRLAYNSKRKFQGLPELDPLE-------FLEIINeklklvGMDPSFLSRNVNEG--F 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 531 SGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDK-AREGRTTIVIAH--RLSTIRNADVIAGFEDGVIVE 607
Cdd:CHL00131 153 SGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKlMTSENSIILITHyqRLLDYIKPDYVHVMQNGKIIK 232
|
250
....*....|
gi 338817954 608 QGShSELMKK 617
Cdd:CHL00131 233 TGD-AELAKE 241
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
140-332 |
1.26e-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: 67.11 E-value: 1.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 140 GRQIKKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDDVSKISEGIGDKVGMFFQAIATFFAGFIVGFIRGWKLTLV-IM 218
Cdd:cd18589 65 SRIHSRLQGLVFAAVLRQEIAFFDSNQTGDIVSRVTTDTEDMSESLSENLSLLMWYLARGLFLFIFMLWLSPKLALLtAL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 219 AISPILGLSTAV--WAKILSTFSDKELAAYAKAGAvaeEALGAIRTVIAFGGQNKELERYQKHLENAKKIGIKKAISANI 296
Cdd:cd18589 145 GLPLLLLVPKFVgkFQQSLAVQVQKSLARANQVAV---ETFSAMKTVRSFANEEGEAQRYRQRLQKTYRLNKKEAAAYAV 221
|
170 180 190
....*....|....*....|....*....|....*....
gi 338817954 297 SM---GIAFLLIYASyalAFWYGSTLVISKEYTIGNAMT 332
Cdd:cd18589 222 SMwtsSFSGLALKVG---ILYYGGQLVTAGTVSSGDLVT 257
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
144-335 |
1.39e-11 |
|
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: 66.70 E-value: 1.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 144 KKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDdVSKISEGIGDKVGMFFQAIATFFAGFIVGFIRGWKLTLVIMAISPI 223
Cdd:cd18570 75 IRLILGYFKHLLKLPLSFFETRKTGEIISRFND-ANKIREAISSTTISLFLDLLMVIISGIILFFYNWKLFLITLLIIPL 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 224 LGLSTAVWAKILSTFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKELERYQKHLENAKKIGIKKAISANISMGIAFL 303
Cdd:cd18570 154 YILIILLFNKPFKKKNREVMESNAELNSYLIESLKGIETIKSLNAEEQFLKKIEKKFSKLLKKSFKLGKLSNLQSSIKGL 233
|
170 180 190
....*....|....*....|....*....|....*..
gi 338817954 304 LIYASYALAFWYGSTLVISKEYTIG-----NAMTVFF 335
Cdd:cd18570 234 ISLIGSLLILWIGSYLVIKGQLSLGqliafNALLGYF 270
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
749-965 |
1.55e-11 |
|
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen processing 2 (TAP2); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350034 [Multi-domain] Cd Length: 289 Bit Score: 66.59 E-value: 1.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 749 NMFSLVFLGLGVLSFFTFFLQG-----FTFgkAGEILTTRLRSMAFKAMLRQDMSWFDdhKNSTGALSTRLATDAAQVQG 823
Cdd:cd18590 33 NAFTSAIGLMCLFSLGSSLSAGlrgglFMC--TLSRLNLRLRHQLFSSLVQQDIGFFE--KTKTGDLTSRLSTDTTLMSR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 824 ATGTRLALIAQNTANlgTGIIISFIYG--WQLTLLLLSVVPFIAVAgiveMKMLAGNAKRDKKEME----AAGKIATEAI 897
Cdd:cd18590 109 SVALNANVLLRSLVK--TLGMLGFMLSlsWQLTLLTLIEMPLTAIA----QKVYNTYHQKLSQAVQdsiaKAGELAREAV 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 338817954 898 ENIRTVVSLTQERKFESMYVEKLHGPYRNSVRKAHIYGITFSISQAFMYFSYAGCFRFGSYLIVNGHM 965
Cdd:cd18590 183 SSIRTVRSFKAEEEEACRYSEALERTYNLKDRRDTVRAVYLLVRRVLQLGVQVLMLYCGRQLIQSGHL 250
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1036-1259 |
1.62e-11 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 67.06 E-value: 1.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1036 VVFNYPTrANVPVLQGLSLEVKKGQTLALVGSSGCGKS-TVVQLLERFYDP--MAGSVLLDGQE-----AKKLNVqwLRA 1107
Cdd:PRK09473 20 VTFSTPD-GDVTAVNDLNFSLRAGETLGIVGESGSGKSqTAFALMGLLAANgrIGGSATFNGREilnlpEKELNK--LRA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1108 -QLGIVSQEP-----------------ILFDCSIAENIAYGDNSRVVPHDEIVRAAKEANIHPFietlpqkyntrvgdkg 1169
Cdd:PRK09473 97 eQISMIFQDPmtslnpymrvgeqlmevLMLHKGMSKAEAFEESVRMLDAVKMPEARKRMKMYPH---------------- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1170 tQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEALDK-AREGRTCIV-IAHRLSTIQN-ADLIVVIENGK 1246
Cdd:PRK09473 161 -EFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNElKREFNTAIImITHDLGVVAGiCDKVLVMYAGR 239
|
250
....*....|...
gi 338817954 1247 VKEHGTHQQLLAQ 1259
Cdd:PRK09473 240 TMEYGNARDVFYQ 252
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
400-613 |
1.96e-11 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 65.51 E-value: 1.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 400 YPSRANIKILKGLNLKVKSG-----QTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDirnfnvrclreiigvVSQ 474
Cdd:cd03237 1 YTYPTMKKTLGEFTLEVEGGsisesEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDT---------------VSY 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 475 EPVLFSTTIAENIRYgrgnvTMDEIEKAVKEANAYDF-IMKlPQKFDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLL 553
Cdd:cd03237 66 KPQYIKADYEGTVRD-----LLSSITKDFYTHPYFKTeIAK-PLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLL 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 338817954 554 DEATSALDTESEAEVQAALDKAREG--RTTIVIAHrlsTIRNADVIAgfeDGVIVEQGSHSE 613
Cdd:cd03237 140 DEPSAYLDVEQRLMASKVIRRFAENneKTAFVVEH---DIIMIDYLA---DRLIVFEGEPSV 195
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
1043-1252 |
2.10e-11 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 66.00 E-value: 2.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1043 RANVpVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLE-RFYDPMA-------GSVLLDGQEAKKLNVQWL---RAQLGI 1111
Cdd:PRK13547 12 RHRA-ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAgDLTGGGAprgarvtGDVTLNGEPLAAIDAPRLarlRAVLPQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1112 VSQEPILFdcSIAENIAYGDnsrvVPHdeiVRAAKEANIHPFiETLPQKY-----NTRVGDKGTQLSGGQKQRIAIARAL 1186
Cdd:PRK13547 91 AAQPAFAF--SAREIVLLGR----YPH---ARRAGALTHRDG-EIAWQALalagaTALVGRDVTTLSGGELARVQFARVL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 338817954 1187 ---------IRQPRVLLLDEATSALD-TESEKVVQEALDKAREGRT-CIVIAHRLS-TIQNADLIVVIENGKVKEHGT 1252
Cdd:PRK13547 161 aqlwpphdaAQPPRYLLLDEPTAALDlAHQHRLLDTVRRLARDWNLgVLAIVHDPNlAARHADRIAMLADGAIVAHGA 238
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1030-1233 |
3.33e-11 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 65.29 E-value: 3.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1030 SVTFNEVVFNYptRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQWLRAQL 1109
Cdd:PRK15056 6 GIVVNDVTVTW--RNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNLVAYV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1110 GiVSQE-----PILFDcSIAENIAYGDNS---RVVPHD-EIVRAAKEAnihpfIETLPQKYNtRVGdkgtQLSGGQKQRI 1180
Cdd:PRK15056 84 P-QSEEvdwsfPVLVE-DVVMMGRYGHMGwlrRAKKRDrQIVTAALAR-----VDMVEFRHR-QIG----ELSGGQKKRV 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 338817954 1181 AIARALIRQPRVLLLDEATSALDTESEKVVQEALDKAR-EGRTCIVIAHRLSTI 1233
Cdd:PRK15056 152 FLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRdEGKTMLVSTHNLGSV 205
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
416-589 |
3.37e-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: 65.08 E-value: 3.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 416 VKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISI--DGQDIrnfnvrcLREIIGVVSQEpvLFSTTIAENIRYGRGN 493
Cdd:cd03236 23 PREGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFDDppDWDEI-------LDEFRGSELQN--YFTKLLEGDVKVIVKP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 494 VTMDEIEKAVKeANAYDFIMKLPQ--KFDTLVG--------DRG-AQLSGGQKQRIAIARALVRNPKILLLDEATSALDT 562
Cdd:cd03236 94 QYVDLIPKAVK-GKVGELLKKKDErgKLDELVDqlelrhvlDRNiDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDI 172
|
170 180
....*....|....*....|....*...
gi 338817954 563 ESEAEVQAALDK-AREGRTTIVIAHRLS 589
Cdd:cd03236 173 KQRLNAARLIRElAEDDNYVLVVEHDLA 200
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1042-1247 |
4.51e-11 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 67.06 E-value: 4.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1042 TRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLN-----------VQWLRAQLG 1110
Cdd:PRK10982 257 TSLRQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNaneainhgfalVTEERRSTG 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1111 IVSQEPILFDCSIAENIAYGDNSRVVPHDEIvraakEANIHPFIETLPQK---YNTRVGdkgtQLSGGQKQRIAIARALI 1187
Cdd:PRK10982 337 IYAYLDIGFNSLISNIRNYKNKVGLLDNSRM-----KSDTQWVIDSMRVKtpgHRTQIG----SLSGGNQQKVIIGRWLL 407
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 338817954 1188 RQPRVLLLDEATSALDTESE-KVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVIENGKV 1247
Cdd:PRK10982 408 TQPEILMLDEPTRGIDVGAKfEIYQLIAELAKKDKGIIIISSEMPELLGiTDRILVMSNGLV 469
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1047-1247 |
5.06e-11 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 66.90 E-value: 5.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1047 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLerfydpmAGSVLLDG---QEAKKLNVQWL-----RAQLGIVsqepil 1118
Cdd:PRK11147 17 PLLDNAELHIEDNERVCLVGRNGAGKSTLMKIL-------NGEVLLDDgriIYEQDLIVARLqqdppRNVEGTV------ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1119 FDcSIAENIA--------YGDNSRVVPHDE----IVRAAK-------------EANIHPFIETLPQKYNTRVgdkgTQLS 1173
Cdd:PRK11147 84 YD-FVAEGIEeqaeylkrYHDISHLVETDPseknLNELAKlqeqldhhnlwqlENRINEVLAQLGLDPDAAL----SSLS 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 338817954 1174 GGQKQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEALdKAREGrTCIVIAHRLSTIQN-ADLIVVIENGKV 1247
Cdd:PRK11147 159 GGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFL-KTFQG-SIIFISHDRSFIRNmATRIVDLDRGKL 231
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
1048-1270 |
5.94e-11 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 66.83 E-value: 5.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1048 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLE-RFY-DPMAGSVLLDGqeaKKLNVQWLRaQLGIVSQEPILF-DCSIA 1124
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAgRIQgNNFTGTILANN---RKPTKQILK-RTGFVTQDDILYpHLTVR 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1125 ENIAYGDNSRV---VPHDEIVRAAkEANIHPFieTLPQKYNTRVGDKGTQ-LSGGQKQRIAIARALIRQPRVLLLDEATS 1200
Cdd:PLN03211 159 ETLVFCSLLRLpksLTKQEKILVA-ESVISEL--GLTKCENTIIGNSFIRgISGGERKRVSIAHEMLINPSLLILDEPTS 235
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 338817954 1201 ALD-TESEKVVQEALDKAREGRTCIVIAHRLST--IQNADLIVVIENGKVKEHGTHQQLLAqkgiYFSMVNIQ 1270
Cdd:PLN03211 236 GLDaTAAYRLVLTLGSLAQKGKTIVTSMHQPSSrvYQMFDSVLVLSEGRCLFFGKGSDAMA----YFESVGFS 304
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1052-1258 |
6.66e-11 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 66.39 E-value: 6.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1052 LSLEVKKGQTLALVGSSGCGKSTVVQLLERFYD-PMAGSVLLDGQEAKKLN-VQWLRAQLGIVSQEP----ILFDCSIAE 1125
Cdd:TIGR02633 279 VSFSLRRGEILGVAGLVGAGRTELVQALFGAYPgKFEGNVFINGKPVDIRNpAQAIRAGIAMVPEDRkrhgIVPILGVGK 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1126 NIAYGDNSRVVPHDEIVRAAKEANIHPFIETLpqKYNTRVGDKG-TQLSGGQKQRIAIARALIRQPRVLLLDEATSALDT 1204
Cdd:TIGR02633 359 NITLSVLKSFCFKMRIDAAAELQIIGSAIQRL--KVKTASPFLPiGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDV 436
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 338817954 1205 ESEKVVQEALDK-AREGRTCIVIAHRLSTIQN-ADLIVVIENGKVK----EHG-THQQLLA 1258
Cdd:TIGR02633 437 GAKYEIYKLINQlAQEGVAIIVVSSELAEVLGlSDRVLVIGEGKLKgdfvNHAlTQEQVLA 497
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
1031-1231 |
7.40e-11 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 66.70 E-value: 7.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1031 VTFNEVVF-NYP--TRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYdPMAGSVLLDGQEAKklnvqwlra 1107
Cdd:TIGR00954 447 YQDNGIKFeNIPlvTPNGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELW-PVYGGRLTKPAKGK--------- 516
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1108 qLGIVSQEPILFDCSIAENIAYGDNSrvvpHDEIVRAAKEANIHPFIETLPQKYN-TR------VGDKGTQLSGGQKQRI 1180
Cdd:TIGR00954 517 -LFYVPQRPYMTLGTLRDQIIYPDSS----EDMKRRGLSDKDLEQILDNVQLTHIlEReggwsaVQDWMDVLSGGEKQRI 591
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 338817954 1181 AIARALIRQPRVLLLDEATSALDTESEKVVQEALDKAreGRTCIVIAHRLS 1231
Cdd:TIGR00954 592 AMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCREF--GITLFSVSHRKS 640
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
753-971 |
7.60e-11 |
|
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: 64.73 E-value: 7.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 753 LVFLGLGVLSFFTFFLQGFTFGKAGEILTTRLRSMAFKAMLRQDMSWFDdhKNSTGALSTRLATDAAQVQGA--TGTRLA 830
Cdd:cd18548 43 LLMLLLALLGLIAGILAGYFAAKASQGFGRDLRKDLFEKIQSFSFAEID--KFGTSSLITRLTNDVTQVQNFvmMLLRML 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 831 LIAqnTANLGTGIIISFIYGWQLTLLLLSVVPFIAVAGIVEMKMLAGNAKRDKKEMEAAGKIATEAIENIRTVVSLTQE- 909
Cdd:cd18548 121 VRA--PIMLIGAIIMAFRINPKLALILLVAIPILALVVFLIMKKAIPLFKKVQKKLDRLNRVVRENLTGIRVIRAFNREd 198
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 338817954 910 ---RKFESMyVEKLhgpYRNSVRKAHIYGITFSISQAFMYFSYAGCFRFGSYLIVNGHMRFKDVI 971
Cdd:cd18548 199 yeeERFDKA-NDDL---TDTSLKAGRLMALLNPLMMLIMNLAIVAILWFGGHLINAGSLQVGDLV 259
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1041-1247 |
8.07e-11 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 64.72 E-value: 8.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1041 PTRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQWLRaQLGIV----SQep 1116
Cdd:COG4586 30 REYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFKRRKEFAR-RIGVVfgqrSQ-- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1117 ILFDCSIAENIA-----YGdnsrvVPHDEIvraakEANIHPFIETL--PQKYNTRVgdkgTQLSGGQKQRIAIARALIRQ 1189
Cdd:COG4586 107 LWWDLPAIDSFRllkaiYR-----IPDAEY-----KKRLDELVELLdlGELLDTPV----RQLSLGQRMRCELAAALLHR 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 338817954 1190 PRVLLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLSTIQN-ADLIVVIENGKV 1247
Cdd:COG4586 173 PKILFLDEPTIGLDVVSKEAIREFLKEynRERGTTILLTSHDMDDIEAlCDRVIVIDHGRI 233
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1050-1228 |
8.61e-11 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 62.90 E-value: 8.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1050 QGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKL------NVQWLRAQLGIVS----QEPILF 1119
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQrdeyhqDLLYLGHQPGIKTeltaLENLRF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1120 DCSIAEniaygdnsrvVPHDEIVRAAKEA-NIHPFiETLPQKyntrvgdkgtQLSGGQKQRIAIARALIRQPRVLLLDEA 1198
Cdd:PRK13538 98 YQRLHG----------PGDDEALWEALAQvGLAGF-EDVPVR----------QLSAGQQRRVALARLWLTRAPLWILDEP 156
|
170 180 190
....*....|....*....|....*....|.
gi 338817954 1199 TSALDTESEKVVQEALDK-AREGRTCIVIAH 1228
Cdd:PRK13538 157 FTAIDKQGVARLEALLAQhAEQGGMVILTTH 187
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1046-1246 |
1.73e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 65.14 E-value: 1.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1046 VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAK-KLNVQWLRAQLGIVSQE-PILFDCSI 1123
Cdd:PRK10982 11 VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfKSSKEALENGISMVHQElNLVLQRSV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1124 AENIAYGDNSR---VVPHDEIVRAAKEanihpFIETLPQKYNTRvgDKGTQLSGGQKQRIAIARALIRQPRVLLLDEATS 1200
Cdd:PRK10982 91 MDNMWLGRYPTkgmFVDQDKMYRDTKA-----IFDELDIDIDPR--AKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTS 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 338817954 1201 ALdteSEKVVQ---EALDKAREgRTC--IVIAHRLSTI-QNADLIVVIENGK 1246
Cdd:PRK10982 164 SL---TEKEVNhlfTIIRKLKE-RGCgiVYISHKMEEIfQLCDEITILRDGQ 211
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
724-965 |
1.82e-10 |
|
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: 63.62 E-value: 1.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 724 AFSIILSEMIAIFGPG---------DDAVKQQKCNMFSLVFLGLGVLSFFTF---FLQGFTFGKAGEILTTRLRSMAFKA 791
Cdd:cd18570 5 ILILLLSLLITLLGIAgsfffqiliDDIIPSGDINLLNIISIGLILLYLFQSllsYIRSYLLLKLSQKLDIRLILGYFKH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 792 MLRQDMSWFDDHKnsTGALSTRLaTDAAQVQGA-TGTRLALIAQNTANLGTGIIIsFIYGWQLTLLLLSVVPFIAVAGIV 870
Cdd:cd18570 85 LLKLPLSFFETRK--TGEIISRF-NDANKIREAiSSTTISLFLDLLMVIISGIIL-FFYNWKLFLITLLIIPLYILIILL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 871 EMKMLagnAKRDKKEMEAAGKIAT---EAIENIRTVVSLTQERKFesmyVEKLHGPYRNSVRKAHIYGITFSISQAFM-- 945
Cdd:cd18570 161 FNKPF---KKKNREVMESNAELNSyliESLKGIETIKSLNAEEQF----LKKIEKKFSKLLKKSFKLGKLSNLQSSIKgl 233
|
250 260
....*....|....*....|..
gi 338817954 946 --YFSYAGCFRFGSYLIVNGHM 965
Cdd:cd18570 234 isLIGSLLILWIGSYLVIKGQL 255
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
110-328 |
1.89e-10 |
|
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: 63.26 E-value: 1.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 110 MTRYAYYYSGLGGGVLVAAYIQVSFWTLAAGRQIKKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDDVSKISEGIGDKV 189
Cdd:cd18545 39 LLIIALLFLALNLVNWVASRLRIYLMAKVGQRILYDLRQDLFSHLQKLSFSFFDSRPVGKILSRVINDVNSLSDLLSNGL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 190 GMFFQAIATFFAGFIVGFIRGWKLTLVIMAISPILGLSTAVWAKILSTFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQ 269
Cdd:cd18545 119 INLIPDLLTLVGIVIIMFSLNVRLALVTLAVLPLLVLVVFLLRRRARKAWQRVRKKISNLNAYLHESISGIRVIQSFARE 198
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 270 NKELERYQKHLENAKKIGIkKAISANISMGIAFLLIYA-SYALAFWYGSTLVISKEYTIG 328
Cdd:cd18545 199 DENEEIFDELNRENRKANM-RAVRLNALFWPLVELISAlGTALVYWYGGKLVLGGAITVG 257
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1035-1237 |
1.92e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 61.89 E-value: 1.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1035 EVVFNYPTRanvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQWlRAQLGIVSQ 1114
Cdd:PRK13540 6 ELDFDYHDQ---PLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTY-QKQLCFVGH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1115 EP-ILFDCSIAENIAYG--DNSRVVPHDEIVRAAKEANIHPFIETLpqkyntrvgdkgtqLSGGQKQRIAIARALIRQPR 1191
Cdd:PRK13540 82 RSgINPYLTLRENCLYDihFSPGAVGITELCRLFSLEHLIDYPCGL--------------LSSGQKRQVALLRLWMSKAK 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 338817954 1192 VLLLDEATSALDTESEKVVQEALDKAR-EGRTCIVIAHRLSTIQNAD 1237
Cdd:PRK13540 148 LWLLDEPLVALDELSLLTIITKIQEHRaKGGAVLLTSHQDLPLNKAD 194
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
1052-1257 |
2.78e-10 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 62.26 E-value: 2.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1052 LSLEVKKGQTLALVGSSGCGKSTvvqLLERfydpMAG------SVLLDGQ-----EAKKLNVQwlRAQLgiVSQEPILF- 1119
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKST---LLAR----MAGllpgsgSIQFAGQpleawSAAELARH--RAYL--SQQQTPPFa 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1120 -------DCSIAENIAYGDNSRVVphDEIVRAAKeanihpfietLPQKYNTRVGdkgtQLSGGQKQRIAIArALIRQ--- 1189
Cdd:PRK03695 84 mpvfqylTLHQPDKTRTEAVASAL--NEVAEALG----------LDDKLGRSVN----QLSGGEWQRVRLA-AVVLQvwp 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1190 ---P--RVLLLDEATSALDtesekVVQE-ALDK-----AREGRTCIVIAHRLS-TIQNADLIVVIENGKVKEHGTHQQLL 1257
Cdd:PRK03695 147 dinPagQLLLLDEPMNSLD-----VAQQaALDRllselCQQGIAVVMSSHDLNhTLRHADRVWLLKQGKLLASGRRDEVL 221
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
407-586 |
3.47e-10 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 64.19 E-value: 3.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 407 KILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDgQDIRnfnvrclreiIGVVSQEPVLFST-TIAE 485
Cdd:TIGR03719 19 EILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQ-PGIK----------VGYLPQEPQLDPTkTVRE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 486 NI-------------------RYGRGNVTMD-------EIEKAVKEANAYDFIMKLPQKFDTL---VGD-RGAQLSGGQK 535
Cdd:TIGR03719 88 NVeegvaeikdaldrfneisaKYAEPDADFDklaaeqaELQEIIDAADAWDLDSQLEIAMDALrcpPWDaDVTKLSGGER 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 338817954 536 QRIAIARALVRNPKILLLDEATSALDTESEAEVQAALdKAREGrTTIVIAH 586
Cdd:TIGR03719 168 RRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHL-QEYPG-TVVAVTH 216
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
1029-1245 |
3.64e-10 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 60.72 E-value: 3.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1029 GSVTFNEVVFNYPT-RANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLL-ERFYD-PMAGSVLLDGQEAKKLnvqwL 1105
Cdd:cd03232 2 SVLTWKNLNYTVPVkGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLaGRKTAgVITGEILINGRPLDKN----F 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1106 RAQLGIVSQEPILFDCSiaeniaygdnsrvvphdeIVRaakeanihpfiETLPQKYNTRvgdkgtQLSGGQKQRIAIARA 1185
Cdd:cd03232 78 QRSTGYVEQQDVHSPNL------------------TVR-----------EALRFSALLR------GLSVEQRKRLTIGVE 122
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 338817954 1186 LIRQPRVLLLDEATSALDTESEKVVQEALDK-AREGRTCIVIAHRLS--TIQNADLIVVIENG 1245
Cdd:cd03232 123 LAAKPSILFLDEPTSGLDSQAAYNIVRFLKKlADSGQAILCTIHQPSasIFEKFDRLLLLKRG 185
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
391-595 |
3.75e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 60.73 E-value: 3.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 391 LEFSDVHFSYPSRAnikILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLREIIG 470
Cdd:PRK13540 2 LDVIELDFDYHDQP---LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 471 VVSQEPVLFSTTIAEN----IRYGRGNVTMDEIEKAVKEANAYDFIMKLpqkfdtlvgdrgaqLSGGQKQRIAIARALVR 546
Cdd:PRK13540 79 VGHRSGINPYLTLRENclydIHFSPGAVGITELCRLFSLEHLIDYPCGL--------------LSSGQKRQVALLRLWMS 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 338817954 547 NPKILLLDEATSALDTESEAEVQAALDKAR-EGRTTIVIAHRLSTIRNAD 595
Cdd:PRK13540 145 KAKLWLLDEPLVALDELSLLTIITKIQEHRaKGGAVLLTSHQDLPLNKAD 194
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1035-1258 |
4.32e-10 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 63.79 E-value: 4.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1035 EVVF---NY----PTRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPM-AGSVLLDGQEAKKLN-VQWL 1105
Cdd:PRK13549 257 EVILevrNLtawdPVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPGRwEGEIFIDGKPVKIRNpQQAI 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1106 RAQLGIVSQEP----ILFDCSIAENIAYGDNSRVVPHDEIVRAAKEANIHPFIETLPQKYNT---RVGdkgtQLSGGQKQ 1178
Cdd:PRK13549 337 AQGIAMVPEDRkrdgIVPVMGVGKNITLAALDRFTGGSRIDDAAELKTILESIQRLKVKTASpelAIA----RLSGGNQQ 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1179 RIAIARALIRQPRVLLLDEATSALDT----ESEKVVQEAldkAREGRTCIVIAHRLSTIQN-ADLIVVIENGKVK----- 1248
Cdd:PRK13549 413 KAVLAKCLLLNPKILILDEPTRGIDVgakyEIYKLINQL---VQQGVAIIVISSELPEVLGlSDRVLVMHEGKLKgdlin 489
|
250
....*....|
gi 338817954 1249 EHGTHQQLLA 1258
Cdd:PRK13549 490 HNLTQEQVME 499
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1030-1252 |
4.32e-10 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 62.84 E-value: 4.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1030 SVTFNEVvfNYPTRAnvpvLQGLSLEVKKGQTLALVGSSGCGKS----TVVQLLERFYDPMAGSVLLDGQEAKKLNVQWL 1105
Cdd:PRK11022 10 SVHFGDE--SAPFRA----VDRISYSVKQGEVVGIVGESGSGKSvsslAIMGLIDYPGRVMAEKLEFNGQDLQRISEKER 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1106 R----AQLGIVSQEPI--LFDC-----SIAENI-AYGDNSRVVPHDEIVRAAKEANIHPfietlPQkynTRVGDKGTQLS 1173
Cdd:PRK11022 84 RnlvgAEVAMIFQDPMtsLNPCytvgfQIMEAIkVHQGGNKKTRRQRAIDLLNQVGIPD-----PA---SRLDVYPHQLS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1174 GGQKQRIAIARALIRQPRVLLLDEATSALD-TESEKVVQEALD-KAREGRTCIVIAHRLSTI-QNADLIVVIENGKVKEH 1250
Cdd:PRK11022 156 GGMSQRVMIAMAIACRPKLLIADEPTTALDvTIQAQIIELLLElQQKENMALVLITHDLALVaEAAHKIIVMYAGQVVET 235
|
..
gi 338817954 1251 GT 1252
Cdd:PRK11022 236 GK 237
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
750-965 |
6.79e-10 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350007 [Multi-domain] Cd Length: 296 Bit Score: 61.76 E-value: 6.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 750 MFSLVFLGLGVLSFFTFFLQGFTFGKAGEILTTRLRSMAFKAMLRQDMSWFDdhKNSTGALSTRLATDAAQVQG-ATGTR 828
Cdd:cd18563 44 LLVLGLAGAYVLSALLGILRGRLLARLGERITADLRRDLYEHLQRLSLSFFD--KRQTGSLMSRVTSDTDRLQDfLSDGL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 829 LALIAQNTANLGTGIIIsFIYGWQLTLLLLSVVPFIAVAGIVEMKML-AGNAKRDKKEMEAAGKIAtEAIENIRTVVSLT 907
Cdd:cd18563 122 PDFLTNILMIIGIGVVL-FSLNWKLALLVLIPVPLVVWGSYFFWKKIrRLFHRQWRRWSRLNSVLN-DTLPGIRVVKAFG 199
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 338817954 908 QErKFESMYVEKLHGPYRNSVRKAH--------IYGITFSISQAFMYFsyagcfrFGSYLIVNGHM 965
Cdd:cd18563 200 QE-KREIKRFDEANQELLDANIRAEklwatffpLLTFLTSLGTLIVWY-------FGGRQVLSGTM 257
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
382-606 |
7.37e-10 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 62.92 E-value: 7.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 382 HKPDNIKGN-LEFSDVHFSYPSRANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPT-EGKISIDGQ--DI 457
Cdd:TIGR02633 248 HEPHEIGDViLEARNLTCWDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKpvDI 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 458 RNfnvrCLREII-------------GVVSQEPVLFSTTIAENIRY-GRGNVTMDEIEKAVKEAnaydfIMKLpqKFDTLV 523
Cdd:TIGR02633 328 RN----PAQAIRagiamvpedrkrhGIVPILGVGKNITLSVLKSFcFKMRIDAAAELQIIGSA-----IQRL--KVKTAS 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 524 GDRG-AQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDK-AREGRTTIVIAHRLstirnADVIaGFE 601
Cdd:TIGR02633 397 PFLPiGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQlAQEGVAIIVVSSEL-----AEVL-GLS 470
|
....*
gi 338817954 602 DGVIV 606
Cdd:TIGR02633 471 DRVLV 475
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
752-965 |
1.08e-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: 1.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 752 SLVFLGLGVLSFFTFFLQGFTFGKAGEILTTRLRSMAFKAMLRQDMSWFDDHKnsTGALSTRLATDAAQVQGATGTRLAL 831
Cdd:cd18546 42 AAAYLAVVLAGWVAQRAQTRLTGRTGERLLYDLRLRVFAHLQRLSLDFHERET--SGRIMTRMTSDIDALSELLQTGLVQ 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 832 IAQNTANLGTGIIISFIYGWQLTLLLLSVVPFIAVAGIVEMKmLAGNAKRDKKEmEAAGKIAT--EAIENIRTVVSLTQE 909
Cdd:cd18546 120 LVVSLLTLVGIAVVLLVLDPRLALVALAALPPLALATRWFRR-RSSRAYRRARE-RIAAVNADlqETLAGIRVVQAFRRE 197
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 910 RKFESMYVEkLHGPYRNSVRKAHIYgitFSISQAFMYF----SYAGCFRFGSYLIVNGHM 965
Cdd:cd18546 198 RRNAERFAE-LSDDYRDARLRAQRL---VAIYFPGVELlgnlATAAVLLVGAWRVAAGTL 253
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
401-588 |
1.27e-09 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 62.25 E-value: 1.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 401 PSRANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYD-PTEGKISIDGQ--DIRNfnvrCLREI---IGVVSQ 474
Cdd:PRK13549 270 PVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGKpvKIRN----PQQAIaqgIAMVPE 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 475 E-------PVLfstTIAENI------RYGRGNVtmdeIEKAVKEANAYDFIMKLPQKFDTLVGdRGAQLSGGQKQRIAIA 541
Cdd:PRK13549 346 DrkrdgivPVM---GVGKNItlaaldRFTGGSR----IDDAAELKTILESIQRLKVKTASPEL-AIARLSGGNQQKAVLA 417
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 338817954 542 RALVRNPKILLLDEATSALDTESEAEVQAALDK-AREGRTTIVIAHRL 588
Cdd:PRK13549 418 KCLLLNPKILILDEPTRGIDVGAKYEIYKLINQlVQQGVAIIVISSEL 465
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
118-343 |
1.28e-09 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349994 [Multi-domain] Cd Length: 294 Bit Score: 60.96 E-value: 1.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 118 SGLGGGVLVAA-------YIQVSFWTLAAGRQIKKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDDVSKISEGIGDKVG 190
Cdd:cd18550 39 VLLALGMVAVAvasallgVVQTYLSARIGQGVMYDLRVQLYAHLQRMSLAFFTRTRTGEIQSRLNNDVGGAQSVVTGTLT 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 191 MFFQAIATFFAGFIVGFIRGWKLTLVIMAISPILGLSTAVWAKILSTFSDKELAAYAKAGAVAEEALGA--IRTVIAFGG 268
Cdd:cd18550 119 SVVSNVVTLVATLVAMLALDWRLALLSLVLLPLFVLPTRRVGRRRRKLTREQQEKLAELNSIMQETLSVsgALLVKLFGR 198
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 338817954 269 QNKELERYQKHLENAKKIGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTIGN--AMTVFFSILIGAFS 343
Cdd:cd18550 199 EDDEAARFARRSRELRDLGVRQALAGRWFFAALGLFTAIGPALVYWVGGLLVIGGGLTIGTlvAFTALLGRLYGPLT 275
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
758-963 |
1.56e-09 |
|
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen processing 1 (TAP1); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350033 [Multi-domain] Cd Length: 289 Bit Score: 60.56 E-value: 1.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 758 LGVLSFFTFFLQGFTFGKAGEILTTRLRSMAFKAMLRQDMSWFDdhKNSTGALSTRLATDAAQVQGATGTRLALIAQNTA 837
Cdd:cd18589 45 LTIASAVSEFVCDLIYNITMSRIHSRLQGLVFAAVLRQEIAFFD--SNQTGDIVSRVTTDTEDMSESLSENLSLLMWYLA 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 838 NLGTGIIISFIYGWQLTLLLLSVVPFIAVAGIVEMKMLAGNAKRDKKEMEAAGKIATEAIENIRTVVSLTQERKFESMYV 917
Cdd:cd18589 123 RGLFLFIFMLWLSPKLALLTALGLPLLLLVPKFVGKFQQSLAVQVQKSLARANQVAVETFSAMKTVRSFANEEGEAQRYR 202
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 338817954 918 EKLHGPYRNSVRKAHIYGI---TFSISQAFMyfsYAGCFRFGSYLIVNG 963
Cdd:cd18589 203 QRLQKTYRLNKKEAAAYAVsmwTSSFSGLAL---KVGILYYGGQLVTAG 248
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
1047-1259 |
1.72e-09 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 59.80 E-value: 1.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1047 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLL--ERFYDPMAGSVLLDGQEAKKLNVQwLRAQLGI--VSQEPI----- 1117
Cdd:PRK09580 15 AILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLagREDYEVTGGTVEFKGKDLLELSPE-DRAGEGIfmAFQYPVeipgv 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1118 ----LFDCSIAENIAYGDnsrvvpHDEIVRAAKEANIHPFIETL--PQKYNTRVGDKGtqLSGGQKQRIAIARALIRQPR 1191
Cdd:PRK09580 94 snqfFLQTALNAVRSYRG------QEPLDRFDFQDLMEEKIALLkmPEDLLTRSVNVG--FSGGEKKRNDILQMAVLEPE 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 338817954 1192 VLLLDEATSALDTESEKVVQEALDKAREG-RTCIVIAH--RLSTIQNADLIVVIENGKVKEHGTH---QQLLAQ 1259
Cdd:PRK09580 166 LCILDESDSGLDIDALKIVADGVNSLRDGkRSFIIVTHyqRILDYIKPDYVHVLYQGRIVKSGDFtlvKQLEEQ 239
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
402-610 |
1.99e-09 |
|
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: 59.94 E-value: 1.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 402 SRANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVqlLQRLYDPTEGKISIDGQDIRNFNV----RCLREIIgVVSQEPV 477
Cdd:cd03271 4 KGARENNLKNIDVDIPLGVLTCVTGVSGSGKSSLI--NDTLYPALARRLHLKKEQPGNHDRieglEHIDKVI-VIDQSPI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 478 -------------LFsTTIAE----------------NIRYgRGNVTMDEIEKAVKEAnaYDFIMKLPQ---KFDTLV-- 523
Cdd:cd03271 81 grtprsnpatytgVF-DEIRElfcevckgkrynretlEVRY-KGKSIADVLDMTVEEA--LEFFENIPKiarKLQTLCdv 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 524 -------GDRGAQLSGGQKQRIAIARALVR---NPKILLLDEATSALDTESEAEVQAALDKARE-GRTTIVIAHRLSTIR 592
Cdd:cd03271 157 glgyiklGQPATTLSGGEAQRIKLAKELSKrstGKTLYILDEPTTGLHFHDVKKLLEVLQRLVDkGNTVVVIEHNLDVIK 236
|
250 260
....*....|....*....|....
gi 338817954 593 NADVI------AGFEDGVIVEQGS 610
Cdd:cd03271 237 CADWIidlgpeGGDGGGQVVASGT 260
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1053-1257 |
3.71e-09 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 60.70 E-value: 3.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1053 SLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGqeaKKLNV----QWLRAqlGIV------SQEPILFDCS 1122
Cdd:PRK11288 273 SFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDG---KPIDIrsprDAIRA--GIMlcpedrKAEGIIPVHS 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1123 IAENIAYGDNSRVVPHDEIVRAAKEA-NIHPFIETLPQKynTRVGD-KGTQLSGGQKQRIAIARALIRQPRVLLLDEATS 1200
Cdd:PRK11288 348 VADNINISARRHHLRAGCLINNRWEAeNADRFIRSLNIK--TPSREqLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTR 425
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 338817954 1201 ALDTESEKVVQEAL-DKAREGRTCIVIAHRLSTIQN-ADLIVVIENGKV-----KEHGTHQQLL 1257
Cdd:PRK11288 426 GIDVGAKHEIYNVIyELAAQGVAVLFVSSDLPEVLGvADRIVVMREGRIagelaREQATERQAL 489
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
708-931 |
6.11e-09 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350051 [Multi-domain] Cd Length: 293 Bit Score: 58.70 E-value: 6.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 708 FVVGTVCAIANGALQPAFSIILSEMIAIFGPGDDAVkqQKCNMFSLVFLGLGVLSFFTFFLQGFTFGKAGEILTTRLRSM 787
Cdd:cd18778 1 LILTLLCALLSTLLGLVPPWLIRELVDLVTIGSKSL--GLLLGLALLLLGAYLLRALLNFLRIYLNHVAEQKVVADLRSD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 788 AFKAMLRQDMSWFDDHknSTGALSTRLATDAAQVQgatgtRLAL--IAQNTANLGTGIIIS---FIYGWQLTLLLLSVVP 862
Cdd:cd18778 79 LYDKLQRLSLRYFDDR--QTGDLMSRVINDVANVE-----RLIAdgIPQGITNVLTLVGVAiilFSINPKLALLTLIPIP 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 338817954 863 FIAVAGIVEMKMLAGNAKRDKKEMEAAGKIATEAIENIRTVVSLTQERKfESMYVEKLHGPYRNSVRKA 931
Cdd:cd18778 152 FLALGAWLYSKKVRPRYRKVREALGELNALLQDNLSGIREIQAFGREEE-EAKRFEALSRRYRKAQLRA 219
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1034-1231 |
1.17e-08 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 57.38 E-value: 1.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1034 NEVVFNYPtrANVPVLQGLSLeVKKGQTLALVGSSGCGKSTVVQLLE--------RFYDP---------MAGSVL----- 1091
Cdd:cd03236 4 DEPVHRYG--PNSFKLHRLPV-PREGQVLGLVGPNGIGKSTALKILAgklkpnlgKFDDPpdwdeildeFRGSELqnyft 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1092 --LDGQEAKKLNVQWlraqlgiVSQEPILFDCSIAENIAYGDNSRVVphDEIVraaKEANIHPFIETlpqkyntrvgdKG 1169
Cdd:cd03236 81 klLEGDVKVIVKPQY-------VDLIPKAVKGKVGELLKKKDERGKL--DELV---DQLELRHVLDR-----------NI 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 338817954 1170 TQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTESE----KVVQEAldkAREGRTCIVIAHRLS 1231
Cdd:cd03236 138 DQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRlnaaRLIREL---AEDDNYVLVVEHDLA 200
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
408-590 |
1.50e-08 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 59.12 E-value: 1.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 408 ILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQ-RLYDPT-EGKISIDGqdiRNFNVRCLREIiGVVSQEPVLFS-TTIA 484
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAgRIQGNNfTGTILANN---RKPTKQILKRT-GFVTQDDILYPhLTVR 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 485 ENIRYGRGNVTMDEIEKAVKEANAYDFI--MKLPQKFDTLVGD---RGaqLSGGQKQRIAIARALVRNPKILLLDEATSA 559
Cdd:PLN03211 159 ETLVFCSLLRLPKSLTKQEKILVAESVIseLGLTKCENTIIGNsfiRG--ISGGERKRVSIAHEMLINPSLLILDEPTSG 236
|
170 180 190
....*....|....*....|....*....|..
gi 338817954 560 LD-TESEAEVQAALDKAREGRTTIVIAHRLST 590
Cdd:PLN03211 237 LDaTAAYRLVLTLGSLAQKGKTIVTSMHQPSS 268
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
384-569 |
1.62e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 59.10 E-value: 1.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 384 PDNIKGN--LEFSDVHFSYPsrANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKIsidgqdIRNFN 461
Cdd:PLN03073 500 PDDRPGPpiISFSDASFGYP--GGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTV------FRSAK 571
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 462 VRclreiIGVVSQEPV----LFSTTIaenirygrgnVTMDEIEKAVKEanaydfimklpQKFDTLVGDRGAQ-------- 529
Cdd:PLN03073 572 VR-----MAVFSQHHVdgldLSSNPL----------LYMMRCFPGVPE-----------QKLRAHLGSFGVTgnlalqpm 625
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 338817954 530 --LSGGQKQRIAIARALVRNPKILLLDEATSALDTES-EAEVQ 569
Cdd:PLN03073 626 ytLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAvEALIQ 668
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
122-342 |
1.97e-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: 57.46 E-value: 1.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 122 GGVLVAAYI-------QVSFWTLAAGRQIKK-IRQKFFHAILRQEMGWFDIKGTTELNTRLTDDVSKISE----GIGDkv 189
Cdd:cd18549 45 GAILLALYIlrtllnyFVTYWGHVMGARIETdMRRDLFEHLQKLSFSFFDNNKTGQLMSRITNDLFDISElahhGPED-- 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 190 gmFFQAIATFFAGFIVGFIRGWKLTLVIMAISPILGLST--------AVWAKILSTFSDkelaayakAGAVAEEALGAIR 261
Cdd:cd18549 123 --LFISIITIIGSFIILLTINVPLTLIVFALLPLMIIFTiyfnkkmkKAFRRVREKIGE--------INAQLEDSLSGIR 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 262 TVIAFGGQNKELERYQK---HLENAKKIGIKkaISANISMGIAFL--LIYASyALAFwyGSTLVISKEYTIGNAMTvfFS 336
Cdd:cd18549 193 VVKAFANEEYEIEKFDEgndRFLESKKKAYK--AMAYFFSGMNFFtnLLNLV-VLVA--GGYFIIKGEITLGDLVA--FL 265
|
....*.
gi 338817954 337 ILIGAF 342
Cdd:cd18549 266 LYVNVF 271
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
389-679 |
2.30e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 58.42 E-value: 2.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 389 GNLEFSDvhfsYPsranikILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQR--LYDptEGKISIDgQDIrnfnvrclr 466
Cdd:PRK11147 9 AWLSFSD----AP------LLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGevLLD--DGRIIYE-QDL--------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 467 eiigVVS---QEP------VLFSTtIAENI--------RYGR--GNVTMDEIEKAVKE----------ANAYDFIMKLPQ 517
Cdd:PRK11147 67 ----IVArlqQDPprnvegTVYDF-VAEGIeeqaeylkRYHDisHLVETDPSEKNLNElaklqeqldhHNLWQLENRINE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 518 KFDTLVGDRGAQL---SGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALdKAREGrTTIVIAHRLSTIRN- 593
Cdd:PRK11147 142 VLAQLGLDPDAALsslSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFL-KTFQG-SIIFISHDRSFIRNm 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 594 ADVIAGFEDGVIVE-QGSHSE-LMKKEGiYFRLVNMQTAgsqilseEFEVELSDEKAagdvapngW-----KARIFRNST 666
Cdd:PRK11147 220 ATRIVDLDRGKLVSyPGNYDQyLLEKEE-ALRVEELQNA-------EFDRKLAQEEV--------WirqgiKARRTRNEG 283
|
330
....*....|....*..
gi 338817954 667 K----KSLKSPHQNRLD 679
Cdd:PRK11147 284 RvralKALRRERSERRE 300
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1040-1252 |
3.28e-08 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 55.88 E-value: 3.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1040 YPTRANVPVLQGLSLEVKKG-----QTLALVGSSGCGKSTVVQLLerfydpmAGSVLLDGQEAKKLNVQwlraqlgiVSQ 1114
Cdd:cd03237 1 YTYPTMKKTLGEFTLEVEGGsisesEVIGILGPNGIGKTTFIKML-------AGVLKPDEGDIEIELDT--------VSY 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1115 EPilfdcsiaENIAYGDNSRVvpHDEIVRAAKEANIHPFIET-------LPQKYNTRVgdkgTQLSGGQKQRIAIARALI 1187
Cdd:cd03237 66 KP--------QYIKADYEGTV--RDLLSSITKDFYTHPYFKTeiakplqIEQILDREV----PELSGGELQRVAIAACLS 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1188 RQPRVLLLDEATSALDTESE----KVVQEALDKARegRTCIVIAHRLSTIQN-ADLIVVIEnGKVKEHGT 1252
Cdd:cd03237 132 KDADIYLLDEPSAYLDVEQRlmasKVIRRFAENNE--KTAFVVEHDIIMIDYlADRLIVFE-GEPSVNGV 198
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
392-563 |
3.74e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 57.65 E-value: 3.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 392 EFSDVHFSYPSRaniKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQ-DIRNFNVRclREIIg 470
Cdd:PRK11147 321 EMENVNYQIDGK---QLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKlEVAYFDQH--RAEL- 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 471 vvsqEPvlfSTTIAENIRYGRGNVTMDEIEKAVKeanAY--DFIMKlPQKFDTLVgdrgAQLSGGQKQRIAIARALVRNP 548
Cdd:PRK11147 395 ----DP---EKTVMDNLAEGKQEVMVNGRPRHVL---GYlqDFLFH-PKRAMTPV----KALSGGERNRLLLARLFLKPS 459
|
170
....*....|....*
gi 338817954 549 KILLLDEATSALDTE 563
Cdd:PRK11147 460 NLLILDEPTNDLDVE 474
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
376-623 |
3.97e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 57.51 E-value: 3.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 376 SFSERGHKPDnikgnlEFSDVHFSYPSRanIKILKGLNLKVKSGQ-----TVALVGNSGCGKSTTVQLLQRLYDPTEG-- 448
Cdd:PRK13409 325 EFEERPPRDE------SERETLVEYPDL--TKKLGDFSLEVEGGEiyegeVIGIVGPNGIGKTTFAKLLAGVLKPDEGev 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 449 ----KISIDGQDIR-NFNVR---CLREIigvvsqePVLFSTTIAENirygrgnvtmdEIEKAvkeanaydfiMKLPQKFD 520
Cdd:PRK13409 397 dpelKISYKPQYIKpDYDGTvedLLRSI-------TDDLGSSYYKS-----------EIIKP----------LQLERLLD 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 521 TLVGDrgaqLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKAREGR--TTIVIAHRLSTIrnaDVIA 598
Cdd:PRK13409 449 KNVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEEReaTALVVDHDIYMI---DYIS 521
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 338817954 599 gfeDGVIV---EQGSH-------------SELMKKEGIYFR 623
Cdd:PRK13409 522 ---DRLMVfegEPGKHghasgpmdmregmNRFLKELGITFR 559
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
408-585 |
4.27e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 57.81 E-value: 4.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 408 ILKGLNLKVKSGQTVALVGNSGCGKST-----TVQLLQRLYDpTEGKISIDG---QDIRNFnvrcLREIIGVVSQEPVLF 479
Cdd:TIGR00956 76 ILKPMDGLIKPGELTVVLGRPGSGCSTllktiASNTDGFHIG-VEGVITYDGitpEEIKKH----YRGDVVYNAETDVHF 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 480 -STTIAENIRYG--------RGNvTMDEIEKAVKEANAYDFIMKLPQKFDTLVGD---RGaqLSGGQKQRIAIARALVRN 547
Cdd:TIGR00956 151 pHLTVGETLDFAarcktpqnRPD-GVSREEYAKHIADVYMATYGLSHTRNTKVGNdfvRG--VSGGERKRVSIAEASLGG 227
|
170 180 190
....*....|....*....|....*....|....*....
gi 338817954 548 PKILLLDEATSALDTESEAEVQAAL-DKAREGRTTIVIA 585
Cdd:TIGR00956 228 AKIQCWDNATRGLDSATALEFIRALkTSANILDTTPLVA 266
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
416-601 |
4.61e-08 |
|
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: 54.12 E-value: 4.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 416 VKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGqdirnfnvrclreiigvvsqepvlfsttiaenirygrgnvt 495
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDG----------------------------------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 496 mdeIEKAVKeanaydfimklPQKFDtlvgdrgaqLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKA 575
Cdd:cd03222 61 ---ITPVYK-----------PQYID---------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRL 117
|
170 180
....*....|....*....|....*....
gi 338817954 576 RE--GRTTIVIAHRLSTIRN-ADVIAGFE 601
Cdd:cd03222 118 SEegKKTALVVEHDLAVLDYlSDRIHVFE 146
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
487-614 |
4.85e-08 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 57.72 E-value: 4.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 487 IRYgRGNVTMDEIEKAVKEAnaYDFIMKLP---QKFDTLVgDRGAQ----------LSGGQKQRIAIARALVR---NPKI 550
Cdd:TIGR00630 778 VKY-KGKNIADVLDMTVEEA--YEFFEAVPsisRKLQTLC-DVGLGyirlgqpattLSGGEAQRIKLAKELSKrstGRTL 853
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 338817954 551 LLLDEATSALDTESEAE----VQAALDKareGRTTIVIAHRLSTIRNADVI------AGFEDGVIVEQGSHSEL 614
Cdd:TIGR00630 854 YILDEPTTGLHFDDIKKllevLQRLVDK---GNTVVVIEHNLDVIKTADYIidlgpeGGDGGGTVVASGTPEEV 924
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1033-1261 |
5.10e-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: 57.72 E-value: 5.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1033 FNEVVFNYPTRANvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKlNVQWLRAQLGIV 1112
Cdd:TIGR01257 1940 LNELTKVYSGTSS-PAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT-NISDVHQNMGYC 2017
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1113 SQEPILFDCSIA-ENIAYGDNSRVVPHDEIVRAAKEAnihpfIETLPQK-YNTRVGdkGTqLSGGQKQRIAIARALIRQP 1190
Cdd:TIGR01257 2018 PQFDAIDDLLTGrEHLYLYARLRGVPAEEIEKVANWS-----IQSLGLSlYADRLA--GT-YSGGNKRKLSTAIALIGCP 2089
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 338817954 1191 RVLLLDEATSALDTESEKVVQEAL-DKAREGRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHGTHQQLLAQKG 1261
Cdd:TIGR01257 2090 PLVLLDEPTTGMDPQARRMLWNTIvSIIREGRAVVLTSHSMEECEAlCTRLAIMVKGAFQCLGTIQHLKSKFG 2162
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1055-1239 |
7.11e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 56.74 E-value: 7.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1055 EVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLldgqeaKKLNV----QWLRA-QLGIVSQepilFDCSIAENIay 1129
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVD------PELKIsykpQYIKPdYDGTVED----LLRSITDDL-- 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1130 gDNSRVVPhdEIVRaakeanihPFieTLPQKYNTRVGDkgtqLSGGQKQRIAIARALIRQPRVLLLDEATSALDTESEKV 1209
Cdd:PRK13409 429 -GSSYYKS--EIIK--------PL--QLERLLDKNVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLA 491
|
170 180 190
....*....|....*....|....*....|..
gi 338817954 1210 VQEALDKAREGR--TCIVIAHRLSTIqnaDLI 1239
Cdd:PRK13409 492 VAKAIRRIAEEReaTALVVDHDIYMI---DYI 520
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
406-611 |
7.60e-08 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 57.16 E-value: 7.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 406 IKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLL--QRLYDPTEGKISIDG-----QDIRNFNVRCLREII---GVVSQE 475
Cdd:PLN03140 893 LQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLagRKTGGYIEGDIRISGfpkkqETFARISGYCEQNDIhspQVTVRE 972
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 476 PVLFSTTIAENIRYGRGNVTM--DEIEKAVKEANAYDFIMKLPqkfdtlvGDRGaqLSGGQKQRIAIARALVRNPKILLL 553
Cdd:PLN03140 973 SLIYSAFLRLPKEVSKEEKMMfvDEVMELVELDNLKDAIVGLP-------GVTG--LSTEQRKRLTIAVELVANPSIIFM 1043
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 338817954 554 DEATSALDTESEAEVQAAL-DKAREGRTTIVIAHRLSTirnaDVIAGFEDGVIVEQGSH 611
Cdd:PLN03140 1044 DEPTSGLDARAAAIVMRTVrNTVDTGRTVVCTIHQPSI----DIFEAFDELLLMKRGGQ 1098
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
1164-1240 |
8.47e-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: 54.93 E-value: 8.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1164 RVGDKGTQLSGGQKQRIAIARALIRQPR---VLLLDEATSALDTESEKVVQEALDKARE-GRTCIVIAHRLSTIQNADLI 1239
Cdd:cd03271 162 KLGQPATTLSGGEAQRIKLAKELSKRSTgktLYILDEPTTGLHFHDVKKLLEVLQRLVDkGNTVVVIEHNLDVIKCADWI 241
|
.
gi 338817954 1240 V 1240
Cdd:cd03271 242 I 242
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
120-340 |
9.34e-08 |
|
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: 55.29 E-value: 9.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 120 LGGGVLVAAYIQVSF-------WTLAAGRQIKKIRQKFFHAILRQEMGWFDIKGTTELNTRLtDDVSKISEGIGDkvgmf 192
Cdd:cd18782 44 IGVVMLVAALLEAVLtalrtylFTDTANRIDLELGGTIIDHLLRLPLGFFDKRPVGELSTRI-SELDTIRGFLTG----- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 193 fQAIATFF-AGFIVGFIR-----GWKLTLVIMAISPILGLSTAVWAKILSTFSDKELAAYAKAGAVAEEALGAIRTVIAf 266
Cdd:cd18782 118 -TALTTLLdVLFSVIYIAvlfsySPLLTLVVLATVPLQLLLTFLFGPILRRQIRRRAEASAKTQSYLVESLTGIQTVKA- 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 267 ggQNKEL-------ERYQKHLENAKKIGIKKAISANISMGIAFLliyaSYALAFWYGSTLVISKEYTIGNAMTvfFSILI 339
Cdd:cd18782 196 --QNAELkarwrwqNRYARSLGEGFKLTVLGTTSGSLSQFLNKL----SSLLVLWVGAYLVLRGELTLGQLIA--FRILS 267
|
.
gi 338817954 340 G 340
Cdd:cd18782 268 G 268
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
407-564 |
9.97e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 56.28 E-value: 9.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 407 KILKGLNLKVKSGQTVALVGNSGCGKSTtvqLLqrlydptegKIsIDGQDiRNFN--VRCLREI-IGVVSQEPVLFST-T 482
Cdd:PRK11819 21 QILKDISLSFFPGAKIGVLGLNGAGKST---LL---------RI-MAGVD-KEFEgeARPAPGIkVGYLPQEPQLDPEkT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 483 IAENIRYGRGNVT----------------MDEIEKAVKE----------ANAYDFIMKLPQKFDTL---VGDRG-AQLSG 532
Cdd:PRK11819 87 VRENVEEGVAEVKaaldrfneiyaayaepDADFDALAAEqgelqeiidaADAWDLDSQLEIAMDALrcpPWDAKvTKLSG 166
|
170 180 190
....*....|....*....|....*....|..
gi 338817954 533 GQKQRIAIARALVRNPKILLLDEATSALDTES 564
Cdd:PRK11819 167 GERRRVALCRLLLEKPDMLLLDEPTNHLDAES 198
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
713-910 |
1.09e-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: 349994 [Multi-domain] Cd Length: 294 Bit Score: 54.80 E-value: 1.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 713 VCAIANGALQPAFSIILSEMIaifgpgDDAVKQQkcNMFSLVFL-----GLGVLSFFTFFLQGFTFGKAGEILTTRLRSM 787
Cdd:cd18550 6 LLILLSALLGLLPPLLLREII------DDALPQG--DLGLLVLLalgmvAVAVASALLGVVQTYLSARIGQGVMYDLRVQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 788 AFKAMLRQDMSWFDDHKnsTGALSTRLATDAAQVQGATGTRLALIAQNTANLGTGIIISFIYGWQLTLLLLSVVP-FIAV 866
Cdd:cd18550 78 LYAHLQRMSLAFFTRTR--TGEIQSRLNNDVGGAQSVVTGTLTSVVSNVVTLVATLVAMLALDWRLALLSLVLLPlFVLP 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 338817954 867 AGIVemkmlaGNAKRdkkemeaagKIATEAIENIRTVVSLTQER 910
Cdd:cd18550 156 TRRV------GRRRR---------KLTREQQEKLAELNSIMQET 184
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
381-588 |
1.26e-07 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 56.56 E-value: 1.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 381 GHKPDNIKGNlEFSDVHFSYPSRANIKILKGlnlkVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNf 460
Cdd:TIGR01257 1932 GNKTDILRLN-ELTKVYSGTSSPAVDRLCVG----VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT- 2005
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 461 NVRCLREIIGVVSQ-EPVLFSTTIAENIR-YGR-GNVTMDEIEKAvkeANAYDFIMKLPQKFDTLVGdrgaQLSGGQKQR 537
Cdd:TIGR01257 2006 NISDVHQNMGYCPQfDAIDDLLTGREHLYlYARlRGVPAEEIEKV---ANWSIQSLGLSLYADRLAG----TYSGGNKRK 2078
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 338817954 538 IAIARALVRNPKILLLDEATSALDTESEAEV-QAALDKAREGRTTIVIAHRL 588
Cdd:TIGR01257 2079 LSTAIALIGCPPLVLLDEPTTGMDPQARRMLwNTIVSIIREGRAVVLTSHSM 2130
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
426-561 |
1.41e-07 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 56.29 E-value: 1.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 426 GNSGCGKSTTVQLLQRLYDPTEGKISIDGQ--DIRNFNVRcLReiIGVVSQEpvlFST----TIAENIR-----YGrgnV 494
Cdd:NF033858 299 GSNGCGKSTTMKMLTGLLPASEGEAWLFGQpvDAGDIATR-RR--VGYMSQA---FSLygelTVRQNLElharlFH---L 369
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 338817954 495 TMDEIEKAVKEanaydfimkLPQKFD--TLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEATSALD 561
Cdd:NF033858 370 PAAEIAARVAE---------MLERFDlaDVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVD 429
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
416-588 |
1.46e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 55.97 E-value: 1.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 416 VKSGQTVALVGNSGCGKSTTVQLLQrlydptegkisidGQDIRNFnvrclreiiGVVSQEPvlfstTIAENIRYGRGNVT 495
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILS-------------GELIPNL---------GDYEEEP-----SWDEVLKRFRGTEL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 496 MDEIEK----AVKEANAYDFIMKLPQKFDTLVGD-------RGA-------------------QLSGGQKQRIAIARALV 545
Cdd:PRK13409 149 QNYFKKlyngEIKVVHKPQYVDLIPKVFKGKVREllkkvdeRGKldevverlglenildrdisELSGGELQRVAIAAALL 228
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 338817954 546 RNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRL 588
Cdd:PRK13409 229 RDADFYFFDEPTSYLDIRQRLNVARLIRELAEGKYVLVVEHDL 271
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
122-342 |
1.61e-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: 350051 [Multi-domain] Cd Length: 293 Bit Score: 54.46 E-value: 1.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 122 GGVLVAAYIQVSFWT--------LAAGRQIKKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDDVSKISEGIGDKVGMFF 193
Cdd:cd18778 43 ALLLLGAYLLRALLNflriylnhVAEQKVVADLRSDLYDKLQRLSLRYFDDRQTGDLMSRVINDVANVERLIADGIPQGI 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 194 QAIATFFAGFIVGFIRGWKLTLVIMAISPILGLSTAVWAKILSTFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKEL 273
Cdd:cd18778 123 TNVLTLVGVAIILFSINPKLALLTLIPIPFLALGAWLYSKKVRPRYRKVREALGELNALLQDNLSGIREIQAFGREEEEA 202
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 338817954 274 ERYQKHLENAKkigiKKAISANISMGIAFLLIY----ASYALAFWYGSTLVISKEYTIGNamTVFFSILIGAF 342
Cdd:cd18778 203 KRFEALSRRYR----KAQLRAMKLWAIFHPLMEfltsLGTVLVLGFGGRLVLAGELTIGD--LVAFLLYLGLF 269
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
126-344 |
1.63e-07 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350009 [Multi-domain] Cd Length: 313 Bit Score: 54.49 E-value: 1.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 126 VAAYIQVSFWTLAAGRQIKKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDDVSKISEGIGDKVGMFFQAIATFFAGFIV 205
Cdd:cd18565 69 LFQYLSGVLWRRFAQRVQHDLRTDTYDHVQRLDMAFFEDRQTGDLMSVLNNDVNQLERFLDDGANSIIRVVVTVLGIGAI 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 206 GFIRGWKLTLVIMAISPILGLSTAVWAKILSTFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKELERYQKHLENAKk 285
Cdd:cd18565 149 LFYLNWQLALVALLPVPLIIAGTYWFQRRIEPRYRAVREAVGDLNARLENNLSGIAVIKAFTAEDFERERVADASEEYR- 227
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 338817954 286 igiKKAISAnISMGIAF-----LLIYASYALAFWYGSTLVISKEYTIGNAMTVffsiliGAFSV 344
Cdd:cd18565 228 ---DANWRA-IRLRAAFfpvirLVAGAGFVATFVVGGYWVLDGPPLFTGTLTV------GTLVT 281
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
407-611 |
1.68e-07 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 55.56 E-value: 1.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 407 KILKGLNLKVKSGQ-----TVALVGNSGCGKSTTVQLLQRLYDPTEG------KISIDGQDIRNFNVRCLREIIGVVSQE 475
Cdd:COG1245 349 KSYGGFSLEVEGGEiregeVLGIVGPNGIGKTTFAKILAGVLKPDEGevdedlKISYKPQYISPDYDGTVEEFLRSANTD 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 476 PvlFSTTIAENirygrgnvtmdEIEKAvkeanaydfiMKLPQKFDTLVGDrgaqLSGGQKQRIAIARALVRNPKILLLDE 555
Cdd:COG1245 429 D--FGSSYYKT-----------EIIKP----------LGLEKLLDKNVKD----LSGGELQRVAIAACLSRDADLYLLDE 481
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 338817954 556 ATSALDTESEAEVQAALDKAREGR--TTIVIAHRLSTIrnaDVIAgfeDGVIV---EQGSH 611
Cdd:COG1245 482 PSAHLDVEQRLAVAKAIRRFAENRgkTAMVVDHDIYLI---DYIS---DRLMVfegEPGVH 536
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
144-342 |
2.01e-07 |
|
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: 54.05 E-value: 2.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 144 KKIRQKFFHAILRQEMGWFDIKGTTELNTRLtDDVSKISEGIGDKVGMFFQAIATFFAGFIVGFIRGWKLTLVIMAISPI 223
Cdd:cd18555 75 KSLMSDFFEHLLKLPYSFFENRSSGDLLFRA-NSNVYIRQILSNQVISLIIDLLLLVIYLIYMLYYSPLLTLIVLLLGLL 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 224 LGLSTAVWAKILSTFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKELERYQKHLENAKKIGIKKAISANISMGIAFL 303
Cdd:cd18555 154 IVLLLLLTRKKIKKLNQEEIVAQTKVQSYLTETLYGIETIKSLGSEKNIYKKWENLFKKQLKAFKKKERLSNILNSISSS 233
|
170 180 190
....*....|....*....|....*....|....*....
gi 338817954 304 LIYASYALAFWYGSTLVISKEYTIGnaMTVFFSILIGAF 342
Cdd:cd18555 234 IQFIAPLLILWIGAYLVINGELTLG--ELIAFSSLAGSF 270
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
151-340 |
2.08e-07 |
|
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: 54.13 E-value: 2.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 151 FHAILRQEMGWFDIKGTTELNTRLTDdVSKISEgigdkvgmFF--QAIATF----FAG--FIVGFIRGWKLTLVIMAISP 222
Cdd:cd18566 82 FEHLLSLPLSFFEREPSGAHLERLNS-LEQIRE--------FLtgQALLALldlpFVLifLGLIWYLGGKLVLVPLVLLG 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 223 ILglstAVWAKILSTFSDKELAAYAKAGAVAE----EALGAIRTVIAFGGQNKELERYQKHLENAKKIGIKKAISANISM 298
Cdd:cd18566 153 LF----VLVAILLGPILRRALKERSRADERRQnfliETLTGIHTIKAMAMEPQMLRRYERLQANAAYAGFKVAKINAVAQ 228
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 338817954 299 GIAFLLIYASYALAFWYGSTLVISKEYTIGnaMTVFFSILIG 340
Cdd:cd18566 229 TLGQLFSQVSMVAVVAFGALLVINGDLTVG--ALIACTMLSG 268
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
705-965 |
2.27e-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: 2.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 705 WPYFVVGTVCAIANGALQPAFSIILSEMI-AIFGPGDdavkQQKCNMFSLVFLGLGVLSFFTFFLQGFTFGKAGEILTTR 783
Cdd:cd18540 1 KKLLILLIILMLLVALLDAVFPLLTKYAIdHFITPGT----LDGLTGFILLYLGLILIQALSVFLFIRLAGKIEMGVSYD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 784 LRSMAFKAMLRQDMSWFDdhKNSTGALSTRLATDAAQVQGATGTRLALIAQNTANLGTGIIISFIYGWQLTLLLLSVVPF 863
Cdd:cd18540 77 LRKKAFEHLQTLSFSYFD--KTPVGWIMARVTSDTQRLGEIISWGLVDLVWGITYMIGILIVMLILNWKLALIVLAVVPV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 864 IA-VAGIVEMKMLAGNAKRDKKEMEAAGKIaTEAIENIRTVVSLTQERKFESMYVEKLHGPYRNSVRKAHIYGITFSISQ 942
Cdd:cd18540 155 LAvVSIYFQKKILKAYRKVRKINSRITGAF-NEGITGAKTTKTLVREEKNLREFKELTEEMRRASVRAARLSALFLPIVL 233
|
250 260
....*....|....*....|...
gi 338817954 943 AFMYFSYAGCFRFGSYLIVNGHM 965
Cdd:cd18540 234 FLGSIATALVLWYGGILVLAGAI 256
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
413-606 |
2.51e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 54.92 E-value: 2.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 413 NLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRnfnVRCLREII--GVV------SQEPVLFSTTIA 484
Cdd:PRK11288 273 SFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPID---IRSPRDAIraGIMlcpedrKAEGIIPVHSVA 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 485 ENIRYG--RGNVTMDEIEKAVKEA-NAYDFIMKLPQKF---DTLVGdrgaQLSGGQKQRIAIARALVRNPKILLLDEATS 558
Cdd:PRK11288 350 DNINISarRHHLRAGCLINNRWEAeNADRFIRSLNIKTpsrEQLIM----NLSGGNQQKAILGRWLSEDMKVILLDEPTR 425
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 338817954 559 ALDTESEAEVQAAL-DKAREGRTTIVIAHRLstirnADVIaGFEDGVIV 606
Cdd:PRK11288 426 GIDVGAKHEIYNVIyELAAQGVAVLFVSSDL-----PEVL-GVADRIVV 468
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
1053-1259 |
2.87e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 54.64 E-value: 2.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1053 SLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGS--------VLLDGQEAKKL-NVQWLRAQLGIVSQEPILFDCSI 1123
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGErqsqfshiTRLSFEQLQKLvSDEWQRNNTDMLSPGEDDTGRTT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1124 AENIAYG--DNSRVVphdeivRAAKEANIHPFIETlPQKYntrvgdkgtqLSGGQKQRIAIARALIRQPRVLLLDEATSA 1201
Cdd:PRK10938 103 AEIIQDEvkDPARCE------QLAQQFGITALLDR-RFKY----------LSTGETRKTLLCQALMSEPDLLILDEPFDG 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1202 LDTESEKVVQEALDK-AREGRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHGTHQQLLAQ 1259
Cdd:PRK10938 166 LDVASRQQLAELLASlHQSGITLVLVLNRFDEIPDfVQFAGVLADCTLAETGEREEILQQ 225
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1047-1258 |
3.92e-07 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 54.24 E-value: 3.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1047 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQWLRAQlGIV------SQEPILFD 1120
Cdd:PRK10762 266 PGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDGLAN-GIVyisedrKRDGLVLG 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1121 CSIAENI---AYGDNSRvvPHDEIVRAAKEANIHPFIETLPQKYNTRVGDKGTqLSGGQKQRIAIARALIRQPRVLLLDE 1197
Cdd:PRK10762 345 MSVKENMsltALRYFSR--AGGSLKHADEQQAVSDFIRLFNIKTPSMEQAIGL-LSGGNQQKVAIARGLMTRPKVLILDE 421
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 338817954 1198 ATSALDTESEKVVQEALDKAR-EGRTCIVIAHRLSTIQN-ADLIVVIENGKV-----KEHGTHQQLLA 1258
Cdd:PRK10762 422 PTRGVDVGAKKEIYQLINQFKaEGLSIILVSSEMPEVLGmSDRILVMHEGRIsgeftREQATQEKLMA 489
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
417-590 |
5.41e-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: 5.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 417 KSGQTVALVGNSGCGKSTTVQLLQrlydptegkisidGQDIRNFnvrclreiiGVVSQEPvlfstTIAENIRYGRGNVTM 496
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILS-------------GELKPNL---------GDYDEEP-----SWDEVLKRFRGTELQ 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 497 DEIEK----AVKEANAYDFIMKLPQKFDTLVGD-------RGA-------------------QLSGGQKQRIAIARALVR 546
Cdd:COG1245 150 DYFKKlangEIKVAHKPQYVDLIPKVFKGTVREllekvdeRGKldelaeklglenildrdisELSGGELQRVAIAAALLR 229
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 338817954 547 NPKILLLDEATSALDTESEAEVQAAL-DKAREGRTTIVIAHRLST 590
Cdd:COG1245 230 DADFYFFDEPSSYLDIYQRLNVARLIrELAEEGKYVLVVEHDLAI 274
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
749-965 |
6.38e-07 |
|
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: 52.59 E-value: 6.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 749 NMFSLVFLGLGVLSFFTFFLQGF---TFGKAGEILTTRLRSMAFKAMLRQDMSWFDdhKNSTGALSTRLAtDAAQVQGAT 825
Cdd:cd18566 39 PTLQVLVIGVVIAILLESLLRLLrsyILAWIGARFDHRLSNAAFEHLLSLPLSFFE--REPSGAHLERLN-SLEQIREFL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 826 GTRLALIAQNTANLGTGIIISFIYGWQLTLLLLSVVPFIAVAGIVEMKMLAGNAKRDKKEMEAAGKIATEAIENIRTVVS 905
Cdd:cd18566 116 TGQALLALLDLPFVLIFLGLIWYLGGKLVLVPLVLLGLFVLVAILLGPILRRALKERSRADERRQNFLIETLTGIHTIKA 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 906 LTQERKFESMYVEKLHGPYRNSVRKAHIYGITFSISQAFMYFSYAGCFRFGSYLIVNGHM 965
Cdd:cd18566 196 MAMEPQMLRRYERLQANAAYAGFKVAKINAVAQTLGQLFSQVSMVAVVAFGALLVINGDL 255
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
1145-1240 |
6.40e-07 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 53.86 E-value: 6.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1145 AKEANIHPFIETLPQ---KYnTRVGDKGTQLSGGQKQRIAIARALIRQ---PRVLLLDEATSALDTESEK----VVQEAL 1214
Cdd:TIGR00630 801 EAVPSISRKLQTLCDvglGY-IRLGQPATTLSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLHFDDIKklleVLQRLV 879
|
90 100
....*....|....*....|....*.
gi 338817954 1215 DKareGRTCIVIAHRLSTIQNADLIV 1240
Cdd:TIGR00630 880 DK---GNTVVVIEHNLDVIKTADYII 902
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1053-1215 |
7.12e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 53.80 E-value: 7.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1053 SLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVlldgQEAKKLNVQWL---RAQLgivsqEPilfDCSIAENIAY 1129
Cdd:PRK11147 339 SAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI----HCGTKLEVAYFdqhRAEL-----DP---EKTVMDNLAE 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1130 GDNsrvvphdEIVRAAKEANIHPFIETL---PQKYNTRVgdkgTQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTES 1206
Cdd:PRK11147 407 GKQ-------EVMVNGRPRHVLGYLQDFlfhPKRAMTPV----KALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVET 475
|
....*....
gi 338817954 1207 EKVVQEALD 1215
Cdd:PRK11147 476 LELLEELLD 484
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1170-1206 |
7.41e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 53.58 E-value: 7.41e-07
10 20 30
....*....|....*....|....*....|....*..
gi 338817954 1170 TQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTES 1206
Cdd:PRK11819 162 TKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES 198
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
1047-1262 |
8.32e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 53.36 E-value: 8.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1047 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVlldgqeakklnvQWL-RAQLGIVSQEP--------I 1117
Cdd:PRK15064 333 PLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV------------KWSeNANIGYYAQDHaydfendlT 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1118 LFDCsIAENIAYGDNSRVV---------PHDEIVRAAKeanihpfietlpqkyntrvgdkgtQLSGGQKQRIAIARALIR 1188
Cdd:PRK15064 401 LFDW-MSQWRQEGDDEQAVrgtlgrllfSQDDIKKSVK------------------------VLSGGEKGRMLFGKLMMQ 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1189 QPRVLLLDEATSALDTESEKVVQEALDKArEGrTCIVIAH------RLSTiqnaDLIVVIENGKVKEHGTHQQLLAQKGI 1262
Cdd:PRK15064 456 KPNVLVMDEPTNHMDMESIESLNMALEKY-EG-TLIFVSHdrefvsSLAT----RIIEITPDGVVDFSGTYEEYLRSQGI 529
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1170-1206 |
1.12e-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: 53.02 E-value: 1.12e-06
10 20 30
....*....|....*....|....*....|....*..
gi 338817954 1170 TQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTES 1206
Cdd:TIGR03719 160 TKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAES 196
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
413-615 |
1.18e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 52.71 E-value: 1.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 413 NLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLREIigvVSQEPVLFSTTIAENIRYGRG 492
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQLQKL---VSDEWQRNNTDMLSPGEDDTG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 493 NVTMDEIEKAVKEANAydfIMKLPQKF--DTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQA 570
Cdd:PRK10938 100 RTTAEIIQDEVKDPAR---CEQLAQQFgiTALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAE 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 338817954 571 ALDK-AREGRTTIVIAHRLSTIRN-ADVIAGFEDGVIVEQGSHSELM 615
Cdd:PRK10938 177 LLASlHQSGITLVLVLNRFDEIPDfVQFAGVLADCTLAETGEREEIL 223
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
740-965 |
1.35e-06 |
|
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) and similar proteins. These transporter subunits include HylB, PrtD, CyaB, CvaB, RsaD, HasD, LipB, and LapB, among many others. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). Most targeted proteins are not cleaved at the N terminus, but rather carry signals located toward the extreme C terminus to direct type I secretion. However, the 10 kDa Escherichia coli colicin V (CvaB) targets the ABC transporter using a cleaved, N-terminal signal sequence. Almost all transport substrates of the type I system have critical functions in attacking host cells either directly or by being essential for host colonization. The ABC-dependent T1SS transports various molecules, from ions, drugs, to proteins of various sizes up to 900 kDa. The molecules secreted vary in size from the small Escherichia coli peptide colicin V, (10 kDa) to the Pseudomonas fluorescens cell adhesion protein LapA of 520 kDa. The best characterized are the RTX toxins such as the adenylate cyclase (CyaA) toxin from Bordetella pertussis, the causative agent of whooping cough, and the lipases such as LipA. Type I secretion is also involved in export of non-protein substrates such as cyclic beta-glucans and polysaccharides.
Pssm-ID: 349999 [Multi-domain] Cd Length: 294 Bit Score: 51.74 E-value: 1.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 740 DDAVKQQKCNMFSLVFLGLGVLSFFTF---FLQGFTFGKAGEILTTRLRSMAFKAMLRQDMSWFDdhKNSTGALSTRlAT 816
Cdd:cd18555 30 DNVIVPGNLNLLNVLGIGILILFLLYGlfsFLRGYIIIKLQTKLDKSLMSDFFEHLLKLPYSFFE--NRSSGDLLFR-AN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 817 DAAQVQGATGTRLALIAQNTANLGTGIIISFIYGWQLTLLLLSVVPFIAVAGIVEMKMLAgnaKRDKKEMEAAGK---IA 893
Cdd:cd18555 107 SNVYIRQILSNQVISLIIDLLLLVIYLIYMLYYSPLLTLIVLLLGLLIVLLLLLTRKKIK---KLNQEEIVAQTKvqsYL 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 338817954 894 TEAIENIRTVVSLTQERKFESMYVEKLHGPYRNSVRKAHIYGITFSISQAFMYFSYAGCFRFGSYLIVNGHM 965
Cdd:cd18555 184 TETLYGIETIKSLGSEKNIYKKWENLFKKQLKAFKKKERLSNILNSISSSIQFIAPLLILWIGAYLVINGEL 255
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
402-609 |
1.70e-06 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 49.63 E-value: 1.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 402 SRANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQllQRLYdpTEGKISIDGQDIRNFnvrclREIIGVVSQepvlFST 481
Cdd:cd03238 4 SGANVHNLQNLDVSIPLNVLVVVTGVSGSGKSTLVN--EGLY--ASGKARLISFLPKFS-----RNKLIFIDQ----LQF 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 482 TIAENIRYgrgnvtmdeiekavkeanaydfiMKLPQKFDTLvgdrgaqlSGGQKQRIAIARALVRNPK--ILLLDEATSA 559
Cdd:cd03238 71 LIDVGLGY-----------------------LTLGQKLSTL--------SGGELQRVKLASELFSEPPgtLFILDEPSTG 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 338817954 560 LDTESEAEVQAALDKAR-EGRTTIVIAHRLSTIRNADVI------AGFEDGVIVEQG 609
Cdd:cd03238 120 LHQQDINQLLEVIKGLIdLGNTVILIEHNLDVLSSADWIidfgpgSGKSGGKVVFSG 176
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
749-965 |
1.93e-06 |
|
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: 51.31 E-value: 1.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 749 NMFSLVFLGLGVLSFFTFFLQGFTFGKAGEILTTRLRSMAFKAMLRQDMSWFDdhKNSTGALSTRLATDAAQVQGA-TGT 827
Cdd:cd18545 40 LIIALLFLALNLVNWVASRLRIYLMAKVGQRILYDLRQDLFSHLQKLSFSFFD--SRPVGKILSRVINDVNSLSDLlSNG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 828 RLALIAqNTANLGTGIIISFIYGWQLTLLLLSVVPFIAVAgiveMKMLAGNAKRdkKEMEAAGKIAT------EAIENIR 901
Cdd:cd18545 118 LINLIP-DLLTLVGIVIIMFSLNVRLALVTLAVLPLLVLV----VFLLRRRARK--AWQRVRKKISNlnaylhESISGIR 190
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 338817954 902 TVVSLTQE----RKFESMYVEKLHGpYRNSVRKAHIYG----ITFSISQAFMYFsyagcfrFGSYLIVNGHM 965
Cdd:cd18545 191 VIQSFAREdeneEIFDELNRENRKA-NMRAVRLNALFWplveLISALGTALVYW-------YGGKLVLGGAI 254
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1056-1242 |
2.07e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 52.12 E-value: 2.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1056 VKKGQTLALVGSSGCGKSTVVQLL---------------------ERFydpmAGSVLLDgqEAKKLNVQWLRAQLGI--V 1112
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILsgelipnlgdyeeepswdevlKRF----RGTELQN--YFKKLYNGEIKVVHKPqyV 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1113 SQEPILFDCSIAENIAYGDNSRVVphDEIVraaKEANIHPFIEtlpQKYNtrvgdkgtQLSGGQKQRIAIARALIRQPRV 1192
Cdd:PRK13409 170 DLIPKVFKGKVRELLKKVDERGKL--DEVV---ERLGLENILD---RDIS--------ELSGGELQRVAIAAALLRDADF 233
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 338817954 1193 LLLDEATSALDtesekvVQEALDKAR------EGRTCIVIAHRLSTIQN-ADLIVVI 1242
Cdd:PRK13409 234 YFFDEPTSYLD------IRQRLNVARlirelaEGKYVLVVEHDLAVLDYlADNVHIA 284
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
1055-1252 |
2.24e-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: 52.09 E-value: 2.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1055 EVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVlldgqeAKKLNV----QWLRAQLGIVSQEpILFDcSIAENIayg 1130
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV------DEDLKIsykpQYISPDYDGTVEE-FLRS-ANTDDF--- 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1131 DNSRVvpHDEIVRaakeanihPF-IETLpqkYNTRVGDkgtqLSGGQKQRIAIARALIRQPRVLLLDEATSALDTESEKV 1209
Cdd:COG1245 431 GSSYY--KTEIIK--------PLgLEKL---LDKNVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLA 493
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 338817954 1210 VQEALDKAREGR--TCIVIAHRLSTIqnaDLI---VVIENGKVKEHGT 1252
Cdd:COG1245 494 VAKAIRRFAENRgkTAMVVDHDIYLI---DYIsdrLMVFEGEPGVHGH 538
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
1057-1242 |
3.02e-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: 51.71 E-value: 3.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1057 KKGQTLALVGSSGCGKSTVVQLLerfydpmAGSvlldgqeakklnvqwLRAQLGIVSQEPilfdcSIAENIAYGDNSRVV 1136
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKIL-------SGE---------------LKPNLGDYDEEP-----SWDEVLKRFRGTELQ 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1137 PHDEIVRAAK-EANIHP-FIETLPQKYNTRVGD-------KG-------------------TQLSGGQKQRIAIARALIR 1188
Cdd:COG1245 150 DYFKKLANGEiKVAHKPqYVDLIPKVFKGTVREllekvdeRGkldelaeklglenildrdiSELSGGELQRVAIAAALLR 229
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 338817954 1189 QPRVLLLDEATSALD----TESEKVVQEAldkAREGRTCIVIAHRLSTIQN-ADLIVVI 1242
Cdd:COG1245 230 DADFYFFDEPSSYLDiyqrLNVARLIREL---AEEGKYVLVVEHDLAILDYlADYVHIL 285
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
146-338 |
3.46e-06 |
|
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: 50.17 E-value: 3.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 146 IRQKFFHAILRQEMGWFDIKGTTELNTRLTDDVSKISEGIGdKVGMFFQAIATFFAGFIVGFIRGWKLTLVIMAISPILG 225
Cdd:cd18543 74 LRTDLFAHLQRLDGAFHDRWQSGQLLSRATSDLSLVQRFLA-FGPFLLGNLLTLVVGLVVMLVLSPPLALVALASLPPLV 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 226 LSTAVWAKILSTFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKELERYQKHLENAKKIGIKKA-ISANISMGIAfLL 304
Cdd:cd18543 153 LVARRFRRRYFPASRRAQDQAGDLATVVEESVTGIRVVKAFGRERRELDRFEAAARRLRATRLRAArLRARFWPLLE-AL 231
|
170 180 190
....*....|....*....|....*....|....
gi 338817954 305 IYASYALAFWYGSTLVISKEYTIGnAMTVFFSIL 338
Cdd:cd18543 232 PELGLAAVLALGGWLVANGSLTLG-TLVAFSAYL 264
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
391-620 |
3.70e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 51.05 E-value: 3.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 391 LEFSDVHFSYPSRaniKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKIsidgQDIRNFNvrclreiIG 470
Cdd:PRK15064 320 LEVENLTKGFDNG---PLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV----KWSENAN-------IG 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 471 VVSQEPV--------LFS-----TTIAEN---IR--YGRGNVTMDEIEKAVKeanaydfimklpqkfdtlvgdrgaQLSG 532
Cdd:PRK15064 386 YYAQDHAydfendltLFDwmsqwRQEGDDeqaVRgtLGRLLFSQDDIKKSVK------------------------VLSG 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 533 GQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKArEGrTTIVIAH------RLSTirnaDVIAGFEDGVIV 606
Cdd:PRK15064 442 GEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESIESLNMALEKY-EG-TLIFVSHdrefvsSLAT----RIIEITPDGVVD 515
|
250
....*....|....
gi 338817954 607 EQGSHSELMKKEGI 620
Cdd:PRK15064 516 FSGTYEEYLRSQGI 529
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
1031-1254 |
5.91e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 50.63 E-value: 5.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1031 VTFNEVVFNYPtraNVPVL-QGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLldgQEAKklnvqwlrAQL 1109
Cdd:PLN03073 509 ISFSDASFGYP---GGPLLfKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVF---RSAK--------VRM 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1110 GIVSQEPIlfdcsiaeniaYGDNSRVVPHDEIVRAakeanihpFIETLPQKYNTRVGDKGTQ----------LSGGQKQR 1179
Cdd:PLN03073 575 AVFSQHHV-----------DGLDLSSNPLLYMMRC--------FPGVPEQKLRAHLGSFGVTgnlalqpmytLSGGQKSR 635
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 338817954 1180 IAIARALIRQPRVLLLDEATSALDTESEKVVQEALDKAREGrtCIVIAHRLSTIQNA-DLIVVIENGKVKE-HGTHQ 1254
Cdd:PLN03073 636 VAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGLVLFQGG--VLMVSHDEHLISGSvDELWVVSEGKVTPfHGTFH 710
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
118-335 |
5.93e-06 |
|
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: 49.80 E-value: 5.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 118 SGLGGGVLVAAYIQVSFWTLAAGRQIKKI----RQKFFHAILRQEMGWFDIKGTTELNTRLTDDVSKISEGIGDKVGMFF 193
Cdd:cd18546 42 AAAYLAVVLAGWVAQRAQTRLTGRTGERLlydlRLRVFAHLQRLSLDFHERETSGRIMTRMTSDIDALSELLQTGLVQLV 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 194 QAIATFFAGFIVGFIRGWKLTLVIMAISPILGLSTaVW----------------AKILSTFSdkelaayakagavaeEAL 257
Cdd:cd18546 122 VSLLTLVGIAVVLLVLDPRLALVALAALPPLALAT-RWfrrrssrayrrareriAAVNADLQ---------------ETL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 258 GAIRTVIAFGGQNKELERYQKHLENAKKIGIKkaisANISMGIAF----LLIYASYALAFWYGSTLVISKEYTIGnAMTV 333
Cdd:cd18546 186 AGIRVVQAFRRERRNAERFAELSDDYRDARLR----AQRLVAIYFpgveLLGNLATAAVLLVGAWRVAAGTLTVG-VLVA 260
|
..
gi 338817954 334 FF 335
Cdd:cd18546 261 FL 262
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
1044-1240 |
7.33e-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: 47.70 E-value: 7.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1044 ANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQllERFYDPMAGSVLLDGQEAKKLNVQWLrAQLGIVsqepilfdcsI 1123
Cdd:cd03238 6 ANVHNLQNLDVSIPLNVLVVVTGVSGSGKSTLVN--EGLYASGKARLISFLPKFSRNKLIFI-DQLQFL----------I 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1124 AENIAYgdnsrvvphdeivraakeanihpfiETLPQKYNTrvgdkgtqLSGGQKQRIAIARALIRQPR--VLLLDEATSA 1201
Cdd:cd03238 73 DVGLGY-------------------------LTLGQKLST--------LSGGELQRVKLASELFSEPPgtLFILDEPSTG 119
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 338817954 1202 LDTESEKVVQEALDKAR-EGRTCIVIAHRLSTIQNADLIV 1240
Cdd:cd03238 120 LHQQDINQLLEVIKGLIdLGNTVILIEHNLDVLSSADWII 159
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
1132-1246 |
7.40e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 50.49 E-value: 7.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1132 NSRVVPHDEIVRAAKEANIHPFIETLPQKYNTRVGD---KGtqLSGGQKQRIAIARALIRQPRVLLLDEATSALDTESek 1208
Cdd:TIGR00956 169 QNRPDGVSREEYAKHIADVYMATYGLSHTRNTKVGNdfvRG--VSGGERKRVSIAEASLGGAKIQCWDNATRGLDSAT-- 244
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 338817954 1209 vvqeALDKAREGRTCIVIAHRLSTI------QNA----DLIVVIENGK 1246
Cdd:TIGR00956 245 ----ALEFIRALKTSANILDTTPLVaiyqcsQDAyelfDKVIVLYEGY 288
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
402-620 |
9.50e-06 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 49.78 E-value: 9.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 402 SRANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIR-NFNVRCLREIIGVVSQ---EPV 477
Cdd:PRK09700 272 TSRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISpRSPLDAVKKGMAYITEsrrDNG 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 478 LFST-TIAENI------RYGRGNVTMDEIEKAVKEANAYDFIMKLPQKFDTlVGDRGAQLSGGQKQRIAIARALVRNPKI 550
Cdd:PRK09700 352 FFPNfSIAQNMaisrslKDGGYKGAMGLFHEVDEQRTAENQRELLALKCHS-VNQNITELSGGNQQKVLISKWLCCCPEV 430
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 338817954 551 LLLDEATSALDTESEAEVQAALDK-AREGRTTIVIAHRLSTIRNA-DVIAGFEDGVIVEQGSHSELMKKEGI 620
Cdd:PRK09700 431 IIFDEPTRGIDVGAKAEIYKVMRQlADDGKVILMVSSELPEIITVcDRIAVFCEGRLTQILTNRDDMSEEEI 502
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
391-613 |
1.04e-05 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 49.93 E-value: 1.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 391 LEFSDVHFSYPSRAnikILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIdGQDIRnfnvrclreiIG 470
Cdd:TIGR03719 323 IEAENLTKAFGDKL---LIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETVK----------LA 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 471 VVSQ--EPVLFSTTIAENIRYGrgnvtMDEIEKAVKEAN--AY----DFIMKLPQKfdtLVGdrgaQLSGGQKQRIAIAR 542
Cdd:TIGR03719 389 YVDQsrDALDPNKTVWEEISGG-----LDIIKLGKREIPsrAYvgrfNFKGSDQQK---KVG----QLSGGERNRVHLAK 456
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 338817954 543 ALVRNPKILLLDEATSALDTESEAEVQAALDKAreGRTTIVIAH-RLSTIRNADVIAGFEDGVIVE--QGSHSE 613
Cdd:TIGR03719 457 TLKSGGNVLLLDEPTNDLDVETLRALEEALLNF--AGCAVVISHdRWFLDRIATHILAFEGDSHVEwfEGNFSE 528
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
203-342 |
1.07e-05 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS (type 1 secretion systems), such as heterocyst differentiation protein HetC. HetC is similar to ABC protein exporters of T1SS (type 1 secretion systems) and is involved in early regulation of heterocyst differentiation in the filamentous cynobacterium Anabaena sp. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. ABC-transporter proteins in this group carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion.
Pssm-ID: 350012 [Multi-domain] Cd Length: 294 Bit Score: 48.71 E-value: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 203 FIVGFIRGWKLTLVIMAISPILGLSTAVWAKILSTFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKELERYQKHLEN 282
Cdd:cd18568 133 LGLMFYYNLQLTLIVLAFIPLYVLLTLLSSPKLKRNSREIFQANAEQQSFLVEALTGIATIKALAAERPIRWRWENKFAK 212
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 338817954 283 AKKIGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTIGN--AMTVFFSILIGAF 342
Cdd:cd18568 213 ALNTRFRGQKLSIVLQLISSLINHLGTIAVLWYGAYLVISGQLTIGQlvAFNMLFGSVINPL 274
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1048-1232 |
1.41e-05 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 49.16 E-value: 1.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1048 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLdGQEAKklnvqwlraqLGIVSQ--EPILFDCSIAE 1125
Cdd:TIGR03719 337 LIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETVK----------LAYVDQsrDALDPNKTVWE 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1126 NIAYGdnsrvvpHDEIVRAAKEANIHPFIetlpQKYNTRVGD---KGTQLSGGQKQRIAIARALIRQPRVLLLDEATSAL 1202
Cdd:TIGR03719 406 EISGG-------LDIIKLGKREIPSRAYV----GRFNFKGSDqqkKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDL 474
|
170 180 190
....*....|....*....|....*....|....*.
gi 338817954 1203 DTESEKVVQEALDKAreGRTCIVIAH------RLST 1232
Cdd:TIGR03719 475 DVETLRALEEALLNF--AGCAVVISHdrwfldRIAT 508
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1048-1214 |
1.42e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 49.40 E-value: 1.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1048 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLdgqeAKKLnvqwlraQLGIVSQEPILFdcsiaeni 1127
Cdd:PRK10636 327 ILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL----AKGI-------KLGYFAQHQLEF-------- 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1128 AYGDNSrvvPHDEIVRAAkeanihpfietlPQKYNTRV----------GDKGT----QLSGGQKQRIAIARALIRQPRVL 1193
Cdd:PRK10636 388 LRADES---PLQHLARLA------------PQELEQKLrdylggfgfqGDKVTeetrRFSGGEKARLVLALIVWQRPNLL 452
|
170 180
....*....|....*....|.
gi 338817954 1194 LLDEATSALDTESEKVVQEAL 1214
Cdd:PRK10636 453 LLDEPTNHLDLDMRQALTEAL 473
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
749-971 |
1.86e-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: 47.97 E-value: 1.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 749 NMFSLVFLGLGVLSFFTFFLQGFTFGKAGEILTTRLRSMAFKAMLRQDMSWFDdhKNSTGALSTRLAtDAAQVQG-ATGT 827
Cdd:cd18782 42 YVIGVVMLVAALLEAVLTALRTYLFTDTANRIDLELGGTIIDHLLRLPLGFFD--KRPVGELSTRIS-ELDTIRGfLTGT 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 828 RLALIAqNTANLGTGIIISFIYGWQLTLLLLSVVPFIAVAGIVEMKMLagnAKRDKKEMEAAGKIAT---EAIENIRTVV 904
Cdd:cd18782 119 ALTTLL-DVLFSVIYIAVLFSYSPLLTLVVLATVPLQLLLTFLFGPIL---RRQIRRRAEASAKTQSylvESLTGIQTVK 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 338817954 905 SLTQERKFESMYvEKLHGPYRNSVRKAHIYGITFS-ISQAFMYFSYAGCFRFGSYLIVNGHMRFKDVI 971
Cdd:cd18782 195 AQNAELKARWRW-QNRYARSLGEGFKLTVLGTTSGsLSQFLNKLSSLLVLWVGAYLVLRGELTLGQLI 261
|
|
| ABC_6TM_CyaB_HlyB_like |
cd18588 |
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ... |
203-343 |
1.92e-05 |
|
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: 47.88 E-value: 1.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 203 FIVGFIRGWKLTLVIMAISPILGLSTAVWAKILSTFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKELERYQKHLEN 282
Cdd:cd18588 133 LAVMFYYSPTLTLIVLASLPLYALLSLLVTPILRRRLEEKFQRGAENQSFLVETVTGIETVKSLAVEPQFQRRWEELLAR 212
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 338817954 283 AKKIGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTIGnaMTVFFSILIGAFS 343
Cdd:cd18588 213 YVKASFKTANLSNLASQIVQLIQKLTTLAILWFGAYLVMDGELTIG--QLIAFNMLAGQVS 271
|
|
| ABC_6TM_CyaB_HlyB_like |
cd18588 |
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ... |
843-965 |
3.18e-05 |
|
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: 47.49 E-value: 3.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 843 IIISFIYGWQLTLLLLSVVPFIAVAGIVEMKMLagNAKRDKKEMEAAGKIA--TEAIENIRTVVSLTQERKFESMYVEKL 920
Cdd:cd18588 133 LAVMFYYSPTLTLIVLASLPLYALLSLLVTPIL--RRRLEEKFQRGAENQSflVETVTGIETVKSLAVEPQFQRRWEELL 210
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 338817954 921 HGPYRNSVRKAHIYGITFSISQAFMYFSYAGCFRFGSYLIVNGHM 965
Cdd:cd18588 211 ARYVKASFKTANLSNLASQIVQLIQKLTTLAILWFGAYLVMDGEL 255
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
412-620 |
3.20e-05 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 48.12 E-value: 3.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 412 LNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVR-CLRE----------------------- 467
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAqRLARglvylpedrqssglyldaplawn 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 468 IIGVVSQEPVLFSTTIAENI---RYGRG-NVTMDEIEKAVKeanaydfimklpqkfdtlvgdrgaQLSGGQKQRIAIARA 543
Cdd:PRK15439 362 VCALTHNRRGFWIKPARENAvleRYRRAlNIKFNHAEQAAR------------------------TLSGGNQQKVLIAKC 417
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 338817954 544 LVRNPKILLLDEATSALDTESEAEV-QAALDKAREGRTTIVIAHRLstirnaDVIAGFEDGVIV-EQGSHSELMKKEGI 620
Cdd:PRK15439 418 LEASPQLLIVDEPTRGVDVSARNDIyQLIRSIAAQNVAVLFISSDL------EEIEQMADRVLVmHQGEISGALTGAAI 490
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1042-1249 |
3.44e-05 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 47.86 E-value: 3.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1042 TRANVPVLQGLSLEVKKGQTLALVGSSGCGKStvvQLLERFY--DPMA-GSVLLDGQEAK-KLNVQWLRAQLGIVSQ--- 1114
Cdd:PRK09700 272 TSRDRKKVRDISFSVCRGEILGFAGLVGSGRT---ELMNCLFgvDKRAgGEIRLNGKDISpRSPLDAVKKGMAYITEsrr 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1115 EPILF-DCSIAENIA---------YGDNSRVVPHDEIVRAAKEANihpfiETLPQKYNTrVGDKGTQLSGGQKQRIAIAR 1184
Cdd:PRK09700 349 DNGFFpNFSIAQNMAisrslkdggYKGAMGLFHEVDEQRTAENQR-----ELLALKCHS-VNQNITELSGGNQQKVLISK 422
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 338817954 1185 ALIRQPRVLLLDEATSALDTESEKVVQEALDK-AREGRTCIVIAHRLSTIQNA-DLIVVIENGKVKE 1249
Cdd:PRK09700 423 WLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQlADDGKVILMVSSELPEIITVcDRIAVFCEGRLTQ 489
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
1055-1243 |
3.68e-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: 3.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1055 EVKKGQTLALVGSSGCGKSTVVQLlerfydpMAGSVLLDGQeakklNVQWlraqlgivsqepilfdcsiaeniaygdnsr 1134
Cdd:cd03222 21 VVKEGEVIGIVGPNGTGKTTAVKI-------LAGQLIPNGD-----NDEW------------------------------ 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1135 vvphDEIVRAAKeanihpfietlPQKyntrvgdkgTQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEAL 1214
Cdd:cd03222 59 ----DGITPVYK-----------PQY---------IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAI 114
|
170 180 190
....*....|....*....|....*....|..
gi 338817954 1215 DKARE--GRTCIVIAHRLSTIQN-ADLIVVIE 1243
Cdd:cd03222 115 RRLSEegKKTALVVEHDLAVLDYlSDRIHVFE 146
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
1164-1240 |
3.72e-05 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 48.15 E-value: 3.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1164 RVGDKGTQLSGGQKQRIAIARALIRQP--RVL-LLDEATSALDTES----EKVVQEALDKareGRTCIVIAHRLSTIQNA 1236
Cdd:PRK00349 823 KLGQPATTLSGGEAQRVKLAKELSKRStgKTLyILDEPTTGLHFEDirklLEVLHRLVDK---GNTVVVIEHNLDVIKTA 899
|
....
gi 338817954 1237 DLIV 1240
Cdd:PRK00349 900 DWII 903
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
426-597 |
3.83e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 46.02 E-value: 3.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 426 GNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFnvrclreiigvvsQEPvlFSTTIAENIRYgrgNVTMDEIEKAVKE 505
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNI-------------AKP--YCTYIGHNLGL---KLEMTVFENLKFW 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 506 ANAYDFIMKLPQ-----KFDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALD-KAREGR 579
Cdd:PRK13541 95 SEIYNSAETLYAaihyfKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLIVmKANSGG 174
|
170
....*....|....*...
gi 338817954 580 TTIVIAHRLSTIRNADVI 597
Cdd:PRK13541 175 IVLLSSHLESSIKSAQIL 192
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
409-568 |
3.99e-05 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 47.69 E-value: 3.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 409 LKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVR-CLREIIGVVSQEP-----VL---- 478
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQdGLANGIVYISEDRkrdglVLgmsv 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 479 ---FSTTIAENIRYGRGNVTMDEIEKAVKeanayDFIM----KLPQKfDTLVGDrgaqLSGGQKQRIAIARALVRNPKIL 551
Cdd:PRK10762 348 kenMSLTALRYFSRAGGSLKHADEQQAVS-----DFIRlfniKTPSM-EQAIGL----LSGGNQQKVAIARGLMTRPKVL 417
|
170
....*....|....*..
gi 338817954 552 LLDEATSALDTESEAEV 568
Cdd:PRK10762 418 ILDEPTRGVDVGAKKEI 434
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
406-607 |
4.23e-05 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 47.42 E-value: 4.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 406 IKILKGLNLKVKSGQTVALVGNSGCGKSTTVqLLQRLYDPTEGKisidgqdiRNF-------NVRCLREIIGVvsQEPVL 478
Cdd:NF000106 26 VKAVDGVDLDVREGTVLGVLGP*GAA**RGA-LPAHV*GPDAGR--------RPWrf*twcaNRRALRRTIG*--HRPVR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 479 FSTTIAENiryGRGNVTMDEIEKAVKEANAYDFIMKLPQKFD--TLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEA 556
Cdd:NF000106 95 *GRRESFS---GRENLYMIGR*LDLSRKDARARADELLERFSltEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEP 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 338817954 557 TSALDTESEAEV-QAALDKAREGRTTIV----------IAHRLSTIRNADVIAgfeDGVIVE 607
Cdd:NF000106 172 TTGLDPRTRNEVwDEVRSMVRDGATVLLttqymeeaeqLAHELTVIDRGRVIA---DGKVDE 230
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
146-342 |
4.59e-05 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349984 [Multi-domain] Cd Length: 295 Bit Score: 46.70 E-value: 4.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 146 IRQKFFHAILRQEMGWFDIKGTTELNTRLTDDVSKISE----GIGDkvgmFFQAIATFFAGFIVGFIRGWKLTLVIMAIS 221
Cdd:cd18540 77 LRKKAFEHLQTLSFSYFDKTPVGWIMARVTSDTQRLGEiiswGLVD----LVWGITYMIGILIVMLILNWKLALIVLAVV 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 222 PILGLsTAVW----------------AKILSTFSdkelaayakagavaeEALGAIRTVIAFGGQNKELERYQKHLENAKK 285
Cdd:cd18540 153 PVLAV-VSIYfqkkilkayrkvrkinSRITGAFN---------------EGITGAKTTKTLVREEKNLREFKELTEEMRR 216
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 338817954 286 IGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTIGnAMTVFFSILIGAF 342
Cdd:cd18540 217 ASVRAARLSALFLPIVLFLGSIATALVLWYGGILVLAGAITIG-TLVAFISYATQFF 272
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
409-647 |
4.94e-05 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 46.73 E-value: 4.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 409 LKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQdirnfnVRCLREIIGVVSQepvlfsTTIAENIR 488
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGE------VSVIAISAGLSGQ------LTGIENIE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 489 YGR--GNVTMDEIEKAVKEANAY----DFIMKLPQKFdtlvgdrgaqlSGGQKQRIAIARALVRNPKILLLDEATSALDt 562
Cdd:PRK13546 108 FKMlcMGFKRKEIKAMTPKIIEFselgEFIYQPVKKY-----------SSGMRAKLGFSINITVNPDILVIDEALSVGD- 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 563 esEAEVQAALDKARE----GRTTIVIAHRLSTIRN-ADVIAGFEDGVIVEQGSHSELMKKegiYFRLVNMQTAGSQILSE 637
Cdd:PRK13546 176 --QTFAQKCLDKIYEfkeqNKTIFFVSHNLGQVRQfCTKIAWIEGGKLKDYGELDDVLPK---YEAFLNDFKKKSKAEQK 250
|
250
....*....|
gi 338817954 638 EFEVELSDEK 647
Cdd:PRK13546 251 EFRNKLDESR 260
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
1166-1261 |
5.31e-05 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 47.04 E-value: 5.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1166 GDKGTQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTESE-KVVQEALDKAREGRTCIVIAHRLSTI-QNADLIVVIE 1243
Cdd:NF000106 139 GRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRnEVWDEVRSMVRDGATVLLTTQYMEEAeQLAHELTVID 218
|
90
....*....|....*...
gi 338817954 1244 NGKVKEHGTHQQLLAQKG 1261
Cdd:NF000106 219 RGRVIADGKVDELKTKVG 236
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
372-595 |
5.95e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 47.32 E-value: 5.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 372 PKIDSFSERGHKPDNIKgNLEFSDVHFSYPSRaniKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRlyDPTEG--- 448
Cdd:PRK10938 243 PEPDEPSARHALPANEP-RIVLNNGVVSYNDR---PILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG--DHPQGysn 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 449 KISIDGQ---------DIRNFnvrclreiIGVVSQEPVL---FSTTIAENIRYGrgnvTMDEI--EKAVKEANaydfiMK 514
Cdd:PRK10938 317 DLTLFGRrrgsgetiwDIKKH--------IGYVSSSLHLdyrVSTSVRNVILSG----FFDSIgiYQAVSDRQ-----QK 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 515 LPQKFDTLVG--DRGAQ-----LSGGQkQRIA-IARALVRNPKILLLDEATSALDTESEAEVQAALDK-AREGRTTIV-- 583
Cdd:PRK10938 380 LAQQWLDILGidKRTADapfhsLSWGQ-QRLAlIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVlISEGETQLLfv 458
|
250 260
....*....|....*....|..
gi 338817954 584 ----------IAHRLSTIRNAD 595
Cdd:PRK10938 459 shhaedapacITHRLEFVPDGD 480
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
1041-1203 |
6.13e-05 |
|
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: 45.33 E-value: 6.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1041 PTRANVPVLQGLSLEVKKGQTLALVGSSGCGKST----VVQLLERFYDPmAGSVLLDGQEAKKLNVQWlRAQLGIVSQEp 1116
Cdd:cd03233 15 KGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTllkaLANRTEGNVSV-EGDIHYNGIPYKEFAEKY-PGEIIYVSEE- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1117 ilfdcsiaeniaygdnsrvvphdeivraakeaNIHPFIETLPQKYNTRVGDKGTQ----LSGGQKQRIAIARALIRQPRV 1192
Cdd:cd03233 92 --------------------------------DVHFPTLTVRETLDFALRCKGNEfvrgISGGERKRVSIAEALVSRASV 139
|
170
....*....|.
gi 338817954 1193 LLLDEATSALD 1203
Cdd:cd03233 140 LCWDNSTRGLD 150
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
1034-1237 |
6.21e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 47.32 E-value: 6.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1034 NEVVFNYPTRanvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYdPMAGS--VLLDGQeakklnvqwlraQLGi 1111
Cdd:PRK10938 264 NNGVVSYNDR---PILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDH-PQGYSndLTLFGR------------RRG- 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1112 vSQEPIlFDcsIAENIAYGDNS-----RVVP----------HDEI--VRAAKEANihpfiETLPQKY------NTRVGDK 1168
Cdd:PRK10938 327 -SGETI-WD--IKKHIGYVSSSlhldyRVSTsvrnvilsgfFDSIgiYQAVSDRQ-----QKLAQQWldilgiDKRTADA 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1169 GTQ-LSGGQkQRIA-IARALIRQPRVLLLDEATSALDTESEKVVQEALDK-AREGRT--------------CivIAHRLS 1231
Cdd:PRK10938 398 PFHsLSWGQ-QRLAlIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVlISEGETqllfvshhaedapaC--ITHRLE 474
|
....*.
gi 338817954 1232 TIQNAD 1237
Cdd:PRK10938 475 FVPDGD 480
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1171-1258 |
6.57e-05 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 46.72 E-value: 6.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1171 QLSGGQKQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTI-QNADLIVVIENGKV 1247
Cdd:PRK15093 158 ELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQnnNTTILLISHDLQMLsQWADKINVLYCGQT 237
|
90
....*....|.
gi 338817954 1248 KEHGTHQQLLA 1258
Cdd:PRK15093 238 VETAPSKELVT 248
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
113-230 |
7.45e-05 |
|
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: 46.34 E-value: 7.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 113 YAYYYSGLGGGVLVAAYIQVSFWTLAAGRQIKKIRQKFFHAILRQEMGWFDikgTTE----LNtRLTDDVSKISEGIGDK 188
Cdd:cd18580 41 LGVYAALLVLASVLLVLLRWLLFVLAGLRASRRLHDKLLRSVLRAPMSFFD---TTPsgriLN-RFSKDIGLIDEELPLA 116
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 338817954 189 VGMFFQAIATFFAGFIvgfirgwkltlVIMAISPILGLSTAV 230
Cdd:cd18580 117 LLDFLQSLFSVLGSLI-----------VIAIVSPYFLIVLPP 147
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
1171-1228 |
8.20e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 47.16 E-value: 8.20e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 338817954 1171 QLSGGQKQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEALDKAreGRTCIVIAH 1228
Cdd:PLN03073 344 TFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKW--PKTFIVVSH 399
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
530-585 |
8.54e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 46.65 E-value: 8.54e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 338817954 530 LSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEV-QAALDKAREGRTTIVIA 585
Cdd:PRK10982 392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIyQLIAELAKKDKGIIIIS 448
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
1066-1239 |
9.09e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 44.86 E-value: 9.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1066 GSSGCGKSTVVQLLERFYDPMAGSVL---LDGQEAKKLNVQWLRAQLGIVSqepilfDCSIAENIAYGdnSRVVPHDEIV 1142
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGNIYyknCNINNIAKPYCTYIGHNLGLKL------EMTVFENLKFW--SEIYNSAETL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1143 RAAkeanIHPFietlpqKYNTRVGDKGTQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEALD-KAREGR 1221
Cdd:PRK13541 105 YAA----IHYF------KLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLIVmKANSGG 174
|
170
....*....|....*...
gi 338817954 1222 TCIVIAHRLSTIQNADLI 1239
Cdd:PRK13541 175 IVLLSSHLESSIKSAQIL 192
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
525-609 |
9.54e-05 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 45.33 E-value: 9.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 525 DRGAQ-LSGGQKQRIAIARALVRNPK--ILLLDEATSALDTESEAEVQAALDKARE-GRTTIVIAHRLSTIRNADVI--- 597
Cdd:cd03270 132 SRSAPtLSGGEAQRIRLATQIGSGLTgvLYVLDEPSIGLHPRDNDRLIETLKRLRDlGNTVLVVEHDEDTIRAADHVidi 211
|
90
....*....|....*
gi 338817954 598 ---AGFEDGVIVEQG 609
Cdd:cd03270 212 gpgAGVHGGEIVAQG 226
|
|
| ABC_6TM_MRP7_D2_like |
cd18605 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ... |
749-920 |
1.06e-04 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and similar proteins; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated protein 7 (MRP7), which belongs to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350049 [Multi-domain] Cd Length: 300 Bit Score: 45.60 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 749 NMFSLVFLGLGVL-SFFTFFlQGFTFGKAGEILTTRLRSMAFKAMLRQDMSWFDdhKNSTGALSTRLATDAAQVQGATGT 827
Cdd:cd18605 42 NFFLTVYGFLAGLnSLFTLL-RAFLFAYGGLRAARRLHNKLLSSILFAKMSFFD--KTPVGRILNRFSSDVYTIDDSLPF 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 828 RL-ALIAQNTANLGTGIIISFIYGWqltlLLLSVVPFIAVAGIVEMKMLAGNakRDKKEMEAA--GKIAT---EAIENIR 901
Cdd:cd18605 119 ILnILLAQLFGLLGYLVVICYQLPW----LLLLLLPLAFIYYRIQRYYRATS--RELKRLNSVnlSPLYThfsETLKGLV 192
|
170
....*....|....*....
gi 338817954 902 TVVSLTQERKFESMYVEKL 920
Cdd:cd18605 193 TIRAFRKQERFLKEYLEKL 211
|
|
| ABC_ATPase |
pfam09818 |
ATPase of the ABC class; This is the C-terminal ATPase domain from bacterial ABC class ATPases. ... |
1056-1201 |
1.10e-04 |
|
ATPase of the ABC class; This is the C-terminal ATPase domain from bacterial ABC class ATPases. This entry also includes MRB1590 from Trypanosoma brucei brucei has a central ATPase domain homologous to this domain.
Pssm-ID: 462914 Cd Length: 282 Bit Score: 45.66 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1056 VKKGQTLaLVGSSGCGKSTVVQLLER-FYDPMAGsvllDGQEakklnvqwlraqlGIVSqepilfdcsiaeniaygDNSR 1134
Cdd:pfam09818 77 IPKGITL-IVGGGFHGKSTLLEALERgVYNHIPG----DGRE-------------FVVT-----------------DPDA 121
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 338817954 1135 VVPHDEIVRAAKEANIHPFIETLPQkyntrvGDKGTQL-----SGGQKQRIAIARALIRQPRVLLLDEATSA 1201
Cdd:pfam09818 122 VKIRAEDGRSVHGVDISPFINNLPP------GKDTTDFstedaSGSTSQAANIMEALEAGASLLLIDEDTSA 187
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
529-600 |
1.13e-04 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 43.89 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 529 QLSGGQKQRIAIARAL----VRNPKILLLDEATSALDTEseaEVQAALDKARE----GRTTIVIAHRLSTIRNADVIAGF 600
Cdd:cd03227 77 QLSGGEKELSALALILalasLKPRPLYILDEIDRGLDPR---DGQALAEAILEhlvkGAQVIVITHLPELAELADKLIHI 153
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
529-586 |
1.37e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 46.39 E-value: 1.37e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 338817954 529 QLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKAreGRTTIVIAH 586
Cdd:PLN03073 344 TFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKW--PKTFIVVSH 399
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
1171-1240 |
1.57e-04 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 43.50 E-value: 1.57e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 338817954 1171 QLSGGQKQRIAIARALI---RQPRVL-LLDEATSALDTESEKVVQEALDKAR-EGRTCIVIAHRLSTIQNADLIV 1240
Cdd:cd03227 77 QLSGGEKELSALALILAlasLKPRPLyILDEIDRGLDPRDGQALAEAILEHLvKGAQVIVITHLPELAELADKLI 151
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
402-597 |
2.41e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 45.59 E-value: 2.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 402 SRANIKILKGLNLKVKSGQTVALVGNSGCGKSTTV---------QLLQRLYDPT----EGKI----------------SI 452
Cdd:PRK00635 604 SKATKHNLKDLTISLPLGRLTVVTGVSGSGKSSLIndtlvpaveEFIEQGFCSNlsiqWGAIsrlvhitrdlpgrsqrSI 683
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 453 DGQDIRNFN---------VRCLR-----------EIIGVVSQEPVLFSTTIAEN--------------------IRYGRG 492
Cdd:PRK00635 684 PLTYIKAFDdlrelfaeqPRSKRlgltkshfsfnTPLGACAECQGLGSITTTDNrtsipcpsclgkrflpqvleVRYKGK 763
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 493 NVTmDEIEKAVKEANayDFIMKLP---QKFDTL---------VGDRGAQLSGGQKQRIAIARAL---VRNPKILLLDEAT 557
Cdd:PRK00635 764 NIA-DILEMTAYEAE--KFFLDEPsihEKIHALcslgldylpLGRPLSSLSGGEIQRLKLAYELlapSKKPTLYVLDEPT 840
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 338817954 558 SALDTES-EAEVQAALDKAREGRTTIVIAHRLSTIRNADVI 597
Cdd:PRK00635 841 TGLHTHDiKALIYVLQSLTHQGHTVVIIEHNMHVVKVADYV 881
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
401-584 |
4.01e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 44.40 E-value: 4.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 401 PSRANIKILKGLNLKVKSGQTVALVGNSGCGKS-TTVQLLQRLYDP-TEGKISIDGQDIRNFNVRCL-----------RE 467
Cdd:NF040905 268 PLHPERKVVDDVSLNVRRGEIVGIAGLMGAGRTeLAMSVFGRSYGRnISGTVFKDGKEVDVSTVSDAidaglayvtedRK 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 468 IIGVVSQEPVLFSTTIAENIRYGRGNVtMDEIEKaVKEANAY--DFIMKLPQKFDTLVgdrgaQLSGGQKQRIAIARALV 545
Cdd:NF040905 348 GYGLNLIDDIKRNITLANLGKVSRRGV-IDENEE-IKVAEEYrkKMNIKTPSVFQKVG-----NLSGGNQQKVVLSKWLF 420
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 338817954 546 RNPKILLLDEATSALDTESEAEVQAALDK-AREGRTTIVI 584
Cdd:NF040905 421 TDPDVLILDEPTRGIDVGAKYEIYTIINElAAEGKGVIVI 460
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
1042-1261 |
4.08e-04 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 44.73 E-value: 4.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1042 TRAnvpvLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLerfydpmAGsvlldgqeAKKL---NVQWL---------RAQL 1109
Cdd:NF033858 14 TVA----LDDVSLDIPAGCMVGLIGPDGVGKSSLLSLI-------AG--------ARKIqqgRVEVLggdmadarhRRAV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1110 GivsqeP-ILF-----------DCSIAENIAY-GdnsRVVPHDeivRAAKEANI---------HPFIETLPQKyntrvgd 1167
Cdd:NF033858 75 C-----PrIAYmpqglgknlypTLSVFENLDFfG---RLFGQD---AAERRRRIdellratglAPFADRPAGK------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1168 kgtqLSGGQKQRIAIARALIRQPRVLLLDEATSALDTESEKvvQ-----EALDKAREGRTCIViahrlST--IQNA---D 1237
Cdd:NF033858 137 ----LSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLSRR--QfweliDRIRAERPGMSVLV-----ATayMEEAerfD 205
|
250 260
....*....|....*....|....
gi 338817954 1238 LIVVIENGKVKEHGTHQQLLAQKG 1261
Cdd:NF033858 206 WLVAMDAGRVLATGTPAELLARTG 229
|
|
| ABC_6TM_CvaB_RaxB_like |
cd18567 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ... |
724-965 |
5.02e-04 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 secretion systems, CvaB and RaxB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the peptidase-containing ABC transporter subunit of T1SS (Type 1 secretion systems), such as Escherichia coli colicin V secretion/processing ATP-binding protein CvaB and putative ABC transporter RaxB. These ABC-transporter proteins carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion. RaxB is part of the T1SS RaxABC, which is responsible for the type 1-dependent secretion of the bacterial quorum-sensing molecule AvrXa21. Both CvaB and RaxB belong to a subgroup of T1SS ABC transporters that contain a C39 peptidase domain. T1SS are found in pathogenic Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium.
Pssm-ID: 350011 [Multi-domain] Cd Length: 294 Bit Score: 43.60 E-value: 5.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 724 AFSIILsEMIAIFGPG------DDAVKQQKCNMFSLVFLGLGVLSFF---TFFLQGFTFGKAGEILTTRLRSMAFKAMLR 794
Cdd:cd18567 9 LLSLAL-ELFALASPLylqlviDEVIVSGDRDLLTVLAIGFGLLLLLqalLSALRSWLVLYLSTSLNLQWTSNLFRHLLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 795 QDMSWFddHKNSTGALSTRL-ATDAAQ---VQGATGTRL-ALIAqntanLGTGIIIsFIYGWQLTLLllsVVPFIAVAGI 869
Cdd:cd18567 88 LPLSYF--EKRHLGDIVSRFgSLDEIQqtlTTGFVEALLdGLMA-----ILTLVMM-FLYSPKLALI---VLAAVALYAL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 870 VEMKMLAGNAKRDKKEMEAAGKIATEAIENIRTVVSL-------TQERKFESMYVEKLhgpyrNSVRKAHIYGITFS-IS 941
Cdd:cd18567 157 LRLALYPPLRRATEEQIVASAKEQSHFLETIRGIQTIklfgreaEREARWLNLLVDAI-----NADIRLQRLQILFSaAN 231
|
250 260
....*....|....*....|....
gi 338817954 942 QAFMYFSYAGCFRFGSYLIVNGHM 965
Cdd:cd18567 232 GLLFGLENILVIYLGALLVLDGEF 255
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
399-597 |
7.20e-04 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 42.21 E-value: 7.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 399 SYPSRANIKILKGLNLkvksgqtvaLVGNSGCGKSTTVQLLqrlydptegKISIDGQDIRNFNVRC-LREIIGVVS---Q 474
Cdd:cd03240 11 SFHERSEIEFFSPLTL---------IVGQNGAGKTTIIEAL---------KYALTGELPPNSKGGAhDPKLIREGEvraQ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 475 EPVLFSTTIAENIrygrgnvtmdeieKAVKEANAYDFIMKLPQ-KFDTLVGDRGAQLSGGQKQ------RIAIARALVRN 547
Cdd:cd03240 73 VKLAFENANGKKY-------------TITRSLAILENVIFCHQgESNWPLLDMRGRCSGGEKVlasliiRLALAETFGSN 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 338817954 548 PKILLLDEATSALDTESEAEVQAALDKAREG---RTTIVIAHRLSTIRNADVI 597
Cdd:cd03240 140 CGILALDEPTTNLDEENIEESLAEIIEERKSqknFQLIVITHDEELVDAADHI 192
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
508-621 |
7.93e-04 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 43.91 E-value: 7.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 508 AYDF---IMKLPQKFDTLV---------GDRGAQLSGGQKQRIAIARALVRNP--KIL-LLDEATSALDTESEA---EV- 568
Cdd:PRK00349 797 ALEFfeaIPKIARKLQTLVdvglgyiklGQPATTLSGGEAQRVKLAKELSKRStgKTLyILDEPTTGLHFEDIRkllEVl 876
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 338817954 569 QAALDKareGRTTIVIAHRLSTIRNADVIA--GFEDGV----IVEQGSHSELMKKEGIY 621
Cdd:PRK00349 877 HRLVDK---GNTVVVIEHNLDVIKTADWIIdlGPEGGDgggeIVATGTPEEVAKVEASY 932
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
529-615 |
8.05e-04 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 43.25 E-value: 8.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 529 QLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKARE--GRTTIVIAHRLSTIRN-ADVIAGFEDGVI 605
Cdd:PRK15093 158 ELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQnnNTTILLISHDLQMLSQwADKINVLYCGQT 237
|
90
....*....|
gi 338817954 606 VEQGSHSELM 615
Cdd:PRK15093 238 VETAPSKELV 247
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
843-965 |
1.45e-03 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS (type 1 secretion systems), such as heterocyst differentiation protein HetC. HetC is similar to ABC protein exporters of T1SS (type 1 secretion systems) and is involved in early regulation of heterocyst differentiation in the filamentous cynobacterium Anabaena sp. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. ABC-transporter proteins in this group carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion.
Pssm-ID: 350012 [Multi-domain] Cd Length: 294 Bit Score: 42.16 E-value: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 843 IIISFIYGWQLTLLLLSVVP-FIAVAGIVEMKMLAGNAKRDKKEMEAAGKIaTEAIENIRTVVSLTQERKFESmYVEKLH 921
Cdd:cd18568 133 LGLMFYYNLQLTLIVLAFIPlYVLLTLLSSPKLKRNSREIFQANAEQQSFL-VEALTGIATIKALAAERPIRW-RWENKF 210
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 338817954 922 GPYRNSVRKAHIYGITFS-ISQAFMYFSYAGCFRFGSYLIVNGHM 965
Cdd:cd18568 211 AKALNTRFRGQKLSIVLQlISSLINHLGTIAVLWYGAYLVISGQL 255
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
1170-1240 |
1.58e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 42.71 E-value: 1.58e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 338817954 1170 TQLSGGQKQRIAIARALIR--QPRVL-LLDEATSALDTESEKVVQEALDKARE-GRTCIVIAHRLSTIQNADLIV 1240
Cdd:COG0178 825 TTLSGGEAQRVKLASELSKrsTGKTLyILDEPTTGLHFHDIRKLLEVLHRLVDkGNTVVVIEHNLDVIKTADWII 899
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1159-1215 |
1.61e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 42.80 E-value: 1.61e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 338817954 1159 QKyntRVGdkgtQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEALD 1215
Cdd:PRK11819 440 QK---KVG----VLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVETLRALEEALL 489
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
530-623 |
1.96e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 42.69 E-value: 1.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 530 LSGGQKQRIAIARAL------VrnpkILLLDEATSAL---DTESEAEVqaaLDKARE-GRTTIVIAHRLSTIRNADVI-- 597
Cdd:TIGR00630 489 LSGGEAQRIRLATQIgsgltgV----LYVLDEPSIGLhqrDNRRLINT---LKRLRDlGNTLIVVEHDEDTIRAADYVid 561
|
90 100 110
....*....|....*....|....*....|....
gi 338817954 598 ----AGFEDGVIVEQGSHSELMKKE----GIYFR 623
Cdd:TIGR00630 562 igpgAGEHGGEVVASGTPEEILANPdsltGQYLS 595
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
530-621 |
3.12e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 41.94 E-value: 3.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 530 LSGGQKQRIAIARALVR--NPKIL-LLDEATSALDTEseaEVQ---AALDKARE-GRTTIVIAHRLSTIRNAD-VI---- 597
Cdd:COG0178 827 LSGGEAQRVKLASELSKrsTGKTLyILDEPTTGLHFH---DIRkllEVLHRLVDkGNTVVVIEHNLDVIKTADwIIdlgp 903
|
90 100
....*....|....*....|....*
gi 338817954 598 -AGFEDGVIVEQGSHSELMKKEGIY 621
Cdd:COG0178 904 eGGDGGGEIVAEGTPEEVAKVKASY 928
|
|
| PRK01889 |
PRK01889 |
GTPase RsgA; Reviewed |
1049-1079 |
4.10e-03 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234988 [Multi-domain] Cd Length: 356 Bit Score: 41.07 E-value: 4.10e-03
10 20 30
....*....|....*....|....*....|..
gi 338817954 1049 LQGLSLEVKKGQTLALVGSSGCGKSTVV-QLL 1079
Cdd:PRK01889 185 LDVLAAWLSGGKTVALLGSSGVGKSTLVnALL 216
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
1165-1251 |
5.22e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 41.35 E-value: 5.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 1165 VGDKGTQLSGGQKQRIAIARALI---RQPRVLLLDEATSALDTESEKVVQEALDK-AREGRTCIVIAHRLSTIQNADLIV 1240
Cdd:PRK00635 1693 LGQNLSSLSLSEKIAIKIAKFLYlppKHPTLFLLDEIATSLDNQQKSALLVQLRTlVSLGHSVIYIDHDPALLKQADYLI 1772
|
90
....*....|.
gi 338817954 1241 VIENGKVKEHG 1251
Cdd:PRK00635 1773 EMGPGSGKTGG 1783
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
1172-1240 |
8.29e-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: 39.16 E-value: 8.29e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 338817954 1172 LSGGQKQRIAIARALIRQPRVLL--LDEATSALDTESEKVVQEALDKARE-GRTCIVIAHRLSTIQNADLIV 1240
Cdd:cd03270 138 LSGGEAQRIRLATQIGSGLTGVLyvLDEPSIGLHPRDNDRLIETLKRLRDlGNTVLVVEHDEDTIRAADHVI 209
|
|
| ABC_6TM_VMR1_D2_like |
cd18604 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
114-280 |
8.56e-03 |
|
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: 39.76 E-value: 8.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 114 AYY---YSGLGGGVLVAAYIQVSFWTLAAGRQIKKIRQKFFHAILRQEMGWFDikgTT---ELNTRLTDDVSKISEGIGD 187
Cdd:cd18604 43 LYYlgiYALISLLSVLLGTLRYLLFFFGSLRASRKLHERLLHSVLRAPLRWLD---TTpvgRILNRFSKDIETIDSELAD 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338817954 188 KVGMFFQAIATFFAGFIVGFIRGWKL---TLVIMAISPILG---LSTAVWAK---------ILSTFSdkelaayakagav 252
Cdd:cd18604 120 SLSSLLESTLSLLVILIAIVVVSPAFllpAVVLAALYVYIGrlyLRASRELKrlesvarspILSHFG------------- 186
|
170 180
....*....|....*....|....*...
gi 338817954 253 aeEALGAIRTVIAFGGQnkelERYQKHL 280
Cdd:cd18604 187 --ETLAGLVTIRAFGAE----ERFIEEM 208
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1170-1240 |
9.68e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 40.34 E-value: 9.68e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 338817954 1170 TQLSGGQKQRIAIarALI-----RQPRVL-LLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIV 1240
Cdd:pfam02463 1076 DLLSGGEKTLVAL--ALIfaiqkYKPAPFyLLDEIDAALDDQNVSRVANLLKELSKNAQFIVISLREEMLEKADKLV 1150
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