|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
1-1216 |
1.07e-177 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 563.50 E-value: 1.07e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1 MFLGTLMAIAHGSGLPLMMIVFGEMTDKFvdNTGNFSLPVNFSLSMLnpgrileeemtryayyysglGGGVLVAAYIQVS 80
Cdd:PTZ00265 62 LGVSFVCATISGGTLPFFVSVFGVIMKNM--NLGENVNDIIFSLVLI--------------------GIFQFILSFISSF 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 81 FWTLAAGRQIKKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDDVSKISEGIGDKVGMFFQAIATFFAGFIVGFIRGWKL 160
Cdd:PTZ00265 120 CMDVVTTKILKTLKLEFLKSVFYQDGQFHDNNPGSKLTSDLDFYLEQVNAGIGTKFITIFTYASAFLGLYIWSLFKNARL 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 161 TLVIMAISPILGLSTAVWAKILSTFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKELERYQKHLENAKKIGIKKAIS 240
Cdd:PTZ00265 200 TLCITCVFPLIYICGVICNKKVKINKKTSLLYNNNTMSIIEEALVGIRTVVSYCGEKTILKKFNLSEKLYSKYILKANFM 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 241 ANISMGIAFLLIYASYALAFWYGSTLVIS--------KEYTIGNAMTVFFSILIGAFSVGQAAPCIDAFANARGAAYVIF 312
Cdd:PTZ00265 280 ESLHIGMINGFILASYAFGFWYGTRIIISdlsnqqpnNDFHGGSVISILLGVLISMFMLTIILPNITEYMKSLEATNSLY 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 313 DIIDNNPKIDSfSERGHKPDNIKgNLEFSDVHFSYPSRANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDP 392
Cdd:PTZ00265 360 EIINRKPLVEN-NDDGKKLKDIK-KIQFKNVRFHYDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDP 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 393 TEGKISI-DGQDIRNFNVRCLREIIGVVSQEPVLFSTTIAENIRYG----------------RGNVTMD----------- 444
Cdd:PTZ00265 438 TEGDIIInDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKYSlyslkdlealsnyyneDGNDSQEnknkrnscrak 517
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 445 ------------------------------EIEKAVKEANAYDFIMKLPQKFDTLVGDRGAQLSGGQKQRIAIARALVRN 494
Cdd:PTZ00265 518 cagdlndmsnttdsneliemrknyqtikdsEVVDVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRN 597
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 495 PKILLLDEATSALDTESEAEVQAALD--KAREGRTTIVIAHRLSTIRNADVI---------------------------- 544
Cdd:PTZ00265 598 PKILILDEATSSLDNKSEYLVQKTINnlKGNENRITIIIAHRLSTIRYANTIfvlsnrergstvdvdiigedptkdnken 677
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 545 -------------------AGFEDGVIVEQGSHSELMK-KEGIYFRLVNMQTAGSQILSEEFEVELSDEKAAG-DVAPNG 603
Cdd:PTZ00265 678 nnknnkddnnnnnnnnnnkINNAGSYIIEQGTHDALMKnKNGIYYTMINNQKVSSKKSSNNDNDKDSDMKSSAyKDSERG 757
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 604 WKARIFRNSTKKSLKSPHQNR----LDEETNELDANvPPVSFLKVLKLNKTEWPY---------------FVVGTVCAIA 664
Cdd:PTZ00265 758 YDPDEMNGNSKHENESASNKKsckmSDENASENNAG-GKLPFLRNLFKRKPKAPNnlrivyreifsykkdVTIIALSILV 836
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 665 NGALQPAFSIILSEMIA-IFgpgDDAVKQQKCNMFSLVFLGLGVLSFFTFFLQGFTFGKAGEILTTRLRSMAFKAMLRQD 743
Cdd:PTZ00265 837 AGGLYPVFALLYAKYVStLF---DFANLEANSNKYSLYILVIAIAMFISETLKNYYNNVIGEKVEKTMKRRLFENILYQE 913
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 744 MSWFDDHKNSTGALSTRLATDAAQVQGATGTRLALIAQNTANLGTGIIISFiYGWQLTLLLLSVVPFIAVAGIVEMKMLA 823
Cdd:PTZ00265 914 ISFFDQDKHAPGLLSAHINRDVHLLKTGLVNNIVIFTHFIVLFLVSMVMSF-YFCPIVAAVLTGTYFIFMRVFAIRARLT 992
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 824 GNAKRDKKEMEAAGKI----------------ATEAIENIRTVVSLTQERKFESMYVEKLHGPYRNSVRKAHIYGITFSI 887
Cdd:PTZ00265 993 ANKDVEKKEINQPGTVfaynsddeifkdpsflIQEAFYNMNTVIIYGLEDYFCNLIEKAIDYSNKGQKRKTLVNSMLWGF 1072
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 888 SQAFMYFSYAGCFRFGSYLIVNGHMRFKDVI-LVFSAIVLGAVAlGHASSFAPDYAKAKLSAAYLFSLFERQPLIDSYSG 966
Cdd:PTZ00265 1073 SQSAQLFINSFAYWFGSFLIRRGTILVDDFMkSLFTFLFTGSYA-GKLMSLKGDSENAKLSFEKYYPLIIRKSNIDVRDN 1151
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 967 EGLW---PDKFEGSVTFNEVVFNYPTRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYD------------ 1031
Cdd:PTZ00265 1152 GGIRiknKNDIKGKIEIMDVNFRYISRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDlkndhhivfkne 1231
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1032 ------------------------------------------PMAGSVLLDGQEAKKLNVQWLRAQLGIVSQEPILFDCS 1069
Cdd:PTZ00265 1232 htndmtneqdyqgdeeqnvgmknvnefsltkeggsgedstvfKNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMS 1311
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1070 IAENIAYG--DNSRvvphDEIVRAAKEANIHPFIETLPQKYNTRVGDKGTQLSGGQKQRIAIARALIRQPRVLLLDEATS 1147
Cdd:PTZ00265 1312 IYENIKFGkeDATR----EDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATS 1387
|
1370 1380 1390 1400 1410 1420 1430
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568932737 1148 ALDTESEKVVQEAL----DKAreGRTCIVIAHRLSTIQNADLIVVIENGK-----VKEHGTHQQLL-AQKGIYFSMVNI 1216
Cdd:PTZ00265 1388 SLDSNSEKLIEKTIvdikDKA--DKTIITIAHRIASIKRSDKIVVFNNPDrtgsfVQAHGTHEELLsVQDGVYKKYVKL 1464
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
1-579 |
2.30e-177 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 534.74 E-value: 2.30e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1 MFLGTLMAIAHGSGLPLMMIVFGEMTDKFVDNtGNFSLpvnfslsmlnpgrileeeMTRYAYYYSGLGGGVLVAAYIQVS 80
Cdd:COG1132 23 LILALLLLLLSALLELLLPLLLGRIIDALLAG-GDLSA------------------LLLLLLLLLGLALLRALLSYLQRY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 81 FWTLAAGRQIKKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDDVSKISEGIGDKVGMFFQAIATFFAGFIVGFIRGWKL 160
Cdd:COG1132 84 LLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDWRL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 161 TLVIMAISPILGLSTAVWAKILSTFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKELERYQKHLENAKKIGIKKAIS 240
Cdd:COG1132 164 ALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAARL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 241 ANISMGIAFLLIYASYALAFWYGSTLVISKEYTIGNAMTVFFSILIGAFSVGQAAPCIDAFANARGAAYVIFDIIDNNPK 320
Cdd:COG1132 244 SALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEPPE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 321 IDSfSERGHKPDNIKGNLEFSDVHFSYPSraNIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISID 400
Cdd:COG1132 324 IPD-PPGAVPLPPVRGEIEFENVSFSYPG--DRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILID 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 401 GQDIRNFNVRCLREIIGVVSQEPVLFSTTIAENIRYGRGNVTMDEIEKAVKEANAYDFIMKLPQKFDTLVGDRGAQLSGG 480
Cdd:COG1132 401 GVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGG 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 481 QKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTIRNADVIAGFEDGVIVEQGSHSE 560
Cdd:COG1132 481 QRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEE 560
|
570
....*....|....*....
gi 568932737 561 LMKKEGIYFRLVNMQTAGS 579
Cdd:COG1132 561 LLARGGLYARLYRLQFGEE 579
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
640-1221 |
3.61e-169 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 513.56 E-value: 3.61e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 640 SFLKVLKLNKTEWPYFVVGTVCAIANGALQPAFSIILSEMI-AIFGPGDdavkQQKCNMFSLVFLGLGVLSFFTFFLQGF 718
Cdd:COG1132 8 LLRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIdALLAGGD----LSALLLLLLLLLGLALLRALLSYLQRY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 719 TFGKAGEILTTRLRSMAFKAMLRQDMSWFDDHknSTGALSTRLATDAAQVQGATGTRLALIAQNTANLGTGIIISFIYGW 798
Cdd:COG1132 84 LLARLAQRVVADLRRDLFEHLLRLPLSFFDRR--RTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDW 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 799 QLTLLLLSVVPFIAVAGIVEMKMLAGNAKRDKKEMEAAGKIATEAIENIRTVVSLTQERKFESMYVEKLHGPYRNSVRKA 878
Cdd:COG1132 162 RLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 879 HIYGITFSISQAFMYFSYAGCFRFGSYLIVNGHMRFKDVILVFSAIVLGAVALGHASSFAPDYAKAKLSAAYLFSLFERQ 958
Cdd:COG1132 242 RLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEP 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 959 PLIDSYSGEGLwPDKFEGSVTFNEVVFNYPtrANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVL 1038
Cdd:COG1132 322 PEIPDPPGAVP-LPPVRGEIEFENVSFSYP--GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRIL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1039 LDGQEAKKLNVQWLRAQLGIVSQEPILFDCSIAENIAYGDNSrvVPHDEIVRAAKEANIHPFIETLPQKYNTRVGDKGTQ 1118
Cdd:COG1132 399 IDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPD--ATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVN 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1119 LSGGQKQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIENGKVKEHG 1198
Cdd:COG1132 477 LSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQG 556
|
570 580
....*....|....*....|...
gi 568932737 1199 THQQLLAQKGIYFSMVNIQAGTQ 1221
Cdd:COG1132 557 THEELLARGGLYARLYRLQFGEE 579
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
339-575 |
1.35e-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: 1.35e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 339 EFSDVHFSYPSRANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLREIIGV 418
Cdd:cd03249 2 EFKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 419 VSQEPVLFSTTIAENIRYGRGNVTMDEIEKAVKEANAYDFIMKLPQKFDTLVGDRGAQLSGGQKQRIAIARALVRNPKIL 498
Cdd:cd03249 82 VSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKIL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568932737 499 LLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTIRNADVIAGFEDGVIVEQGSHSELMKKEGIYFRLVNMQ 575
Cdd:cd03249 162 LLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKAQ 238
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
978-1217 |
1.43e-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: 1.43e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 978 VTFNEVVFNYPTRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQWLRAQLG 1057
Cdd:cd03249 1 IEFKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1058 IVSQEPILFDCSIAENIAYGDNSRVVphDEIVRAAKEANIHPFIETLPQKYNTRVGDKGTQLSGGQKQRIAIARALIRQP 1137
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYGKPDATD--EEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1138 RVLLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIENGKVKEHGTHQQLLAQKGIYFSMVNIQ 1217
Cdd:cd03249 159 KILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKAQ 238
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
67-576 |
1.43e-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: 1.43e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 67 LGGGVLVAAYIQV------SFWTLAAGRQI-KKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDdVSKISEGIGDKVGMF 139
Cdd:COG2274 198 LAIGLLLALLFEGllrllrSYLLLRLGQRIdLRLSSRFFRHLLRLPLSFFESRSVGDLASRFRD-VESIREFLTGSLLTA 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 140 FQAIATFFAGFIVGFIRGWKLTLVIMAISPILGLSTAVWAKILSTFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKE 219
Cdd:COG2274 277 LLDLLFVLIFLIVLFFYSPPLALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRF 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 220 LERYQKHLENAKKIGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTIGnaMTVFFSILIGAF--SVGQAAPC 297
Cdd:COG2274 357 RRRWENLLAKYLNARFKLRRLSNLLSTLSGLLQQLATVALLWLGAYLVIDGQLTLG--QLIAFNILSGRFlaPVAQLIGL 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 298 IDAFANARGAAYVIFDIIDNNPKIDSFSERGHKPdNIKGNLEFSDVHFSYPSRANiKILKGLNLKVKSGQTVALVGNSGC 377
Cdd:COG2274 435 LQRFQDAKIALERLDDILDLPPEREEGRSKLSLP-RLKGDIELENVSFRYPGDSP-PVLDNISLTIKPGERVAIVGRSGS 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 378 GKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLREIIGVVSQEPVLFSTTIAENIRYGRGNVTMDEIEKAVKEANAYD 457
Cdd:COG2274 513 GKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPDATDEEIIEAARLAGLHD 592
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 458 FIMKLPQKFDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLST 537
Cdd:COG2274 593 FIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLST 672
|
490 500 510
....*....|....*....|....*....|....*....
gi 568932737 538 IRNADVIAGFEDGVIVEQGSHSELMKKEGIYFRLVNMQT 576
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; ... |
645-961 |
2.84e-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: 427.64 E-value: 2.84e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 645 LKLNKTEWPYFVVGTVCAIANGALQPAFSIILSEMIAIFGPGDDAVKQQKCNMFSLVFLGLGVLSFFTFFLQGFTFGKAG 724
Cdd:cd18578 1 LKLNKPEWPLLLLGLIGAIIAGAVFPVFAILFSKLISVFSLPDDDELRSEANFWALMFLVLAIVAGIAYFLQGYLFGIAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 725 EILTTRLRSMAFKAMLRQDMSWFDDHKNSTGALSTRLATDAAQVQGATGTRLALIAQNTANLGTGIIISFIYGWQLTLLL 804
Cdd:cd18578 81 ERLTRRLRKLAFRAILRQDIAWFDDPENSTGALTSRLSTDASDVRGLVGDRLGLILQAIVTLVAGLIIAFVYGWKLALVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 805 LSVVPFIAVAGIVEMKMLAGNAKRDKKEMEAAGKIATEAIENIRTVVSLTQERKFESMYVEKLHGPYRNSVRKAHIYGIT 884
Cdd:cd18578 161 LATVPLLLLAGYLRMRLLSGFEEKNKKAYEESSKIASEAVSNIRTVASLTLEDYFLEKYEEALEEPLKKGLRRALISGLG 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568932737 885 FSISQAFMYFSYAGCFRFGSYLIVNGHMRFKDVILVFSAIVLGAVALGHASSFAPDYAKAKLSAAYLFSLFERQPLI 961
Cdd:cd18578 241 FGLSQSLTFFAYALAFWYGGRLVANGEYTFEQFFIVFMALIFGAQSAGQAFSFAPDIAKAKAAAARIFRLLDRKPEI 317
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
1-311 |
1.30e-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: 418.22 E-value: 1.30e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1 MFLGTLMAIAHGSGLPLMMIVFGEMTDKFVdNTGNFSLPVNFS--LSMLNPGRILEEEMTRYAYYYSGLGGGVLVAAYIQ 78
Cdd:cd18558 1 MVVGILCAIIHGGLLPAFMVIFGDMTDSFT-NGGMTNITGNSSglNSSAGPFEKLEEEMTLYAYYYLIIGAIVLITAYIQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 79 VSFWTLAAGRQIKKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDDVSKISEGIGDKVGMFFQAIATFFAGFIVGFIRGW 158
Cdd:cd18558 80 GSFWGLAAGRQTKKIRYKFFHAIMRQEIGWFDVNDTGELNTRLADDVSKINEGIGDKIGVIFQNIATFGTGFIIGFIRGW 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 159 KLTLVIMAISPILGLSTAVWAKILSTFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKELERYQKHLENAKKIGIKKA 238
Cdd:cd18558 160 KLTLVILAISPVLGLSAVVWAKILSGFTDKEKKAYAKAGAVAEEVLEAFRTVIAFGGQQKEETRYAQNLEIAKRNGIKKA 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568932737 239 ISANISMGIAFLLIYASYALAFWYGSTLVISKEYTIGNAMTVFFSILIGAFSVGQAAPCIDAFANARGAAYVI 311
Cdd:cd18558 240 ITFNISMGAAFLLIYASYALAFWYGTYLVTQQEYSIGEVLTVFFSVLIGAFSAGQQVPSIEAFANARGAAYHI 312
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
23-572 |
1.93e-132 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 421.82 E-value: 1.93e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 23 GEMTDKFVDNTGNFSLPVN-FSLSMLNPGRILEEemtryayyysGLGGGVLvaayiqvsfwTLAAGRQIKKIRQKFFHAI 101
Cdd:TIGR00958 185 GRVIDTLGGDKGPPALASAiFFMCLLSIASSVSA----------GLRGGSF----------NYTMARINLRIREDLFRSL 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 102 LRQEMGWFDIKGTTELNTRLTDDVSKISEGIGDKVGMFFQAIATFFAGFIVGFIRGWKLTLVIMAISPILGLSTAVWAKI 181
Cdd:TIGR00958 245 LRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLVMLLGLLGFMLWLSPRLTMVTLINLPLVFLAEKVFGKR 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 182 LSTFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKELERYQKHLENAKKIGIKKAISANISMGIAFLLIYASYALAFW 261
Cdd:TIGR00958 325 YQLLSEELQEAVAKANQVAEEALSGMRTVRSFAAEEGEASRFKEALEETLQLNKRKALAYAGYLWTTSVLGMLIQVLVLY 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 262 YGSTLVISKEYTIGNamtvFFSILIGAFSVGQAAPCIDAFAN----ARGAAYVIFDIIDNNPKIDSfsERGHKPDNIKGN 337
Cdd:TIGR00958 405 YGGQLVLTGKVSSGN----LVSFLLYQEQLGEAVRVLSYVYSgmmqAVGASEKVFEYLDRKPNIPL--TGTLAPLNLEGL 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 338 LEFSDVHFSYPSRANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLREIIG 417
Cdd:TIGR00958 479 IEFQDVSFSYPNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVA 558
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 418 VVSQEPVLFSTTIAENIRYGRGNVTMDEIEKAVKEANAYDFIMKLPQKFDTLVGDRGAQLSGGQKQRIAIARALVRNPKI 497
Cdd:TIGR00958 559 LVGQEPVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRV 638
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568932737 498 LLLDEATSALDTESEAEVQAalDKAREGRTTIVIAHRLSTIRNADVIAGFEDGVIVEQGSHSELMKKEGIYFRLV 572
Cdd:TIGR00958 639 LILDEATSALDAECEQLLQE--SRSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQGCYKHLV 711
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
637-1218 |
2.87e-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: 2.87e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 637 PPVSFLKVLKLNKTEWPYFVVGTVCAIANGALQPAFSIILseMIAIfgpgDDAVKQQkcNMFSLVFLGLGVLSFFTF--- 713
Cdd:COG2274 140 KPFGLRWFLRLLRRYRRLLLQVLLASLLINLLALATPLFT--QVVI----DRVLPNQ--DLSTLWVLAIGLLLALLFegl 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 714 --FLQGFTFGKAGEILTTRLRSMAFKAMLRQDMSWFDdhKNSTGALSTRLaTDAAQVQGATGTRLALIAQNTANLGTGII 791
Cdd:COG2274 212 lrLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFE--SRSVGDLASRF-RDVESIREFLTGSLLTALLDLLFVLIFLI 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 792 ISFIYGWQLTLLLLSVVPFIAVAGIVEMKMLAgnaKRDKKEMEAAGKIAT---EAIENIRTVVSLTQERKFESMYVEKLH 868
Cdd:COG2274 289 VLFFYSPPLALVVLLLIPLYVLLGLLFQPRLR---RLSREESEASAKRQSllvETLRGIETIKALGAESRFRRRWENLLA 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 869 GPYRNSVRKAHIYGITFSISQAFMYFSYAGCFRFGSYLIVNGHMRFkDVILVFSAIVLGAVA-LGHASSFAPDYAKAKLS 947
Cdd:COG2274 366 KYLNARFKLRRLSNLLSTLSGLLQQLATVALLWLGAYLVIDGQLTL-GQLIAFNILSGRFLApVAQLIGLLQRFQDAKIA 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 948 AAYLFSLFERQPliDSYSGEG-LWPDKFEGSVTFNEVVFNYPtRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLL 1026
Cdd:COG2274 445 LERLDDILDLPP--EREEGRSkLSLPRLKGDIELENVSFRYP-GDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLL 521
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1027 ERFYDPMAGSVLLDGQEAKKLNVQWLRAQLGIVSQEPILFDCSIAENIAYGDNSrvVPHDEIVRAAKEANIHPFIETLPQ 1106
Cdd:COG2274 522 LGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPD--ATDEEIIEAARLAGLHDFIEALPM 599
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1107 KYNTRVGDKGTQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLI 1186
Cdd:COG2274 600 GYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRI 679
|
570 580 590
....*....|....*....|....*....|..
gi 568932737 1187 VVIENGKVKEHGTHQQLLAQKGIYFSMVNIQA 1218
Cdd:COG2274 680 IVLDKGRIVEDGTHEELLARKGLYAELVQQQL 711
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
63-575 |
2.56e-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: 400.62 E-value: 2.56e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 63 YYSGLGGGVLVAA---YIQVSFWTLAAGRQIKKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDDVSKISEGIGDKVGMF 139
Cdd:TIGR02204 60 YFAFLLVVALVLAlgtAARFYLVTWLGERVVADIRRAVFAHLISLSPSFFDKNRSGEVVSRLTTDTTLLQSVIGSSLSMA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 140 FQAIATFFAGFIVGFIRGWKLTLVIMAISPILGLSTAVWAKILSTFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKE 219
Cdd:TIGR02204 140 LRNALMCIGGLIMMFITSPKLTSLVLLAVPLVLLPILLFGRRVRKLSRESQDRIADAGSYAGETLGAIRTVQAFGHEDAE 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 220 LERYQKHLENAKKIGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTIGN-AMTVFFSILIGAfSVGQAAPCI 298
Cdd:TIGR02204 220 RSRFGGAVEKAYEAARQRIRTRALLTAIVIVLVFGAIVGVLWVGAHDVIAGKMSAGTlGQFVFYAVMVAG-SIGTLSEVW 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 299 DAFANARGAAYVIFDIIDNNPKIDSFSERGHKPDNIKGNLEFSDVHFSYPSRANIKILKGLNLKVKSGQTVALVGNSGCG 378
Cdd:TIGR02204 299 GELQRAAGAAERLIELLQAEPDIKAPAHPKTLPVPLRGEIEFEQVNFAYPARPDQPALDGLNLTVRPGETVALVGPSGAG 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 379 KSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLREIIGVVSQEPVLFSTTIAENIRYGRGNVTMDEIEKAVKEANAYDF 458
Cdd:TIGR02204 379 KSTLFQLLLRFYDPQSGRILLDGVDLRQLDPAELRARMALVPQDPVLFAASVMENIRYGRPDATDEEVEAAARAAHAHEF 458
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 459 IMKLPQKFDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTI 538
Cdd:TIGR02204 459 ISALPEGYDTYLGERGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDAESEQLVQQALETLMKGRTTLIIAHRLATV 538
|
490 500 510
....*....|....*....|....*....|....*..
gi 568932737 539 RNADVIAGFEDGVIVEQGSHSELMKKEGIYFRLVNMQ 575
Cdd:TIGR02204 539 LKADRIVVMDQGRIVAQGTHAELIAKGGLYARLARLQ 575
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
628-1214 |
1.79e-123 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 397.56 E-value: 1.79e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 628 ETNELDANVPPVSFlKVLKLNKTEWPYFVVGTV---CAIANGALQPAFSiilSEMIAIFGpGDDAVKQQKCNMFSLVFLG 704
Cdd:TIGR00958 137 EAEQGQSETADLLF-RLLGLSGRDWPWLISAFVfltLSSLGEMFIPFYT---GRVIDTLG-GDKGPPALASAIFFMCLLS 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 705 LGvlSFFTFFLQGFTFGKAGEILTTRLRSMAFKAMLRQDMSWFDDHKnsTGALSTRLATDAAQVQGATGTRLALIAQNTA 784
Cdd:TIGR00958 212 IA--SSVSAGLRGGSFNYTMARINLRIREDLFRSLLRQDLGFFDENK--TGELTSRLSSDTQTMSRSLSLNVNVLLRNLV 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 785 NLGTGIIISFIYGWQLTLLLLSVVPFIAVAGIVEMKMLAGNAKRDKKEMEAAGKIATEAIENIRTVVSLTQERKFESMYV 864
Cdd:TIGR00958 288 MLLGLLGFMLWLSPRLTMVTLINLPLVFLAEKVFGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFAAEEGEASRFK 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 865 EKLHGPYRNSVRKAHIYGITFSISQAFMYFSYAGCFRFGSYLIVNGHMRfKDVILVFsaiVLGAVALGHA----SSFAPD 940
Cdd:TIGR00958 368 EALEETLQLNKRKALAYAGYLWTTSVLGMLIQVLVLYYGGQLVLTGKVS-SGNLVSF---LLYQEQLGEAvrvlSYVYSG 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 941 YAKAKLSAAYLFSLFERQPLIdSYSGEgLWPDKFEGSVTFNEVVFNYPTRANVPVLQGLSLEVKKGQTLALVGSSGCGKS 1020
Cdd:TIGR00958 444 MMQAVGASEKVFEYLDRKPNI-PLTGT-LAPLNLEGLIEFQDVSFSYPNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKS 521
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1021 TVVQLLERFYDPMAGSVLLDGQEAKKLNVQWLRAQLGIVSQEPILFDCSIAENIAYGDNSrvVPHDEIVRAAKEANIHPF 1100
Cdd:TIGR00958 522 TVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTD--TPDEEIMAAAKAANAHDF 599
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1101 IETLPQKYNTRVGDKGTQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEalDKAREGRTCIVIAHRLSTI 1180
Cdd:TIGR00958 600 IMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQE--SRSRASRTVLLIAHRLSTV 677
|
570 580 590
....*....|....*....|....*....|....
gi 568932737 1181 QNADLIVVIENGKVKEHGTHQQLLAQKGIYFSMV 1214
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; ... |
1-311 |
3.16e-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: 374.12 E-value: 3.16e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1 MFLGTLMAIAHGSGLPLMMIVFGEMTDKFVDNTGNFSLPVNFslsmlnpgrilEEEMTRYAYYYSGLGGGVLVAAYIQVS 80
Cdd:cd18577 1 LIIGLLAAIAAGAALPLMTIVFGDLFDAFTDFGSGESSPDEF-----------LDDVNKYALYFVYLGIGSFVLSYIQTA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 81 FWTLAAGRQIKKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDDVSKISEGIGDKVGMFFQAIATFFAGFIVGFIRGWKL 160
Cdd:cd18577 70 CWTITGERQARRIRKRYLKALLRQDIAWFDKNGAGELTSRLTSDTNLIQDGIGEKLGLLIQSLSTFIAGFIIAFIYSWKL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 161 TLVIMAISPILGLSTAVWAKILSTFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKELERYQKHLENAKKIGIKKAIS 240
Cdd:cd18577 150 TLVLLATLPLIAIVGGIMGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKALEKARKAGIKKGLV 229
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568932737 241 ANISMGIAFLLIYASYALAFWYGSTLVISKEYTIGNAMTVFFSILIGAFSVGQAAPCIDAFANARGAAYVI 311
Cdd:cd18577 230 SGLGLGLLFFIIFAMYALAFWYGSRLVRDGEISPGDVLTVFFAVLIGAFSLGQIAPNLQAFAKARAAAAKI 300
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
73-575 |
1.53e-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: 1.53e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 73 VAAYIQVSFWTLAAGRQIKKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDDVSKISEGIGDKVGMFFQAIATFFAGFIV 152
Cdd:TIGR02203 69 ICSFVSTYLLSWVSNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIV 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 153 GFIRGWKLTLVIMAISPILGLSTAVWAKILSTFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKELERYQKHLENAKK 232
Cdd:TIGR02203 149 LLYYSWQLTLIVVVMLPVLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFDAVSNRNRR 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 233 IGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTIGNaMTVFFSiligafSVGQAAPCIDAFANARG------ 306
Cdd:TIGR02203 229 LAMKMTSAGSISSPITQLIASLALAVVLFIALFQAQAGSLTAGD-FTAFIT------AMIALIRPLKSLTNVNApmqrgl 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 307 -AAYVIFDIIDNNPKIDsfsERGHKPDNIKGNLEFSDVHFSYPSRaNIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQL 385
Cdd:TIGR02203 302 aAAESLFTLLDSPPEKD---TGTRAIERARGDVEFRNVTFRYPGR-DRPALDSISLVIEPGETVALVGRSGSGKSTLVNL 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 386 LQRLYDPTEGKISIDGQDIRNFNVRCLREIIGVVSQEPVLFSTTIAENIRYGR-GNVTMDEIEKAVKEANAYDFIMKLPQ 464
Cdd:TIGR02203 378 IPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRtEQADRAEIERALAAAYAQDFVDKLPL 457
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 465 KFDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTIRNADVI 544
Cdd:TIGR02203 458 GLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRI 537
|
490 500 510
....*....|....*....|....*....|.
gi 568932737 545 AGFEDGVIVEQGSHSELMKKEGIYFRLVNMQ 575
Cdd:TIGR02203 538 VVMDDGRIVERGTHNELLARNGLYAQLHNMQ 568
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
338-571 |
1.06e-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: 1.06e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 338 LEFSDVHFSYPSRANiKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLREIIG 417
Cdd:cd03251 1 VEFKNVTFRYPGDGP-PVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 418 VVSQEPVLFSTTIAENIRYGRGNVTMDEIEKAVKEANAYDFIMKLPQKFDTLVGDRGAQLSGGQKQRIAIARALVRNPKI 497
Cdd:cd03251 80 LVSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568932737 498 LLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTIRNADVIAGFEDGVIVEQGSHSELMKKEGIYFRL 571
Cdd:cd03251 160 LILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKL 233
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
683-1217 |
1.55e-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: 369.41 E-value: 1.55e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 683 FGPGDDAVKQQKCNMFSLVFLGLGVLSFFTFFLqgftFGKAGEILTTRLRSMAFKAMLRQDMSWFDdhKNSTGALSTRLA 762
Cdd:TIGR02204 49 FSKDSSGLLNRYFAFLLVVALVLALGTAARFYL----VTWLGERVVADIRRAVFAHLISLSPSFFD--KNRSGEVVSRLT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 763 TDAAQVQGATGTRLALIAQNTANLGTGIIISFIYGWQLTLLLLSVVPFIAVAGIVEMKMLAGNAKRDKKEMEAAGKIATE 842
Cdd:TIGR02204 123 TDTTLLQSVIGSSLSMALRNALMCIGGLIMMFITSPKLTSLVLLAVPLVLLPILLFGRRVRKLSRESQDRIADAGSYAGE 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 843 AIENIRTVVSLTQERKFESMYVEKLHGPYRNSVRKAHIYGITFSISQAFMYFSYAGCFRFGSYLIVNGHMRFKDV-ILVF 921
Cdd:TIGR02204 203 TLGAIRTVQAFGHEDAERSRFGGAVEKAYEAARQRIRTRALLTAIVIVLVFGAIVGVLWVGAHDVIAGKMSAGTLgQFVF 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 922 SAIVLGAvALGHASSFAPDYAKAKLSAAYLFSLFERQPLIDSYSGEGLWPDKFEGSVTFNEVVFNYPTRANVPVLQGLSL 1001
Cdd:TIGR02204 283 YAVMVAG-SIGTLSEVWGELQRAAGAAERLIELLQAEPDIKAPAHPKTLPVPLRGEIEFEQVNFAYPARPDQPALDGLNL 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1002 EVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQWLRAQLGIVSQEPILFDCSIAENIAYG--DN 1079
Cdd:TIGR02204 362 TVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDLRQLDPAELRARMALVPQDPVLFAASVMENIRYGrpDA 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1080 SRvvphDEIVRAAKEANIHPFIETLPQKYNTRVGDKGTQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTESEKVVQE 1159
Cdd:TIGR02204 442 TD----EEVEAAARAAHAHEFISALPEGYDTYLGERGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDAESEQLVQQ 517
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 568932737 1160 ALDKAREGRTCIVIAHRLSTIQNADLIVVIENGKVKEHGTHQQLLAQKGIYFSMVNIQ 1217
Cdd:TIGR02204 518 ALETLMKGRTTLIIAHRLATVLKADRIVVMDQGRIVAQGTHAELIAKGGLYARLARLQ 575
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
209-580 |
6.08e-114 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 368.76 E-value: 6.08e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 209 TVIAFGGQNKELERYQKHLENAKKIGIKKAISAN---------ISMGIAFLLIYASYAlafwygstlVISKEYTIGNamt 279
Cdd:COG5265 230 TVKYFGNEAREARRYDEALARYERAAVKSQTSLAllnfgqaliIALGLTAMMLMAAQG---------VVAGTMTVGD--- 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 280 vfFsILIGAFSVGQAAPCidafaNARGAAY-----------VIFDIIDNNPKIDSfserghKPDNI-----KGNLEFSDV 343
Cdd:COG5265 298 --F-VLVNAYLIQLYIPL-----NFLGFVYreirqaladmeRMFDLLDQPPEVAD------APDAPplvvgGGEVRFENV 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 344 HFSY-PSRaniKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLREIIGVVSQE 422
Cdd:COG5265 364 SFGYdPER---PILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQD 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 423 PVLFSTTIAENIRYGRGNVTMDEIEKAVKEANAYDFIMKLPQKFDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDE 502
Cdd:COG5265 441 TVLFNDTIAYNIAYGRPDASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDE 520
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568932737 503 ATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTIRNADVIAGFEDGVIVEQGSHSELMKKEGIYFRLVNMQTAGSQ 580
Cdd:COG5265 521 ATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLYAQMWARQQEEEE 598
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
86-575 |
3.85e-109 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 355.10 E-value: 3.85e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 86 AGRQIKKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDD------------VSKISEGigdkvgmffqaiATFFAGFIVG 153
Cdd:PRK11176 93 SGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDseqvassssgalITVVREG------------ASIIGLFIMM 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 154 FIRGWKLTLVIMAISPILGLSTAVWAKILSTFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKELERYQKHLENAKKI 233
Cdd:PRK11176 161 FYYSWQLSLILIVIAPIVSIAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNRMRQQ 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 234 GIKKAISANISMGIAFLLiyASYALAF--WYGSTLVISKEYTIGnAMTVFFSILIGAFSVGQAAPCIDA-FANARGAAYV 310
Cdd:PRK11176 241 GMKMVSASSISDPIIQLI--ASLALAFvlYAASFPSVMDTLTAG-TITVVFSSMIALMRPLKSLTNVNAqFQRGMAACQT 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 311 IFDIIDNNPKIDsfsERGHKPDNIKGNLEFSDVHFSYPSRaNIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLY 390
Cdd:PRK11176 318 LFAILDLEQEKD---EGKRVIERAKGDIEFRNVTFTYPGK-EVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFY 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 391 DPTEGKISIDGQDIRNFNVRCLREIIGVVSQEPVLFSTTIAENIRYGRGNV-TMDEIEKAVKEANAYDFIMKLPQKFDTL 469
Cdd:PRK11176 394 DIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYARTEQySREQIEEAARMAYAMDFINKMDNGLDTV 473
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 470 VGDRGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTIRNADVIAGFED 549
Cdd:PRK11176 474 IGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVED 553
|
490 500
....*....|....*....|....*.
gi 568932737 550 GVIVEQGSHSELMKKEGIYFRLVNMQ 575
Cdd:PRK11176 554 GEIVERGTHAELLAQNGVYAQLHKMQ 579
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
338-575 |
2.31e-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: 2.31e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 338 LEFSDVHFSY-PSRaniKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLREII 416
Cdd:cd03253 1 IEFENVTFAYdPGR---PVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 417 GVVSQEPVLFSTTIAENIRYGRGNVTMDEIEKAVKEANAYDFIMKLPQKFDTLVGDRGAQLSGGQKQRIAIARALVRNPK 496
Cdd:cd03253 78 GVVPQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568932737 497 ILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTIRNADVIAGFEDGVIVEQGSHSELMKKEGIYFRLVNMQ 575
Cdd:cd03253 158 ILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMWKAQ 236
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
978-1210 |
1.87e-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: 334.58 E-value: 1.87e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 978 VTFNEVVFNYPTRANvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQWLRAQLG 1057
Cdd:cd03251 1 VEFKNVTFRYPGDGP-PVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1058 IVSQEPILFDCSIAENIAYGDnsRVVPHDEIVRAAKEANIHPFIETLPQKYNTRVGDKGTQLSGGQKQRIAIARALIRQP 1137
Cdd:cd03251 80 LVSQDVFLFNDTVAENIAYGR--PGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568932737 1138 RVLLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIENGKVKEHGTHQQLLAQKGIY 1210
Cdd:cd03251 158 PILILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVY 230
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
640-1220 |
1.94e-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: 347.09 E-value: 1.94e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 640 SFLKVLKLNKTEWPYFVVGTVCAIANGALQPAFSIILSEMI-AIFGPGDdavkQQKCNMFSLVFLGLGVLSFFTFFLQGF 718
Cdd:TIGR02203 1 TFRRLWSYVRPYKAGLVLAGVAMILVAATESTLAALLKPLLdDGFGGRD----RSVLWWVPLVVIGLAVLRGICSFVSTY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 719 TFGKAGEILTTRLRSMAFKAMLRQDMSWFDdhKNSTGALSTRLATDAAQVQGATGTRLALIAQNTANLGTGIIISFIYGW 798
Cdd:TIGR02203 77 LLSWVSNKVVRDIRVRMFEKLLGLPVSFFD--RQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIVLLYYSW 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 799 QLTLLLLSVVPFIAVAGIVEMKMLAGNAKRDKKEMEAAGKIATEAIENIRTVVSLTQE----RKFESMYVEKLhgpyRNS 874
Cdd:TIGR02203 155 QLTLIVVVMLPVLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQayetRRFDAVSNRNR----RLA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 875 VRKAHIYGITFSISQAFMYFSYAGCFRFGSYLIVNGHMRFKDVILVFSAIVLGAVALGHASSFAPDYAKAKLSAAYLFSL 954
Cdd:TIGR02203 231 MKMTSAGSISSPITQLIASLALAVVLFIALFQAQAGSLTAGDFTAFITAMIALIRPLKSLTNVNAPMQRGLAAAESLFTL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 955 FERQPLIDSysgEGLWPDKFEGSVTFNEVVFNYPTRaNVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMA 1034
Cdd:TIGR02203 311 LDSPPEKDT---GTRAIERARGDVEFRNVTFRYPGR-DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDS 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1035 GSVLLDGQEAKKLNVQWLRAQLGIVSQEPILFDCSIAENIAYGDnSRVVPHDEIVRAAKEANIHPFIETLPQKYNTRVGD 1114
Cdd:TIGR02203 387 GQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGR-TEQADRAEIERALAAAYAQDFVDKLPLGLDTPIGE 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1115 KGTQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIENGKV 1194
Cdd:TIGR02203 466 NGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRI 545
|
570 580
....*....|....*....|....*.
gi 568932737 1195 KEHGTHQQLLAQKGIYFSMVNIQAGT 1220
Cdd:TIGR02203 546 VERGTHNELLARNGLYAQLHNMQFRE 571
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
951-1218 |
1.96e-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: 1.96e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 951 LFSLFERQPLI-DSYSGEGLWPDkfEGSVTFNEVVFNY-PTRanvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLER 1028
Cdd:COG5265 332 MFDLLDQPPEVaDAPDAPPLVVG--GGEVRFENVSFGYdPER---PILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFR 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1029 FYDPMAGSVLLDGQEAKKLNVQWLRAQLGIVSQEPILFDCSIAENIAYG--DNSRvvphDEIVRAAKEANIHPFIETLPQ 1106
Cdd:COG5265 407 FYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAYGrpDASE----EEVEAAARAAQIHDFIESLPD 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1107 KYNTRVGDKGTQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLI 1186
Cdd:COG5265 483 GYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEI 562
|
250 260 270
....*....|....*....|....*....|..
gi 568932737 1187 VVIENGKVKEHGTHQQLLAQKGIYFSMVNIQA 1218
Cdd:COG5265 563 LVLEAGRIVERGTHAELLAQGGLYAQMWARQQ 594
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
655-951 |
3.14e-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: 329.24 E-value: 3.14e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 655 FVVGTVCAIANGALQPAFSIILSEMIAIFGPGDDAVK-----------------QQKCNMFSLVFLGLGVLSFFTFFLQG 717
Cdd:cd18558 1 MVVGILCAIIHGGLLPAFMVIFGDMTDSFTNGGMTNItgnssglnssagpfeklEEEMTLYAYYYLIIGAIVLITAYIQG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 718 FTFGKAGEILTTRLRSMAFKAMLRQDMSWFDdhKNSTGALSTRLATDAAQVQGATGTRLALIAQNTANLGTGIIISFIYG 797
Cdd:cd18558 81 SFWGLAAGRQTKKIRYKFFHAIMRQEIGWFD--VNDTGELNTRLADDVSKINEGIGDKIGVIFQNIATFGTGFIIGFIRG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 798 WQLTLLLLSVVPFIAVAGIVEMKMLAGNAKRDKKEMEAAGKIATEAIENIRTVVSLTQERKFESMYVEKLHGPYRNSVRK 877
Cdd:cd18558 159 WKLTLVILAISPVLGLSAVVWAKILSGFTDKEKKAYAKAGAVAEEVLEAFRTVIAFGGQQKEETRYAQNLEIAKRNGIKK 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568932737 878 AHIYGITFSISQAFMYFSYAGCFRFGSYLIVNGHMR-FKDVILVFSAIVLGAVALGHASSFAPdYAKAKLSAAYL 951
Cdd:cd18558 239 AITFNISMGAAFLLIYASYALAFWYGTYLVTQQEYSiGEVLTVFFSVLIGAFSAGQQVPSIEA-FANARGAAYHI 312
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
336-566 |
2.19e-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: 2.19e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 336 GNLEFSDVHFSYpsRANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLREI 415
Cdd:cd03254 1 GEIEFENVNFSY--DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 416 IGVVSQEPVLFSTTIAENIRYGRGNVTMDEIEKAVKEANAYDFIMKLPQKFDTLVGDRGAQLSGGQKQRIAIARALVRNP 495
Cdd:cd03254 79 IGVVLQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568932737 496 KILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTIRNADVIAGFEDGVIVEQGSHSELMKKEG 566
Cdd:cd03254 159 KILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
978-1217 |
2.44e-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: 2.44e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 978 VTFNEVVFNYPTraNVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQWLRAQLG 1057
Cdd:cd03253 1 IEFENVTFAYDP--GRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1058 IVSQEPILFDCSIAENIAYGDNSrvVPHDEIVRAAKEANIHPFIETLPQKYNTRVGDKGTQLSGGQKQRIAIARALIRQP 1137
Cdd:cd03253 79 VVPQDTVLFNDTIGYNIRYGRPD--ATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1138 RVLLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIENGKVKEHGTHQQLLAQKGIYFSMVNIQ 1217
Cdd:cd03253 157 PILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMWKAQ 236
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
239-575 |
3.70e-97 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 322.30 E-value: 3.70e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 239 ISANISMGIAFLLiyasyalafwyGSTLVISKEYTIGN--AMTVFFSILIG------AF--SVGQAAPCIDAFanargaa 308
Cdd:PRK13657 248 AASTITMLAILVL-----------GAALVQKGQLRVGEvvAFVGFATLLIGrldqvvAFinQVFMAAPKLEEF------- 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 309 yviFDIIDNNPKIDsfsERGHKPD--NIKGNLEFSDVHFSYPSRAniKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLL 386
Cdd:PRK13657 310 ---FEVEDAVPDVR---DPPGAIDlgRVKGAVEFDDVSFSYDNSR--QGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLL 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 387 QRLYDPTEGKISIDGQDIRNFNVRCLREIIGVVSQEPVLFSTTIAENIRYGRGNVTMDEIEKAVKEANAYDFIMKLPQKF 466
Cdd:PRK13657 382 QRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIERKPDGY 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 467 DTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTIRNADVIAG 546
Cdd:PRK13657 462 DTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILV 541
|
330 340
....*....|....*....|....*....
gi 568932737 547 FEDGVIVEQGSHSELMKKEGIYFRLVNMQ 575
Cdd:PRK13657 542 FDNGRVVESGSFDELVARGGRFAALLRAQ 570
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
302-566 |
9.78e-96 |
|
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: 9.78e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 302 ANARGAAYVIFDIIDNNPKIdsfSERGHKPDNIKGN--LEFSDVHFSYPSRANIkiLKGLNLKVKSGQTVALVGNSGCGK 379
Cdd:COG4988 302 ANGIAAAEKIFALLDAPEPA---APAGTAPLPAAGPpsIELEDVSFSYPGGRPA--LDGLSLTIPPGERVALVGPSGAGK 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 380 STTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLREIIGVVSQEPVLFSTTIAENIRYGRGNVTMDEIEKAVKEANAYDFI 459
Cdd:COG4988 377 STLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPDASDEELEAALEAAGLDEFV 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 460 MKLPQKFDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTIR 539
Cdd:COG4988 457 AALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLA 536
|
250 260
....*....|....*....|....*..
gi 568932737 540 NADVIAGFEDGVIVEQGSHSELMKKEG 566
Cdd:COG4988 537 QADRILVLDDGRIVEQGTHEELLAKNG 563
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
976-1208 |
1.23e-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: 1.23e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 976 GSVTFNEVVFNYptRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQWLRAQ 1055
Cdd:cd03254 1 GEIEFENVNFSY--DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1056 LGIVSQEPILFDCSIAENIAYGDNSrvVPHDEIVRAAKEANIHPFIETLPQKYNTRVGDKGTQLSGGQKQRIAIARALIR 1135
Cdd:cd03254 79 IGVVLQDTFLFSGTIMENIRLGRPN--ATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLR 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568932737 1136 QPRVLLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIENGKVKEHGTHQQLLAQKG 1208
Cdd:cd03254 157 DPKILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
82-571 |
3.20e-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: 3.20e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 82 WTLaagRQIKKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDDVskisegigDKVGMFF-QAIATFFAGFIVGFIrgwkL 160
Cdd:COG4987 82 ATL---RLLADLRVRLYRRLEPLAPAGLARLRSGDLLNRLVADV--------DALDNLYlRVLLPLLVALLVILA----A 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 161 TLVIMAISPILGLSTA-------VWAKILSTFSDKELAAYAKAG-----AVAEEALGAIRTVIAFGGQNKELERYQKHLE 228
Cdd:COG4987 147 VAFLAFFSPALALVLAlglllagLLLPLLAARLGRRAGRRLAAAraalrARLTDLLQGAAELAAYGALDRALARLDAAEA 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 229 NAKKIGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTiGNAMTVFFSILIGAFSVgqAAPCIDAFAN---AR 305
Cdd:COG4987 227 RLAAAQRRLARLSALAQALLQLAAGLAVVAVLWLAAPLVAAGALS-GPLLALLVLAALALFEA--LAPLPAAAQHlgrVR 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 306 GAAYVIFDIIDNNPKIDSFSERGHKPDNikGNLEFSDVHFSYPSRANIkILKGLNLKVKSGQTVALVGNSGCGKSTTVQL 385
Cdd:COG4987 304 AAARRLNELLDAPPAVTEPAEPAPAPGG--PSLELEDVSFRYPGAGRP-VLDGLSLTLPPGERVAIVGPSGSGKSTLLAL 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 386 LQRLYDPTEGKISIDGQDIRNFNVRCLREIIGVVSQEPVLFSTTIAENIRYGRGNVTMDEIEKAVKEANAYDFIMKLPQK 465
Cdd:COG4987 381 LLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPDATDEELWAALERVGLGDWLAALPDG 460
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 466 FDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTIRNADVIA 545
Cdd:COG4987 461 LDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRIL 540
|
490 500
....*....|....*....|....*.
gi 568932737 546 GFEDGVIVEQGSHSELMKKEGIYFRL 571
Cdd:COG4987 541 VLEDGRIVEQGTHEELLAQNGRYRQL 566
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
731-1219 |
7.32e-92 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 307.72 E-value: 7.32e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 731 LRSMAFKAMLRQDMSWFDdhKNSTGALSTRLATDAAQVQGATGTRLALIAQNTANLGTGIIISFIYGWQLTLLLLSVVPF 810
Cdd:PRK11176 100 MRRRLFGHMMGMPVSFFD--KQSTGTLLSRITYDSEQVASSSSGALITVVREGASIIGLFIMMFYYSWQLSLILIVIAPI 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 811 IAVAgiveMKMLAGNAKRDKKEMEAA-GKIATEAIENIR--TVVSLTQERKFESMYVEKLHGPYR-NSVRKAHIYGITFS 886
Cdd:PRK11176 178 VSIA----IRVVSKRFRNISKNMQNTmGQVTTSAEQMLKghKEVLIFGGQEVETKRFDKVSNRMRqQGMKMVSASSISDP 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 887 ISQAFMYFSYAGCFRFGSYLIVNGHMRFKDVILVFSAIVLGAVALGHASSFAPDYAKAKLSAAYLFSLFERQPLIDSYSG 966
Cdd:PRK11176 254 IIQLIASLALAFVLYAASFPSVMDTLTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGMAACQTLFAILDLEQEKDEGKR 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 967 EglwPDKFEGSVTFNEVVFNYPTRaNVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKK 1046
Cdd:PRK11176 334 V---IERAKGDIEFRNVTFTYPGK-EVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRD 409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1047 LNVQWLRAQLGIVSQEPILFDCSIAENIAYGDN---SRvvphDEIVRAAKEANIHPFIETLPQKYNTRVGDKGTQLSGGQ 1123
Cdd:PRK11176 410 YTLASLRNQVALVSQNVHLFNDTIANNIAYARTeqySR----EQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQ 485
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1124 KQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIENGKVKEHGTHQQL 1203
Cdd:PRK11176 486 RQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAEL 565
|
490
....*....|....*.
gi 568932737 1204 LAQKGIYFSMVNIQAG 1219
Cdd:PRK11176 566 LAQNGVYAQLHKMQFG 581
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
933-1208 |
3.61e-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: 296.67 E-value: 3.61e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 933 HASsfapdyAKAKLSAAYLFSLFErQPLIDSYSGEGLWPDKFEGSVTFNEVVFNYPTRAnvPVLQGLSLEVKKGQTLALV 1012
Cdd:COG4988 299 HAR------ANGIAAAEKIFALLD-APEPAAPAGTAPLPAAGPPSIELEDVSFSYPGGR--PALDGLSLTIPPGERVALV 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1013 GSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQWLRAQLGIVSQEPILFDCSIAENIAYGDnsRVVPHDEIVRAA 1092
Cdd:COG4988 370 GPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGR--PDASDEELEAAL 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1093 KEANIHPFIETLPQKYNTRVGDKGTQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEALDKAREGRTCIV 1172
Cdd:COG4988 448 EAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVIL 527
|
250 260 270
....*....|....*....|....*....|....*.
gi 568932737 1173 IAHRLSTIQNADLIVVIENGKVKEHGTHQQLLAQKG 1208
Cdd:COG4988 528 ITHRLALLAQADRILVLDDGRIVEQGTHEELLAKNG 563
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
969-1194 |
1.64e-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: 1.64e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 969 LWPDKFEGSVTFNEVVFNYPTRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLN 1048
Cdd:cd03248 3 LAPDHLKGIVKFQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1049 VQWLRAQLGIVSQEPILFDCSIAENIAYGDNSrvVPHDEIVRAAKEANIHPFIETLPQKYNTRVGDKGTQLSGGQKQRIA 1128
Cdd:cd03248 83 HKYLHSKVSLVGQEPVLFARSLQDNIAYGLQS--CSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568932737 1129 IARALIRQPRVLLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIENGKV 1194
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 ... |
145-576 |
3.94e-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: 3.94e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 145 TFFAgfiVGFIRGWKLTLVIMAISPILGLSTAVWAKILSTFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKELERYQ 224
Cdd:TIGR01846 268 VFLA---VMFFYSPTLTGVVIGSLVCYALLSVFVGPILRKRVEDKFERSAAATSFLVESVTGIETIKATATEPQFQNRWD 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 225 KHLENAKKIGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTIGNamTVFFSILIGAFS--VGQAAPCIDAFA 302
Cdd:TIGR01846 345 RQLAAYVAASFRVTNLGNIAGQAIELIQKLTFAILLWFGAHLVIGGALSPGQ--LVAFNMLAGRVTqpVLRLAQLWQDFQ 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 303 NARGAAYVIFDIIdNNPKIDSFSERGHKPdNIKGNLEFSDVHFSYPSRANiKILKGLNLKVKSGQTVALVGNSGCGKSTT 382
Cdd:TIGR01846 423 QTGIALERLGDIL-NSPTEPRSAGLAALP-ELRGAITFENIRFRYAPDSP-EVLSNLNLDIKPGEFIGIVGPSGSGKSTL 499
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 383 VQLLQRLYDPTEGKISIDGQDIRNFNVRCLREIIGVVSQEPVLFSTTIAENIRYGRGNVTMDEIEKAVKEANAYDFIMKL 462
Cdd:TIGR01846 500 TKLLQRLYTPQHGQVLVDGVDLAIADPAWLRRQMGVVLQENVLFSRSIRDNIALCNPGAPFEHVIHAAKLAGAHDFISEL 579
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 463 PQKFDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTIRNAD 542
Cdd:TIGR01846 580 PQGYNTEVGEKGANLSGGQRQRIAIARALVGNPRILIFDEATSALDYESEALIMRNMREICRGRTVIIIAHRLSTVRACD 659
|
410 420 430
....*....|....*....|....*....|....
gi 568932737 543 VIAGFEDGVIVEQGSHSELMKKEGIYFRLVNMQT 576
Cdd:TIGR01846 660 RIIVLEKGQIAESGRHEELLALQGLYARLWQQQS 693
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
338-550 |
2.07e-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: 269.25 E-value: 2.07e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 338 LEFSDVHFSYPSRANiKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLREIIG 417
Cdd:cd03228 1 IEFKNVSFSYPGRPK-PVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 418 VVSQEPVLFSTTIAENIrygrgnvtmdeiekavkeanaydfimklpqkfdtlvgdrgaqLSGGQKQRIAIARALVRNPKI 497
Cdd:cd03228 80 YVPQDPFLFSGTIRENI------------------------------------------LSGGQRQRIAIARALLRDPPI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 568932737 498 LLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTIRNADVIAGFEDG 550
Cdd:cd03228 118 LILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDG 170
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
727-1216 |
5.86e-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: 5.86e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 727 LTTRLRSMAFKAMLRQDMSWFddHKNSTGALSTRLATDAAQVQGATgtrLALIAQNTANLGTGIIISFIYGWQLTLLLLS 806
Cdd:COG4987 86 LLADLRVRLYRRLEPLAPAGL--ARLRSGDLLNRLVADVDALDNLY---LRVLLPLLVALLVILAAVAFLAFFSPALALV 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 807 VVPFIAVAGIVeMKMLAG--NAKRDKKEMEAAGKIATEAIENIRTVVSLT----QERKFESmyVEKLHGPYRNSVRKAHI 880
Cdd:COG4987 161 LALGLLLAGLL-LPLLAArlGRRAGRRLAAARAALRARLTDLLQGAAELAaygaLDRALAR--LDAAEARLAAAQRRLAR 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 881 Y-GITFSISQAFMYFSYAGCFRFGSYLIVNGHMRFKDV-ILVFSAIVLGAVALGHASSFApDYAKAKLSAAYLFSLFERQ 958
Cdd:COG4987 238 LsALAQALLQLAAGLAVVAVLWLAAPLVAAGALSGPLLaLLVLAALALFEALAPLPAAAQ-HLGRVRAAARRLNELLDAP 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 959 PLIdSYSGEGLWPDKFeGSVTFNEVVFNYPTrANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVL 1038
Cdd:COG4987 317 PAV-TEPAEPAPAPGG-PSLELEDVSFRYPG-AGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSIT 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1039 LDGQEAKKLNVQWLRAQLGIVSQEPILFDCSIAENIAYGDNSrvVPHDEIVRAAKEANIHPFIETLPQKYNTRVGDKGTQ 1118
Cdd:COG4987 394 LGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPD--ATDEELWAALERVGLGDWLAALPDGLDTWLGEGGRR 471
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1119 LSGGQKQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIENGKVKEHG 1198
Cdd:COG4987 472 LSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQG 551
|
490
....*....|....*...
gi 568932737 1199 THQQLLAQKGIYFSMVNI 1216
Cdd:COG4987 552 THEELLAQNGRYRQLYQR 569
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
338-575 |
5.93e-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: 5.93e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 338 LEFSDVHFSYPSRANIkILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLREIIG 417
Cdd:cd03252 1 ITFEHVRFRYKPDGPV-ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 418 VVSQEPVLFSTTIAENIRYGRGNVTMDEIEKAVKEANAYDFIMKLPQKFDTLVGDRGAQLSGGQKQRIAIARALVRNPKI 497
Cdd:cd03252 80 VVLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568932737 498 LLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTIRNADVIAGFEDGVIVEQGSHSELMKKEGIYFRLVNMQ 575
Cdd:cd03252 160 LIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQLQ 237
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
331-552 |
3.40e-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: 3.40e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 331 PDNIKGNLEFSDVHFSYPSRANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVR 410
Cdd:cd03248 5 PDHLKGIVKFQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 411 CLREIIGVVSQEPVLFSTTIAENIRYGRGNVTMDEIEKAVKEANAYDFIMKLPQKFDTLVGDRGAQLSGGQKQRIAIARA 490
Cdd:cd03248 85 YLHSKVSLVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568932737 491 LVRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTIRNADVIAGFEDGVI 552
Cdd:cd03248 165 LIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
978-1217 |
1.08e-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: 1.08e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 978 VTFNEVVFNYptRANVP-VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQWLRAQL 1056
Cdd:cd03252 1 ITFEHVRFRY--KPDGPvILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1057 GIVSQEPILFDCSIAENIAYGDNSrvVPHDEIVRAAKEANIHPFIETLPQKYNTRVGDKGTQLSGGQKQRIAIARALIRQ 1136
Cdd:cd03252 79 GVVLQENVLFNRSIRDNIALADPG--MSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1137 PRVLLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIENGKVKEHGTHQQLLAQKGIYFSMVNI 1216
Cdd:cd03252 157 PRILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQL 236
|
.
gi 568932737 1217 Q 1217
Cdd:cd03252 237 Q 237
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
655-951 |
2.83e-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: 268.19 E-value: 2.83e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 655 FVVGTVCAIANGALQPAFSIILSEMIAIF-----GPGDDAVKQQKCNMFSLVFLGLGVLSFFTFFLQGFTFGKAGEILTT 729
Cdd:cd18577 1 LIIGLLAAIAAGAALPLMTIVFGDLFDAFtdfgsGESSPDEFLDDVNKYALYFVYLGIGSFVLSYIQTACWTITGERQAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 730 RLRSMAFKAMLRQDMSWFDdhKNSTGALSTRLATDAAQVQGATGTRLALIAQNTANLGTGIIISFIYGWQLTLLLLSVVP 809
Cdd:cd18577 81 RIRKRYLKALLRQDIAWFD--KNGAGELTSRLTSDTNLIQDGIGEKLGLLIQSLSTFIAGFIIAFIYSWKLTLVLLATLP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 810 FIAVAGIVEMKMLAGNAKRDKKEMEAAGKIATEAIENIRTVVSLTQERKFESMYVEKLHGPYRNSVRKAHIYGITFSISQ 889
Cdd:cd18577 159 LIAIVGGIMGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKALEKARKAGIKKGLVSGLGLGLLF 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568932737 890 AFMYFSYAGCFRFGSYLIVNGHMRFKDVILVFSAIVLGAVALGHASSFAPDYAKAKLSAAYL 951
Cdd:cd18577 239 FIIFAMYALAFWYGSRLVRDGEISPGDVLTVFFAVLIGAFSLGQIAPNLQAFAKARAAAAKI 300
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
792-1208 |
1.88e-79 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 273.38 E-value: 1.88e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 792 ISFIYGWQLTLLLLS-VVPFIAVAGIVEMKMLAGNAKRDKKEMEAAGKiATEAIENIRTVVSLTQERKfesmYVEKLHGp 870
Cdd:PRK13657 150 LALFMNWRLSLVLVVlGIVYTLITTLVMRKTKDGQAAVEEHYHDLFAH-VSDAIGNVSVVQSYNRIEA----ETQALRD- 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 871 YRNSVRKAHI-----YGITFSISQAFMYFSYAGCFRFGSYLIVNGHMRFKDVILVFSAIVLGAVALGHASSFApdyAKAK 945
Cdd:PRK13657 224 IADNLLAAQMpvlswWALASVLNRAASTITMLAILVLGAALVQKGQLRVGEVVAFVGFATLLIGRLDQVVAFI---NQVF 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 946 LSAAYLFSLF----------ERQPLIDsysgeglwPDKFEGSVTFNEVVFNYPTRAnvPVLQGLSLEVKKGQTLALVGSS 1015
Cdd:PRK13657 301 MAAPKLEEFFevedavpdvrDPPGAID--------LGRVKGAVEFDDVSFSYDNSR--QGVEDVSFEAKPGQTVAIVGPT 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1016 GCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQWLRAQLGIVSQEPILFDCSIAENIAYGDNSrvVPHDEIVRAAKEA 1095
Cdd:PRK13657 371 GAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRPD--ATDEEMRAAAERA 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1096 NIHPFIETLPQKYNTRVGDKGTQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEALDKAREGRTCIVIAH 1175
Cdd:PRK13657 449 QAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAH 528
|
410 420 430
....*....|....*....|....*....|...
gi 568932737 1176 RLSTIQNADLIVVIENGKVKEHGTHQQLLAQKG 1208
Cdd:PRK13657 529 RLSTVRNADRILVFDNGRVVESGSFDELVARGG 561
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
978-1193 |
8.10e-79 |
|
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: 8.10e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 978 VTFNEVVFNYPTRANvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQWLRAQLG 1057
Cdd:cd03228 1 IEFKNVSFSYPGRPK-PVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1058 IVSQEPILFDCSIAENIaygdnsrvvphdeivraakeanihpfietlpqkyntrvgdkgtqLSGGQKQRIAIARALIRQP 1137
Cdd:cd03228 80 YVPQDPFLFSGTIRENI--------------------------------------------LSGGQRQRIAIARALLRDP 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 568932737 1138 RVLLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIENGK 1193
Cdd:cd03228 116 PILILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
653-1210 |
1.28e-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: 1.28e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 653 PYFVVGTVCAIANGALQPAFSIILSEMIAIfgpgddavkQQKCNMFSLVFLGLGVLSFFTFFLQGFTfgkagEILTTRLR 732
Cdd:TIGR03796 157 LYLLLAGLLLVLPGLVIPAFSQIFVDEILV---------QGRQDWLRPLLLGMGLTALLQGVLTWLQ-----LYYLRRLE 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 733 ---SMAFKA-----MLRQDMSWFDdhKNSTGALSTRLATdAAQVQGATGTRLALIAQNTANLGTGIIISFIYGWQLTLLL 804
Cdd:TIGR03796 223 iklAVGMSArflwhILRLPVRFFA--QRHAGDIASRVQL-NDQVAEFLSGQLATTALDAVMLVFYALLMLLYDPVLTLIG 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 805 lsvvpfIAVAGIVEMKMLAGNAKR---DKKEMEAAGKIATEAIENIRTVVSLtQERKFESMYVEKLHGPYRNSVRKAHIY 881
Cdd:TIGR03796 300 ------IAFAAINVLALQLVSRRRvdaNRRLQQDAGKLTGVAISGLQSIETL-KASGLESDFFSRWAGYQAKLLNAQQEL 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 882 GITFSI----SQAFMYFSYAGCFRFGSYLIVNGHMR------FKDVILVFSAIVLGAVALGHA-SSFAPDYAKAKLSAAY 950
Cdd:TIGR03796 373 GVLTQIlgvlPTLLTSLNSALILVVGGLRVMEGQLTigmlvaFQSLMSSFLEPVNNLVGFGGTlQELEGDLNRLDDVLRN 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 951 -LFSLFERQPLIDSYSGEglwPDKFEGSVTFNEVVFNYpTRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERF 1029
Cdd:TIGR03796 453 pVDPLLEEPEGSAATSEP---PRRLSGYVELRNITFGY-SPLEPPLIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGL 528
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1030 YDPMAGSVLLDGQEAKKLNVQWLRAQLGIVSQEPILFDCSIAENIAYGDNSrvVPHDEIVRAAKEANIHPFIETLPQKYN 1109
Cdd:TIGR03796 529 YQPWSGEILFDGIPREEIPREVLANSVAMVDQDIFLFEGTVRDNLTLWDPT--IPDADLVRACKDAAIHDVITSRPGGYD 606
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1110 TRVGDKGTQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEALdkAREGRTCIVIAHRLSTIQNADLIVVI 1189
Cdd:TIGR03796 607 AELAEGGANLSGGQRQRLEIARALVRNPSILILDEATSALDPETEKIIDDNL--RRRGCTCIIVAHRLSTIRDCDEIIVL 684
|
570 580
....*....|....*....|.
gi 568932737 1190 ENGKVKEHGTHQQLLAQKGIY 1210
Cdd:TIGR03796 685 ERGKVVQRGTHEELWAVGGAY 705
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
1-289 |
1.18e-76 |
|
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: 254.49 E-value: 1.18e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1 MFLGTLMAIAHGSGLPLMMIVFGEMTDKFVDNtgnfslpvnfslsmlnpGRILEEEMTRYAYYYSGLGGGVLVAAYIQVS 80
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLPD-----------------GDPETQALNVYSLALLLLGLAQFILSFLQSY 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 81 FWTLAAGRQIKKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDDVSKISEGIGDKVGMFFQAIATFFAGFIVGFIRGWKL 160
Cdd:pfam00664 64 LLNHTGERLSRRLRRKLFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 161 TLVIMAISPILGLSTAVWAKILSTFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKELERYQKHLENAKKIGIKKAIS 240
Cdd:pfam00664 144 TLVLLAVLPLYILVSAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVA 223
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 568932737 241 ANISMGIAFLLIYASYALAFWYGSTLVISKEYTIGN--AMTVFFSILIGAF 289
Cdd:pfam00664 224 NGLSFGITQFIGYLSYALALWFGAYLVISGELSVGDlvAFLSLFAQLFGPL 274
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
794-1219 |
1.63e-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: 267.76 E-value: 1.63e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 794 FIYGWQLTLLLLSVVPF-----IAVAGIVEMKMlagnakRDKKEMEAAGK-IATEAIENIRTVVSLTQERKFESMYVEKL 867
Cdd:TIGR01846 274 FFYSPTLTGVVIGSLVCyallsVFVGPILRKRV------EDKFERSAAATsFLVESVTGIETIKATATEPQFQNRWDRQL 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 868 HGPYRNSVRKAHIYGITFSISQAFMYFSYAGCFRFGSYLIVNGHMRFKDVIL--VFSAIVLGAVAlgHASSFAPDYAKAK 945
Cdd:TIGR01846 348 AAYVAASFRVTNLGNIAGQAIELIQKLTFAILLWFGAHLVIGGALSPGQLVAfnMLAGRVTQPVL--RLAQLWQDFQQTG 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 946 LSAAYLFSLFErQPLIDSYSGEGLWPdKFEGSVTFNEVVFNYPTRAnVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQL 1025
Cdd:TIGR01846 426 IALERLGDILN-SPTEPRSAGLAALP-ELRGAITFENIRFRYAPDS-PEVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKL 502
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1026 LERFYDPMAGSVLLDGQEAKKLNVQWLRAQLGIVSQEPILFDCSIAENIAYGDNSrvVPHDEIVRAAKEANIHPFIETLP 1105
Cdd:TIGR01846 503 LQRLYTPQHGQVLVDGVDLAIADPAWLRRQMGVVLQENVLFSRSIRDNIALCNPG--APFEHVIHAAKLAGAHDFISELP 580
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1106 QKYNTRVGDKGTQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADL 1185
Cdd:TIGR01846 581 QGYNTEVGEKGANLSGGQRQRIAIARALVGNPRILIFDEATSALDYESEALIMRNMREICRGRTVIIIAHRLSTVRACDR 660
|
410 420 430
....*....|....*....|....*....|....
gi 568932737 1186 IVVIENGKVKEHGTHQQLLAQKGIYFSMVNIQAG 1219
Cdd:TIGR01846 661 IIVLEKGQIAESGRHEELLALQGLYARLWQQQSG 694
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
1-321 |
1.66e-75 |
|
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: 252.76 E-value: 1.66e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1 MFLGTLMAIAHGSGLPLMMIVFGEMTDkfvdntgNFSLPvnfslsmlnPGRILEEEMTRYAYYYSGLGGGVLVAAYIQVS 80
Cdd:cd18578 11 LLLGLIGAIIAGAVFPVFAILFSKLIS-------VFSLP---------DDDELRSEANFWALMFLVLAIVAGIAYFLQGY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 81 FWTLAAGRQIKKIRQKFFHAILRQEMGWFDIKG--TTELNTRLTDDVSKISEGIGDKVGMFFQAIATFFAGFIVGFIRGW 158
Cdd:cd18578 75 LFGIAGERLTRRLRKLAFRAILRQDIAWFDDPEnsTGALTSRLSTDASDVRGLVGDRLGLILQAIVTLVAGLIIAFVYGW 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 159 KLTLVIMAISPILGLSTAVWAKILSTFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKELERYQKHLENAKKIGIKKA 238
Cdd:cd18578 155 KLALVGLATVPLLLLAGYLRMRLLSGFEEKNKKAYEESSKIASEAVSNIRTVASLTLEDYFLEKYEEALEEPLKKGLRRA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 239 ISANISMGIAFLLIYASYALAFWYGSTLVISKEYTIGNAMTVFFSILIGAFSVGQAAPCIDAFANARGAAYVIFDIIDNN 318
Cdd:cd18578 235 LISGLGFGLSQSLTFFAYALAFWYGGRLVANGEYTFEQFFIVFMALIFGAQSAGQAFSFAPDIAKAKAAAARIFRLLDRK 314
|
...
gi 568932737 319 PKI 321
Cdd:cd18578 315 PEI 317
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
657-1222 |
6.50e-74 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 270.36 E-value: 6.50e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 657 VGTVCAIANGALQPAFSIILSEMIAIFGPGDDAVKQqkcnMFSLVFLGLG--VLSFFTFFLQGFTFGKageILTTrLRSM 734
Cdd:PTZ00265 64 VSFVCATISGGTLPFFVSVFGVIMKNMNLGENVNDI----IFSLVLIGIFqfILSFISSFCMDVVTTK---ILKT-LKLE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 735 AFKAMLRQDMSWFDDHKNSTgaLSTRLATDAAQVQGATGTRLALIAQNTANLGTGIIISFIYGWQLTLLLLSVVPFIAVA 814
Cdd:PTZ00265 136 FLKSVFYQDGQFHDNNPGSK--LTSDLDFYLEQVNAGIGTKFITIFTYASAFLGLYIWSLFKNARLTLCITCVFPLIYIC 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 815 GIVEMKMLAGNAKRDKKEMEAAGKIATEAIENIRTVVSLTQERKFESMY--VEKLHGPY---RNSVRKAHIYGItfsisQ 889
Cdd:PTZ00265 214 GVICNKKVKINKKTSLLYNNNTMSIIEEALVGIRTVVSYCGEKTILKKFnlSEKLYSKYilkANFMESLHIGMI-----N 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 890 AFMYFSYAGCFRFGSYLIV--------NGHMRFKDVILVFSAIVLGAVALGHASSFAPDYAKAKLSAAYLFSLFERQPLI 961
Cdd:PTZ00265 289 GFILASYAFGFWYGTRIIIsdlsnqqpNNDFHGGSVISILLGVLISMFMLTIILPNITEYMKSLEATNSLYEIINRKPLV 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 962 DSYS-GEGLWPDKfegSVTFNEVVFNYPTRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLL- 1039
Cdd:PTZ00265 369 ENNDdGKKLKDIK---KIQFKNVRFHYDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIn 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1040 DGQEAKKLNVQWLRAQLGIVSQEPILFDCSIAENIAY------------------------GDNSR-------------- 1081
Cdd:PTZ00265 446 DSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKYslyslkdlealsnyynedgndsqeNKNKRnscrakcagdlndm 525
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1082 -----------------VVPHDEIVRAAKEANIHPFIETLPQKYNTRVGDKGTQLSGGQKQRIAIARALIRQPRVLLLDE 1144
Cdd:PTZ00265 526 snttdsneliemrknyqTIKDSEVVDVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDE 605
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1145 ATSALDTESEKVVQEALD--KAREGRTCIVIAHRLSTIQNADLIVVIENGK----------------------------- 1193
Cdd:PTZ00265 606 ATSSLDNKSEYLVQKTINnlKGNENRITIIIAHRLSTIRYANTIFVLSNRErgstvdvdiigedptkdnkennnknnkdd 685
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 568932737 1194 ------------------VKEHGTHQQLLAQK-GIYFSMVNIQAGTQN 1222
Cdd:PTZ00265 686 nnnnnnnnnnkinnagsyIIEQGTHDALMKNKnGIYYTMINNQKVSSK 733
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
239-572 |
1.32e-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: 256.74 E-value: 1.32e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 239 ISANISMgIAFLLIyasyalafwyGSTLVISKEYTIGNAMTV--FFSILIGAFSvgQAAPCIDAFANARGAAYVIFDIID 316
Cdd:TIGR01192 248 MASTISM-MCILVI----------GTVLVIKGELSVGEVIAFigFANLLIGRLD--QMSGFITQIFEARAKLEDFFDLED 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 317 NNPKIDSFSERGHKPdNIKGNLEFSDVHFSYPSRAniKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGK 396
Cdd:TIGR01192 315 SVFQREEPADAPELP-NVKGAVEFRHITFEFANSS--QGVFDVSFEAKAGQTVAIVGPTGAGKTTLINLLQRVYDPTVGQ 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 397 ISIDGQDIRNFNVRCLREIIGVVSQEPVLFSTTIAENIRYGRGNVTMDEIEKAVKEANAYDFIMKLPQKFDTLVGDRGAQ 476
Cdd:TIGR01192 392 ILIDGIDINTVTRESLRKSIATVFQDAGLFNRSIRENIRLGREGATDEEVYEAAKAAAAHDFILKRSNGYDTLVGERGNR 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 477 LSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTIRNADVIAGFEDGVIVEQG 556
Cdd:TIGR01192 472 LSGGERQRLAIARAILKNAPILVLDEATSALDVETEARVKNAIDALRKNRTTFIIAHRLSTVRNADLVLFLDQGRLIEKG 551
|
330
....*....|....*.
gi 568932737 557 SHSELMKKEGIYFRLV 572
Cdd:TIGR01192 552 SFQELIQKDGRFYKLL 567
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
65-572 |
3.08e-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: 250.25 E-value: 3.08e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 65 SGLGGGVLVAAYIQVSfwTLAAGRqikkirqkFFHAILRQEMGWF------DIKGTTELNTRLTDDVS-KISEGIGDKVG 137
Cdd:TIGR03796 211 TWLQLYYLRRLEIKLA--VGMSAR--------FLWHILRLPVRFFaqrhagDIASRVQLNDQVAEFLSgQLATTALDAVM 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 138 MFFQAIATFfagfivgfIRGWKLTLVIMAISPILGLSTAVWAKILSTFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQN 217
Cdd:TIGR03796 281 LVFYALLML--------LYDPVLTLIGIAFAAINVLALQLVSRRRVDANRRLQQDAGKLTGVAISGLQSIETLKASGLES 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 218 KELER---YQKHLENA-KKIGIKKAISANISMGIAFLliyaSYALAFWYGSTLVISKEYTIGnaMTVFFSILIGAFS--- 290
Cdd:TIGR03796 353 DFFSRwagYQAKLLNAqQELGVLTQILGVLPTLLTSL----NSALILVVGGLRVMEGQLTIG--MLVAFQSLMSSFLepv 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 291 ---VGQAAPCIDAFAN-ARgaayviFDIIDNNPKIDSFSERGHKPDN------IKGNLEFSDVHFSYpSRANIKILKGLN 360
Cdd:TIGR03796 427 nnlVGFGGTLQELEGDlNR------LDDVLRNPVDPLLEEPEGSAATsepprrLSGYVELRNITFGY-SPLEPPLIENFS 499
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 361 LKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLREIIGVVSQEPVLFSTTIAENIRYGRGN 440
Cdd:TIGR03796 500 LTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIPREVLANSVAMVDQDIFLFEGTVRDNLTLWDPT 579
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 441 VTMDEIEKAVKEANAYDFIMKLPQKFDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALd 520
Cdd:TIGR03796 580 IPDADLVRACKDAAIHDVITSRPGGYDAELAEGGANLSGGQRQRLEIARALVRNPSILILDEATSALDPETEKIIDDNL- 658
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 568932737 521 kAREGRTTIVIAHRLSTIRNADVIAGFEDGVIVEQGSHSELMKKEGIYFRLV 572
Cdd:TIGR03796 659 -RRRGCTCIIVAHRLSTIRDCDEIIVLERGKVVQRGTHEELWAVGGAYARLI 709
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
655-929 |
2.67e-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: 233.69 E-value: 2.67e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 655 FVVGTVCAIANGALQPAFSIILSEMIAIFGPGDDAVKQqKCNMFSLVFLGLGVLSFFTFFLQGFTFGKAGEILTTRLRSM 734
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLPDGDPETQ-ALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 735 AFKAMLRQDMSWFDdhKNSTGALSTRLATDAAQVQGATGTRLALIAQNTANLGTGIIISFIYGWQLTLLLLSVVPFIAVA 814
Cdd:pfam00664 80 LFKKILRQPMSFFD--TNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 815 GIVEMKMLAGNAKRDKKEMEAAGKIATEAIENIRTVVSLTQERKFESMYVEKLHGPYRNSVRKAHIYGITFSISQAFMYF 894
Cdd:pfam00664 158 SAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYL 237
|
250 260 270
....*....|....*....|....*....|....*..
gi 568932737 895 SYAGCFRFGSYLIVNGHMRFKDVI--LVFSAIVLGAV 929
Cdd:pfam00664 238 SYALALWFGAYLVISGELSVGDLVafLSLFAQLFGPL 274
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
794-1217 |
5.13e-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: 5.13e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 794 FIYGWQLTL----LLLSVVPFIAVAGIVEMKMLagnakrdKKEMEAAGKIATEAIENIRTVVSL----TQERKFesMYVE 865
Cdd:TIGR03797 271 FYYSWKLALvavaLALVAIAVTLVLGLLQVRKE-------RRLLELSGKISGLTVQLINGISKLrvagAENRAF--ARWA 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 866 KLHGPYRNSVRKAH-IYGITFSISQAFMYFSYAGCFRFGSYLIVNGHMRFKDvILVFSAivlgavALGHASSFAPDYAKA 944
Cdd:TIGR03797 342 KLFSRQRKLELSAQrIENLLTVFNAVLPVLTSAALFAAAISLLGGAGLSLGS-FLAFNT------AFGSFSGAVTQLSNT 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 945 KLSAAYLFSLFER-QPLIDS---YSGEGLWPDKFEGSVTFNEVVFNYptRANVP-VLQGLSLEVKKGQTLALVGSSGCGK 1019
Cdd:TIGR03797 415 LISILAVIPLWERaKPILEAlpeVDEAKTDPGKLSGAIEVDRVTFRY--RPDGPlILDDVSLQIEPGEFVAIVGPSGSGK 492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1020 STVVQLLERFYDPMAGSVLLDGQEAKKLNVQWLRAQLGIVSQEPILFDCSIAENIAYGDnsrVVPHDEIVRAAKEANIHP 1099
Cdd:TIGR03797 493 STLLRLLLGFETPESGSVFYDGQDLAGLDVQAVRRQLGVVLQNGRLMSGSIFENIAGGA---PLTLDEAWEAARMAGLAE 569
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1100 FIETLPQKYNTRVGDKGTQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEALDKAREGRtcIVIAHRLST 1179
Cdd:TIGR03797 570 DIRAMPMGMHTVISEGGGTLSGGQRQRLLIARALVRKPRILLFDEATSALDNRTQAIVSESLERLKVTR--IVIAHRLST 647
|
410 420 430
....*....|....*....|....*....|....*...
gi 568932737 1180 IQNADLIVVIENGKVKEHGTHQQLLAQKGIYFSMVNIQ 1217
Cdd:TIGR03797 648 IRNADRIYVLDAGRVVQQGTYDELMAREGLFAQLARRQ 685
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
336-556 |
1.46e-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: 1.46e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 336 GNLEFSDVHFSYPSrANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLREI 415
Cdd:cd03245 1 GRIEFRNVSFSYPN-QEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 416 IGVVSQEPVLFSTTIAENIRYGRGNVTMDEIEKAVKEANAYDFIMKLPQKFDTLVGDRGAQLSGGQKQRIAIARALVRNP 495
Cdd:cd03245 80 IGYVPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568932737 496 KILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTIRNADVIAGFEDGVIVEQG 556
Cdd:cd03245 160 PILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
300-544 |
1.20e-66 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 234.87 E-value: 1.20e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 300 AFANARGAAYVIFDIIDNNPKIdsFSERGHKPDNIKGNLEFSDVHFSYPSRANIkiLKGLNLKVKSGQTVALVGNSGCGK 379
Cdd:TIGR02857 286 ARADGVAAAEALFAVLDAAPRP--LAGKAPVTAAPASSLEFSGVSVAYPGRRPA--LRPVSFTVPPGERVALVGPSGAGK 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 380 STTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLREIIGVVSQEPVLFSTTIAENIRYGRGNVTMDEIEKAVKEANAYDFI 459
Cdd:TIGR02857 362 STLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLARPDASDAEIREALERAGLDEFV 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 460 MKLPQKFDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTIR 539
Cdd:TIGR02857 442 AALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAA 521
|
....*
gi 568932737 540 NADVI 544
Cdd:TIGR02857 522 LADRI 526
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
336-557 |
5.08e-66 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 222.37 E-value: 5.08e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 336 GNLEFSDVHFSYpsRANIK-ILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLRE 414
Cdd:cd03244 1 GDIEFKNVSLRY--RPNLPpVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 415 IIGVVSQEPVLFSTTIAENI----RYgrgnvTMDEIEKAVKEANAYDFIMKLPQKFDTLVGDRGAQLSGGQKQRIAIARA 490
Cdd:cd03244 79 RISIIPQDPVLFSGTIRSNLdpfgEY-----SDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568932737 491 LVRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTIRNADVIAGFEDGVIVEQGS 557
Cdd:cd03244 154 LLRKSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
102-575 |
6.46e-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: 6.46e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 102 LRQEMGWFDIKGTTELNTRlTDDVSKISEGIGDKvgMFFQAIATFFAGFIVG--FIRGWKLTLVIMAISPILGLSTAVWA 179
Cdd:TIGR03797 220 LRLPVSFFRQYSTGDLASR-AMGISQIRRILSGS--TLTTLLSGIFALLNLGlmFYYSWKLALVAVALALVAIAVTLVLG 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 180 KILSTFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKELERYQKHLENAKKIGIKKAISANI-SMGIAFLLIYASYAL 258
Cdd:TIGR03797 297 LLQVRKERRLLELSGKISGLTVQLINGISKLRVAGAENRAFARWAKLFSRQRKLELSAQRIENLlTVFNAVLPVLTSAAL 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 259 aFWYGSTLVISKEYTIGNAMTvfFSILIGAFSVGqaapcIDAFANARGAAYVIF-------DIIDNNPKIDsfsERGHKP 331
Cdd:TIGR03797 377 -FAAAISLLGGAGLSLGSFLA--FNTAFGSFSGA-----VTQLSNTLISILAVIplwerakPILEALPEVD---EAKTDP 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 332 DNIKGNLEFSDVHFSYPSRANIkILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRC 411
Cdd:TIGR03797 446 GKLSGAIEVDRVTFRYRPDGPL-ILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLDVQA 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 412 LREIIGVVSQEPVLFSTTIAENIrYGRGNVTMDEIEKAVKEANAYDFIMKLPQKFDTLVGDRGAQLSGGQKQRIAIARAL 491
Cdd:TIGR03797 525 VRRQLGVVLQNGRLMSGSIFENI-AGGAPLTLDEAWEAARMAGLAEDIRAMPMGMHTVISEGGGTLSGGQRQRLLIARAL 603
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 492 VRNPKILLLDEATSALDTESEAEVQAALDKAREGRttIVIAHRLSTIRNADVIAGFEDGVIVEQGSHSELMKKEGIYFRL 571
Cdd:TIGR03797 604 VRKPRILLFDEATSALDNRTQAIVSESLERLKVTR--IVIAHRLSTIRNADRIYVLDAGRVVQQGTYDELMAREGLFAQL 681
|
....
gi 568932737 572 VNMQ 575
Cdd:TIGR03797 682 ARRQ 685
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
976-1194 |
3.23e-65 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 220.15 E-value: 3.23e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 976 GSVTFNEVVFNYPTRANvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQWLRAQ 1055
Cdd:cd03245 1 GRIEFRNVSFSYPNQEI-PALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1056 LGIVSQEPILFDCSIAENIAYGDnsRVVPHDEIVRAAKEANIHPFIETLPQKYNTRVGDKGTQLSGGQKQRIAIARALIR 1135
Cdd:cd03245 80 IGYVPQDVTLFYGTLRDNITLGA--PLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLN 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 568932737 1136 QPRVLLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIENGKV 1194
Cdd:cd03245 158 DPPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
73-603 |
2.63e-64 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 229.21 E-value: 2.63e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 73 VAAYIQVSFWTL----AAGRQIKKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDDVSKISEGIGDKVGMFFQAIATFFA 148
Cdd:PRK10789 47 VVVYLLRYVWRVllfgASYQLAVELREDFYRQLSRQHPEFYLRHRTGDLMARATNDVDRVVFAAGEGVLTLVDSLVMGCA 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 149 GFIVGFIR-GWKLTLVIMAISPILGLSTAVWAKIL-----------STFSDKelaayakagavAEEALGAIRTVIAFGgq 216
Cdd:PRK10789 127 VLIVMSTQiSWQLTLLALLPMPVMAIMIKRYGDQLherfklaqaafSSLNDR-----------TQESLTSIRMIKAFG-- 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 217 nkeLERYQKHL--ENAKKIGIKKA----ISANISMGIaFLLIYASYALAFWYGSTLVISKEYTIGnAMTVFFSILigafs 290
Cdd:PRK10789 194 ---LEDRQSALfaADAEDTGKKNMrvarIDARFDPTI-YIAIGMANLLAIGGGSWMVVNGSLTLG-QLTSFVMYL----- 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 291 vGQAAPCIDAFA---N--ARG-AAYV-IFDIIDNNPKIDSfserGHKP-DNIKGNLEFSDVHFSYPsRANIKILKGLNLK 362
Cdd:PRK10789 264 -GLMIWPMLALAwmfNivERGsAAYSrIRAMLAEAPVVKD----GSEPvPEGRGELDVNIRQFTYP-QTDHPALENVNFT 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 363 VKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLREIIGVVSQEPVLFSTTIAENIRYGRGNVT 442
Cdd:PRK10789 338 LKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNIALGRPDAT 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 443 MDEIEKAVKEANAYDFIMKLPQKFDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKA 522
Cdd:PRK10789 418 QQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQW 497
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 523 REGRTTIVIAHRLSTIRNADVIAGFEDGVIVEQGSHSELMKKEGIYFRLVNMQtagsqilseEFEVELSDEKAAGDVAPN 602
Cdd:PRK10789 498 GEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSGWYRDMYRYQ---------QLEAALDDAPEIREEAVD 568
|
.
gi 568932737 603 G 603
Cdd:PRK10789 569 A 569
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
975-1206 |
1.83e-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: 1.83e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 975 EGSVTFNEVVFNYPtRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKklnvQWLRA 1054
Cdd:COG4618 328 KGRLSVENLTVVPP-GSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLS----QWDRE 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1055 QLG--I--VSQEPILFDCSIAENIA-YGDnsrvVPHDEIVRAAKEANIHPFIETLPQKYNTRVGDKGTQLSGGQKQRIAI 1129
Cdd:COG4618 403 ELGrhIgyLPQDVELFDGTIAENIArFGD----ADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGL 478
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568932737 1130 ARALIRQPRVLLLDEATSALDTESEKVVQEALDKARE-GRTCIVIAHRLSTIQNADLIVVIENGKVKEHGTHQQLLAQ 1206
Cdd:COG4618 479 ARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKArGATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
940-1189 |
2.08e-63 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 225.63 E-value: 2.08e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 940 DYAKAKLSAAYLFSLFERQPLIDSYSGEGLWPDkfEGSVTFNEVVFNYPTRAnvPVLQGLSLEVKKGQTLALVGSSGCGK 1019
Cdd:TIGR02857 286 ARADGVAAAEALFAVLDAAPRPLAGKAPVTAAP--ASSLEFSGVSVAYPGRR--PALRPVSFTVPPGERVALVGPSGAGK 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1020 STVVQLLERFYDPMAGSVLLDGQEAKKLNVQWLRAQLGIVSQEPILFDCSIAENIAYGDnsRVVPHDEIVRAAKEANIHP 1099
Cdd:TIGR02857 362 STLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLAR--PDASDAEIREALERAGLDE 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1100 FIETLPQKYNTRVGDKGTQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLST 1179
Cdd:TIGR02857 440 FVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLAL 519
|
250
....*....|
gi 568932737 1180 IQNADLIVVI 1189
Cdd:TIGR02857 520 AALADRIVVL 529
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
727-1217 |
1.10e-62 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 224.59 E-value: 1.10e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 727 LTTRLRSMAFKAMLRQDMSWFDDHKnsTGALSTRLATDAAQVQGATGTR-LALIAQNTANLGTGIIISFIYGWQLTLLLL 805
Cdd:PRK10789 67 LAVELREDFYRQLSRQHPEFYLRHR--TGDLMARATNDVDRVVFAAGEGvLTLVDSLVMGCAVLIVMSTQISWQLTLLAL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 806 SVVPFIAVAgivemkmlagnAKRDKKEMEAAGKIATEAIE--NIRTVVSLTQERKFESMYVEKLHGPY---------RNS 874
Cdd:PRK10789 145 LPMPVMAIM-----------IKRYGDQLHERFKLAQAAFSslNDRTQESLTSIRMIKAFGLEDRQSALfaadaedtgKKN 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 875 VRKAHI---YGITFSISQAFMYFSYAGCfrfGSYLIVNGHMrfkdvilvfsaivlgavALGHASSFA--------PDYAK 943
Cdd:PRK10789 214 MRVARIdarFDPTIYIAIGMANLLAIGG---GSWMVVNGSL-----------------TLGQLTSFVmylglmiwPMLAL 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 944 AKL-------SAAY--LFSLFERQPLIDSysGEGLWPDKfEGSVTFNEVVFNYPTrANVPVLQGLSLEVKKGQTLALVGS 1014
Cdd:PRK10789 274 AWMfnivergSAAYsrIRAMLAEAPVVKD--GSEPVPEG-RGELDVNIRQFTYPQ-TDHPALENVNFTLKPGQMLGICGP 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1015 SGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQWLRAQLGIVSQEPILFDCSIAENIAYG--DNSRvvphDEIVRAA 1092
Cdd:PRK10789 350 TGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNIALGrpDATQ----QEIEHVA 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1093 KEANIHPFIETLPQKYNTRVGDKGTQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEALDKAREGRTCIV 1172
Cdd:PRK10789 426 RLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVII 505
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 568932737 1173 IAHRLSTIQNADLIVVIENGKVKEHGTHQQLLAQKGIYFSMVNIQ 1217
Cdd:PRK10789 506 SAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSGWYRDMYRYQ 550
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
73-573 |
2.40e-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: 226.93 E-value: 2.40e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 73 VAAYIQVSFWTLAAGRQIKKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDdVSKISEGIGDKV-GMFFQAIATFFAGFI 151
Cdd:TIGR01193 211 ILSYIQIFLLNVLGQRLSIDIILSYIKHLFELPMSFFSTRRTGEIVSRFTD-ASSIIDALASTIlSLFLDMWILVIVGLF 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 152 VGFiRGWKLTLVIMAISPILGLSTAVWAKILSTFSDKELAAYAKAGAVAEEALGAIRTVIAFGGqnkELERYQK------ 225
Cdd:TIGR01193 290 LVR-QNMLLFLLSLLSIPVYAVIIILFKRTFNKLNHDAMQANAVLNSSIIEDLNGIETIKSLTS---EAERYSKidsefg 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 226 -HLENAKKIGIKKAISANISMGIAFLLIyasyALAFWYGSTLVISKEYTIGNAMTvfFSILIGAFsvgqaapcIDAFANa 304
Cdd:TIGR01193 366 dYLNKSFKYQKADQGQQAIKAVTKLILN----VVILWTGAYLVMRGKLTLGQLIT--FNALLSYF--------LTPLEN- 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 305 rgaayvifdIIDNNPK----------------IDSFSERGHKPD---NIKGNLEFSDVHFSYPSRANIkiLKGLNLKVKS 365
Cdd:TIGR01193 431 ---------IINLQPKlqaarvannrlnevylVDSEFINKKKRTelnNLNGDIVINDVSYSYGYGSNI--LSDISLTIKM 499
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 366 GQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLREIIGVVSQEPVLFSTTIAENIRYG-RGNVTMD 444
Cdd:TIGR01193 500 NSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLGaKENVSQD 579
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 445 EIEKAVKEANAYDFIMKLPQKFDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKARE 524
Cdd:TIGR01193 580 EIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQD 659
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 568932737 525 gRTTIVIAHRLSTIRNADVIAGFEDGVIVEQGSHSELMKKEGIYFRLVN 573
Cdd:TIGR01193 660 -KTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYASLIH 707
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
277-571 |
6.60e-62 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 222.39 E-value: 6.60e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 277 AMTVF-----FSILI---GAFS-VGQaapCIdafanarGAAYVIFDIIDNNPKIdSFSERgHKPDNIKGNLEFSDVHFSY 347
Cdd:PRK11160 281 ALFVFaalaaFEALMpvaGAFQhLGQ---VI-------ASARRINEITEQKPEV-TFPTT-STAAADQVSLTLNNVSFTY 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 348 PSRANiKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLREIIGVVSQEPVLFS 427
Cdd:PRK11160 349 PDQPQ-PVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFS 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 428 TTIAENIRYGRGNVTmDEIEKAVKEANAYDFIMKLPQKFDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEATSAL 507
Cdd:PRK11160 428 ATLRDNLLLAAPNAS-DEALIEVLQQVGLEKLLEDDKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGL 506
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568932737 508 DTESEAEVQAALDKAREGRTTIVIAHRLSTIRNADVIAGFEDGVIVEQGSHSELMKKEGIYFRL 571
Cdd:PRK11160 507 DAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQGRYYQL 570
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
344-1222 |
2.55e-61 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 230.63 E-value: 2.55e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 344 HFSYPSRANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKiSIDgqdirnfnvrcLREIIGVVSQEP 423
Cdd:PLN03232 621 YFSWDSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETS-SVV-----------IRGSVAYVPQVS 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 424 VLFSTTIAENIRYGrGNVTMDEIEKAVK-EANAYDFIMkLPQKFDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDE 502
Cdd:PLN03232 689 WIFNATVRENILFG-SDFESERYWRAIDvTALQHDLDL-LPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDD 766
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 503 ATSALDTESEAEV-QAALDKAREGRTTIVIAHRLSTIRNADVIAGFEDGVIVEQGSHSELMKKEGIYFRLvnMQTAGSqi 581
Cdd:PLN03232 767 PLSALDAHVAHQVfDSCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELSKSGSLFKKL--MENAGK-- 842
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 582 LSEEFEVELSDEKAA--GDVAPNGWKARIFRNSTK-KSLKSPHQNRLDEETNELDANVppvsflkVLKLNKTEWPYFVVG 658
Cdd:PLN03232 843 MDATQEVNTNDENILklGPTVTIDVSERNLGSTKQgKRGRSVLVKQEERETGIISWNV-------LMRYNKAVGGLWVVM 915
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 659 T--VCAIANGALQPAFSIILSemiaiFGPGDDAVKQQKCNMFSLVFLGLGVLSFFTFFLQGFTFGKAGEILTTRLRSMAF 736
Cdd:PLN03232 916 IllVCYLTTEVLRVSSSTWLS-----IWTDQSTPKSYSPGFYIVVYALLGFGQVAVTFTNSFWLISSSLHAAKRLHDAML 990
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 737 KAMLRQDMSWFddHKNSTGALSTRLATDAAQvqgatgtrlalIAQNTANLGTGIIISFiygWQL--TLLLLSVVPFIAVA 814
Cdd:PLN03232 991 NSILRAPMLFF--HTNPTGRVINRFSKDIGD-----------IDRNVANLMNMFMNQL---WQLlsTFALIGTVSTISLW 1054
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 815 GIVEMKML-------AGNAKRDKKEMEAAGKIATEAI--ENIRTVVSLTQERKFESMyvEKLHGPYRN------------ 873
Cdd:PLN03232 1055 AIMPLLILfyaaylyYQSTSREVRRLDSVTRSPIYAQfgEALNGLSSIRAYKAYDRM--AKINGKSMDnnirftlantss 1132
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 874 ----SVRKAHIYGITFSISQAFMYFSYAGcfrfgsyliVNGHMRFKDVI-LVFSAIV----LGAVALGHASSFAPDYAKA 944
Cdd:PLN03232 1133 nrwlTIRLETLGGVMIWLTATFAVLRNGN---------AENQAGFASTMgLLLSYTLnittLLSGVLRQASKAENSLNSV 1203
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 945 KLSAAYLFSLFERQPLIDSYSGEGLWPDKfeGSVTFNEVVFNYptRANVP-VLQGLSLEVKKGQTLALVGSSGCGKSTVV 1023
Cdd:PLN03232 1204 ERVGNYIDLPSEATAIIENNRPVSGWPSR--GSIKFEDVHLRY--RPGLPpVLHGLSFFVSPSEKVGVVGRTGAGKSSML 1279
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1024 QLLERFYDPMAGSVLLDGQEAKKLNVQWLRAQLGIVSQEPILFDCSIAENIAygdnsrvvPHDE-----IVRAAKEANIH 1098
Cdd:PLN03232 1280 NALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNID--------PFSEhndadLWEALERAHIK 1351
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1099 PFIETLPQKYNTRVGDKGTQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLS 1178
Cdd:PLN03232 1352 DVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLN 1431
|
890 900 910 920
....*....|....*....|....*....|....*....|....
gi 568932737 1179 TIQNADLIVVIENGKVKEHGTHQQLLAQKGIYFSMVNIQAGTQN 1222
Cdd:PLN03232 1432 TIIDCDKILVLSSGQVLEYDSPQELLSRDTSAFFRMVHSTGPAN 1475
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
356-1213 |
2.66e-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: 2.66e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 356 LKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQdirnfnvrclreiIGVVSQEPVLFSTTIAENIR 435
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS-------------VAYVPQQAWIQNDSLRENIL 720
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 436 YGRGnvTMDEIEKAVKEANAY--DFIMkLPQKFDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEA 513
Cdd:TIGR00957 721 FGKA--LNEKYYQQVLEACALlpDLEI-LPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGK 797
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 514 EVqaaLDKA------REGRTTIVIAHRLSTIRNADVIAGFEDGVIVEQGSHSELMKKEGIYFR-LVNMQTAGSQILSEEF 586
Cdd:TIGR00957 798 HI---FEHVigpegvLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAFAEfLRTYAPDEQQGHLEDS 874
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 587 EVEL-SDEKAAGDVAPNGW------KARIFRNSTKKSLKSPHQNRLDEETNELDANVPPVSFLKVLKLNKTE-------- 651
Cdd:TIGR00957 875 WTALvSGEGKEAKLIENGMlvtdvvGKQLQRQLSASSSDSGDQSRHHGSSAELQKAEAKEETWKLMEADKAQtgqvelsv 954
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 652 -WPY---------------FVVGTVCAIANGALQPAFSiilsemiaifgpgDDAV---KQQKCNMFSLVFLGLGVLSFFT 712
Cdd:TIGR00957 955 yWDYmkaiglfitflsiflFVCNHVSALASNYWLSLWT-------------DDPMvngTQNNTSLRLSVYGALGILQGFA 1021
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 713 FFLQGFTFGKAGEILTTRLRSMAFKAMLRQDMSWFDdhKNSTGALSTRLATDAAQVQGATGTRLALIAQNTAN-LGTGII 791
Cdd:TIGR00957 1022 VFGYSMAVSIGGIQASRVLHQDLLHNKLRSPMSFFE--RTPSGNLVNRFSKELDTVDSMIPPVIKMFMGSLFNvIGALIV 1099
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 792 ISFIygwqlTLLLLSVVPFIAVAGIVEMKMLAGNAkRDKKEMEAAGKIATEAIENiRTVVSLTQERKFEsmyveklhgpy 871
Cdd:TIGR00957 1100 ILLA-----TPIAAVIIPPLGLLYFFVQRFYVASS-RQLKRLESVSRSPVYSHFN-ETLLGVSVIRAFE----------- 1161
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 872 rNSVRKAHIYGITFSISQAfMYFSYAGCFRF---GSYLIVNGHMRFKDVILVFSAIVLGAVALGHASSFA---------- 938
Cdd:TIGR00957 1162 -EQERFIHQSDLKVDENQK-AYYPSIVANRWlavRLECVGNCIVLFAALFAVISRHSLSAGLVGLSVSYSlqvtfylnwl 1239
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 939 -----------------PDYAKAKLSAAYLfslferqplIDSYSGEGLWPDKfeGSVTFNEVVFNYPTRANVpVLQGLSL 1001
Cdd:TIGR00957 1240 vrmssemetnivaverlKEYSETEKEAPWQ---------IQETAPPSGWPPR--GRVEFRNYCLRYREDLDL-VLRHINV 1307
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1002 EVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQWLRAQLGIVSQEPILFDCSIAENI----AYG 1077
Cdd:TIGR00957 1308 TIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLdpfsQYS 1387
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1078 DnsrvvphDEIVRAAKEANIHPFIETLPQKYNTRVGDKGTQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTESEKVV 1157
Cdd:TIGR00957 1388 D-------EEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLI 1460
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|....*.
gi 568932737 1158 QEALDKAREGRTCIVIAHRLSTIQNADLIVVIENGKVKEHGTHQQLLAQKGIYFSM 1213
Cdd:TIGR00957 1461 QSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRGIFYSM 1516
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
335-564 |
2.98e-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: 2.98e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 335 KGNLEFSDVHFSYPSRANIkILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLRE 414
Cdd:COG4618 328 KGRLSVENLTVVPPGSKRP-ILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGR 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 415 IIGVVSQEPVLFSTTIAENI-RYGrgNVTMDEIEKAVKEANAYDFIMKLPQKFDTLVGDRGAQLSGGQKQRIAIARALVR 493
Cdd:COG4618 407 HIGYLPQDVELFDGTIAENIaRFG--DADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYG 484
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568932737 494 NPKILLLDEATSALDTESEAEVQAALDKARE-GRTTIVIAHRLSTIRNADVIAGFEDGVIVEQGSHSELMKK 564
Cdd:COG4618 485 DPRLVVLDEPNSNLDDEGEAALAAAIRALKArGATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
976-1199 |
1.36e-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: 206.96 E-value: 1.36e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 976 GSVTFNEVVFNYptRAN-VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQWLRA 1054
Cdd:cd03244 1 GDIEFKNVSLRY--RPNlPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1055 QLGIVSQEPILFDCSIAENIA----YGDnsrvvphDEIVRAAKEANIHPFIETLPQKYNTRVGDKGTQLSGGQKQRIAIA 1130
Cdd:cd03244 79 RISIIPQDPVLFSGTIRSNLDpfgeYSD-------EELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568932737 1131 RALIRQPRVLLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIENGKVKEHGT 1199
Cdd:cd03244 152 RALLRKSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
947-1213 |
3.84e-58 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 211.22 E-value: 3.84e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 947 SAAYLFSLFERQPLIdSYSGEGLWPDKfEGSVTFNEVVFNYPTRANvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLL 1026
Cdd:PRK11160 310 SARRINEITEQKPEV-TFPTTSTAAAD-QVSLTLNNVSFTYPDQPQ-PVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLL 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1027 ERFYDPMAGSVLLDGQEAKKLNVQWLRAQLGIVSQEPILFDCSIAENIAYgdnsrvvphdeivrAAKEANIHPFIETL-- 1104
Cdd:PRK11160 387 TRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLL--------------AAPNASDEALIEVLqq 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1105 ---------PQKYNTRVGDKGTQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEALDKAREGRTCIVIAH 1175
Cdd:PRK11160 453 vgleklledDKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITH 532
|
250 260 270
....*....|....*....|....*....|....*...
gi 568932737 1176 RLSTIQNADLIVVIENGKVKEHGTHQQLLAQKGIYFSM 1213
Cdd:PRK11160 533 RLTGLEQFDRICVMDNGQIIEQGTHQELLAQQGRYYQL 570
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
702-1223 |
1.12e-57 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 210.34 E-value: 1.12e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 702 FLGLGVLSFFTFFLQGFTFGKAGEILTTRLRSMAFKAMLRQDMSWFDDHknSTGALSTRLATDAAQVQGATGTRLALIAQ 781
Cdd:PRK10790 71 YVGLQLLAAGLHYAQSLLFNRAAVGVVQQLRTDVMDAALRQPLSAFDTQ--PVGQLISRVTNDTEVIRDLYVTVVATVLR 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 782 NTANLGTGIIISFIYGWQLTLLLLSVVPFIAVAGIVEMKMLAGNAKRDKKEMEAAGKIATEAIENIRTVVSLTQERKF-E 860
Cdd:PRK10790 149 SAALIGAMLVAMFSLDWRMALVAIMIFPAVLVVMVIYQRYSTPIVRRVRAYLADINDGFNEVINGMSVIQQFRQQARFgE 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 861 SMyveklhgpyrNSVRKAHiygitfsisqafmYFSYAGCFRFGSYLIvnghmrfKDVILVFSAIVL------------GA 928
Cdd:PRK10790 229 RM----------GEASRSH-------------YMARMQTLRLDGFLL-------RPLLSLFSALILcgllmlfgfsasGT 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 929 VALGHASSFApdyakaklsaAYLFSLFErqPLID-----------SYSGEGLwpdkFE------------------GSVT 979
Cdd:PRK10790 279 IEVGVLYAFI----------SYLGRLNE--PLIElttqqsmlqqaVVAGERV----FElmdgprqqygnddrplqsGRID 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 980 FNEVVFNYptRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQWLRAQLGIV 1059
Cdd:PRK10790 343 IDNVSFAY--RDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMV 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1060 SQEPILFDCSIAENIAYGdnsRVVPHDEIVRAAKEANIHPFIETLPQKYNTRVGDKGTQLSGGQKQRIAIARALIRQPRV 1139
Cdd:PRK10790 421 QQDPVVLADTFLANVTLG---RDISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQI 497
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1140 LLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIENGKVKEHGTHQQLLAQKGIYFSMVNIQAG 1219
Cdd:PRK10790 498 LILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQGRYWQMYQLQLA 577
|
....
gi 568932737 1220 TQNL 1223
Cdd:PRK10790 578 GEEL 581
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
342-1214 |
2.07e-57 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 218.45 E-value: 2.07e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 342 DVHFSYPSRANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQ-LLQRLYDPTEGKISIDGQdirnfnvrclreiIGVVS 420
Cdd:PLN03130 619 NGYFSWDSKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISaMLGELPPRSDASVVIRGT-------------VAYVP 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 421 QEPVLFSTTIAENIRYGrGNVTMDEIEKAVKEANAYDFIMKLPQKFDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLL 500
Cdd:PLN03130 686 QVSWIFNATVRDNILFG-SPFDPERYERAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIF 764
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 501 DEATSALDTESEAEV-QAALDKAREGRTTIVIAHRLSTIRNADVIAGFEDGVIVEQGSHSELMKKEGIYFRLvnMQTAGS 579
Cdd:PLN03130 765 DDPLSALDAHVGRQVfDKCIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSNNGPLFQKL--MENAGK 842
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 580 QILSEEFEVELSDEKAAGDVAPNGWKARIFRNSTKKSlKSPHQNRLDEETNELDANVppVSFlKVLKLNKTEWP-YFVVG 658
Cdd:PLN03130 843 MEEYVEENGEEEDDQTSSKPVANGNANNLKKDSSSKK-KSKEGKSVLIKQEERETGV--VSW-KVLERYKNALGgAWVVM 918
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 659 TV--CAIANGALQPAFSIILSEMIAIFGPgddavKQQKCNMFSLVFlglGVLSFftfflqgftfgkaGEILTT------- 729
Cdd:PLN03130 919 ILflCYVLTEVFRVSSSTWLSEWTDQGTP-----KTHGPLFYNLIY---ALLSF-------------GQVLVTllnsywl 977
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 730 ---------RLRSMAFKAMLRQDMSWFddHKNSTGALSTRLATDaaqvqgatgtrLALIAQNTANLGTGIIISFiygWQL 800
Cdd:PLN03130 978 imsslyaakRLHDAMLGSILRAPMSFF--HTNPLGRIINRFAKD-----------LGDIDRNVAVFVNMFLGQI---FQL 1041
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 801 --TLLLLSVVPFIAVAGIveMKMLAG---------NAKRDKKEMEaagkiateaienirtvvSLTQERKFeSMYVEKLHG 869
Cdd:PLN03130 1042 lsTFVLIGIVSTISLWAI--MPLLVLfygaylyyqSTAREVKRLD-----------------SITRSPVY-AQFGEALNG 1101
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 870 -----PYRNSVRKAHIYGITFSISQAFMYFSYAGCFRFGSYL-IVNGHMrfkdVILVFSAIVLGAVALGHASSFAP---- 939
Cdd:PLN03130 1102 lstirAYKAYDRMAEINGRSMDNNIRFTLVNMSSNRWLAIRLeTLGGLM----IWLTASFAVMQNGRAENQAAFAStmgl 1177
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 940 --DYA-------KAKLSAAYL----FSLFER-----------QPLIDSYSGEGLWPDKfeGSVTFNEVVFNYptRANVP- 994
Cdd:PLN03130 1178 llSYAlnitsllTAVLRLASLaensLNAVERvgtyidlpseaPLVIENNRPPPGWPSS--GSIKFEDVVLRY--RPELPp 1253
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 995 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQWLRAQLGIVSQEPILFDCSIAENI 1074
Cdd:PLN03130 1254 VLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNL 1333
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1075 -AYGDNSRVvphdEIVRAAKEANIHPFIETLPQKYNTRVGDKGTQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTES 1153
Cdd:PLN03130 1334 dPFNEHNDA----DLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRT 1409
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568932737 1154 EKVVQEALDKarEGRTC--IVIAHRLSTIQNADLIVVIENGKVKEHGTHQQLLAQKGIYFS-MV 1214
Cdd:PLN03130 1410 DALIQKTIRE--EFKSCtmLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEGSAFSkMV 1471
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
668-1215 |
3.18e-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: 208.83 E-value: 3.18e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 668 LQPAFSIILSEMIAIFGPgddavkQQKCNMFSLVFLGL-------GVLSFFtfflQGFTFGKAGEILTTRLRSMAFKAML 740
Cdd:TIGR01193 171 ISIAGSYYLQKIIDTYIP------HKMMGTLGIISIGLiiayiiqQILSYI----QIFLLNVLGQRLSIDIILSYIKHLF 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 741 RQDMSWFDDHKnsTGALSTRLaTDAAQVQGATG-TRLALIAqntaNLGTGIIISFIYGWQ---LTLLLLSVVPFIAVAGI 816
Cdd:TIGR01193 241 ELPMSFFSTRR--TGEIVSRF-TDASSIIDALAsTILSLFL----DMWILVIVGLFLVRQnmlLFLLSLLSIPVYAVIII 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 817 VEMKMLAgnaKRDKKEMEAAGKIATEAIEN---IRTVVSLTQE----RKFESMYVEKLHGPYRNS----VRKAHIYGITF 885
Cdd:TIGR01193 314 LFKRTFN---KLNHDAMQANAVLNSSIIEDlngIETIKSLTSEaerySKIDSEFGDYLNKSFKYQkadqGQQAIKAVTKL 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 886 SISQAFMYFsyagcfrfGSYLIVNGHMRFKDVIlVFSAIV-LGAVALGHASSFAPDYAKAK-----LSAAYLF-SLFERQ 958
Cdd:TIGR01193 391 ILNVVILWT--------GAYLVMRGKLTLGQLI-TFNALLsYFLTPLENIINLQPKLQAARvannrLNEVYLVdSEFINK 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 959 PLIDSYSgeglwpdKFEGSVTFNEVVFNYPTraNVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVL 1038
Cdd:TIGR01193 462 KKRTELN-------NLNGDIVINDVSYSYGY--GSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEIL 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1039 LDGQEAKKLNVQWLRAQLGIVSQEPILFDCSIAENIAYGdNSRVVPHDEIVRAAKEANIHPFIETLPQKYNTRVGDKGTQ 1118
Cdd:TIGR01193 533 LNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLG-AKENVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSS 611
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1119 LSGGQKQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEALDKAREgRTCIVIAHRLSTIQNADLIVVIENGKVKEHG 1198
Cdd:TIGR01193 612 ISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQD-KTIIFVAHRLSVAKQSDKIIVLDHGKIIEQG 690
|
570
....*....|....*..
gi 568932737 1199 THQQLLAQKGIYFSMVN 1215
Cdd:TIGR01193 691 SHDELLDRNGFYASLIH 707
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
336-591 |
6.07e-55 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 202.26 E-value: 6.07e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 336 GNLEFSDVHFSYpsRANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLREI 415
Cdd:PRK10790 339 GRIDIDNVSFAY--RDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQG 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 416 IGVVSQEPVLFSTTIAENIRYGRgNVTMDEIEKAVKEANAYDFIMKLPQKFDTLVGDRGAQLSGGQKQRIAIARALVRNP 495
Cdd:PRK10790 417 VAMVQQDPVVLADTFLANVTLGR-DISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTP 495
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 496 KILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTIRNADVIAGFEDGVIVEQGSHSELMKKEGIYFRLVNMQ 575
Cdd:PRK10790 496 QILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQGRYWQMYQLQ 575
|
250
....*....|....*.
gi 568932737 576 TAGSQILSEEFEVELS 591
Cdd:PRK10790 576 LAGEELAASVREEESL 591
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
85-535 |
4.10e-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: 198.35 E-value: 4.10e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 85 AAGRQIKKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDDVskisEGIGDkvgMFFQAIATFFAGFIVGFIrgwkLTLVI 164
Cdd:TIGR02868 80 AALRSLGALRVRVYERLARQALAGRRRLRRGDLLGRLGADV----DALQD---LYVRVIVPAGVALVVGAA----AVAAI 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 165 MAISP----ILGLSTAVWAKILSTFS-----DKELAAYAKAGAVAEEALGAIR---TVIAFGGQNKELERYQKHLENAKK 232
Cdd:TIGR02868 149 AVLSVpaalILAAGLLLAGFVAPLVSlraarAAEQALARLRGELAAQLTDALDgaaELVASGALPAALAQVEEADRELTR 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 233 IGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTiGNAMTVFFSILIGAFSVGQAAP-CIDAFANARGAAYVI 311
Cdd:TIGR02868 229 AERRAAAATALGAALTLLAAGLAVLGALWAGGPAVADGRLA-PVTLAVLVLLPLAAFEAFAALPaAAQQLTRVRAAAERI 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 312 FDIIDNNPKIDSFSERGHKPDNIKG-NLEFSDVHFSYPSRAniKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLY 390
Cdd:TIGR02868 308 VEVLDAAGPVAEGSAPAAGAVGLGKpTLELRDLSAGYPGAP--PVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLL 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 391 DPTEGKISIDGQDIRNFNVRCLREIIGVVSQEPVLFSTTIAENIRYGRGNVTMDEIEKAVKEANAYDFIMKLPQKFDTLV 470
Cdd:TIGR02868 386 DPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPDATDEELWAALERVGLADWLRALPDGLDTVL 465
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568932737 471 GDRGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRL 535
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 ... |
202-564 |
6.02e-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: 6.02e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 202 EALGAIRTViafggQNKELERYQKHLENAKKIGIKKAISANISMgiAFLLIYASYALAFwyGSTLVISKEYTIGnaMTVF 281
Cdd:TIGR01842 194 EAMGMMGNL-----TKRWGRFHSKYLSAQSAASDRAGMLSNLSK--YFRIVLQSLVLGL--GAYLAIDGEITPG--MMIA 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 282 FSILigafsVGQAAPCID-------AFANARGAAYVIFDIIDNNPkidsFSERGHKPDNIKGNLEFSDVHFSYPSrANIK 354
Cdd:TIGR01842 263 GSIL-----VGRALAPIDgaiggwkQFSGARQAYKRLNELLANYP----SRDPAMPLPEPEGHLSVENVTIVPPG-GKKP 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 355 ILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLREIIGVVSQEPVLFSTTIAENI 434
Cdd:TIGR01842 333 TLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKHIGYLPQDVELFPGTVAENI 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 435 -RYGRgNVTMDEIEKAVKEANAYDFIMKLPQKFDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEA 513
Cdd:TIGR01842 413 aRFGE-NADPEKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQ 491
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 568932737 514 EVQAALDKAR-EGRTTIVIAHRLSTIRNADVIAGFEDGVIVEQGSHSELMKK 564
Cdd:TIGR01842 492 ALANAIKALKaRGITVVVITHRPSLLGCVDKILVLQDGRIARFGERDEVLAK 543
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
300-571 |
8.91e-54 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 198.92 E-value: 8.91e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 300 AFANARGAAYVIFDIIDNNpkiDSFSERGHKPDNIKGNLEFSDVHFSYPSRANIKILKGLNLKVKSGQTVALVGNSGCGK 379
Cdd:PRK11174 313 AKAQAVGAAESLVTFLETP---LAHPQQGEKELASNDPVTIEAEDLEILSPDGKTLAGPLNFTLPAGQRIALVGPSGAGK 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 380 STTVQLLqrL-YDPTEGKISIDGQDIRNFNVRCLREIIGVVSQEPVLFSTTIAENIRYGRGNVTMDEIEKAVKEANAYDF 458
Cdd:PRK11174 390 TSLLNAL--LgFLPYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGNPDASDEQLQQALENAWVSEF 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 459 IMKLPQKFDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTI 538
Cdd:PRK11174 468 LPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLEDL 547
|
250 260 270
....*....|....*....|....*....|...
gi 568932737 539 RNADVIAGFEDGVIVEQGSHSELMKKEGIYFRL 571
Cdd:PRK11174 548 AQWDQIWVMQDGQIVQQGDYAELSQAGGLFATL 580
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
338-561 |
1.73e-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: 183.92 E-value: 1.73e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 338 LEFSDVHFSYpsrANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYD-----PTEGKISIDGQDIR--NFNVR 410
Cdd:cd03260 1 IELRDLNVYY---GDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYdlDVDVL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 411 CLREIIGVVSQEPVLFSTTIAENIRYG---RGNVTMDEIEKAVKEANAydfIMKLPQKfdtlVGDR--GAQLSGGQKQRI 485
Cdd:cd03260 78 ELRRRVGMVFQKPNPFPGSIYDNVAYGlrlHGIKLKEELDERVEEALR---KAALWDE----VKDRlhALGLSGGQQQRL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568932737 486 AIARALVRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLS-TIRNADVIAGFEDGVIVEQGSHSEL 561
Cdd:cd03260 151 CLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQqAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
999-1213 |
1.04e-51 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 192.75 E-value: 1.04e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 999 LSLEVKKGQTLALVGSSGCGKSTVVQLLERFYdPMAGSVLLDGQEAKKLNVQWLRAQLGIVSQEPILFDCSIAENIAYGD 1078
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGN 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1079 NSrvVPHDEIVRAAKEANIHPFIETLPQKYNTRVGDKGTQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTESEKVVQ 1158
Cdd:PRK11174 448 PD--ASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVM 525
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 568932737 1159 EALDKAREGRTCIVIAHRLSTIQNADLIVVIENGKVKEHGTHQQLLAQKGIYFSM 1213
Cdd:PRK11174 526 QALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATL 580
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
338-565 |
1.15e-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: 1.15e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 338 LEFSDVHFSYPSraNIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLREIIG 417
Cdd:COG1122 1 IELENLSFSYPG--GTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 418 VVSQEPV--LFSTTIAENIRYG---RGnVTMDEIEKAVKEA----NAYDFIMKLPQkfdtlvgdrgaQLSGGQKQRIAIA 488
Cdd:COG1122 79 LVFQNPDdqLFAPTVEEDVAFGpenLG-LPREEIRERVEEAlelvGLEHLADRPPH-----------ELSGGQKQRVAIA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568932737 489 RALVRNPKILLLDEATSALDTESEAEVQAALDK-AREGRTTIVIAHRLSTI-RNADVIAGFEDGVIVEQGSHSELMKKE 565
Cdd:COG1122 147 GVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRlNKEGKTVIIVTHDLDLVaELADRVIVLDDGRIVADGTPREVFSDY 225
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
338-562 |
3.81e-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: 3.81e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 338 LEFSDVHFSYPSRAN--IKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLREI 415
Cdd:COG1123 261 LEVRNLSKRYPVRGKggVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 416 ---IGVVSQEPV--LF-STTIAENIRYG---RGNVTMDEIEKAVKEAnaydfiMK---LPQKFdtlvGDR-GAQLSGGQK 482
Cdd:COG1123 341 rrrVQMVFQDPYssLNpRMTVGDIIAEPlrlHGLLSRAERRERVAEL------LErvgLPPDL----ADRyPHELSGGQR 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 483 QRIAIARALVRNPKILLLDEATSALDTESEAEVQAALD--KAREGRTTIVIAHRLSTIRN-ADVIAGFEDGVIVEQGSHS 559
Cdd:COG1123 411 QRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRdlQRELGLTYLFISHDLAVVRYiADRVAVMYDGRIVEDGPTE 490
|
...
gi 568932737 560 ELM 562
Cdd:COG1123 491 EVF 493
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
696-1206 |
4.09e-51 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 189.87 E-value: 4.09e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 696 NMFSLVFLGLGVLSFFTFF-----LQGFTFGKAGEILTTRLRSMAFKAMLRQDMswfddhkNSTGALSTRLATDAAQVQG 770
Cdd:TIGR01842 41 SVPTLLMLTVLALGLYLFLglldaLRSFVLVRIGEKLDGALNQPIFAASFSATL-------RRGSGDGLQALRDLDQLRQ 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 771 ATGtrlaliaqntanlGTGIIISFIYGWQLTLLLLSVV--PFIAVAGIVEMKMLAG----NAKRDKKEME-------AAG 837
Cdd:TIGR01842 114 FLT-------------GPGLFAFFDAPWMPIYLLVCFLlhPWIGILALGGAVVLVGlallNNRATKKPLKeateasiRAN 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 838 KIATEAIENIRTVVSLTQERKFESMYvEKLHGPYRNSVRKAHIYGITFS-ISQAFMYFSYAGCFRFGSYLIVNGHMRFKD 916
Cdd:TIGR01842 181 NLADSALRNAEVIEAMGMMGNLTKRW-GRFHSKYLSAQSAASDRAGMLSnLSKYFRIVLQSLVLGLGAYLAIDGEITPGM 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 917 VILvfSAIVLGAvALG---HASSFAPDYAKAKLSAAYLFSLFERQPLIDsysgEGLWPDKFEGSVTFNEVVFnYPTRANV 993
Cdd:TIGR01842 260 MIA--GSILVGR-ALApidGAIGGWKQFSGARQAYKRLNELLANYPSRD----PAMPLPEPEGHLSVENVTI-VPPGGKK 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 994 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKklnvQWLRAQLG----IVSQEPILFDCS 1069
Cdd:TIGR01842 332 PTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLK----QWDRETFGkhigYLPQDVELFPGT 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1070 IAENIA-YGDNsrvVPHDEIVRAAKEANIHPFIETLPQKYNTRVGDKGTQLSGGQKQRIAIARALIRQPRVLLLDEATSA 1148
Cdd:TIGR01842 408 VAENIArFGEN---ADPEKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSN 484
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 568932737 1149 LDTESEKVVQEALDKAR-EGRTCIVIAHRLSTIQNADLIVVIENGKVKEHGTHQQLLAQ 1206
Cdd:TIGR01842 485 LDEEGEQALANAIKALKaRGITVVVITHRPSLLGCVDKILVLQDGRIARFGERDEVLAK 543
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
339-550 |
8.24e-51 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 178.43 E-value: 8.24e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 339 EFSDVHFSYPSRANiKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLREIIGV 418
Cdd:cd03225 1 ELKNLSFSYPDGAR-PALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 419 VSQEP--VLFSTTIAENIRYGRGN--VTMDEIEKAVKEANAydfimklpqkfdtLVGDRG------AQLSGGQKQRIAIA 488
Cdd:cd03225 80 VFQNPddQFFGPTVEEEVAFGLENlgLPEEEIEERVEEALE-------------LVGLEGlrdrspFTLSGGQKQRVAIA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568932737 489 RALVRNPKILLLDEATSALDTESEAEVQAALDK-AREGRTTIVIAHRLSTIRN-ADVIAGFEDG 550
Cdd:cd03225 147 GVLAMDPDILLLDEPTAGLDPAGRRELLELLKKlKAEGKTIIIVTHDLDLLLElADRVIVLEDG 210
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
338-552 |
3.03e-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: 3.03e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 338 LEFSDVHFSYPSRANiKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLREIIG 417
Cdd:cd03246 1 LEVENVSFRYPGAEP-PVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 418 VVSQEPVLFSTTIAENIrygrgnvtmdeiekavkeanaydfimklpqkfdtlvgdrgaqLSGGQKQRIAIARALVRNPKI 497
Cdd:cd03246 80 YLPQDDELFSGSIAENI------------------------------------------LSGGQRQRLGLARALYGNPRI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 568932737 498 LLLDEATSALDTESEAEVQAALDKARE-GRTTIVIAHRLSTIRNADVIAGFEDGVI 552
Cdd:cd03246 118 LVLDEPNSHLDVEGERALNQAIAALKAaGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
978-1207 |
3.83e-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: 3.83e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 978 VTFNEVVFNYPTraNVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQWLRAQLG 1057
Cdd:COG1122 1 IELENLSFSYPG--GTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1058 IVSQEPI--LFDCSIAENIAYGDNSRVVPHDEIVRAAKEA----NIHPFIETLPQkyntrvgdkgtQLSGGQKQRIAIAR 1131
Cdd:COG1122 79 LVFQNPDdqLFAPTVEEDVAFGPENLGLPREEIRERVEEAlelvGLEHLADRPPH-----------ELSGGQKQRVAIAG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568932737 1132 ALIRQPRVLLLDEATSALDTESEKVVQEALDK-AREGRTCIVIAHRLSTI-QNADLIVVIENGKVKEHGTHQQLLAQK 1207
Cdd:COG1122 148 VLAMEPEVLVLDEPTAGLDPRGRRELLELLKRlNKEGKTVIIVTHDLDLVaELADRVIVLDDGRIVADGTPREVFSDY 225
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
983-1194 |
4.77e-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: 4.77e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 983 VVFNYPTRANvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQWLRAQLGIVSQE 1062
Cdd:cd03246 6 VSFRYPGAEP-PVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGYLPQD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1063 PILFDCSIAENIaygdnsrvvphdeivraakeanihpfietlpqkyntrvgdkgtqLSGGQKQRIAIARALIRQPRVLLL 1142
Cdd:cd03246 85 DELFSGSIAENI--------------------------------------------LSGGQRQRLGLARALYGNPRILVL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 568932737 1143 DEATSALDTESEKVVQEALDKARE-GRTCIVIAHRLSTIQNADLIVVIENGKV 1194
Cdd:cd03246 121 DEPNSHLDVEGERALNQAIAALKAaGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
995-1203 |
5.62e-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: 5.62e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 995 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYD-----PMAGSVLLDGQE--AKKLNVQWLRAQLGIVSQEPILFD 1067
Cdd:cd03260 15 ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDiyDLDVDVLELRRRVGMVFQKPNPFP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1068 CSIAENIAYGDNSR-VVPH---DEIVRAA-KEANIHPfietlpqkyntRVGDK--GTQLSGGQKQRIAIARALIRQPRVL 1140
Cdd:cd03260 95 GSIYDNVAYGLRLHgIKLKeelDERVEEAlRKAALWD-----------EVKDRlhALGLSGGQQQRLCLARALANEPEVL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568932737 1141 LLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHGTHQQL 1203
Cdd:cd03260 164 LLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARvADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
356-505 |
1.05e-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: 167.05 E-value: 1.05e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 356 LKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLREIIGVVSQEPVLFS-TTIAENI 434
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPrLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568932737 435 RYGRgnvTMDEIEKAVKEANAYDFIMKLPQKF--DTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEATS 505
Cdd:pfam00005 81 RLGL---LLKGLSKREKDARAEEALEKLGLGDlaDRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
338-557 |
1.70e-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: 1.70e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 338 LEFSDVHFSYPSRAN-IKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLREI- 415
Cdd:COG1135 2 IELENLSKTFPTKGGpVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAAr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 416 --IGVVSQEPVLFST-TIAENIRY-----GrgnVTMDEIEKAVKE----------ANAYdfimklPqkfdtlvgdrgAQL 477
Cdd:COG1135 82 rkIGMIFQHFNLLSSrTVAENVALpleiaG---VPKAEIRKRVAEllelvglsdkADAY------P-----------SQL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 478 SGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKARE--GRTTIVIAHRLSTIRN-ADVIAGFEDGVIVE 554
Cdd:COG1135 142 SGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRelGLTIVLITHEMDVVRRiCDRVAVLENGRIVE 221
|
...
gi 568932737 555 QGS 557
Cdd:COG1135 222 QGP 224
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
338-556 |
1.77e-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: 1.77e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 338 LEFSDVHFSYPSRaNIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNvRCLREIIG 417
Cdd:cd03247 1 LSINNVSFSYPEQ-EQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 418 VVSQEPVLFSTTIAENIrygrgnvtmdeiekavkeanaydfimklpqkfdtlvgdrGAQLSGGQKQRIAIARALVRNPKI 497
Cdd:cd03247 79 VLNQRPYLFDTTLRNNL---------------------------------------GRRFSGGERQRLALARILLQDAPI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 568932737 498 LLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTIRNADVIAGFEDGVIVEQG 556
Cdd:cd03247 120 VLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
338-533 |
2.80e-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: 2.80e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 338 LEFSDVHFSYPSRaniKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLREIIG 417
Cdd:COG4619 1 LELEGLSFRVGGK---PILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 418 VVSQEPVLFSTTIAENI----RYGRGNVTMDEIEKAVKEANaydfimkLPQKF-DTLVgdrgAQLSGGQKQRIAIARALV 492
Cdd:COG4619 78 YVPQEPALWGGTVRDNLpfpfQLRERKFDRERALELLERLG-------LPPDIlDKPV----ERLSGGERQRLALIRALL 146
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 568932737 493 RNPKILLLDEATSALDTESEAEVQAALDK--AREGRTTIVIAH 533
Cdd:COG4619 147 LQPDVLLLDEPTSALDPENTRRVEELLREylAEEGRAVLWVSH 189
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
338-561 |
3.15e-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: 3.15e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 338 LEFSDVHFSYPSRAN-IKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDI---RNFNVRCLR 413
Cdd:cd03258 2 IELKNVSKVFGDTGGkVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLtllSGKELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 414 EIIGVVSQEPVLFST-TIAENIRYGR--GNVTMDEIEKAVKEanaydfimklpqkFDTLVG--DRG----AQLSGGQKQR 484
Cdd:cd03258 82 RRIGMIFQHFNLLSSrTVFENVALPLeiAGVPKAEIEERVLE-------------LLELVGleDKAdaypAQLSGGQKQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 485 IAIARALVRNPKILLLDEATSALDTESEAEVQAALDK--AREGRTTIVIAHRLSTIRN-ADVIAGFEDGVIVEQGSHSEL 561
Cdd:cd03258 149 VGIARALANNPKVLLCDEATSALDPETTQSILALLRDinRELGLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEEV 228
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
338-556 |
4.24e-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: 4.24e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 338 LEFSDVHFSYPSRAN-IKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLREI- 415
Cdd:cd03257 2 LEVKNLSVSFPTGGGsVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIRr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 416 --IGVVSQEPV-----LFS--TTIAENIRYGRGNVTMDEIEKAVKEA-----NAYDFIMKLPqkfdtlvgdrgAQLSGGQ 481
Cdd:cd03257 82 keIQMVFQDPMsslnpRMTigEQIAEPLRIHGKLSKKEARKEAVLLLlvgvgLPEEVLNRYP-----------HELSGGQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568932737 482 KQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKARE--GRTTIVIAHRLSTIRN-ADVIAGFEDGVIVEQG 556
Cdd:cd03257 151 RQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEelGLTLLFITHDLGVVAKiADRVAVMYAGKIVEEG 228
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
978-1206 |
5.11e-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: 5.11e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 978 VTFNEVVFNYPTRAN--VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLN---VQWL 1052
Cdd:COG1123 261 LEVRNLSKRYPVRGKggVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSrrsLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1053 RAQLGIVSQEPIL-FDC--SIAENIAYG-DNSRVVPHDEIVRAAKE-----------ANIHPFietlpqkyntrvgdkgt 1117
Cdd:COG1123 341 RRRVQMVFQDPYSsLNPrmTVGDIIAEPlRLHGLLSRAERRERVAEllervglppdlADRYPH----------------- 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1118 QLSGGQKQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEALD--KAREGRTCIVIAHRLSTIQN-ADLIVVIENGKV 1194
Cdd:COG1123 404 ELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRdlQRELGLTYLFISHDLAVVRYiADRVAVMYDGRI 483
|
250
....*....|..
gi 568932737 1195 KEHGTHQQLLAQ 1206
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 ... |
980-1193 |
1.78e-46 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 166.10 E-value: 1.78e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 980 FNEVVFNYPTRaNVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQWLRAQLGIV 1059
Cdd:cd03225 2 LKNLSFSYPDG-ARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1060 SQEP--ILFDCSIAENIAYGDNSRVVPHDEIVRAAKEA----NIHPFIETLPQkyntrvgdkgtQLSGGQKQRIAIARAL 1133
Cdd:cd03225 81 FQNPddQFFGPTVEEEVAFGLENLGLPEEEIEERVEEAlelvGLEGLRDRSPF-----------TLSGGQKQRVAIAGVL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568932737 1134 IRQPRVLLLDEATSALDTESEKVVQEALDK-AREGRTCIVIAHRLSTIQN-ADLIVVIENGK 1193
Cdd:cd03225 150 AMDPDILLLDEPTAGLDPAGRRELLELLKKlKAEGKTIIIVTHDLDLLLElADRVIVLEDGK 211
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
994-1194 |
2.90e-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: 2.90e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 994 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQWLRAQLGIVSQEPILFDCSIAEN 1073
Cdd:COG4619 14 PILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYVPQEPALWGGTVRDN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1074 IAYGDNSRVVPHDE--IVRAAKEANIHPFIetlpqkYNTRVgdkgTQLSGGQKQRIAIARALIRQPRVLLLDEATSALDT 1151
Cdd:COG4619 94 LPFPFQLRERKFDRerALELLERLGLPPDI------LDKPV----ERLSGGERQRLALIRALLLQPDVLLLDEPTSALDP 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 568932737 1152 ESEKVVQEALDK--AREGRTCIVIAHRLSTIQN-ADLIVVIENGKV 1194
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 ... |
970-1199 |
3.25e-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: 165.28 E-value: 3.25e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 970 WPDkfEGSVTFNEVVFNYptRANVP-VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLN 1048
Cdd:cd03369 1 WPE--HGEIEVENLSVRY--APDLPpVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1049 VQWLRAQLGIVSQEPILFDCSIAENI-AYGDNSrvvphDEIVRAAkeanihpfietlpqkynTRVGDKGTQLSGGQKQRI 1127
Cdd:cd03369 77 LEDLRSSLTIIPQDPTLFSGTIRSNLdPFDEYS-----DEEIYGA-----------------LRVSEGGLNLSQGQRQLL 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568932737 1128 AIARALIRQPRVLLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIENGKVKEHGT 1199
Cdd:cd03369 135 CLARALLKRPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
338-561 |
1.23e-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: 1.23e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 338 LEFSDVHFSYpsrANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDI--RNFNVRCLREI 415
Cdd:COG1126 2 IEIENLHKSF---GDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLtdSKKDINKLRRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 416 IGVVSQEPVLFS-TTIAENIRYG----RGnvtMDEiEKAVKEAnaydfiMKLPQKfdtlVG--DRG----AQLSGGQKQR 484
Cdd:COG1126 79 VGMVFQQFNLFPhLTVLENVTLApikvKK---MSK-AEAEERA------MELLER----VGlaDKAdaypAQLSGGQQQR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568932737 485 IAIARALVRNPKILLLDEATSALDTESEAEVQAAL-DKAREGRTTIVIAHRLSTIRN-ADVIAGFEDGVIVEQGSHSEL 561
Cdd:COG1126 145 VAIARALAMEPKVMLFDEPTSALDPELVGEVLDVMrDLAKEGMTMVVVTHEMGFAREvADRVVFMDGGRIVEEGPPEEF 223
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
338-573 |
1.26e-45 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 164.47 E-value: 1.26e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 338 LEFSDVHFSYpsrANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRcLREIIG 417
Cdd:COG1131 1 IEVRGLTKRY---GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAE-VRRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 418 VVSQEPVLFST-TIAENIRYGRG--NVTMDEIEKAVKEANAydfIMKLPQKFDTLVGdrgaQLSGGQKQRIAIARALVRN 494
Cdd:COG1131 77 YVPQEPALYPDlTVRENLRFFARlyGLPRKEARERIDELLE---LFGLTDAADRKVG----TLSGGMKQRLGLALALLHD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 495 PKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIA-HRLSTI-RNADVIAGFEDGVIVEQGSHSELMKK--EGIYFR 570
Cdd:COG1131 150 PELLILDEPTSGLDPEARRELWELLRELAAEGKTVLLStHYLEEAeRLCDRVAIIDKGRIVADGTPDELKARllEDVFLE 229
|
...
gi 568932737 571 LVN 573
Cdd:COG1131 230 LTG 232
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
978-1198 |
1.28e-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: 1.28e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 978 VTFNEVVFNYPTRaNVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQwLRAQLG 1057
Cdd:cd03247 1 LSINNVSFSYPEQ-EQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKA-LSSLIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1058 IVSQEPILFDCSIAENIaygdnsrvvphdeivraakeanihpfietlpqkyntrvgdkGTQLSGGQKQRIAIARALIRQP 1137
Cdd:cd03247 79 VLNQRPYLFDTTLRNNL-----------------------------------------GRRFSGGERQRLALARILLQDA 117
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568932737 1138 RVLLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIENGKVKEHG 1198
Cdd:cd03247 118 PIVLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
338-555 |
1.29e-45 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 164.06 E-value: 1.29e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 338 LEFSDVHFSYPSRAN-IKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLREI- 415
Cdd:COG1136 5 LELRNLTKSYGTGEGeVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELARLr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 416 ---IGVVSQEPVLFST-TIAENIRYGR--GNVTMDEIEKAVKEANAY----DFIMKLPqkfdtlvgdrgAQLSGGQKQRI 485
Cdd:COG1136 85 rrhIGFVFQFFNLLPElTALENVALPLllAGVSRKERRERARELLERvglgDRLDHRP-----------SQLSGGQQQRV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568932737 486 AIARALVRNPKILLLDEATSALDTESEAEVQAALDK-AREGRTTIVIA-HRLSTIRNADVIAGFEDGVIVEQ 555
Cdd:COG1136 154 AIARALVNRPKLILADEPTGNLDSKTGEEVLELLRElNRELGTTIVMVtHDPELAARADRVIRLRDGRIVSD 225
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
336-557 |
7.08e-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: 161.43 E-value: 7.08e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 336 GNLEFSDVHFSYpsRANI-KILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLRE 414
Cdd:cd03369 5 GEIEVENLSVRY--APDLpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 415 IIGVVSQEPVLFSTTIAENI-RYGRgnVTMDEIEKAVKeanaydfimklpqkfdtlVGDRGAQLSGGQKQRIAIARALVR 493
Cdd:cd03369 83 SLTIIPQDPTLFSGTIRSNLdPFDE--YSDEEIYGALR------------------VSEGGLNLSQGQRQLLCLARALLK 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568932737 494 NPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTIRNADVIAGFEDGVIVEQGS 557
Cdd:cd03369 143 RPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
338-563 |
8.49e-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: 8.49e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 338 LEFSDVHFSYPSRaniKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLREI-- 415
Cdd:COG1127 6 IEVRNLTKSFGDR---VVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYELrr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 416 -IGVVSQEPVLFST-TIAENIRYG---RGNVTMDEIEKAVkeanaydfIMKLpqkfdTLVGDRGA------QLSGGQKQR 484
Cdd:COG1127 83 rIGMLFQGGALFDSlTVFENVAFPlreHTDLSEAEIRELV--------LEKL-----ELVGLPGAadkmpsELSGGMRKR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 485 IAIARALVRNPKILLLDEATSALDTESEAEVQAALDKARE--GRTTIVIAHRLSTIRN-ADVIAGFEDGVIVEQGSHSEL 561
Cdd:COG1127 150 VALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDelGLTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPEEL 229
|
..
gi 568932737 562 MK 563
Cdd:COG1127 230 LA 231
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
338-556 |
1.06e-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: 1.06e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 338 LEFSDVHFSYPSranIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRclREIIG 417
Cdd:cd03259 1 LELKGLSKTYGS---VRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE--RRNIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 418 VVSQEPVLFST-TIAENIRYG--RGNVTMDEIEKAVKEANAydfimklpqkfdtLVGDRG------AQLSGGQKQRIAIA 488
Cdd:cd03259 76 MVFQDYALFPHlTVAENIAFGlkLRGVPKAEIRARVRELLE-------------LVGLEGllnrypHELSGGQQQRVALA 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568932737 489 RALVRNPKILLLDEATSALDTESEAEVQAALDK--AREGRTTIVIAHRLS-TIRNADVIAGFEDGVIVEQG 556
Cdd:cd03259 143 RALAREPSLLLLDEPLSALDAKLREELREELKElqRELGITTIYVTHDQEeALALADRIAVMNEGRIVQVG 213
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
338-550 |
1.32e-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: 1.32e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 338 LEFSDVHFSYpsrANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIR--NFNVRCLREI 415
Cdd:cd03229 1 LELKNVSKRY---GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTdlEDELPPLRRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 416 IGVVSQEPVLFST-TIAENIRYGrgnvtmdeiekavkeanaydfimklpqkfdtlvgdrgaqLSGGQKQRIAIARALVRN 494
Cdd:cd03229 78 IGMVFQDFALFPHlTVLENIALG---------------------------------------LSGGQQQRVALARALAMD 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 568932737 495 PKILLLDEATSALDTESEAEVQAALD--KAREGRTTIVIAHRLS-TIRNADVIAGFEDG 550
Cdd:cd03229 119 PDVLLLDEPTSALDPITRREVRALLKslQAQLGITVVLVTHDLDeAARLADRVVVLRDG 177
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
60-583 |
4.28e-44 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 175.55 E-value: 4.28e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 60 YAYYYSGLGGGvLVAAYIQVSFWTLAAG-RQIKKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDDVSKISEGIGDKVGM 138
Cdd:PLN03232 952 YIVVYALLGFG-QVAVTFTNSFWLISSSlHAAKRLHDAMLNSILRAPMLFFHTNPTGRVINRFSKDIGDIDRNVANLMNM 1030
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 139 F----FQAIATFFAGFIVGFIRGWkltlvimAISPILGLSTAVWAKILSTFSD-KELAAYAKAGAVAE--EALGAIRTVI 211
Cdd:PLN03232 1031 FmnqlWQLLSTFALIGTVSTISLW-------AIMPLLILFYAAYLYYQSTSREvRRLDSVTRSPIYAQfgEALNGLSSIR 1103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 212 AFGGQNKELERYQKHLENAKKIGIKkAISAN-------ISMGIAFLLIYASYALAFW--------YGSTLVISKEYTIgN 276
Cdd:PLN03232 1104 AYKAYDRMAKINGKSMDNNIRFTLA-NTSSNrwltirlETLGGVMIWLTATFAVLRNgnaenqagFASTMGLLLSYTL-N 1181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 277 AMTVFFSILIGAFSVGQAAPCIDAFANARGAAYVIFDIIDNNPKIDSFSERGhkpdnikgNLEFSDVHFSYpsRANIK-I 355
Cdd:PLN03232 1182 ITTLLSGVLRQASKAENSLNSVERVGNYIDLPSEATAIIENNRPVSGWPSRG--------SIKFEDVHLRY--RPGLPpV 1251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 356 LKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLREIIGVVSQEPVLFSTTIAENIR 435
Cdd:PLN03232 1252 LHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNID 1331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 436 -YGRGNVTmdEIEKAVKEANAYDFIMKLPQKFDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAE 514
Cdd:PLN03232 1332 pFSEHNDA--DLWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSL 1409
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568932737 515 VQAALDKAREGRTTIVIAHRLSTIRNADVIAGFEDGVIVEQGSHSELMKKEG-IYFRLVNMQ-TAGSQILS 583
Cdd:PLN03232 1410 IQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTsAFFRMVHSTgPANAQYLS 1480
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
338-562 |
4.72e-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: 4.72e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 338 LEFSDVHFSYPSRANiKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPT---EGKISIDGQDIRNFNVRCLRE 414
Cdd:COG1123 5 LEVRDLSVRYPGGDV-PAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 415 IIGVVSQEP--VLFSTTIAENIRYG--RGNVTMDEIEKAVKEANAYDFImklpqkfDTLVGDRGAQLSGGQKQRIAIARA 490
Cdd:COG1123 84 RIGMVFQDPmtQLNPVTVGDQIAEAleNLGLSRAEARARVLELLEAVGL-------ERRLDRYPHQLSGGQRQRVAIAMA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568932737 491 LVRNPKILLLDEATSALDTESEAEVQAALDK--AREGRTTIVIAHRLSTI-RNADVIAGFEDGVIVEQGSHSELM 562
Cdd:COG1123 157 LALDPDLLIADEPTTALDVTTQAEILDLLRElqRERGTTVLLITHDLGVVaEIADRVVVMDDGRIVEDGPPEEIL 231
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
989-1198 |
6.44e-44 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 158.84 E-value: 6.44e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 989 TRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQwlRAQLGIVSQEPILFD- 1067
Cdd:cd03259 9 TYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE--RRNIGMVFQDYALFPh 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1068 CSIAENIAYGDNSRVVPHDEIVRAAKEA----NIHPFIETLPqkyntrvgdkgTQLSGGQKQRIAIARALIRQPRVLLLD 1143
Cdd:cd03259 87 LTVAENIAFGLKLRGVPKAEIRARVRELlelvGLEGLLNRYP-----------HELSGGQQQRVALARALAREPSLLLLD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 568932737 1144 EATSALDTESEKVVQEALDK--AREGRTCIVIAHRLS-TIQNADLIVVIENGKVKEHG 1198
Cdd:cd03259 156 EPLSALDAKLREELREELKElqRELGITTIYVTHDQEeALALADRIAVMNEGRIVQVG 213
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
338-562 |
8.19e-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: 8.19e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 338 LEFSDVHFSYPSRAniKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLREIIG 417
Cdd:cd03295 1 IEFENVTKRYGGGK--KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 418 VVSQEPVLFS-TTIAENIrygrGNV-TMDEIEKAVKEANAYDfIMKL----PQKFdtlvGDR-GAQLSGGQKQRIAIARA 490
Cdd:cd03295 79 YVIQQIGLFPhMTVEENI----ALVpKLLKWPKEKIRERADE-LLALvgldPAEF----ADRyPHELSGGQQQRVGVARA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568932737 491 LVRNPKILLLDEATSALDTESEAEVQAALDKARE--GRTTIVIAHRL-STIRNADVIAGFEDGVIVEQGSHSELM 562
Cdd:cd03295 150 LAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQelGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEIL 224
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
338-552 |
1.02e-43 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 158.42 E-value: 1.02e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 338 LEFSDVHFSYPSRAN-IKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLREI- 415
Cdd:cd03255 1 IELKNLSKTYGGGGEkVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 416 ---IGVVSQEPVLFST-TIAENIRYGrgnVTMDEIEKAVKEANAYDFI--MKLPQKFDTLVgdrgAQLSGGQKQRIAIAR 489
Cdd:cd03255 81 rrhIGFVFQSFNLLPDlTALENVELP---LLLAGVPKKERRERAEELLerVGLGDRLNHYP----SELSGGQQQRVAIAR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568932737 490 ALVRNPKILLLDEATSALDTESEAEVQAAL-DKAREGRTTIVIA-HRLSTIRNADVIAGFEDGVI 552
Cdd:cd03255 154 ALANDPKIILADEPTGNLDSETGKEVMELLrELNKEAGTTIVVVtHDPELAEYADRIIELRDGKI 218
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
920-1177 |
1.25e-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: 1.25e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 920 VFSAIVLGAVALGHASSFAPDYA----KAKLSAAYLFSLFERQPLIDSYSG---EGLWPDKFegSVTFNEVVFNYPTRAn 992
Cdd:TIGR02868 272 TLAVLVLLPLAAFEAFAALPAAAqqltRVRAAAERIVEVLDAAGPVAEGSApaaGAVGLGKP--TLELRDLSAGYPGAP- 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 993 vPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQWLRAQLGIVSQEPILFDCSIAE 1072
Cdd:TIGR02868 349 -PVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRE 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1073 N--IAYGDnsrvVPHDEIVRAAKEANIHPFIETLPQKYNTRVGDKGTQLSGGQKQRIAIARALIRQPRVLLLDEATSALD 1150
Cdd:TIGR02868 428 NlrLARPD----ATDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLD 503
|
250 260
....*....|....*....|....*..
gi 568932737 1151 TESEKVVQEALDKAREGRTCIVIAHRL 1177
Cdd:TIGR02868 504 AETADELLEDLLAALSGRTVVLITHHL 530
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
338-565 |
1.64e-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: 1.64e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 338 LEFSDVHFSYPSRAnikILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLREIIG 417
Cdd:COG1120 2 LEAENLSVGYGGRP---VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 418 VVSQEPVL-FSTTIAENIRYGR-------GNVT---MDEIEKAVKEANAYDFIMKLpqkFDTlvgdrgaqLSGGQKQRIA 486
Cdd:COG1120 79 YVPQEPPApFGLTVRELVALGRyphlglfGRPSaedREAVEEALERTGLEHLADRP---VDE--------LSGGERQRVL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 487 IARALVRNPKILLLDEATSALDTESEAEVQAALDK--AREGRTTIVIAHRLS-TIRNADVIAGFEDGVIVEQGSHSELMK 563
Cdd:COG1120 148 IARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRlaRERGRTVVMVLHDLNlAARYADRLVLLKDGRIVAQGPPEEVLT 227
|
..
gi 568932737 564 KE 565
Cdd:COG1120 228 PE 229
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
339-550 |
1.84e-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: 1.84e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 339 EFSDVHFSYPSRaniKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLREIIGV 418
Cdd:cd00267 1 EIENLSFRYGGR---TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 419 VSQepvlfsttiaenirygrgnvtmdeiekavkeanaydfimklpqkfdtlvgdrgaqLSGGQKQRIAIARALVRNPKIL 498
Cdd:cd00267 78 VPQ-------------------------------------------------------LSGGQRQRVALARALLLNPDLL 102
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 568932737 499 LLDEATSALDTESEAEVQAALDK-AREGRTTIVIAHRLSTIRNA-DVIAGFEDG 550
Cdd:cd00267 103 LLDEPTSGLDPASRERLLELLRElAEEGRTVIIVTHDPELAELAaDRVIVLKDG 156
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
338-561 |
1.86e-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: 1.86e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 338 LEFSDVHFSYpsrANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDI-------RNfnvr 410
Cdd:COG3842 6 LELENVSKRY---GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVtglppekRN---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 411 clreiIGVVSQEPVLFS-TTIAENIRYG---RGnVTMDEIEKAVKEANAydfIMKLPQkfdtlVGDRG-AQLSGGQKQRI 485
Cdd:COG3842 79 -----VGMVFQDYALFPhLTVAENVAFGlrmRG-VPKAEIRARVAELLE---LVGLEG-----LADRYpHQLSGGQQQRV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 486 AIARALVRNPKILLLDEATSALDTESEAEVQAALDK--AREGRTTIVIAHRLS---TIrnADVIAGFEDGVIVEQGSHSE 560
Cdd:COG3842 145 ALARALAPEPRVLLLDEPLSALDAKLREEMREELRRlqRELGITFIYVTHDQEealAL--ADRIAVMNDGRIEQVGTPEE 222
|
.
gi 568932737 561 L 561
Cdd:COG3842 223 I 223
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
338-563 |
3.11e-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: 158.04 E-value: 3.11e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 338 LEFSDVHFSYPSRA-NIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLREII 416
Cdd:COG1124 2 LEVRNLSVSYGQGGrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 417 GVVSQEPVL-----FS--TTIAENIR-YGRGNVtMDEIEKAVKEANaydfimkLPqkfDTLVGDRGAQLSGGQKQRIAIA 488
Cdd:COG1124 82 QMVFQDPYAslhprHTvdRILAEPLRiHGLPDR-EERIAELLEQVG-------LP---PSFLDRYPHQLSGGQRQRVAIA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568932737 489 RALVRNPKILLLDEATSALDTESEAEVQAALD--KAREGRTTIVIAHRLSTI-RNADVIAGFEDGVIVEQGSHSELMK 563
Cdd:COG1124 151 RALILEPELLLLDEPTSALDVSVQAEILNLLKdlREERGLTYLFVSHDLAVVaHLCDRVAVMQNGRIVEELTVADLLA 228
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
338-567 |
3.26e-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: 3.26e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 338 LEFSDVHFSYPSrANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNF-NVRCLREII 416
Cdd:TIGR04520 1 IEVENVSFSYPE-SEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEeNLWEIRKKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 417 GVVSQEP--VLFSTTIAENIRYGRGN--VTMDEIEKAVKEA----NAYDFIMKLPQKfdtlvgdrgaqLSGGQKQRIAIA 488
Cdd:TIGR04520 80 GMVFQNPdnQFVGATVEDDVAFGLENlgVPREEMRKRVDEAlklvGMEDFRDREPHL-----------LSGGQKQRVAIA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 489 RALVRNPKILLLDEATSALDTESEAEVQAALDKAR--EGRTTIVIAHRLSTIRNADVIAGFEDGVIVEQG------SHSE 560
Cdd:TIGR04520 149 GVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNkeEGITVISITHDMEEAVLADRVIVMNKGKIVAEGtpreifSQVE 228
|
....*..
gi 568932737 561 LMKKEGI 567
Cdd:TIGR04520 229 LLKEIGL 235
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
987-1198 |
7.85e-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: 7.85e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 987 YPTRAN-VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQWL---RAQLGIVSQE 1062
Cdd:cd03257 11 FPTGGGsVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRkirRKEIQMVFQD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1063 PI-----LFdcSIAENIAygdnsrvvphdEIVRAAKEANIHPFIETLPQKYNTRVGDKGT-------QLSGGQKQRIAIA 1130
Cdd:cd03257 91 PMsslnpRM--TIGEQIA-----------EPLRIHGKLSKKEARKEAVLLLLVGVGLPEEvlnryphELSGGQRQRVAIA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568932737 1131 RALIRQPRVLLLDEATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHG 1198
Cdd:cd03257 158 RALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEelGLTLLFITHDLGVVAKiADRVAVMYAGKIVEEG 228
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
996-1147 |
1.64e-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: 152.42 E-value: 1.64e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 996 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQWLRAQLGIVSQEPILF-DCSIAENI 1074
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFpRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568932737 1075 AYGdnsrvVPHDEIVRAAKEANIHPFIETLPQKY--NTRVGDKGTQLSGGQKQRIAIARALIRQPRVLLLDEATS 1147
Cdd:pfam00005 81 RLG-----LLLKGLSKREKDARAEEALEKLGLGDlaDRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
978-1196 |
1.71e-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: 1.71e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 978 VTFNEVVFNYPT-RANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEakklnVQWLRAQL 1056
Cdd:cd03293 1 LEVRNVSKTYGGgGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEP-----VTGPGPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1057 GIVSQEPILFD-CSIAENIAYGDNSRVVPHDEIVRAAKEAnihpfIEtlpqkyntRVGDKGT------QLSGGQKQRIAI 1129
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNVALGLELQGVPKAEARERAEEL-----LE--------LVGLSGFenayphQLSGGMRQRVAL 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568932737 1130 ARALIRQPRVLLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLS-TIQNADLIVVIEN--GKVKE 1196
Cdd:cd03293 143 ARALAVDPDVLLLDEPFSALDALTREQLQEELLDiwRETGKTVLLVTHDIDeAVFLADRVVVLSArpGRIVA 214
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
990-1205 |
4.93e-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: 4.93e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 990 RANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQWLRAQLGIVSQEPIL---- 1065
Cdd:COG1124 15 GRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRVQMVFQDPYAslhp 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1066 ---FDCSIAE--NIAYGDNSRvvphDEIVRAAKEANIHP-FIETLPQkyntrvgdkgtQLSGGQKQRIAIARALIRQPRV 1139
Cdd:COG1124 95 rhtVDRILAEplRIHGLPDRE----ERIAELLEQVGLPPsFLDRYPH-----------QLSGGQRQRVAIARALILEPEL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568932737 1140 LLLDEATSALDTesekVVQ-EALD-----KAREGRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHGTHQQLLA 1205
Cdd:COG1124 160 LLLDEPTSALDV----SVQaEILNllkdlREERGLTYLFVSHDLAVVAHlCDRVAVMQNGRIVEELTVADLLA 228
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
992-1206 |
1.16e-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: 1.16e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 992 NVPVLQGLSLEVKKGQTLALVGSSGCGKSTV---VQLLERfydPMAGSVLLDGQE--AKKLNVQWLRAQLGIVSQEPILF 1066
Cdd:COG1126 13 DLEVLKGISLDVEKGEVVVIIGPSGSGKSTLlrcINLLEE---PDSGTITVDGEDltDSKKDINKLRRKVGMVFQQFNLF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1067 -DCSIAENIAYGdnSRVV---PHDEIVRAAKEAnihpfietLpqkynTRVG--DKG----TQLSGGQKQRIAIARALIRQ 1136
Cdd:COG1126 90 pHLTVLENVTLA--PIKVkkmSKAEAEERAMEL--------L-----ERVGlaDKAdaypAQLSGGQQQRVAIARALAME 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568932737 1137 PRVLLLDEATSALDTEsekVVQEALD--K--AREGRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHGTHQQLLAQ 1206
Cdd:COG1126 155 PKVMLFDEPTSALDPE---LVGEVLDvmRdlAKEGMTMVVVTHEMGFAREvADRVVFMDGGRIVEEGPPEEFFEN 226
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
338-533 |
1.49e-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: 153.71 E-value: 1.49e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 338 LEFSDVHFSYPSRAN-IKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRclreiI 416
Cdd:COG1116 8 LELRGVSKRFPTGGGgVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPD-----R 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 417 GVVSQEPVLFS-TTIAENIRYGrgnVTMDEIEKAVKEANAYDFImklpqkfdTLVGDRGA------QLSGGQKQRIAIAR 489
Cdd:COG1116 83 GVVFQEPALLPwLTVLDNVALG---LELRGVPKAERRERARELL--------ELVGLAGFedayphQLSGGMRQRVAIAR 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 568932737 490 ALVRNPKILLLDEATSALDTESEAEVQAALDK--AREGRTTIVIAH 533
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 ... |
338-533 |
2.84e-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: 2.84e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 338 LEFSDVHFSYPS-RANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRclreiI 416
Cdd:cd03293 1 LEVRNVSKTYGGgGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD-----R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 417 GVVSQEPVLFS-TTIAENIRYG---RGnVTMDEIEKAVKEANA----YDFIMKLPqkfdtlvgdrgAQLSGGQKQRIAIA 488
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNVALGlelQG-VPKAEARERAEELLElvglSGFENAYP-----------HQLSGGMRQRVALA 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 568932737 489 RALVRNPKILLLDEATSALDTESEAEVQAALDK--AREGRTTIVIAH 533
Cdd:cd03293 144 RALAVDPDVLLLDEPFSALDALTREQLQEELLDiwRETGKTVLLVTH 190
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
978-1196 |
3.71e-41 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 151.35 E-value: 3.71e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 978 VTFNEVVFNYPTRAN-VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQL---LERfydPMAGSVLLDGQEAKKLN----V 1049
Cdd:COG1136 5 LELRNLTKSYGTGEGeVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNIlggLDR---PTSGEVLIDGQDISSLSerelA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1050 QWLRAQLGIVSQEPILFDC-SIAENIA----YGDNSRVVPHDEIVRAAKEANIHPFIETLPqkyntrvgdkgTQLSGGQK 1124
Cdd:COG1136 82 RLRRRHIGFVFQFFNLLPElTALENVAlpllLAGVSRKERRERARELLERVGLGDRLDHRP-----------SQLSGGQQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568932737 1125 QRIAIARALIRQPRVLLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLSTIQNADLIVVIENGKVKE 1196
Cdd:COG1136 151 QRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRElnRELGTTIVMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
338-563 |
4.69e-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: 4.69e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 338 LEFSDVHFSYPSRaniKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLREI-- 415
Cdd:cd03261 1 IELRGLTKSFGGR---TVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLrr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 416 -IGVVSQEPVLF-STTIAENIRYG---RGNVTMDEIEKAVKeanaydfiMKLpqkfdTLVGDRG------AQLSGGQKQR 484
Cdd:cd03261 78 rMGMLFQSGALFdSLTVFENVAFPlreHTRLSEEEIREIVL--------EKL-----EAVGLRGaedlypAELSGGMKKR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 485 IAIARALVRNPKILLLDEATSALDTESEAEVQA-ALD-KAREGRTTIVIAHRLSTIRN-ADVIAGFEDGVIVEQGSHSEL 561
Cdd:cd03261 145 VALARALALDPELLLYDEPTAGLDPIASGVIDDlIRSlKKELGLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPEEL 224
|
..
gi 568932737 562 MK 563
Cdd:cd03261 225 RA 226
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
977-1199 |
9.30e-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: 9.30e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 977 SVTFNEVVFNYptrANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQwlRAQL 1056
Cdd:COG3842 5 ALELENVSKRY---GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPE--KRNV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1057 GIVSQEPILF-DCSIAENIAYGDNSRVVPHDEIVRAAKEA----NIHPFIETLPqkyntrvgdkgTQLSGGQKQRIAIAR 1131
Cdd:COG3842 80 GMVFQDYALFpHLTVAENVAFGLRMRGVPKAEIRARVAELlelvGLEGLADRYP-----------HQLSGGQQQRVALAR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568932737 1132 ALIRQPRVLLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLS---TIqnADLIVVIENGKVKEHGT 1199
Cdd:COG3842 149 ALAPEPRVLLLDEPLSALDAKLREEMREELRRlqRELGITFIYVTHDQEealAL--ADRIAVMNDGRIEQVGT 219
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
978-1206 |
1.02e-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: 158.14 E-value: 1.02e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 978 VTFNEVVFNYPTRAnVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDP---MAGSVLLDGQEAKKLNVQWLRA 1054
Cdd:COG1123 5 LEVRDLSVRYPGGD-VPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHggrISGEVLLDGRDLLELSEALRGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1055 QLGIVSQEPI--LFDCSIAENIAYGDNSRVVPHDEIVRAAKEANIHPFIETLPQKYNTrvgdkgtQLSGGQKQRIAIARA 1132
Cdd:COG1123 84 RIGMVFQDPMtqLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPH-------QLSGGQRQRVAIAMA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568932737 1133 LIRQPRVLLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLSTI-QNADLIVVIENGKVKEHGTHQQLLAQ 1206
Cdd:COG1123 157 LALDPDLLIADEPTTALDVTTQAEILDLLRElqRERGTTVLLITHDLGVVaEIADRVVVMDDGRIVEDGPPEEILAA 233
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
338-552 |
1.05e-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: 1.05e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 338 LEFSDVHFSYpsrANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRN--FNVRCLREI 415
Cdd:cd03262 1 IEIKNLHKSF---GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDdkKNINELRQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 416 IGVVSQEPVLFS-TTIAENIRYGRgnVTMDEIEKAVKEANAYDFIMK--LPQKFDtlvgDRGAQLSGGQKQRIAIARALV 492
Cdd:cd03262 78 VGMVFQQFNLFPhLTVLENITLAP--IKVKGMSKAEAEERALELLEKvgLADKAD----AYPAQLSGGQQQRVAIARALA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568932737 493 RNPKILLLDEATSALDTESEAEVQAAL-DKAREGRTTIVIAHRLSTIRN-ADVIAGFEDGVI 552
Cdd:cd03262 152 MNPKVMLFDEPTSALDPELVGEVLDVMkDLAEEGMTMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
978-1206 |
2.85e-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: 2.85e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 978 VTFNEVVFNYPTRAN-VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQ---LLERfydPMAGSVLLDGQEAKKLN---VQ 1050
Cdd:cd03258 2 IELKNVSKVFGDTGGkVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRcinGLER---PTSGSVLVDGTDLTLLSgkeLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1051 WLRAQLGIVSQEPILFDC-SIAENIAYGDNSRVVPHDEIVRAAKEanihpfieTLPQkyntrVG--DKG----TQLSGGQ 1123
Cdd:cd03258 79 KARRRIGMIFQHFNLLSSrTVFENVALPLEIAGVPKAEIEERVLE--------LLEL-----VGleDKAdaypAQLSGGQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1124 KQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHGTH 1200
Cdd:cd03258 146 KQRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDinRELGLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTV 225
|
....*.
gi 568932737 1201 QQLLAQ 1206
Cdd:cd03258 226 EEVFAN 231
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
978-1207 |
4.13e-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: 4.13e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 978 VTFNEVVFNYPtRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAK-KLNVQWLRAQL 1056
Cdd:TIGR04520 1 IEVENVSFSYP-ESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLdEENLWEIRKKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1057 GIVSQEPilfD----CSIAEN-IAYGDNSRVVPHDEIVR----AAKEANIHPFIETLPQKyntrvgdkgtqLSGGQKQRI 1127
Cdd:TIGR04520 80 GMVFQNP---DnqfvGATVEDdVAFGLENLGVPREEMRKrvdeALKLVGMEDFRDREPHL-----------LSGGQKQRV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1128 AIARALIRQPRVLLLDEATSALDTESEKVVQEALDKAR--EGRTCIVIAHRLSTIQNADLIVVIENGKVKEHGTHQQLLA 1205
Cdd:TIGR04520 146 AIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNkeEGITVISITHDMEEAVLADRVIVMNKGKIVAEGTPREIFS 225
|
..
gi 568932737 1206 QK 1207
Cdd:TIGR04520 226 QV 227
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
992-1206 |
4.15e-40 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 148.67 E-value: 4.15e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 992 NVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQWlRAQLGIVSQEPILF-DCSI 1070
Cdd:COG1131 12 DKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEV-RRRIGYVPQEPALYpDLTV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1071 AENIAYGDNSRVVPHDEIVRAAKEAnihpfIET--LPQKYNTRVGdkgtQLSGGQKQRIAIARALIRQPRVLLLDEATSA 1148
Cdd:COG1131 91 RENLRFFARLYGLPRKEARERIDEL-----LELfgLTDAADRKVG----TLSGGMKQRLGLALALLHDPELLILDEPTSG 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1149 LDTESEKVVQEALDK-AREGRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHGTHQQLLAQ 1206
Cdd:COG1131 162 LDPEARRELWELLRElAAEGKTVLLSTHYLEEAERlCDRVAIIDKGRIVADGTPDELKAR 221
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
338-578 |
5.68e-40 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 152.15 E-value: 5.68e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 338 LEFSDVHFSYpsrANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDI-------RNfnvr 410
Cdd:COG3839 4 LELENVSKSY---GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVtdlppkdRN---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 411 clreiIGVVSQEPVLF-STTIAENIRYG---RGnVTMDEIEKAVKEANAydfIMKLpqkfDTLVGDRGAQLSGGQKQRIA 486
Cdd:COG3839 77 -----IAMVFQSYALYpHMTVYENIAFPlklRK-VPKAEIDRRVREAAE---LLGL----EDLLDRKPKQLSGGQRQRVA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 487 IARALVRNPKILLLDEATSALD------TESE-AEVQAALdkareGRTTIVIAHRLS---TIrnADVIAGFEDGVIVEQG 556
Cdd:COG3839 144 LGRALVREPKVFLLDEPLSNLDaklrveMRAEiKRLHRRL-----GTTTIYVTHDQVeamTL--ADRIAVMNDGRIQQVG 216
|
250 260
....*....|....*....|..
gi 568932737 557 SHSELmkkegiYFRLVNMQTAG 578
Cdd:COG3839 217 TPEEL------YDRPANLFVAG 232
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
338-556 |
1.24e-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: 1.24e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 338 LEFSDVHFSYpsrANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYD--P---TEGKISIDGQDI--RNFNVR 410
Cdd:COG1117 12 IEVRNLNVYY---GDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDliPgarVEGEILLDGEDIydPDVDVV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 411 CLREIIGVVSQEPVLFSTTIAENIRYG------RGNVTMDEI-EKAVKEANAYDfimklpqkfdtLVGDR----GAQLSG 479
Cdd:COG1117 89 ELRRRVGMVFQKPNPFPKSIYDNVAYGlrlhgiKSKSELDEIvEESLRKAALWD-----------EVKDRlkksALGLSG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 480 GQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKAREgRTTIVI-------AHRLStirnaDVIAGFEDGVI 552
Cdd:COG1117 158 GQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKK-DYTIVIvthnmqqAARVS-----DYTAFFYLGEL 231
|
....
gi 568932737 553 VEQG 556
Cdd:COG1117 232 VEFG 235
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
58-311 |
1.51e-39 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This group includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins.
Pssm-ID: 350001 [Multi-domain] Cd Length: 289 Bit Score: 148.86 E-value: 1.51e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 58 TRYAYYYSGLGGGVLVAAYIQVSFWTLAAGRQIKKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDDVSKISEGIGDKVG 137
Cdd:cd18557 36 NELALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFSSLLRQEIAFFDKHKTGELTSRLSSDTSVLQSAVTDNLS 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 138 MFFQAIATFFAGFIVGFIRGWKLTLVIMAISPILGLSTAVWAKILSTFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQN 217
Cdd:cd18557 116 QLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASKIYGRYIRKLSKEVQDALAKAGQVAEESLSNIRTVRSFSAEE 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 218 KELERYQKHLENAKKIGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTIGNAMT-VFFSILIgAFSVGQAAP 296
Cdd:cd18557 196 KEIRRYSEALDRSYRLARKKALANALFQGITSLLIYLSLLLVLWYGGYLVLSGQLTVGELTSfILYTIMV-ASSVGGLSS 274
|
250
....*....|....*
gi 568932737 297 CIDAFANARGAAYVI 311
Cdd:cd18557 275 LLADIMKALGASERV 289
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
983-1204 |
1.64e-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: 1.64e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 983 VVFNYPTRanvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQWLRAQLGIVSQE 1062
Cdd:COG1120 7 LSVGYGGR---PVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYVPQE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1063 PIL-FDCSIAENIAYG------DNSRVVPHD-EIVRAA-KEANIHPFIEtlpQKYntrvgdkgTQLSGGQKQRIAIARAL 1133
Cdd:COG1120 84 PPApFGLTVRELVALGryphlgLFGRPSAEDrEAVEEAlERTGLEHLAD---RPV--------DELSGGERQRVLIARAL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568932737 1134 IRQPRVLLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLS-TIQNADLIVVIENGKVKEHGTHQQLL 1204
Cdd:COG1120 153 AQEPPLLLLDEPTSHLDLAHQLEVLELLRRlaRERGRTVVMVLHDLNlAARYADRLVLLKDGRIVAQGPPEEVL 226
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
338-566 |
2.50e-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: 146.54 E-value: 2.50e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 338 LEFSDVHFSYPSRaniKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLREIiG 417
Cdd:COG4555 2 IEVENLSKKYGKV---PALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQI-G 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 418 VVSQEPVLFST-TIAENIRY-GRGNvtmdEIEKAVKEANAYDFI--MKLPQKFDTLVGDrgaqLSGGQKQRIAIARALVR 493
Cdd:COG4555 78 VLPDERGLYDRlTVRENIRYfAELY----GLFDEELKKRIEELIelLGLEEFLDRRVGE----LSTGMKKKVALARALVH 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568932737 494 NPKILLLDEATSALDTESEAEVQAALDKAR-EGRTTIVIAHRLSTIRN-ADVIAGFEDGVIVEQGSHSELMKKEG 566
Cdd:COG4555 150 DPKVLLLDEPTNGLDVMARRLLREILRALKkEGKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEIG 224
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
978-1196 |
2.62e-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: 2.62e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 978 VTFNEVVFNYPTRAN-VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEakklnVQWLRAQL 1056
Cdd:COG1116 8 LELRGVSKRFPTGGGgVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKP-----VTGPGPDR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1057 GIVSQEPILFD-CSIAENIAYGDNSRVVPHDEIVRAAKEAnihpfIEtlpqkyntRVGDKG------TQLSGGQKQRIAI 1129
Cdd:COG1116 83 GVVFQEPALLPwLTVLDNVALGLELRGVPKAERRERAREL-----LE--------LVGLAGfedaypHQLSGGMRQRVAI 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568932737 1130 ARALIRQPRVLLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAH------RLstiqnADLIVVIEN--GKVKE 1196
Cdd:COG1116 150 ARALANDPEVLLMDEPFGALDALTRERLQDELLRlwQETGKTVLFVTHdvdeavFL-----ADRVVVLSArpGRIVE 221
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
345-1210 |
2.93e-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: 2.93e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 345 FSYPSRANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQdirnfnvrclreiIGVVSQEPV 424
Cdd:TIGR01271 431 FSNFSLYVTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR-------------ISFSPQTSW 497
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 425 LFSTTIAENIRYGrgnVTMDEIE--KAVKEANAYDFIMKLPQKFDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDE 502
Cdd:TIGR01271 498 IMPGTIKDNIIFG---LSYDEYRytSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDS 574
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 503 ATSALDTESEAEV-QAALDKAREGRTTIVIAHRLSTIRNADVIAGFEDGVIVEQGSHSELMKKEGIY------------- 568
Cdd:TIGR01271 575 PFTHLDVVTEKEIfESCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAKRPDFsslllgleafdnf 654
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 569 ------------------------------------------------------------FRLVNMQTAGSQILSEEFEV 588
Cdd:TIGR01271 655 saerrnsiltetlrrvsidgdstvfsgpetikqsfkqpppefaekrkqsiilnpiasarkFSFVQMGPQKAQATTIEDAV 734
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 589 -ELSDEKAA--------------GDVAPNGW----------------------KARIFRNSTKKSLKSPHQNRL------ 625
Cdd:TIGR01271 735 rEPSERKFSlvpedeqgeeslprGNQYHHGLqhqaqrrqsvlqlmthsnrgenRREQLQTSFRKKSSITQQNELaseldi 814
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 626 -------------DEETNELD---------ANVPPVS----FLKVLKLNKTEWPYFVVGTVCAIANGALQPAFSIILSEM 679
Cdd:TIGR01271 815 ysrrlskdsvyeiSEEINEEDlkecfaderENVFETTtwntYLRYITTNRNLVFVLIFCLVIFLAEVAASLLGLWLITDN 894
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 680 IAIFG--PGDDAVKQQKCNMFSL------------VFLGLGVLSFFTFFLQGFTFGKAGEILTTRLRSMAFKAMLRQDMS 745
Cdd:TIGR01271 895 PSAPNyvDQQHANASSPDVQKPViitptsayyifyIYVGTADSVLALGFFRGLPLVHTLLTVSKRLHEQMLHSVLQAPMA 974
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 746 WFDDHKnsTGALSTRLATDAAQVQGATG-TRLALIAQNTANLGTGIIISFIYGWqltlLLLSVVPFIAVAGIVEMKMLAG 824
Cdd:TIGR01271 975 VLNTMK--AGRILNRFTKDMAIIDDMLPlTLFDFIQLTLIVLGAIFVVSVLQPY----IFIAAIPVAVIFIMLRAYFLRT 1048
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 825 NAKRDKKEMEAAGKIATEAIENIR---TVVSLTQERKFESMYVEKLHGPYRN-SVRKAHIYGITFSISQAFMYFSYAGCF 900
Cdd:TIGR01271 1049 SQQLKQLESEARSPIFSHLITSLKglwTIRAFGRQSYFETLFHKALNLHTANwFLYLSTLRWFQMRIDIIFVFFFIAVTF 1128
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 901 -RFGSYLIVNGHMrfkDVILVFSAIVLGAVALGHASSFAPDYAKAKLSAAYLF-SLFERQP---------------LIDS 963
Cdd:TIGR01271 1129 iAIGTNQDGEGEV---GIILTLAMNILSTLQWAVNSSIDVDGLMRSVSRVFKFiDLPQEEPrpsggggkyqlstvlVIEN 1205
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 964 YSGEGLWPDkfEGSVTFNEVVFNYpTRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDpMAGSVLLDGQE 1043
Cdd:TIGR01271 1206 PHAQKCWPS--GGQMDVQGLTAKY-TEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVS 1281
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1044 AKKLNVQWLRAQLGIVSQEPILFDCSIAENIaygDNSRVVPHDEIVRAAKEANIHPFIETLPQKYNTRVGDKGTQLSGGQ 1123
Cdd:TIGR01271 1282 WNSVTLQTWRKAFGVIPQKVFIFSGTFRKNL---DPYEQWSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGH 1358
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1124 KQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIENGKVKEHGTHQQL 1203
Cdd:TIGR01271 1359 KQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKL 1438
|
....*..
gi 568932737 1204 LAQKGIY 1210
Cdd:TIGR01271 1439 LNETSLF 1445
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
338-563 |
3.56e-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: 3.56e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 338 LEFSDVHFSYPSRAN-IKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDP---TEGKISIDGQDIRNFNVRCLR 413
Cdd:COG0444 2 LEVRNLKVYFPTRRGvVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 414 EI----IGVVSQEPvlFS---------TTIAENIRYGRGnVTMDEIEKAVKEA-------NAYDFIMKLPQkfdtlvgdr 473
Cdd:COG0444 82 KIrgreIQMIFQDP--MTslnpvmtvgDQIAEPLRIHGG-LSKAEARERAIELlervglpDPERRLDRYPH--------- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 474 gaQLSGGQKQRIAIARALVRNPKILLLDEATSALDteseAEVQAA-LD-----KAREGRTTIVIAHRLSTIRN-ADVIA- 545
Cdd:COG0444 150 --ELSGGMRQRVMIARALALEPKLLIADEPTTALD----VTIQAQiLNllkdlQRELGLAILFITHDLGVVAEiADRVAv 223
|
250 260
....*....|....*....|
gi 568932737 546 --GfedGVIVEQGSHSELMK 563
Cdd:COG0444 224 myA---GRIVEEGPVEELFE 240
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
978-1193 |
5.21e-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: 5.21e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 978 VTFNEVVFNYPTRANV--PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLL--ErfYDPMAGSVLLDGQEAkklnvqwlr 1053
Cdd:cd03250 1 ISVEDASFTWDSGEQEtsFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALlgE--LEKLSGSVSVPGSIA--------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1054 aqlgIVSQEPILFDCSIAENIAYG---DNSRVvphDEIVRAAKeanIHPFIETLPQKYNTRVGDKGTQLSGGQKQRIAIA 1130
Cdd:cd03250 70 ----YVSQEPWIQNGTIRENILFGkpfDEERY---EKVIKACA---LEPDLEILPDGDLTEIGEKGINLSGGQKQRISLA 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568932737 1131 RALIRQPRVLLLDEATSALDTES-----EKVVQEALdkaREGRTCIVIAHRLSTIQNADLIVVIENGK 1193
Cdd:cd03250 140 RAVYSDADIYLLDDPLSAVDAHVgrhifENCILGLL---LNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
987-1199 |
5.33e-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: 5.33e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 987 YPTRAN-VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQ---LLERfydPMAGSVLLDGQEAKKLNVQWLRA---QLGIV 1059
Cdd:COG1135 11 FPTKGGpVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRcinLLER---PTSGSVLVDGVDLTALSERELRAarrKIGMI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1060 SQEPILFD-CSIAENIAY-----GdnsrvVPHDEIvraakEANIHPFIEtlpqkyntRVG--DKG----TQLSGGQKQRI 1127
Cdd:COG1135 88 FQHFNLLSsRTVAENVALpleiaG-----VPKAEI-----RKRVAELLE--------LVGlsDKAdaypSQLSGGQKQRV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568932737 1128 AIARALIRQPRVLLLDEATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHGT 1199
Cdd:COG1135 150 GIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRelGLTIVLITHEMDVVRRiCDRVAVLENGRIVEQGP 224
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
338-552 |
8.25e-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: 8.25e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 338 LEFSDVHFSYPSRaniKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNfNVRCLREIIG 417
Cdd:cd03230 1 IEVRNLSKRYGKK---TALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 418 VVSQEPVLFST-TIAENIRYgrgnvtmdeiekavkeanaydfimklpqkfdtlvgdrgaqlSGGQKQRIAIARALVRNPK 496
Cdd:cd03230 77 YLPEEPSLYENlTVRENLKL-----------------------------------------SGGMKQRLALAQALLHDPE 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 568932737 497 ILLLDEATSALDTESEAEVQAALDK-AREGRTTIVIAHRLSTIRN-ADVIAGFEDGVI 552
Cdd:cd03230 116 LLILDEPTSGLDPESRREFWELLRElKKEGKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
981-1206 |
1.08e-38 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 145.93 E-value: 1.08e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 981 NEVVFNYPtRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQWLRAQLGIVS 1060
Cdd:PRK13635 9 EHISFRYP-DAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGMVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1061 QEPilfD-----CSIAENIAYGDNSRVVPHDEIVR----AAKEANIHPFIETLPQKyntrvgdkgtqLSGGQKQRIAIAR 1131
Cdd:PRK13635 88 QNP---DnqfvgATVQDDVAFGLENIGVPREEMVErvdqALRQVGMEDFLNREPHR-----------LSGGQKQRVAIAG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1132 ALIRQPRVLLLDEATSALDTESEkvvQEALD-----KAREGRTCIVIAHRLSTIQNADLIVVIENGKVKEHGTHQQLLAQ 1206
Cdd:PRK13635 154 VLALQPDIIILDEATSMLDPRGR---REVLEtvrqlKEQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFKS 230
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
338-561 |
1.60e-38 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 144.43 E-value: 1.60e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 338 LEFSDVHFSYPSRAniKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLREI-- 415
Cdd:COG3638 3 LELRNLSKRYPGGT--PALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRLrr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 416 -IGVVSQEPVLFS-TTIAENI-----------RYGRGNVTMDEIEKAvkeanaydfimklpqkFDTL--VG------DRG 474
Cdd:COG3638 81 rIGMIFQQFNLVPrLSVLTNVlagrlgrtstwRSLLGLFPPEDRERA----------------LEALerVGladkayQRA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 475 AQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAAL-DKARE-GRTTIVIAHRLSTIRN-ADVIAGFEDGV 551
Cdd:COG3638 145 DQLSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLrRIAREdGITVVVNLHQVDLARRyADRIIGLRDGR 224
|
250
....*....|
gi 568932737 552 IVEQGSHSEL 561
Cdd:COG3638 225 VVFDGPPAEL 234
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
339-567 |
2.87e-38 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 144.36 E-value: 2.87e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 339 EFSDVHFSYPSRANIkILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLREIIGV 418
Cdd:PRK13632 9 KVENVSFSYPNSENN-ALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 419 VSQEP---VLFSTT---IA---ENIRYGRgNVTMDEIEKAVKEANAYDFIMKLPQKfdtlvgdrgaqLSGGQKQRIAIAR 489
Cdd:PRK13632 88 IFQNPdnqFIGATVeddIAfglENKKVPP-KKMKDIIDDLAKKVGMEDYLDKEPQN-----------LSGGQKQRVAIAS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 490 ALVRNPKILLLDEATSALDTESEAEVQAALDKAREGR--TTIVIAHRLSTIRNADVIAGFEDGVIVEQGSHSELMKKEGI 567
Cdd:PRK13632 156 VLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRkkTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEILNNKEI 235
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
339-560 |
4.08e-38 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 146.48 E-value: 4.08e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 339 EFSDVHFSYPSRAN-IKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLREI-- 415
Cdd:PRK11153 3 ELKNISKVFPQGGRtIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKArr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 416 -IGVVSQE-PVLFSTTIAENIRYGR--GNVTMDEIEKAVKE----------ANAYdfimklPqkfdtlvgdrgAQLSGGQ 481
Cdd:PRK11153 83 qIGMIFQHfNLLSSRTVFDNVALPLelAGTPKAEIKARVTEllelvglsdkADRY------P-----------AQLSGGQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 482 KQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKA-REGRTTIV-IAHRLSTIRN-ADVIAGFEDGVIVEQGSH 558
Cdd:PRK11153 146 KQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDInRELGLTIVlITHEMDVVKRiCDRVAVIDAGRLVEQGTV 225
|
..
gi 568932737 559 SE 560
Cdd:PRK11153 226 SE 227
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
338-554 |
6.04e-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: 6.04e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 338 LEFSDVHFSYPsrANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQD---IRNFNVRCLRE 414
Cdd:COG2884 2 IRFENVSKRYP--GGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDlsrLKRREIPYLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 415 IIGVVSQE-PVLFSTTIAENIRY-----GRgnvTMDEIEKAVKEAnaydfIMK--LPQKFDTLVgdrgAQLSGGQKQRIA 486
Cdd:COG2884 80 RIGVVFQDfRLLPDRTVYENVALplrvtGK---SRKEIRRRVREV-----LDLvgLSDKAKALP----HELSGGEQQRVA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568932737 487 IARALVRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIA-HRLSTIRNAD--VIAgFEDGVIVE 554
Cdd:COG2884 148 IARALVNRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIAtHDLELVDRMPkrVLE-LEDGRLVR 217
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
979-1208 |
1.02e-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: 141.92 E-value: 1.02e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 979 TFNEVVFNYPtraNVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNvQWLRAQLGI 1058
Cdd:COG4555 3 EVENLSKKYG---KVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEP-REARRQIGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1059 VSQEPILFD-CSIAENIAYGDNSRVVPHDEIVRAAKEanihpFIE--TLPQKYNTRVGDkgtqLSGGQKQRIAIARALIR 1135
Cdd:COG4555 79 LPDERGLYDrLTVRENIRYFAELYGLFDEELKKRIEE-----LIEllGLEEFLDRRVGE----LSTGMKKKVALARALVH 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568932737 1136 QPRVLLLDEATSALDTESEKVVQEALDKAREGRTCIVIA-HRLSTIQN-ADLIVVIENGKVKEHGTHQQLLAQKG 1208
Cdd:COG4555 150 DPKVLLLDEPTNGLDVMARRLLREILRALKKEGKTVLFSsHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEIG 224
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
995-1203 |
1.10e-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: 1.10e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 995 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYD--P---MAGSVLLDGQE--AKKLNVQWLRAQLGIVSQEPILFD 1067
Cdd:COG1117 26 ALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDliPgarVEGEILLDGEDiyDPDVDVVELRRRVGMVFQKPNPFP 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1068 CSIAENIAYG-----DNSRVVpHDEIVRAA-KEANihpfietLPQKYNTRVGDKGTQLSGGQKQRIAIARALIRQPRVLL 1141
Cdd:COG1117 106 KSIYDNVAYGlrlhgIKSKSE-LDEIVEESlRKAA-------LWDEVKDRLKKSALGLSGGQQQRLCIARALAVEPEVLL 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568932737 1142 LDEATSALDTESEKVVQEALDKAREgRTCIVI-------AHRLStiqnaDLIVVIENGKVKEHGTHQQL 1203
Cdd:COG1117 178 MDEPTSALDPISTAKIEELILELKK-DYTIVIvthnmqqAARVS-----DYTAFFYLGELVEFGPTEQI 240
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
360-562 |
1.16e-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: 142.78 E-value: 1.16e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 360 NLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLREI----IGVVSQEPVLF-STTIAENI 434
Cdd:cd03294 44 SLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELrrkkISMVFQSFALLpHRTVLENV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 435 RYG---RGNVTMDEIEKAVKEANAY---DFIMKLPQkfdtlvgdrgaQLSGGQKQRIAIARALVRNPKILLLDEATSALD 508
Cdd:cd03294 124 AFGlevQGVPRAEREERAAEALELVgleGWEHKYPD-----------ELSGGMQQRVGLARALAVDPDILLMDEAFSALD 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 568932737 509 TESEAEVQAALDK--AREGRTTIVIAHRLS-TIRNADVIAGFEDGVIVEQGSHSELM 562
Cdd:cd03294 193 PLIRREMQDELLRlqAELQKTIVFITHDLDeALRLGDRIAIMKDGRLVQVGTPEEIL 249
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
978-1194 |
1.46e-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: 140.70 E-value: 1.46e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 978 VTFNEVVFNYPTRAN-VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQWL---- 1052
Cdd:cd03255 1 IELKNLSKTYGGGGEkVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1053 RAQLGIVSQE----PILfdcSIAENIAYGDNSRVVPHDEIVRAAKEAnihpfIET--LPQKYNTRVGdkgtQLSGGQKQR 1126
Cdd:cd03255 81 RRHIGFVFQSfnllPDL---TALENVELPLLLAGVPKKERRERAEEL-----LERvgLGDRLNHYPS----ELSGGQQQR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1127 IAIARALIRQPRVLLLDEATSALDTESEKVVQEAL-DKAREGRTCIVIA-HRLSTIQNADLIVVIENGKV 1194
Cdd:cd03255 149 VAIARALANDPKIILADEPTGNLDSETGKEVMELLrELNKEAGTTIVVVtHDPELAEYADRIIELRDGKI 218
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
979-1193 |
1.64e-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: 1.64e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 979 TFNEVVFNYPTRanvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQWLRAQLGI 1058
Cdd:cd00267 1 EIENLSFRYGGR---TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1059 VSQepilfdcsiaeniaygdnsrvvphdeivraakeanihpfietlpqkyntrvgdkgtqLSGGQKQRIAIARALIRQPR 1138
Cdd:cd00267 78 VPQ---------------------------------------------------------LSGGQRQRVALARALLLNPD 100
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 568932737 1139 VLLLDEATSALDTESEKVVQEALDK-AREGRTCIVIAHRLSTIQNA-DLIVVIENGK 1193
Cdd:cd00267 101 LLLLDEPTSGLDPASRERLLELLRElAEEGRTVIIVTHDPELAELAaDRVIVLKDGK 157
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
989-1193 |
1.81e-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: 1.81e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 989 TRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLN--VQWLRAQLGIVSQEPILF 1066
Cdd:cd03229 9 RYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEdeLPPLRRRIGMVFQDFALF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1067 -DCSIAENIAYGdnsrvvphdeivraakeanihpfietlpqkyntrvgdkgtqLSGGQKQRIAIARALIRQPRVLLLDEA 1145
Cdd:cd03229 89 pHLTVLENIALG-----------------------------------------LSGGQQQRVALARALAMDPDVLLLDEP 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 568932737 1146 TSALDTESEKVVQEALD--KAREGRTCIVIAHRLSTIQN-ADLIVVIENGK 1193
Cdd:cd03229 128 TSALDPITRREVRALLKslQAQLGITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
335-571 |
2.37e-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: 2.37e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 335 KGNLEFSDVHFSYPSRANIkILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLRE 414
Cdd:TIGR00957 1282 RGRVEFRNYCLRYREDLDL-VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRF 1360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 415 IIGVVSQEPVLFSTTIAENIRyGRGNVTMDEIEKAVKEANAYDFIMKLPQKFDTLVGDRGAQLSGGQKQRIAIARALVRN 494
Cdd:TIGR00957 1361 KITIIPQDPVLFSGSLRMNLD-PFSQYSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRK 1439
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568932737 495 PKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTIRNADVIAGFEDGVIVEQGSHSELMKKEGIYFRL 571
Cdd:TIGR00957 1440 TKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRGIFYSM 1516
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
338-561 |
2.45e-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: 2.45e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 338 LEFSDVHFSYPSraNIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLREI-- 415
Cdd:cd03256 1 IEVENLSKTYPN--GKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLrr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 416 -IGVVSQEPVLFS-TTIAENIRYGR-----------GNVTMDEIEKAVKEANAYDFIMKLPQkfdtlvgdRGAQLSGGQK 482
Cdd:cd03256 79 qIGMIFQQFNLIErLSVLENVLSGRlgrrstwrslfGLFPKEEKQRALAALERVGLLDKAYQ--------RADQLSGGQQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 483 QRIAIARALVRNPKILLLDEATSALDTESEAEVQAAL-DKARE-GRTTIVIAHRLSTIR-NADVIAGFEDGVIVEQGSHS 559
Cdd:cd03256 151 QRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLkRINREeGITVIVSLHQVDLAReYADRIVGLKDGRIVFDGPPA 230
|
..
gi 568932737 560 EL 561
Cdd:cd03256 231 EL 232
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
60-569 |
8.85e-37 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 151.81 E-value: 8.85e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 60 YAYYYSGLG-GGVLVAayIQVSFW----TLAAGrqiKKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDDVSKISEGIGD 134
Cdd:PLN03130 955 YNLIYALLSfGQVLVT--LLNSYWlimsSLYAA---KRLHDAMLGSILRAPMSFFHTNPLGRIINRFAKDLGDIDRNVAV 1029
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 135 KVGMF----FQAIATFFagfIVGFIRgwklTLVIMAISPILGLSTAVWAKILSTFSD-KELAAYAKAGAVAE--EALGAI 207
Cdd:PLN03130 1030 FVNMFlgqiFQLLSTFV---LIGIVS----TISLWAIMPLLVLFYGAYLYYQSTAREvKRLDSITRSPVYAQfgEALNGL 1102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 208 RTVIAFGGQNKELERYQKHLENAKKIGIKKaISANISMGIAF-----LLIY--ASYAL----------AFWYGSTLVISK 270
Cdd:PLN03130 1103 STIRAYKAYDRMAEINGRSMDNNIRFTLVN-MSSNRWLAIRLetlggLMIWltASFAVmqngraenqaAFASTMGLLLSY 1181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 271 EYTIGNAMTvffsiligafSVGQAAPCIDAFANA--RGAAYVifDIIDNNPKIdsfsERGHKPDN---IKGNLEFSDVHF 345
Cdd:PLN03130 1182 ALNITSLLT----------AVLRLASLAENSLNAveRVGTYI--DLPSEAPLV----IENNRPPPgwpSSGSIKFEDVVL 1245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 346 SYpsRANIK-ILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLREIIGVVSQEPV 424
Cdd:PLN03130 1246 RY--RPELPpVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPV 1323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 425 LFSTTIAENIR-YGRGNVTmdEIEKAVKEANAYDFIMKLPQKFDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEA 503
Cdd:PLN03130 1324 LFSGTVRFNLDpFNEHNDA--DLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEA 1401
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568932737 504 TSALDTESEAEVQAALDKAREGRTTIVIAHRLSTIRNADVIAGFEDGVIVEQGSHSELMKKEGIYF 569
Cdd:PLN03130 1402 TAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEGSAF 1467
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
52-308 |
1.22e-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: 140.38 E-value: 1.22e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 52 ILEEEMTRYAYYYSGLGGGVLVAA---YIQVSFWTLAAGRQIKKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDDVSKI 128
Cdd:cd07346 30 IPAGDLSLLLWIALLLLLLALLRAllsYLRRYLAARLGQRVVFDLRRDLFRHLQRLSLSFFDRNRTGDLMSRLTSDVDAV 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 129 SEGIGDKVGMFFQAIATFFAGFIVGFIRGWKLTLVIMAISPILGLSTAVWAKILSTFSDKELAAYAKAGAVAEEALGAIR 208
Cdd:cd07346 110 QNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILRYFRRRIRKASREVRESLAELSAFLQESLSGIR 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 209 TVIAFGGQNKELERYQKHLENAKKIGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTIGnAMTVFFSILIGA 288
Cdd:cd07346 190 VVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTALGTALVLLYGGYLVLQGSLTIG-ELVAFLAYLGML 268
|
250 260
....*....|....*....|.
gi 568932737 289 FS-VGQAAPCIDAFANARGAA 308
Cdd:cd07346 269 FGpIQRLANLYNQLQQALASL 289
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
658-950 |
2.05e-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: 139.62 E-value: 2.05e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 658 GTVCAIANGALQPAFSIILSEMIAIFGPGDDavkQQKCNMFSLVFLGLGVLSFFTFFLQGFTFGKAGEILTTRLRSMAFK 737
Cdd:cd18557 1 GLLFLLISSAAQLLLPYLIGRLIDTIIKGGD---LDVLNELALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 738 AMLRQDMSWFDDHKnsTGALSTRLATDAAQVQGATGTRLALIAQNTANLGTGIIISFIYGWQLTLLLLSVVPFIAVAGIV 817
Cdd:cd18557 78 SLLRQEIAFFDKHK--TGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASKI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 818 EMKMLAGNAKRDKKEMEAAGKIATEAIENIRTVVSLTQERKFESMYVEKLHGPYRNSVRKAHIYGITFSISQAFMYFSYA 897
Cdd:cd18557 156 YGRYIRKLSKEVQDALAKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQGITSLLIYLSLL 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 568932737 898 GCFRFGSYLIVNGHMRFKDVI--LVFSAIVlgAVALGHASSFAPDYAKAkLSAAY 950
Cdd:cd18557 236 LVLWYGGYLVLSGQLTVGELTsfILYTIMV--ASSVGGLSSLLADIMKA-LGASE 287
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
655-948 |
2.24e-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: 139.61 E-value: 2.24e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 655 FVVGTVCAIANGALQPAFSIILSEMIAIFGPGDDavkQQKCNMFSLVFLGLGVLSFFTFFLQGFTFGKAGEILTTRLRSM 734
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLLIDDVIPAGD---LSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 735 AFKAMLRQDMSWFDdhKNSTGALSTRLATDAAQVQGATGTRLALIAQNTANLGTGIIISFIYGWQLTLLLLSVVPFIAVA 814
Cdd:cd07346 78 LFRHLQRLSLSFFD--RNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 815 GIVEMKMLAGNAKRDKKEMEAAGKIATEAIENIRTVVSLTQERKFESMYVEKLHGPYRNSVRKAHIYGITFSISQAFMYF 894
Cdd:cd07346 156 LRYFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTAL 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 568932737 895 SYAGCFRFGSYLIVNGHMRFKDVILVFSAIVLGAVALGHASSFAPDYAKAKLSA 948
Cdd:cd07346 236 GTALVLLYGGYLVLQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASL 289
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
994-1205 |
2.31e-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: 2.31e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 994 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNV---QWLRAQLGIVSQEPILFDC-S 1069
Cdd:COG1127 19 VVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEkelYELRRRIGMLFQGGALFDSlT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1070 IAENIAYG-DNSRVVPHDEIVRAAKEAnihpfIEtlpqkyntRVGDKGT------QLSGGQKQRIAIARALIRQPRVLLL 1142
Cdd:COG1127 99 VFENVAFPlREHTDLSEAEIRELVLEK-----LE--------LVGLPGAadkmpsELSGGMRKRVALARALALDPEILLY 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568932737 1143 DEATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHGTHQQLLA 1205
Cdd:COG1127 166 DEPTAGLDPITSAVIDELIRELRDelGLTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPEELLA 231
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
338-550 |
2.43e-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: 2.43e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 338 LEFSDVHFSYPSRANI--KILKGLNLKVKSGQTVALVGNSGCGKSTtvqLLQRL---YDPTEGKISIDGQdirnfnvrcl 412
Cdd:cd03250 1 ISVEDASFTWDSGEQEtsFTLKDINLEVPKGELVAIVGPVGSGKSS---LLSALlgeLEKLSGSVSVPGS---------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 413 reiIGVVSQEPVLFSTTIAENIRYGRgnvTMDEIE-KAVKEANA--YDFIMkLPQKFDTLVGDRGAQLSGGQKQRIAIAR 489
Cdd:cd03250 68 ---IAYVSQEPWIQNGTIRENILFGK---PFDEERyEKVIKACAlePDLEI-LPDGDLTEIGEKGINLSGGQKQRISLAR 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568932737 490 ALVRNPKILLLDEATSALDTESEAEV--QAALDKAREGRTTIVIAHRLSTIRNADVIAGFEDG 550
Cdd:cd03250 141 AVYSDADIYLLDDPLSAVDAHVGRHIfeNCILGLLLNNKTRILVTHQLQLLPHADQIVVLDNG 203
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
980-1209 |
4.27e-36 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 138.20 E-value: 4.27e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 980 FNEVVFNYPTRANvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQWLRAQLGIV 1059
Cdd:PRK13632 10 VENVSFSYPNSEN-NALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGII 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1060 SQEPilfD-----CSIAENIAYGDNSRVVPHDE----IVRAAKEANIHPFIETLPQKyntrvgdkgtqLSGGQKQRIAIA 1130
Cdd:PRK13632 89 FQNP---DnqfigATVEDDIAFGLENKKVPPKKmkdiIDDLAKKVGMEDYLDKEPQN-----------LSGGQKQRVAIA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1131 RALIRQPRVLLLDEATSALDTESEKVVQEALDKAREGR--TCIVIAHRLSTIQNADLIVVIENGKVKEHGTHQQLLAQKG 1208
Cdd:PRK13632 155 SVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRkkTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEILNNKE 234
|
.
gi 568932737 1209 I 1209
Cdd:PRK13632 235 I 235
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
336-572 |
4.55e-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: 137.73 E-value: 4.55e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 336 GNLEFSDVHFSYPSraNIK-ILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLRE 414
Cdd:cd03288 18 GEIKIHDLCVRYEN--NLKpVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 415 IIGVVSQEPVLFSTTIAENIRYGRgNVTMDEIEKAVKEANAYDFIMKLPQKFDTLVGDRGAQLSGGQKQRIAIARALVRN 494
Cdd:cd03288 96 RLSIILQDPILFSGSIRFNLDPEC-KCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRK 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568932737 495 PKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTIRNADVIAGFEDGVIVEQGSHSELM-KKEGIYFRLV 572
Cdd:cd03288 175 SSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLaQEDGVFASLV 253
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
342-533 |
4.67e-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: 135.85 E-value: 4.67e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 342 DVHFSYpsRANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGqdiRNFNVRCLREIIGVVSQ 421
Cdd:cd03226 4 NISFSY--KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNG---KPIKAKERRKSIGYVMQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 422 EP--VLFSTTIAENIRYGRGNVTMD--EIEKAVKEANAYDFIMKLPQkfdtlvgdrgaQLSGGQKQRIAIARALVRNPKI 497
Cdd:cd03226 79 DVdyQLFTDSVREELLLGLKELDAGneQAETVLKDLDLYALKERHPL-----------SLSGGQKQRLAIAAALLSGKDL 147
|
170 180 190
....*....|....*....|....*....|....*..
gi 568932737 498 LLLDEATSALDTESEAEVQAALDK-AREGRTTIVIAH 533
Cdd:cd03226 148 LIFDEPTSGLDYKNMERVGELIRElAAQGKAVIVITH 184
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
338-565 |
6.88e-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: 6.88e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 338 LEFSDVHFSYPSRaniKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNfnvrcLREIIG 417
Cdd:COG1121 7 IELENLTVSYGGR---PVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRR-----ARRRIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 418 VVSQEPVL---FSTTIAENI---RYGRGNVTM-------DEIEKAVKEANAYDFImklpqkfDTLVGdrgaQLSGGQKQR 484
Cdd:COG1121 79 YVPQRAEVdwdFPITVRDVVlmgRYGRRGLFRrpsradrEAVDEALERVGLEDLA-------DRPIG----ELSGGQQQR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 485 IAIARALVRNPKILLLDEATSALDTESEAEVQAALDK-AREGRTTIVIAHRLSTIR-NADVIAGFEDGVIVEqGSHSELM 562
Cdd:COG1121 148 VLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRElRREGKTILVVTHDLGAVReYFDRVLLLNRGLVAH-GPPEEVL 226
|
...
gi 568932737 563 KKE 565
Cdd:COG1121 227 TPE 229
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
994-1214 |
7.50e-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: 136.96 E-value: 7.50e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 994 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQWLRAQLGIVSQEPILFDCSIAEN 1073
Cdd:cd03288 35 PVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFN 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1074 IaygDNSRVVPHDEIVRAAKEANIHPFIETLPQKYNTRVGDKGTQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTES 1153
Cdd:cd03288 115 L---DPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMAT 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568932737 1154 EKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIENGKVKEHGTHQQLLAQK-GIYFSMV 1214
Cdd:cd03288 192 ENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEdGVFASLV 253
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
977-1206 |
1.33e-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: 1.33e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 977 SVTFNEVVFNYPTRanvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQL---LERfydPMAGSVLLDGQEAK-KLNVQwl 1052
Cdd:COG1118 2 SIEVRNISKRFGSF---TLLDDVSLEIASGELVALLGPSGSGKTTLLRIiagLET---PDSGRIVLNGRDLFtNLPPR-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1053 RAQLGIVSQEPILF-DCSIAENIAYGDNSRVVPHDEIVRAAKE----ANIHPFIETLPqkyntrvgdkgTQLSGGQKQRI 1127
Cdd:COG1118 74 ERRVGFVFQHYALFpHMTVAENIAFGLRVRPPSKAEIRARVEEllelVQLEGLADRYP-----------SQLSGGQRQRV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1128 AIARALIRQPRVLLLDEATSALDT----ESEKVVQEALDkaREGRTCIVIAH------RLstiqnADLIVVIENGKVKEH 1197
Cdd:COG1118 143 ALARALAVEPEVLLLDEPFGALDAkvrkELRRWLRRLHD--ELGGTTVFVTHdqeealEL-----ADRVVVMNQGRIEQV 215
|
....*....
gi 568932737 1198 GTHQQLLAQ 1206
Cdd:COG1118 216 GTPDEVYDR 224
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
978-1205 |
2.04e-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: 2.04e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 978 VTFNEVVFNYPTRanvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNV---QWLRA 1054
Cdd:cd03261 1 IELRGLTKSFGGR---TVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEaelYRLRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1055 QLGIVSQEPILFDC-SIAENIAYG--DNSRVVPH--DEIVRAAKEA-NIHPFIETLPqkyntrvgdkgTQLSGGQKQRIA 1128
Cdd:cd03261 78 RMGMLFQSGALFDSlTVFENVAFPlrEHTRLSEEeiREIVLEKLEAvGLRGAEDLYP-----------AELSGGMKKRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1129 IARALIRQPRVLLLDEATSALD-TESEKVVQEALD-KAREGRTCIVIAHRLSTI-QNADLIVVIENGKVKEHGTHQQLLA 1205
Cdd:cd03261 147 LARALALDPELLLYDEPTAGLDpIASGVIDDLIRSlKKELGLTSIMVTHDLDTAfAIADRIAVLYDGKIVAEGTPEELRA 226
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
55-276 |
2.46e-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: 136.52 E-value: 2.46e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 55 EEMTRYAYYYSGLGGGVLVAAYIQVSFWTLAAGRQIKKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDDVSKISEGIGD 134
Cdd:cd18572 33 EAFYRAVLLLLLLSVLSGLFSGLRGGCFSYAGTRLVRRLRRDLFRSLLRQDIAFFDATKTGELTSRLTSDCQKVSDPLST 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 135 KVGMFFQAIATFFAGFIVGFIRGWKLTLVIMAISPILGLSTAVWAKILSTFSDKELAAYAKAGAVAEEALGAIRTVIAFG 214
Cdd:cd18572 113 NLNVFLRNLVQLVGGLAFMFSLSWRLTLLAFITVPVIALITKVYGRYYRKLSKEIQDALAEANQVAEEALSNIRTVRSFA 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568932737 215 GQNKELERYQKHLENAKKIGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTIGN 276
Cdd:cd18572 193 TEEREARRYERALDKALKLSVRQALAYAGYVAVNTLLQNGTQVLVLFYGGHLVLSGRMSAGQ 254
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
54-294 |
3.50e-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: 136.23 E-value: 3.50e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 54 EEEMTRYAYYYSGLGGGVLVAAYIQVSFWTLAAGRQIKKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDDVSKISEGIG 133
Cdd:cd18780 38 LRALNQAVLILLGVVLIGSIATFLRSWLFTLAGERVVARLRKRLFSAIIAQEIAFFDVTRTGELLNRLSSDTQVLQNAVT 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 134 DKVGMFFQAIATFFAGFIVGFIRGWKLTLVIMAISPILGLSTAVWAKILSTFSDKELAAYAKAGAVAEEALGAIRTVIAF 213
Cdd:cd18780 118 VNLSMLLRYLVQIIGGLVFMFTTSWKLTLVMLSVVPPLSIGAVIYGKYVRKLSKKFQDALAAASTVAEESISNIRTVRSF 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 214 GGQNKELERYQKHLENAKKIGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTIGnAMTVFfsiLIGAFSVGQ 293
Cdd:cd18780 198 AKETKEVSRYSEKINESYLLGKKLARASGGFNGFMGAAAQLAIVLVLWYGGRLVIDGELTTG-LLTSF---LLYTLTVAM 273
|
.
gi 568932737 294 A 294
Cdd:cd18780 274 S 274
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
995-1194 |
4.49e-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: 4.49e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 995 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQE--AKKLNVQWLRAQLGIVSQEPILF-DCSIA 1071
Cdd:cd03262 15 VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKltDDKKNINELRQKVGMVFQQFNLFpHLTVL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1072 ENIAYGdnSRVVPHdeivRAAKEAnihpfiETLPQKYNTRVG--DKGT----QLSGGQKQRIAIARALIRQPRVLLLDEA 1145
Cdd:cd03262 95 ENITLA--PIKVKG----MSKAEA------EERALELLEKVGlaDKADaypaQLSGGQQQRVAIARALAMNPKVMLFDEP 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 568932737 1146 TSALDTEsekVVQEALDK----AREGRTCIVIAHRLSTIQN-ADLIVVIENGKV 1194
Cdd:cd03262 163 TSALDPE---LVGEVLDVmkdlAEEGMTMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
350-562 |
4.67e-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: 4.67e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 350 RANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLREI---IGVVSQEPvlF 426
Cdd:COG4608 28 VGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELRPLrrrMQMVFQDP--Y 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 427 S---------TTIAENIRYgRGNVTMDEIEKAVKEanaydfIMklpqkfdTLVG------DRGA-QLSGGQKQRIAIARA 490
Cdd:COG4608 106 AslnprmtvgDIIAEPLRI-HGLASKAERRERVAE------LL-------ELVGlrpehaDRYPhEFSGGQRQRIGIARA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 491 LVRNPKILLLDEATSALDTESEAEV-------QAALdkareGRTTIVIAHRLSTIRN-ADVIAGFEDGVIVEQGSHSELM 562
Cdd:COG4608 172 LALNPKLIVCDEPVSALDVSIQAQVlnlledlQDEL-----GLTYLFISHDLSVVRHiSDRVAVMYLGKIVEIAPRDELY 246
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
339-541 |
5.03e-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: 5.03e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 339 EFSDVHFSYPSRaniKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRclreiIGV 418
Cdd:cd03235 1 EVEDLTVSYGGH---PVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKR-----IGY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 419 VSQEPVL---FSTTIAENIRYGR----------GNVTMDEIEKAVKEANAYDFImklpqkfdtlvgDRG-AQLSGGQKQR 484
Cdd:cd03235 73 VPQRRSIdrdFPISVRDVVLMGLyghkglfrrlSKADKAKVDEALERVGLSELA------------DRQiGELSGGQQQR 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 568932737 485 IAIARALVRNPKILLLDEATSALDTESEAEVQAALDK-AREGRTTIVIAHRLSTIRNA 541
Cdd:cd03235 141 VLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRElRREGMTILVVTHDLGLVLEY 198
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
978-1205 |
5.11e-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: 5.11e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 978 VTFNEVVFNYPTRAnvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQWLRAQLG 1057
Cdd:cd03295 1 IEFENVTKRYGGGK--KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1058 IVSQEPILF-DCSIAENIAygdnsrVVPHDEIV-RAAKEANIHPFIETL---PQKYNTRVGDkgtQLSGGQKQRIAIARA 1132
Cdd:cd03295 79 YVIQQIGLFpHMTVEENIA------LVPKLLKWpKEKIRERADELLALVgldPAEFADRYPH---ELSGGQQQRVGVARA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568932737 1133 LIRQPRVLLLDEATSALDTESEKVVQEALDKARE--GRTCIVIAHRL-STIQNADLIVVIENGKVKEHGTHQQLLA 1205
Cdd:cd03295 150 LAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQelGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEILR 225
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
339-556 |
5.97e-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: 131.79 E-value: 5.97e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 339 EFSDVHFSYPSRaniKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLREIIGV 418
Cdd:cd03214 1 EVENLSVGYGGR---TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 419 VSQepvlfsttiaenirygrgnvtmdeiekAVKEANAYDFIMKLpqkFDTlvgdrgaqLSGGQKQRIAIARALVRNPKIL 498
Cdd:cd03214 78 VPQ---------------------------ALELLGLAHLADRP---FNE--------LSGGERQRVLLARALAQEPPIL 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568932737 499 LLDEATSALDTESEAEVQAALDK--AREGRTTIVIAHRLS-TIRNADVIAGFEDGVIVEQG 556
Cdd:cd03214 120 LLDEPTSHLDIAHQIELLELLRRlaRERGKTVVMVLHDLNlAARYADRVILLKDGRIVAQG 180
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
338-543 |
8.40e-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: 8.40e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 338 LEFSDVHFSYPsrANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRC---LRE 414
Cdd:cd03292 1 IEFINVTKTYP--NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAipyLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 415 IIGVVSQEPVLFST-TIAENIRYGR--GNVTMDEIEKAVKEANAydfIMKLPQKFDTLvgdrGAQLSGGQKQRIAIARAL 491
Cdd:cd03292 79 KIGVVFQDFRLLPDrNVYENVAFALevTGVPPREIRKRVPAALE---LVGLSHKHRAL----PAELSGGEQQRVAIARAI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568932737 492 VRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIA-----------HRLSTIRNADV 543
Cdd:cd03292 152 VNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVAthakelvdttrHRVIALERGKL 214
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
976-1203 |
1.07e-34 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 136.74 E-value: 1.07e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 976 GSVTFNEVVFNYptrANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQeakklNVQWLRAQ 1055
Cdd:COG3839 2 ASLELENVSKSY---GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGR-----DVTDLPPK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1056 ---LGIVSQEPILFD-CSIAENIAYGDNSRVVPHDEIVRAAKEA----NIHPFIETLPqkyntrvgdkgTQLSGGQKQRI 1127
Cdd:COG3839 74 drnIAMVFQSYALYPhMTVYENIAFPLKLRKVPKAEIDRRVREAaellGLEDLLDRKP-----------KQLSGGQRQRV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1128 AIARALIRQPRVLLLDEATSALD------TESE-KVVQEALdkareGRTCIVIAHRLS---TIqnADLIVVIENGKVKEH 1197
Cdd:COG3839 143 ALGRALVREPKVFLLDEPLSNLDaklrveMRAEiKRLHRRL-----GTTTIYVTHDQVeamTL--ADRIAVMNDGRIQQV 215
|
....*.
gi 568932737 1198 GTHQQL 1203
Cdd:COG3839 216 GTPEEL 221
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
978-1194 |
1.23e-34 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 133.26 E-value: 1.23e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 978 VTFNEVVFNYPtrANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLN---VQWLRA 1054
Cdd:COG3638 3 LELRNLSKRYP--GGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRgraLRRLRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1055 QLGIVSQEPILFD-CSIAENI---AYGDNS------RVVPHDEIVRAAkEAnihpfIET--LPQKYNTRVGdkgtQLSGG 1122
Cdd:COG3638 81 RIGMIFQQFNLVPrLSVLTNVlagRLGRTStwrsllGLFPPEDRERAL-EA-----LERvgLADKAYQRAD----QLSGG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568932737 1123 QKQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEAL-DKARE-GRTCIVIAHRLSTIQN-ADLIVVIENGKV 1194
Cdd:COG3638 151 QQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLrRIAREdGITVVVNLHQVDLARRyADRIIGLRDGRV 225
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
338-561 |
1.31e-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: 1.31e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 338 LEFSDVHFSYPSRaniKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIrNFNVRCLREIIG 417
Cdd:COG1118 3 IEVRNISKRFGSF---TLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDL-FTNLPPRERRVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 418 VVSQEPVLF-STTIAENIRYG--RGNVTMDEIEKAVKE----------ANAYdfimklPqkfdtlvgdrgAQLSGGQKQR 484
Cdd:COG1118 79 FVFQHYALFpHMTVAENIAFGlrVRPPSKAEIRARVEEllelvqleglADRY------P-----------SQLSGGQRQR 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 485 IAIARALVRNPKILLLDEATSALDTESEAEVQAALDK--AREGRTTIVIAH-RLSTIRNADVIAGFEDGVIVEQGSHSEL 561
Cdd:COG1118 142 VALARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRlhDELGGTTVFVTHdQEEALELADRVVVMNQGRIEQVGTPDEV 221
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
978-1198 |
1.64e-34 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 132.10 E-value: 1.64e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 978 VTFNEVVFNYPTraNVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLN---VQWLRA 1054
Cdd:COG2884 2 IRFENVSKRYPG--GREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKrreIPYLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1055 QLGIVSQE-PILFDCSIAENIAY-----GdnsrvVPHDEIVRAAKEAnihpfIET--LPQKYNTRVGdkgtQLSGGQKQR 1126
Cdd:COG2884 80 RIGVVFQDfRLLPDRTVYENVALplrvtG-----KSRKEIRRRVREV-----LDLvgLSDKAKALPH----ELSGGEQQR 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568932737 1127 IAIARALIRQPRVLLLDEATSALDTE-SEKVVqEALDKAREGRTCIVIA-HRLSTIQNADL-IVVIENGKVKEHG 1198
Cdd:COG2884 146 VAIARALVNRPELLLADEPTGNLDPEtSWEIM-ELLEEINRRGTTVLIAtHDLELVDRMPKrVLELEDGRLVRDE 219
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
338-556 |
3.82e-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: 3.82e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 338 LEFSDVHFSYPSRaniKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDI-------RNfnvr 410
Cdd:cd03301 1 VELENVTKRFGNV---TALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVtdlppkdRD---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 411 clreiIGVVSQEPVLF-STTIAENIRYG--RGNVTMDEIEKAVKEANAydfIMKLpqkfDTLVGDRGAQLSGGQKQRIAI 487
Cdd:cd03301 74 -----IAMVFQNYALYpHMTVYDNIAFGlkLRKVPKDEIDERVREVAE---LLQI----EHLLDRKPKQLSGGQRQRVAL 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568932737 488 ARALVRNPKILLLDEATSALDTESEAEVQAALDK--AREGRTTIVIAH-RLSTIRNADVIAGFEDGVIVEQG 556
Cdd:cd03301 142 GRAIVREPKVFLMDEPLSNLDAKLRVQMRAELKRlqQRLGTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
356-564 |
5.06e-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: 5.06e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 356 LKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRclREIIGVVSQEPVLF-STTIAENI 434
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE--KRDISYVPQNYALFpHMTVYKNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 435 RYGRGNVTMD--EIEKAVKEanaydfIMKLpQKFDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESE 512
Cdd:cd03299 93 AYGLKKRKVDkkEIERKVLE------IAEM-LGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTK 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 568932737 513 AEVQAALDKARE--GRTTIVIAHRLSTIRN-ADVIAGFEDGVIVEQGSHSELMKK 564
Cdd:cd03299 166 EKLREELKKIRKefGVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEVFKK 220
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
994-1199 |
1.41e-33 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 133.92 E-value: 1.41e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 994 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQwlRAQLGIVSQEPILF-DCSIAE 1072
Cdd:PRK09452 28 EVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE--NRHVNTVFQSYALFpHMTVFE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1073 NIAYGDNSRVVPHDEIVRAAKEANIHPFIETLPQKyntrvgdKGTQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTE 1152
Cdd:PRK09452 106 NVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQR-------KPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYK 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 568932737 1153 SEKVVQEALdKA--RE-GRTCIVIAH-RLSTIQNADLIVVIENGKVKEHGT 1199
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 ... |
992-1203 |
1.48e-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: 129.66 E-value: 1.48e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 992 NVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAkkLNVQWLRAQLGIVSQEPILF-DCSI 1070
Cdd:cd03300 12 GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI--TNLPPHKRPVNTVFQNYALFpHLTV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1071 AENIAYGDNSRVVPHDEIVRAAKEANIHPFIETLPQKYNTrvgdkgtQLSGGQKQRIAIARALIRQPRVLLLDEATSALD 1150
Cdd:cd03300 90 FENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPS-------QLSGGQQQRVAIARALVNEPKVLLLDEPLGALD 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 568932737 1151 TESEKVVQEALDK--AREGRTCIVIAHRLS-TIQNADLIVVIENGKVKEHGTHQQL 1203
Cdd:cd03300 163 LKLRKDMQLELKRlqKELGITFVFVTHDQEeALTMSDRIAVMNKGKIQQIGTPEEI 218
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
993-1206 |
1.84e-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: 130.46 E-value: 1.84e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 993 VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQWLRA----QLGIVSQEPILF-D 1067
Cdd:cd03294 37 TVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRElrrkKISMVFQSFALLpH 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1068 CSIAENIAYGDNSRVVPHDEIVRAAKEA----NIHPFIETLPQkyntrvgdkgtQLSGGQKQRIAIARALIRQPRVLLLD 1143
Cdd:cd03294 117 RTVLENVAFGLEVQGVPRAEREERAAEAlelvGLEGWEHKYPD-----------ELSGGMQQRVGLARALAVDPDILLMD 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568932737 1144 EATSALDTESEKVVQEALDK--AREGRTCIVIAHRLS-TIQNADLIVVIENGKVKEHGTHQQLLAQ 1206
Cdd:cd03294 186 EAFSALDPLIRREMQDELLRlqAELQKTIVFITHDLDeALRLGDRIAIMKDGRLVQVGTPEEILTN 251
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
978-1206 |
2.08e-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: 2.08e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 978 VTFNEVVFNYPTRanvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLnvqwlRAQLG 1057
Cdd:COG1121 7 IELENLTVSYGGR---PVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA-----RRRIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1058 IVSQE-------PIlfdcSIAENIAYGDNSRVVP-------HDEIVRAA-KEANIHPFIetlpqkyNTRVGdkgtQLSGG 1122
Cdd:COG1121 79 YVPQRaevdwdfPI----TVRDVVLMGRYGRRGLfrrpsraDREAVDEAlERVGLEDLA-------DRPIG----ELSGG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1123 QKQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEALDK-AREGRTCIVIAHRLSTI-QNADLIVVIeNGKVKEHGTH 1200
Cdd:COG1121 144 QQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRElRREGKTILVVTHDLGAVrEYFDRVLLL-NRGLVAHGPP 222
|
....*.
gi 568932737 1201 QQLLAQ 1206
Cdd:COG1121 223 EEVLTP 228
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
338-562 |
2.36e-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: 2.36e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 338 LEFSDVHFSYPSRANI--------KILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLyDPTEGKISIDGQDIRNFN- 408
Cdd:COG4172 276 LEARDLKVWFPIKRGLfrrtvghvKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRL-IPSEGEIRFDGQDLDGLSr 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 409 --VRCLREIIGVVSQEPvlFST-----TIAENIRYG----RGNVTMDEIEKAVKEAnaydfimkLPQkfdtlVG-DRGA- 475
Cdd:COG4172 355 raLRPLRRRMQVVFQDP--FGSlsprmTVGQIIAEGlrvhGPGLSAAERRARVAEA--------LEE-----VGlDPAAr 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 476 -----QLSGGQKQRIAIARALVRNPKILLLDEATSALDteseAEVQAA-LD-----KAREGRTTIVIAHRLSTIRN-ADV 543
Cdd:COG4172 420 hryphEFSGGQRQRIAIARALILEPKLLVLDEPTSALD----VSVQAQiLDllrdlQREHGLAYLFISHDLAVVRAlAHR 495
|
250
....*....|....*....
gi 568932737 544 IAGFEDGVIVEQGSHSELM 562
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 ... |
338-562 |
2.64e-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: 2.64e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 338 LEFSDVHFSYpsrANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNV-RCLREII 416
Cdd:cd03224 1 LEVENLNAGY---GKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPhERARAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 417 GVVSQEPVLFST-TIAENIRYGRGNVTMDEIEKAVKEAnaYDFIMKLPQKFDTLVGdrgaQLSGGQKQRIAIARALVRNP 495
Cdd:cd03224 78 GYVPEGRRIFPElTVEENLLLGAYARRRAKRKARLERV--YELFPRLKERRKQLAG----TLSGGEQQMLAIARALMSRP 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568932737 496 KILLLDEATSALDTESEAEVQAALDKAREGRTTIVI----AHRLSTIrnADVIAGFEDGVIVEQGSHSELM 562
Cdd:cd03224 152 KLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLveqnARFALEI--ADRAYVLERGRVVLEGTAAELL 220
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
981-1194 |
4.86e-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: 4.86e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 981 NEVVFNYPTRanvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQwLRAQLGIVS 1060
Cdd:cd03230 4 RNLSKRYGKK---TALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEE-VKRRIGYLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1061 QEPILF-DCSIAENIaygdnsrvvphdeivraakeanihpfietlpqkyntrvgdkgtQLSGGQKQRIAIARALIRQPRV 1139
Cdd:cd03230 80 EEPSLYeNLTVRENL-------------------------------------------KLSGGMKQRLALAQALLHDPEL 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 568932737 1140 LLLDEATSALDTESEKVVQEALDK-AREGRTCIVIAHRLSTIQN-ADLIVVIENGKV 1194
Cdd:cd03230 117 LILDEPTSGLDPESRREFWELLRElKKEGKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
978-1206 |
1.01e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 128.70 E-value: 1.01e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 978 VTFNEVVFNYPTRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQWLRAQLG 1057
Cdd:PRK13650 5 IEVKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1058 IVSQEP--ILFDCSIAENIAYGDNSRVVPHDEIVRAAKEA----NIHPFIETLPQKyntrvgdkgtqLSGGQKQRIAIAR 1131
Cdd:PRK13650 85 MVFQNPdnQFVGATVEDDVAFGLENKGIPHEEMKERVNEAlelvGMQDFKEREPAR-----------LSGGQKQRVAIAG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568932737 1132 ALIRQPRVLLLDEATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTIQNADLIVVIENGKVKEHGTHQQLLAQ 1206
Cdd:PRK13650 154 AVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDdyQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFSR 230
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
355-561 |
1.07e-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: 1.07e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 355 ILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNfnVRCLREIIGVVSQEPVLFS-TTIAEN 433
Cdd:cd03300 15 ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITN--LPPHKRPVNTVFQNYALFPhLTVFEN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 434 IRYG--RGNVTMDEIEKAVKEAnaydfiMKLPQkFDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTES 511
Cdd:cd03300 93 IAFGlrLKKLPKAEIKERVAEA------LDLVQ-LEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 568932737 512 EAEVQAALDK--AREGRTTIVIAHRLS-TIRNADVIAGFEDGVIVEQGSHSEL 561
Cdd:cd03300 166 RKDMQLELKRlqKELGITFVFVTHDQEeALTMSDRIAVMNKGKIQQIGTPEEI 218
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
993-1194 |
1.61e-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: 1.61e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 993 VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQwlRAQ-LGI--VSQEPILF-DC 1068
Cdd:COG1129 17 VKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPR--DAQaAGIaiIHQELNLVpNL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1069 SIAENIAYGD---NSRVVPHDEIVRAAKEA------NIHPfietlpqkyNTRVGDkgtqLSGGQKQRIAIARALIRQPRV 1139
Cdd:COG1129 95 SVAENIFLGReprRGGLIDWRAMRRRARELlarlglDIDP---------DTPVGD----LSVAQQQLVEIARALSRDARV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1140 LLLDEATSAL-DTESE---KVVQEaLdkAREGRTCIVIAHRLSTIQN-ADLIVVIENGKV 1194
Cdd:COG1129 162 LILDEPTASLtEREVErlfRIIRR-L--KAQGVAIIYISHRLDEVFEiADRVTVLRDGRL 218
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
995-1204 |
2.25e-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: 2.25e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 995 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQwlRAQLGIVSQEPILF-DCSIAEN 1073
Cdd:cd03299 14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE--KRDISYVPQNYALFpHMTVYKN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1074 IAYGDNSRVVPHDEIVRAAKEANIHPFIETLPQKYNTRvgdkgtqLSGGQKQRIAIARALIRQPRVLLLDEATSALDTES 1153
Cdd:cd03299 92 IAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPET-------LSGGEQQRVAIARALVVNPKILLLDEPFSALDVRT 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 568932737 1154 EKVVQEALDKARE--GRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHGTHQQLL 1204
Cdd:cd03299 165 KEKLREELKKIRKefGVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEVF 218
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
338-577 |
2.38e-32 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 130.45 E-value: 2.38e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 338 LEFSDVHFSYPSRaniKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNfnVRCLREIIG 417
Cdd:PRK09452 15 VELRGISKSFDGK---EVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITH--VPAENRHVN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 418 VVSQEPVLFS-TTIAENIRYG--RGNVTMDEIEKAVKEAnaydfiMKLPQkFDTLVGDRGAQLSGGQKQRIAIARALVRN 494
Cdd:PRK09452 90 TVFQSYALFPhMTVFENVAFGlrMQKTPAAEITPRVMEA------LRMVQ-LEEFAQRKPHQLSGGQQQRVAIARAVVNK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 495 PKILLLDEATSALDTESEAEVQAALdKA--RE-GRTTIVIAH-RLSTIRNADVIAGFEDGVIVEQGSHSElmkkegIYFR 570
Cdd:PRK09452 163 PKVLLLDESLSALDYKLRKQMQNEL-KAlqRKlGITFVFVTHdQEEALTMSDRIVVMRDGRIEQDGTPRE------IYEE 235
|
....*..
gi 568932737 571 LVNMQTA 577
Cdd:PRK09452 236 PKNLFVA 242
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
992-1203 |
2.52e-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: 2.52e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 992 NVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQwlRAQLGIVSQEPILF-DCSI 1070
Cdd:cd03296 14 DFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQ--ERNVGFVFQHYALFrHMTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1071 AENIAYG----DNSRVVPHDEIVRAAKEANIHPFIETLPQKYNTrvgdkgtQLSGGQKQRIAIARALIRQPRVLLLDEAT 1146
Cdd:cd03296 92 FDNVAFGlrvkPRSERPPEAEIRAKVHELLKLVQLDWLADRYPA-------QLSGGQRQRVALARALAVEPKVLLLDEPF 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1147 SALDTESEKVVQEALDKARE--GRTCIVIAHRLS-TIQNADLIVVIENGKVKEHGTHQQL 1203
Cdd:cd03296 165 GALDAKVRKELRRWLRRLHDelHVTTVFVTHDQEeALEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
989-1203 |
2.90e-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: 2.90e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 989 TRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLN---VQWLRAQLGIVSQEPil 1065
Cdd:COG4608 27 TVGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSgreLRPLRRRMQMVFQDP-- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1066 FDC-----SIAENIAYG-DNSRVVPHDEIVRAAKEAnihpfIET--LPQKYNTRVGDkgtQLSGGQKQRIAIARALIRQP 1137
Cdd:COG4608 105 YASlnprmTVGDIIAEPlRIHGLASKAERRERVAEL-----LELvgLRPEHADRYPH---EFSGGQRQRIGIARALALNP 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568932737 1138 RVLLLDEATSALDtesekV-VQ-------EALdKAREGRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHGTHQQL 1203
Cdd:COG4608 177 KLIVCDEPVSALD-----VsIQaqvlnllEDL-QDELGLTYLFISHDLSVVRHiSDRVAVMYLGKIVEIAPRDEL 245
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
338-563 |
3.41e-32 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 127.05 E-value: 3.41e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 338 LEFSDVHFSYPSrANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLREIIG 417
Cdd:PRK13635 6 IRVEHISFRYPD-AATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 418 VVSQEP--VLFSTTIAENIRYGRGN--VTMDE----IEKAVKEANAYDFIMKLPqkfdtlvgdrgAQLSGGQKQRIAIAR 489
Cdd:PRK13635 85 MVFQNPdnQFVGATVQDDVAFGLENigVPREEmverVDQALRQVGMEDFLNREP-----------HRLSGGQKQRVAIAG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568932737 490 ALVRNPKILLLDEATSALDTESEAEVQAALD--KAREGRTTIVIAHRLSTIRNADVIAGFEDGVIVEQGSHSELMK 563
Cdd:PRK13635 154 VLALQPDIIILDEATSMLDPRGRREVLETVRqlKEQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFK 229
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
987-1206 |
3.54e-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: 3.54e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 987 YPTRAN-VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMA---GSVLLDGQEAKKLNVQWLRA----QLGI 1058
Cdd:COG0444 11 FPTRRGvVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPGitsGEILFDGEDLLKLSEKELRKirgrEIQM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1059 VSQEP---------ILFdcSIAENI-AYGDNSRVVPHDEIVRAAKEANIHPfietlPQKyntRVGDKGTQLSGGQKQRIA 1128
Cdd:COG0444 91 IFQDPmtslnpvmtVGD--QIAEPLrIHGGLSKAEARERAIELLERVGLPD-----PER---RLDRYPHELSGGMRQRVM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1129 IARALIRQPRVLLLDEATSALDTesekVVQ-EALD-----KAREGRTCIVIAHRLSTI-QNADLIVVIENGKVKEHGTHQ 1201
Cdd:COG0444 161 IARALALEPKLLIADEPTTALDV----TIQaQILNllkdlQRELGLAILFITHDLGVVaEIADRVAVMYAGRIVEEGPVE 236
|
....*
gi 568932737 1202 QLLAQ 1206
Cdd:COG0444 237 ELFEN 241
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
993-1205 |
6.08e-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: 6.08e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 993 VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQwLRAQLGI--VSQEPILF-DCS 1069
Cdd:cd03224 13 SQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPH-ERARAGIgyVPEGRRIFpELT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1070 IAENIAYGDNSRVvphdeivRAAKEANIHPFIETLPQKYnTRVGDKGTQLSGGQKQRIAIARALIRQPRVLLLDEATSAL 1149
Cdd:cd03224 92 VEENLLLGAYARR-------RAKRKARLERVYELFPRLK-ERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568932737 1150 dteSEKVVQE---ALDKAREGRTCIVIAHrlstiQNADLI-------VVIENGKVKEHGTHQQLLA 1205
Cdd:cd03224 164 ---APKIVEEifeAIRELRDEGVTILLVE-----QNARFAleiadraYVLERGRVVLEGTAAELLA 221
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
354-563 |
6.39e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 126.70 E-value: 6.39e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 354 KILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDI--RNFNVRCLREIIGVVSQEP--VLFSTT 429
Cdd:PRK13637 21 KALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdKKVKLSDIRKKVGLVFQYPeyQLFEET 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 430 IAENIRYGRGNVTM--DEIEKAVKEANAydfIMKLPqkFDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEATSAL 507
Cdd:PRK13637 101 IEKDIAFGPINLGLseEEIENRVKRAMN---IVGLD--YEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 568932737 508 DTESEAEVQAALDKARE--GRTTIVIAHRLSTI-RNADVIAGFEDGVIVEQGSHSELMK 563
Cdd:PRK13637 176 DPKGRDEILNKIKELHKeyNMTIILVSHSMEDVaKLADRIIVMNKGKCELQGTPREVFK 234
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
979-1194 |
7.24e-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: 7.24e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 979 TFNEVVFNYPTraNVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQE---AKKLNVQWLRAQ 1055
Cdd:cd03256 2 EVENLSKTYPN--GKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDinkLKGKALRQLRRQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1056 LGIVSQEPILFD-CSIAENIAYGDNSRVVPHDEIVRAAKEANIHPFIETLPQ-----KYNTRVGdkgtQLSGGQKQRIAI 1129
Cdd:cd03256 80 IGMIFQQFNLIErLSVLENVLSGRLGRRSTWRSLFGLFPKEEKQRALAALERvglldKAYQRAD----QLSGGQQQRVAI 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568932737 1130 ARALIRQPRVLLLDEATSALDTESEKVVQEAL-DKARE-GRTCIVIAHRLSTI-QNADLIVVIENGKV 1194
Cdd:cd03256 156 ARALMQQPKLILADEPVASLDPASSRQVMDLLkRINREeGITVIVSLHQVDLArEYADRIVGLKDGRI 223
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
338-561 |
9.40e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 125.96 E-value: 9.40e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 338 LEFSDVHFSYPSraNIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCL--REI 415
Cdd:PRK13639 2 LETRDLKYSYPD--GTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLevRKT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 416 IGVVSQEP--VLFSTTIAENIRYGRGNV--TMDEIEKAVKEA----NAYDFIMKLPQkfdtlvgdrgaQLSGGQKQRIAI 487
Cdd:PRK13639 80 VGIVFQNPddQLFAPTVEEDVAFGPLNLglSKEEVEKRVKEAlkavGMEGFENKPPH-----------HLSGGQKKRVAI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568932737 488 ARALVRNPKILLLDEATSALDTESEAEVQAAL-DKAREGRTTIVIAHRLSTI-RNADVIAGFEDGVIVEQGSHSEL 561
Cdd:PRK13639 149 AGILAMKPEIIVLDEPTSGLDPMGASQIMKLLyDLNKEGITIIISTHDVDLVpVYADKVYVMSDGKIIKEGTPKEV 224
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
338-562 |
9.70e-32 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 124.43 E-value: 9.70e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 338 LEFSDV--HFsypsrANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIR--NFNVRCLR 413
Cdd:PRK09493 2 IEFKNVskHF-----GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpKVDERLIR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 414 EIIGVVSQEPVLFSTTIA-ENIRYG----RGnvtmdeIEKAVKEANAYDFIMKlpqkfdtlVG--DRG----AQLSGGQK 482
Cdd:PRK09493 77 QEAGMVFQQFYLFPHLTAlENVMFGplrvRG------ASKEEAEKQARELLAK--------VGlaERAhhypSELSGGQQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 483 QRIAIARALVRNPKILLLDEATSALDTESEAEVQAAL-DKAREGRTTIVIAHRLSTIRN-ADVIAGFEDGVIVEQGSHSE 560
Cdd:PRK09493 143 QRVAIARALAVKPKLMLFDEPTSALDPELRHEVLKVMqDLAEEGMTMVIVTHEIGFAEKvASRLIFIDKGRIAEDGDPQV 222
|
..
gi 568932737 561 LM 562
Cdd:PRK09493 223 LI 224
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
354-556 |
1.12e-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: 1.12e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 354 KILKGLNLKVK---SGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQ---DIR-NFNVRCLREIIGVVSQEPVLF 426
Cdd:cd03297 8 KRLPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlfDSRkKINLPPQQRKIGLVFQQYALF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 427 S-TTIAENIRYGRGNVTMDEIEKAVKEANAYdfiMKLpqkfDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEATS 505
Cdd:cd03297 88 PhLNVRENLAFGLKRKRNREDRISVDELLDL---LGL----DHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFS 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 568932737 506 ALDTESEAEVQAALDK--AREGRTTIVIAHRLSTI-RNADVIAGFEDGVIVEQG 556
Cdd:cd03297 161 ALDRALRLQLLPELKQikKNLNIPVIFVTHDLSEAeYLADRIVVMEDGRLQYIG 214
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
989-1206 |
1.20e-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: 1.20e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 989 TRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFyDPMAGSVLLDGQEAKKLN---VQWLRAQLGIVSQEPil 1065
Cdd:COG4172 295 TVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRL-IPSEGEIRFDGQDLDGLSrraLRPLRRRMQVVFQDP-- 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1066 FDC-----SIAENIAYGdnsRVVPHDEIVRAAKEANIhpfIETLpqkynTRVG-DKGT------QLSGGQKQRIAIARAL 1133
Cdd:COG4172 372 FGSlsprmTVGQIIAEG---LRVHGPGLSAAERRARV---AEAL-----EEVGlDPAArhryphEFSGGQRQRIAIARAL 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1134 IRQPRVLLLDEATSALDteseKVVQ-EALD-----KAREGRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHGTHQQLLAQ 1206
Cdd:COG4172 441 ILEPKLLVLDEPTSALD----VSVQaQILDllrdlQREHGLAYLFISHDLAVVRAlAHRVMVMKDGKVVEQGPTEQVFDA 516
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
338-544 |
1.40e-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: 122.97 E-value: 1.40e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 338 LEFSDVHFSYPSRAnikILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRcLREIIG 417
Cdd:COG4133 3 LEAENLSCRRGERL---LFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDARED-YRRRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 418 VVSQEPVLFST-TIAENIR-----YGRgNVTMDEIEKAVKEanaydfiMKLPQKFDTLVGdrgaQLSGGQKQRIAIARAL 491
Cdd:COG4133 79 YLGHADGLKPElTVRENLRfwaalYGL-RADREAIDEALEA-------VGLAGLADLPVR----QLSAGQKRRVALARLL 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 568932737 492 VRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIA-HRLSTIRNADVI 544
Cdd:COG4133 147 LSPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTtHQPLELAAARVL 200
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
338-561 |
1.76e-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: 1.76e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 338 LEFSDVHFSYPSranIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLREI-I 416
Cdd:COG1129 5 LEMRGISKSFGG---VKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQAAgI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 417 GVVSQEPVLFST-TIAENI---RYGRGNVTMD--EIEKAVKEANAYdfiMKLPQKFDTLVGDrgaqLSGGQKQRIAIARA 490
Cdd:COG1129 82 AIIHQELNLVPNlSVAENIflgREPRRGGLIDwrAMRRRARELLAR---LGLDIDPDTPVGD----LSVAQQQLVEIARA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568932737 491 LVRNPKILLLDEATSALdteSEAEVQAALD-----KAReGRTTIVIAHRLSTIRN-ADVIAGFEDGVIVEQGSHSEL 561
Cdd:COG1129 155 LSRDARVLILDEPTASL---TEREVERLFRiirrlKAQ-GVAIIYISHRLDEVFEiADRVTVLRDGRLVGTGPVAEL 227
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
354-1215 |
1.97e-31 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 134.14 E-value: 1.97e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 354 KILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQdirnfnvrclreiIGVVSQEPVLFSTTIAEN 433
Cdd:PTZ00243 674 VLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAERS-------------IAYVPQQAWIMNATVRGN 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 434 IRYgrgnvtMDE-----IEKAVK----EANaydfIMKLPQKFDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEAT 504
Cdd:PTZ00243 741 ILF------FDEedaarLADAVRvsqlEAD----LAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPL 810
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 505 SALDTE-SEAEVQAALDKAREGRTTIVIAHRLSTIRNADVIAGFEDGVIVEQGSHSELMKKEgIYFRL-----VNMQTAG 578
Cdd:PTZ00243 811 SALDAHvGERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFMRTS-LYATLaaelkENKDSKE 889
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 579 SQILSEEFEVELSDEKAagdVAPNGwkarifrnstkkslKSPHQNRLDEETNELDANVPPVSFLKVLKLNKTEWPYFVVG 658
Cdd:PTZ00243 890 GDADAEVAEVDAAPGGA---VDHEP--------------PVAKQEGNAEGGDGAALDAAAGRLMTREEKASGSVPWSTYV 952
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 659 TVCAIANGALQPAFSII---LSEMIAI-------------FGPGDDAvkqqkcnmFSLVFLGLGVLSFFTFFLQGFTFGK 722
Cdd:PTZ00243 953 AYLRFCGGLHAAGFVLAtfaVTELVTVssgvwlsmwstrsFKLSAAT--------YLYVYLGIVLLGTFSVPLRFFLSYE 1024
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 723 AGEILTTRLRSMAFKAMLRQDMSWFDdhKNSTGALSTRLATDAAqvqgatgtrlalIAQNTANLGTGIIISFIYGWQLTL 802
Cdd:PTZ00243 1025 AMRRGSRNMHRDLLRSVSRGTMSFFD--TTPLGRILNRFSRDID------------ILDNTLPMSYLYLLQCLFSICSSI 1090
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 803 LLLSVV-PFIAVA----GIVEMK-MLAGNAkrdkkemeaagkiateAIENIRTVVSLTQERKFeSMYVEKLHGpyrnsvr 876
Cdd:PTZ00243 1091 LVTSASqPFVLVAlvpcGYLYYRlMQFYNS----------------ANREIRRIKSVAKSPVF-TLLEEALQG------- 1146
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 877 KAHI--YGITFSISQ-AFMYFSYAgcfrFGSYLIVNGHMRFKDVILVF-SAIVLGAVAL-------GHASSfaPDYAKAK 945
Cdd:PTZ00243 1147 SATItaYGKAHLVMQeALRRLDVV----YSCSYLENVANRWLGVRVEFlSNIVVTVIALigvigtmLRATS--QEIGLVS 1220
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 946 LSAAYLFSLFE------RQ------------------------------PLIDSYSGE-GLWPDKF-------------- 974
Cdd:PTZ00243 1221 LSLTMAMQTTAtlnwlvRQvatveadmnsverllyytdevphedmpeldEEVDALERRtGMAADVTgtvviepasptsaa 1300
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 975 -----EGSVTFNEVVFNYptRANVP-VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLN 1048
Cdd:PTZ00243 1301 phpvqAGSLVFEGVQMRY--REGLPlVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYG 1378
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1049 VQWLRAQLGIVSQEPILFDCSIAENIaygDNSRVVPHDEIVRAAKEANIHPFIETLPQKYNTRVGDKGTQLSGGQKQRIA 1128
Cdd:PTZ00243 1379 LRELRRQFSMIPQDPVLFDGTVRQNV---DPFLEASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMC 1455
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1129 IARALI-RQPRVLLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIENGKVKEHGTHQQL-LAQ 1206
Cdd:PTZ00243 1456 MARALLkKGSGFILMDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELvMNR 1535
|
....*....
gi 568932737 1207 KGIYFSMVN 1215
Cdd:PTZ00243 1536 QSIFHSMVE 1544
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
989-1188 |
2.03e-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: 2.03e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 989 TRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQWlRAQLGIVSQEPILF-D 1067
Cdd:COG4133 11 RRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDY-RRRLAYLGHADGLKpE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1068 CSIAENIA-----YGdnsRVVPHDEIVRAAKEANIHPFIETLPQkyntrvgdkgtQLSGGQKQRIAIARALIRQPRVLLL 1142
Cdd:COG4133 90 LTVRENLRfwaalYG---LRADREAIDEALEAVGLAGLADLPVR-----------QLSAGQKRRVALARLLLSPAPLWLL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 568932737 1143 DEATSALDTESEKVVQEALDKAREGRTCIVIA-HRLSTIQNADLIVV 1188
Cdd:COG4133 156 DEPFTALDAAGVALLAELIAAHLARGGAVLLTtHQPLELAAARVLDL 202
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
696-912 |
2.27e-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: 2.27e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 696 NMFSLVFLGLGVLSFFTFFLQGFTFGKAGEILTTRLRSMAFKAMLRQDMSWFDDHKnsTGALSTRLATDAAQVQGATGTR 775
Cdd:cd18573 41 KTFALALLGVFVVGAAANFGRVYLLRIAGERIVARLRKRLFKSILRQDAAFFDKNK--TGELVSRLSSDTSVVGKSLTQN 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 776 LALIAQNTANLGTGIIISFIYGWQLTLLLLSVVPFIAVAGIVEMKMLAGNAKRDKKEMEAAGKIATEAIENIRTVVSLTQ 855
Cdd:cd18573 119 LSDGLRSLVSGVGGIGMMLYISPKLTLVMLLVVPPIAVGAVFYGRYVRKLSKQVQDALADATKVAEERLSNIRTVRAFAA 198
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 568932737 856 ERKFESMYVEKLHGPYRNSVRKAHIYGITFSISQAFMYFSYAGCFRFGSYLIVNGHM 912
Cdd:cd18573 199 ERKEVERYAKKVDEVFDLAKKEALASGLFFGSTGFSGNLSLLSVLYYGGSLVASGEL 255
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
338-561 |
2.47e-31 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 123.73 E-value: 2.47e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 338 LEFSDVHFSYPSRaniKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYD-----PTEGKISIDGQDI---RNFNV 409
Cdd:PRK14239 6 LQVSDLSVYYNKK---KALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnpevTITGSIVYNGHNIyspRTDTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 410 RcLREIIGVVSQEPVLFSTTIAENIRYG------RGNVTMDE-IEKAVKEANAYDFIMklpqkfDTLvGDRGAQLSGGQK 482
Cdd:PRK14239 83 D-LRKEIGMVFQQPNPFPMSIYENVVYGlrlkgiKDKQVLDEaVEKSLKGASIWDEVK------DRL-HDSALGLSGGQQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 483 QRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTI-RNADVIAGFEDGVIVEQGSHSEL 561
Cdd:PRK14239 155 QRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQAsRISDRTGFFLDGDLIEYNDTKQM 234
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
987-1199 |
2.96e-31 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 126.07 E-value: 2.96e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 987 YPTRAN-VPVLQGLSLEVKKGQTLALVGSSGCGKST---VVQLLERfydPMAGSVLLDGQEAKKLNVQWLRA---QLGIV 1059
Cdd:PRK11153 11 FPQGGRtIHALNNVSLHIPAGEIFGVIGASGAGKSTlirCINLLER---PTSGRVLVDGQDLTALSEKELRKarrQIGMI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1060 SQE-PILFDCSIAENIAY-----GdnsrvVPHDEIvraakEANIHPFIEtlpqkyntRVG--DKG----TQLSGGQKQRI 1127
Cdd:PRK11153 88 FQHfNLLSSRTVFDNVALplelaG-----TPKAEI-----KARVTELLE--------LVGlsDKAdrypAQLSGGQKQRV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568932737 1128 AIARALIRQPRVLLLDEATSALDTESEKVVQEALDKA-RE-GRTCIVIAHRLSTI-QNADLIVVIENGKVKEHGT 1199
Cdd:PRK11153 150 AIARALASNPKVLLCDEATSALDPATTRSILELLKDInRElGLTIVLITHEMDVVkRICDRVAVIDAGRLVEQGT 224
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
978-1194 |
3.52e-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: 3.52e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 978 VTFNEVVFNYPtrANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLN---VQWLRA 1054
Cdd:cd03292 1 IEFINVTKTYP--NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRgraIPYLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1055 QLGIVSQE-PILFDCSIAENIAYGDNSRVVPHDEIVRAAKEAnihpfIETLPQKYNTRvgDKGTQLSGGQKQRIAIARAL 1133
Cdd:cd03292 79 KIGVVFQDfRLLPDRNVYENVAFALEVTGVPPREIRKRVPAA-----LELVGLSHKHR--ALPAELSGGEQQRVAIARAI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568932737 1134 IRQPRVLLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNA--DLIVVIENGKV 1194
Cdd:cd03292 152 VNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTtrHRVIALERGKL 214
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
980-1198 |
3.69e-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: 3.69e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 980 FNEVVFNYPtraNVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLnvqwlRAQLGIV 1059
Cdd:cd03235 2 VEDLTVSYG---GHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE-----RKRIGYV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1060 SQEPIL---FDCSIAENIAYGDNSRVVPHDEIVRAAKEAnihpFIETLpqkynTRVGDKG------TQLSGGQKQRIAIA 1130
Cdd:cd03235 74 PQRRSIdrdFPISVRDVVLMGLYGHKGLFRRLSKADKAK----VDEAL-----ERVGLSEladrqiGELSGGQQQRVLLA 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1131 RALIRQPRVLLLDEATSALDTESEKVVQEALDK-AREGRTCIVIAHRLSTIQN-ADLIVVIeNGKVKEHG 1198
Cdd:cd03235 145 RALVQDPDLLLLDEPFAGVDPKTQEDIYELLRElRREGMTILVVTHDLGLVLEyFDRVLLL-NRTVVASG 213
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
355-561 |
3.75e-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: 3.75e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 355 ILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKI-----SIDGQdiRNFN-----VRCLREIIGVVSQEPV 424
Cdd:PRK11264 18 VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIrvgdiTIDTA--RSLSqqkglIRQLRQHVGFVFQNFN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 425 LFS-TTIAENIRygRGNVTMDEIEKAVKEANAYDFIMKLpqkfdTLVGDRGA---QLSGGQKQRIAIARALVRNPKILLL 500
Cdd:PRK11264 96 LFPhRTVLENII--EGPVIVKGEPKEEATARARELLAKV-----GLAGKETSyprRLSGGQQQRVAIARALAMRPEVILF 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568932737 501 DEATSALDTESEAEVQAALDK-AREGRTTIVIAHRLSTIRN-ADVIAGFEDGVIVEQGSHSEL 561
Cdd:PRK11264 169 DEPTSALDPELVGEVLNTIRQlAQEKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKAL 231
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
983-1198 |
5.05e-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: 120.62 E-value: 5.05e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 983 VVFNYPTRanvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQWLRAQLGIVSQe 1062
Cdd:cd03214 5 LSVGYGGR---TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1063 pilfdcsiaeniaygdnsrvvphdeivrAAKEANIHPFIEtlpQKYNTrvgdkgtqLSGGQKQRIAIARALIRQPRVLLL 1142
Cdd:cd03214 81 ----------------------------ALELLGLAHLAD---RPFNE--------LSGGERQRVLLARALAQEPPILLL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 568932737 1143 DEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLS-TIQNADLIVVIENGKVKEHG 1198
Cdd:cd03214 122 DEPTSHLDIAHQIELLELLRRlaRERGKTVVMVLHDLNlAARYADRVILLKDGRIVAQG 180
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
64-275 |
1.91e-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: 1.91e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 64 YSGLGGGVLVAA---YIQVSFWTLAAGRQIKKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDDVSKISEGIGDKVGMFF 140
Cdd:cd18573 44 ALALLGVFVVGAaanFGRVYLLRIAGERIVARLRKRLFKSILRQDAAFFDKNKTGELVSRLSSDTSVVGKSLTQNLSDGL 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 141 QAIATFFAGFIVGFIRGWKLTLVIMAISPILGLSTAVWAKILSTFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKEL 220
Cdd:cd18573 124 RSLVSGVGGIGMMLYISPKLTLVMLLVVPPIAVGAVFYGRYVRKLSKQVQDALADATKVAEERLSNIRTVRAFAAERKEV 203
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 568932737 221 ERYQKHLENAKKIGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTIG 275
Cdd:cd18573 204 ERYAKKVDEVFDLAKKEALASGLFFGSTGFSGNLSLLSVLYYGGSLVASGELTVG 258
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1000-1206 |
1.93e-30 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 120.63 E-value: 1.93e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1000 SLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVqwlrAQ--LGIVSQEPILFD-CSIAENIAY 1076
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPP----AErpVSMLFQENNLFPhLTVAQNIGL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1077 GDNSR----VVPHDEIVRAAKEANIHPFIETLPQkyntrvgdkgtQLSGGQKQRIAIARALIRQPRVLLLDEATSALD-- 1150
Cdd:COG3840 95 GLRPGlkltAEQRAQVEQALERVGLAGLLDRLPG-----------QLSGGQRQRVALARCLVRKRPILLLDEPFSALDpa 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 568932737 1151 --TESEKVVQEALDkaREGRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHGTHQQLLAQ 1206
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 ... |
995-1195 |
2.22e-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: 119.67 E-value: 2.22e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 995 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGqeaKKLNVQWLRAQLGIVSQEP--ILFDCSIAE 1072
Cdd:cd03226 15 ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNG---KPIKAKERRKSIGYVMQDVdyQLFTDSVRE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1073 NIAYGDNSrvvPHDEIVRAA---KEANIHPFIETLPQkyntrvgdkgtQLSGGQKQRIAIARALIRQPRVLLLDEATSAL 1149
Cdd:cd03226 92 ELLLGLKE---LDAGNEQAEtvlKDLDLYALKERHPL-----------SLSGGQKQRLAIAAALLSGKDLLIFDEPTSGL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 568932737 1150 DTESEKVVQEALDK-AREGRTCIVIAHRLSTIQN-ADLIVVIENGKVK 1195
Cdd:cd03226 158 DYKNMERVGELIRElAAQGKAVIVITHDYEFLAKvCDRVLLLANGAIV 205
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
978-1205 |
2.87e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 121.63 E-value: 2.87e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 978 VTFNEVVFNYPTraNVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLN-VQWLRAQL 1056
Cdd:PRK13644 2 IRLENVSYSYPD--GTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSkLQGIRKLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1057 GIVSQEP--ILFDCSIAENIAYGDNSRVVPHDEIVRAAKEAnihpFIETLPQKYNTRvgdKGTQLSGGQKQRIAIARALI 1134
Cdd:PRK13644 80 GIVFQNPetQFVGRTVEEDLAFGPENLCLPPIEIRKRVDRA----LAEIGLEKYRHR---SPKTLSGGQGQCVALAGILT 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568932737 1135 RQPRVLLLDEATSALDTESEKVVQEALDKA-REGRTCIVIAHRLSTIQNADLIVVIENGKVKEHGTHQQLLA 1205
Cdd:PRK13644 153 MEPECLIFDEVTSMLDPDSGIAVLERIKKLhEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLS 224
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
338-561 |
2.91e-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: 2.91e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 338 LEFSDVHFSYPSRANIkILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLREIiG 417
Cdd:cd03263 1 LQIRNLTKTYKKGTKP-AVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQSL-G 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 418 VVSQEPVLFST-TIAENIRY-----GRGNVTMDEiekavkEANAYDFIMKLPQKFDTLVGDrgaqLSGGQKQRIAIARAL 491
Cdd:cd03263 79 YCPQFDALFDElTVREHLRFyarlkGLPKSEIKE------EVELLLRVLGLTDKANKRART----LSGGMKRKLSLAIAL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568932737 492 VRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTIRN-ADVIAGFEDGVIVEQGSHSEL 561
Cdd:cd03263 149 IGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEAlCDRIAIMSDGKLRCIGSPQEL 219
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
356-561 |
3.40e-30 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 120.14 E-value: 3.40e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 356 LKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRclREIIGVVSQEPVLFS-TTIAENI 434
Cdd:cd03296 18 LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQ--ERNVGFVFQHYALFRhMTVFDNV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 435 RYG------RGNVTMDEIEKAVKEanaydfIMKLPQkFDTLvGDR-GAQLSGGQKQRIAIARALVRNPKILLLDEATSAL 507
Cdd:cd03296 96 AFGlrvkprSERPPEAEIRAKVHE------LLKLVQ-LDWL-ADRyPAQLSGGQRQRVALARALAVEPKVLLLDEPFGAL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 568932737 508 DTESEAEVQAALDKARE--GRTTIVIAHRLS-TIRNADVIAGFEDGVIVEQGSHSEL 561
Cdd:cd03296 168 DAKVRKELRRWLRRLHDelHVTTVFVTHDQEeALEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
978-1204 |
3.82e-30 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 120.20 E-value: 3.82e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 978 VTFNEVVFNYptrANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAK--KLNVQWLRAQ 1055
Cdd:PRK09493 2 IEFKNVSKHF---GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpKVDERLIRQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1056 LGIVSQEPILFDCSIA-ENIAYGDNSrvvphdeiVRAAKEANIHPFIETLPQKYN--TRVGDKGTQLSGGQKQRIAIARA 1132
Cdd:PRK09493 79 AGMVFQQFYLFPHLTAlENVMFGPLR--------VRGASKEEAEKQARELLAKVGlaERAHHYPSELSGGQQQRVAIARA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568932737 1133 LIRQPRVLLLDEATSALDTE-SEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHGTHQQLL 1204
Cdd:PRK09493 151 LAVKPKLMLFDEPTSALDPElRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKvASRLIFIDKGRIAEDGDPQVLI 224
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
338-553 |
3.93e-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: 117.14 E-value: 3.93e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 338 LEFSDVHFSYPsraNIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVR-CLREII 416
Cdd:cd03216 1 LELRGITKRFG---GVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRdARRAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 417 GVVSQepvlfsttiaenirygrgnvtmdeiekavkeanaydfimklpqkfdtlvgdrgaqLSGGQKQRIAIARALVRNPK 496
Cdd:cd03216 78 AMVYQ-------------------------------------------------------LSVGERQMVEIARALARNAR 102
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568932737 497 ILLLDEATSALdteSEAEVQAALD----KAREGRTTIVIAHRLSTIRN-ADVIAGFEDGVIV 553
Cdd:cd03216 103 LLILDEPTAAL---TPAEVERLFKvirrLRAQGVAVIFISHRLDEVFEiADRVTVLRDGRVV 161
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
332-565 |
8.07e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 120.23 E-value: 8.07e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 332 DNIkgnLEFSDVHFSYPSraNIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRC 411
Cdd:PRK13647 2 DNI---IEVEDLHFRYKD--GTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKW 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 412 LREIIGVVSQEP--VLFSTTIAENIRYGRGN--VTMDEIEKAVKEA----NAYDFIMKLPQkfdtlvgdrgaQLSGGQKQ 483
Cdd:PRK13647 77 VRSKVGLVFQDPddQVFSSTVWDDVAFGPVNmgLDKDEVERRVEEAlkavRMWDFRDKPPY-----------HLSYGQKK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 484 RIAIARALVRNPKILLLDEATSALDTESEAEVQAALDK-AREGRTTIVIAHRLS-TIRNADVIAGFEDGVIVEQGSHSEL 561
Cdd:PRK13647 146 RVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRlHNQGKTVIVATHDVDlAAEWADQVIVLKEGRVLAEGDKSLL 225
|
....
gi 568932737 562 MKKE 565
Cdd:PRK13647 226 TDED 229
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
700-912 |
8.89e-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: 120.43 E-value: 8.89e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 700 LVFLGLGVLSFFTFFLQGFTFGKAGEILTTRLRSMAFKAMLRQDMSWFDdhKNSTGALSTRLATDAAQVQGATGTRLALI 779
Cdd:cd18780 46 LILLGVVLIGSIATFLRSWLFTLAGERVVARLRKRLFSAIIAQEIAFFD--VTRTGELLNRLSSDTQVLQNAVTVNLSML 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 780 AQNTANLGTGIIISFIYGWQLTLLLLSVVPFIAVAGIVEMKMLAGNAKRDKKEMEAAGKIATEAIENIRTVVSLTQERKF 859
Cdd:cd18780 124 LRYLVQIIGGLVFMFTTSWKLTLVMLSVVPPLSIGAVIYGKYVRKLSKKFQDALAAASTVAEESISNIRTVRSFAKETKE 203
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 568932737 860 ESMYVEKLHGPYRNSVRKAHIYGITFSISQAFMYFSYAGCFRFGSYLIVNGHM 912
Cdd:cd18780 204 VSRYSEKINESYLLGKKLARASGGFNGFMGAAAQLAIVLVLWYGGRLVIDGEL 256
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
338-561 |
1.10e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 119.84 E-value: 1.10e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 338 LEFSDVHFSYPSRANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLREIIG 417
Cdd:PRK13650 5 IEVKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 418 VVSQEP--VLFSTTIAENIRYGRGN--VTMDEIEKAVKEA----NAYDFIMKLPqkfdtlvgdrgAQLSGGQKQRIAIAR 489
Cdd:PRK13650 85 MVFQNPdnQFVGATVEDDVAFGLENkgIPHEEMKERVNEAlelvGMQDFKEREP-----------ARLSGGQKQRVAIAG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568932737 490 ALVRNPKILLLDEATSALDTESEAEVQAALDKARE--GRTTIVIAHRLSTIRNADVIAGFEDGVIVEQGSHSEL 561
Cdd:PRK13650 154 AVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDdyQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPREL 227
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
996-1194 |
1.20e-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: 117.78 E-value: 1.20e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 996 LQGLSLEVK---KGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQ----EAKKLNVQWLRAQLGIVSQEPILF-D 1067
Cdd:cd03297 10 LPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlfdSRKKINLPPQQRKIGLVFQQYALFpH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1068 CSIAENIAYG-----DNSRVVPHDEIVRAAkeaNIHPFIETLPQkyntrvgdkgtQLSGGQKQRIAIARALIRQPRVLLL 1142
Cdd:cd03297 90 LNVRENLAFGlkrkrNREDRISVDELLDLL---GLDHLLNRYPA-----------QLSGGEKQRVALARALAAQPELLLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 568932737 1143 DEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLSTIQN-ADLIVVIENGKV 1194
Cdd:cd03297 156 DEPFSALDRALRLQLLPELKQikKNLNIPVIFVTHDLSEAEYlADRIVVMEDGRL 210
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
338-554 |
1.31e-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: 118.31 E-value: 1.31e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 338 LEFSDVHFSYPSRAN-IKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFN------VR 410
Cdd:COG4181 9 IELRGLTKTVGTGAGeLTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDedararLR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 411 clREIIGVVSQ-EPVLFSTTIAENI-----RYGRGNVTmdeiEKAVKEANAYDfimklpqkfdtlVGDRG----AQLSGG 480
Cdd:COG4181 89 --ARHVGFVFQsFQLLPTLTALENVmlpleLAGRRDAR----ARARALLERVG------------LGHRLdhypAQLSGG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568932737 481 QKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAAL-DKAREGRTTIVIA-HRLSTIRNADVIAGFEDGVIVE 554
Cdd:COG4181 151 EQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLfELNRERGTTLVLVtHDPALAARCDRVLRLRAGRLVE 226
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
338-561 |
2.06e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 119.04 E-value: 2.06e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 338 LEFSDVHFSYPSRANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLREIIG 417
Cdd:PRK13642 5 LEVENLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 418 VVSQEP--VLFSTTIAENIRYGRGN--VTMDEIEKAVKEA----NAYDFIMKLPqkfdtlvgdrgAQLSGGQKQRIAIAR 489
Cdd:PRK13642 85 MVFQNPdnQFVGATVEDDVAFGMENqgIPREEMIKRVDEAllavNMLDFKTREP-----------ARLSGGQKQRVAVAG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568932737 490 ALVRNPKILLLDEATSALDTESEAEVQAALDKAREGR--TTIVIAHRLSTIRNADVIAGFEDGVIVEQGSHSEL 561
Cdd:PRK13642 154 IIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYqlTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSEL 227
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
338-548 |
2.12e-29 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 118.60 E-value: 2.12e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 338 LEFSDVHFSYPSRaniKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYD-----PTEGKISIDGQDI--RNFNVR 410
Cdd:PRK14258 8 IKVNNLSFYYDTQ---KILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNElesevRVEGRVEFFNQNIyeRRVNLN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 411 CLREIIGVVSQEPVLFSTTIAENIRYG------RGNVTMDEI-EKAVKEANAYDFIMKLPQKfdtlvgdRGAQLSGGQKQ 483
Cdd:PRK14258 85 RLRRQVSMVHPKPNLFPMSVYDNVAYGvkivgwRPKLEIDDIvESALKDADLWDEIKHKIHK-------SALDLSGGQQQ 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568932737 484 RIAIARALVRNPKILLLDEATSALDTESEAEVQAALD--KAREGRTTIVIAHRLSTI-RNADVIAGFE 548
Cdd:PRK14258 158 RLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQslRLRSELTMVIVSHNLHQVsRLSDFTAFFK 225
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
338-565 |
2.43e-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: 2.43e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 338 LEFSDVHFSYPSRaniKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGK-ISIDGQDIRNFNVRCLREII 416
Cdd:COG1119 4 LELRNVTVRRGGK---TILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdVRLFGERRGGEDVWELRKRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 417 GVVSQEpvlfsttIAENIRygrGNVTmdeIEKAVKEAnAYDFIMkLPQKFD-----------TLVG-----DRG-AQLSG 479
Cdd:COG1119 81 GLVSPA-------LQLRFP---RDET---VLDVVLSG-FFDSIG-LYREPTdeqrerarellELLGlahlaDRPfGTLSQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 480 GQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDK-AREGRTTIV-IAHRLStirnaDVIAGF------EDGV 551
Cdd:COG1119 146 GEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKlAAEGAPTLVlVTHHVE-----EIPPGIthvlllKDGR 220
|
250
....*....|....
gi 568932737 552 IVEQGSHSELMKKE 565
Cdd:COG1119 221 VVAAGPKEEVLTSE 234
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
992-1198 |
2.53e-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: 2.53e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 992 NVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQ-----EAKKLNVqwlraqlGIVSQEPILF 1066
Cdd:cd03301 12 NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRdvtdlPPKDRDI-------AMVFQNYALY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1067 -DCSIAENIAYGDNSRVVPHDEIVRAAKEANIHPFIETLPQKyntrvgdKGTQLSGGQKQRIAIARALIRQPRVLLLDEA 1145
Cdd:cd03301 85 pHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDR-------KPKQLSGGQRQRVALGRAIVREPKVFLMDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 568932737 1146 TSALDTESEKVVQEALDK--AREGRTCIVIAH-RLSTIQNADLIVVIENGKVKEHG 1198
Cdd:cd03301 158 LSNLDAKLRVQMRAELKRlqQRLGTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
992-1194 |
2.91e-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: 2.91e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 992 NVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQwlRAQ-LGIvsqepilfdcsi 1070
Cdd:cd03216 12 GVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPR--DARrAGI------------ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1071 aeniaygdnsrvvphdeivraakeANIHpfietlpqkyntrvgdkgtQLSGGQKQRIAIARALIRQPRVLLLDEATSAL- 1149
Cdd:cd03216 78 ------------------------AMVY-------------------QLSVGERQMVEIARALARNARLLILDEPTAALt 114
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 568932737 1150 DTESEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVIENGKV 1194
Cdd:cd03216 115 PAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEiADRVTVLRDGRV 160
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
978-1203 |
3.91e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 117.93 E-value: 3.91e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 978 VTFNEVVFNYPTRANVpVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQWLRAQLG 1057
Cdd:PRK13648 8 IVFKNVSFQYQSDASF-TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1058 IVSQEPI-LFDCSIAE-NIAYGDNSRVVPHDEIVR----AAKEANIHPFIETLPQkyntrvgdkgtQLSGGQKQRIAIAR 1131
Cdd:PRK13648 87 IVFQNPDnQFVGSIVKyDVAFGLENHAVPYDEMHRrvseALKQVDMLERADYEPN-----------ALSGGQKQRVAIAG 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568932737 1132 ALIRQPRVLLLDEATSALDTESEKVVQEALDKAREGR--TCIVIAHRLSTIQNADLIVVIENGKVKEHGTHQQL 1203
Cdd:PRK13648 156 VLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEI 229
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
337-565 |
4.95e-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: 4.95e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 337 NLEFSDVHFSYPSRAnikilKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNV--Rclre 414
Cdd:COG3840 1 MLRLDDLTYRYGDFP-----LRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPaeR---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 415 IIGVVSQEPVLFS-TTIAENIRYG---RGNVTMDE---IEKAVKEANAYDFIMKLPqkfdtlvgdrgAQLSGGQKQRIAI 487
Cdd:COG3840 72 PVSMLFQENNLFPhLTVAQNIGLGlrpGLKLTAEQraqVEQALERVGLAGLLDRLP-----------GQLSGGQRQRVAL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 488 ARALVRNPKILLLDEATSALDTESEAEVQAALDK--AREGRTTIVIAHRLS-TIRNADVIAGFEDGVIVEQGSHSELMKK 564
Cdd:COG3840 141 ARCLVRKRPILLLDEPFSALDPALRQEMLDLVDElcRERGLTVLMVTHDPEdAARIADRVLLVADGRIAADGPTAALLDG 220
|
.
gi 568932737 565 E 565
Cdd:COG3840 221 E 221
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
985-1214 |
5.08e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 117.91 E-value: 5.08e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 985 FNYP--TRAnvpvLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQWLRAQLGIVSQE 1062
Cdd:PRK13647 12 FRYKdgTKA----LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLVFQD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1063 P--ILFDCSIAENIAYGDNSRVVPHDEIVRAAKEA----NIHPFIETLPQkyntrvgdkgtQLSGGQKQRIAIARALIRQ 1136
Cdd:PRK13647 88 PddQVFSSTVWDDVAFGPVNMGLDKDEVERRVEEAlkavRMWDFRDKPPY-----------HLSYGQKKRVAIAGVLAMD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1137 PRVLLLDEATSALDTESEKVVQEALDK-AREGRTCIVIAHRLS-TIQNADLIVVIENGKVKEHG-----THQQLLAQKGI 1209
Cdd:PRK13647 157 PDVIVLDEPMAYLDPRGQETLMEILDRlHNQGKTVIVATHDVDlAAEWADQVIVLKEGRVLAEGdksllTDEDIVEQAGL 236
|
....*
gi 568932737 1210 YFSMV 1214
Cdd:PRK13647 237 RLPLV 241
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
995-1199 |
5.12e-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: 116.77 E-value: 5.12e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 995 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQwLRAQLGIVS--QEPILF-DCSIA 1071
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPH-EIARLGIGRtfQIPRLFpELTVL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1072 ENI----------AYGDNSRVVPHDEIVRAAKEAnihpfIET--LPQKYNTRVGDkgtqLSGGQKQRIAIARALIRQPRV 1139
Cdd:cd03219 94 ENVmvaaqartgsGLLLARARREEREARERAEEL-----LERvgLADLADRPAGE----LSYGQQRRLEIARALATDPKL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568932737 1140 LLLDEATSAL-DTESEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHGT 1199
Cdd:cd03219 165 LLLDEPAAGLnPEETEELAELIRELRERGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGT 226
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
332-565 |
5.83e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 117.54 E-value: 5.83e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 332 DNIkgnLEFSDVHFSYPSRANIKiLKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRC 411
Cdd:PRK13648 5 NSI---IVFKNVSFQYQSDASFT-LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 412 LREIIGVVSQEP--VLFSTTIAENIRYGRGN--VTMDEIEKAVKEA----NAYDFIMKLPQkfdtlvgdrgaQLSGGQKQ 483
Cdd:PRK13648 81 LRKHIGIVFQNPdnQFVGSIVKYDVAFGLENhaVPYDEMHRRVSEAlkqvDMLERADYEPN-----------ALSGGQKQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 484 RIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKAREGR--TTIVIAHRLSTIRNADVIAGFEDGVIVEQGSHSEL 561
Cdd:PRK13648 150 RVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEI 229
|
....
gi 568932737 562 MKKE 565
Cdd:PRK13648 230 FDHA 233
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
655-912 |
6.27e-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: 118.03 E-value: 6.27e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 655 FVVGTVCAIANGALqPAFsiiLSEMI-AIFGPGDDAVKQQKCNMFSLVFLGLGVLSFftffLQGFTFGKAGEILTTRLRS 733
Cdd:cd18572 2 FVFLVVAALSELAI-PHY---TGAVIdAVVADGSREAFYRAVLLLLLLSVLSGLFSG----LRGGCFSYAGTRLVRRLRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 734 MAFKAMLRQDMSWFDDHKnsTGALSTRLATDAAQVQGATGTRLALIAQNTANLGTGIIISFIYGWQLTLLLLSVVPFIAV 813
Cdd:cd18572 74 DLFRSLLRQDIAFFDATK--TGELTSRLTSDCQKVSDPLSTNLNVFLRNLVQLVGGLAFMFSLSWRLTLLAFITVPVIAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 814 AGIVEMKMLAGNAKRDKKEMEAAGKIATEAIENIRTVVSLTQERKFESMYVEKLHGPYRNSVRKAHIYGITFSISQAFMY 893
Cdd:cd18572 152 ITKVYGRYYRKLSKEIQDALAEANQVAEEALSNIRTVRSFATEEREARRYERALDKALKLSVRQALAYAGYVAVNTLLQN 231
|
250
....*....|....*....
gi 568932737 894 FSYAGCFRFGSYLIVNGHM 912
Cdd:cd18572 232 GTQVLVLFYGGHLVLSGRM 250
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
338-555 |
8.97e-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: 8.97e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 338 LEFSDVHFSYPS------RANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFN--- 408
Cdd:TIGR02769 3 LEVRDVTHTYRTgglfgaKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDrkq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 409 VRCLREIIGVVSQE-PVLFS--TTIAENIRYGRGNVT-MDEIEKAVKEANAYDfIMKLPqkfDTLVGDRGAQLSGGQKQR 484
Cdd:TIGR02769 83 RRAFRRDVQLVFQDsPSAVNprMTVRQIIGEPLRHLTsLDESEQKARIAELLD-MVGLR---SEDADKLPRQLSGGQLQR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568932737 485 IAIARALVRNPKILLLDEATSALDTESEAEVQAALDK--AREGRTTIVIAHRLSTI-RNADVIAGFEDGVIVEQ 555
Cdd:TIGR02769 159 INIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKlqQAFGTAYLFITHDLRLVqSFCQRVAVMDKGQIVEE 232
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
332-565 |
1.04e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 117.21 E-value: 1.04e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 332 DNIkgnLEFSDVHFSYPSrANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDP---TEGKISIDGQDIRNFN 408
Cdd:PRK13640 3 DNI---VEFKHVSFTYPD-SKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDGITLTAKT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 409 VRCLREIIGVVSQEP--VLFSTTIAENIRYGRGN--VTMDEIEKAVKEANA----YDFIMKLPQkfdtlvgdrgaQLSGG 480
Cdd:PRK13640 79 VWDIREKVGIVFQNPdnQFVGATVGDDVAFGLENraVPRPEMIKIVRDVLAdvgmLDYIDSEPA-----------NLSGG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 481 QKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKARE--GRTTIVIAHRLSTIRNADVIAGFEDGVIVEQGSH 558
Cdd:PRK13640 148 QKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKknNLTVISITHDIDEANMADQVLVLDDGKLLAQGSP 227
|
....*..
gi 568932737 559 SELMKKE 565
Cdd:PRK13640 228 VEIFSKV 234
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
989-1191 |
1.21e-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: 1.21e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 989 TRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDP---MAGSVLLDGQEAKKLNVQwlRAQLGIVSQEPIL 1065
Cdd:COG4136 10 TLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALPAE--QRRIGILFQDDLL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1066 FD-CSIAENIAYG---DNSRVVPHDEIVRAAKEANIHPFIETLPqkyntrvgdkgTQLSGGQKQRIAIARALIRQPRVLL 1141
Cdd:COG4136 88 FPhLSVGENLAFAlppTIGRAQRRARVEQALEEAGLAGFADRDP-----------ATLSGGQRARVALLRALLAEPRALL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 568932737 1142 LDEATSALDTE-SEKVVQEALDKARE-GRTCIVIAHRLSTIQNADLIVVIEN 1191
Cdd:COG4136 157 LDEPFSKLDAAlRAQFREFVFEQIRQrGIPALLVTHDEEDAPAAGRVLDLGN 208
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
350-554 |
1.38e-28 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 116.32 E-value: 1.38e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 350 RANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFN---VRCLREIIGVVSQEP--- 423
Cdd:PRK10419 22 HQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNraqRKAFRRDIQMVFQDSisa 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 424 VLFSTTIAENIRYG-RGNVTMDEIEKAVKEANAYDfIMKLPqkfDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDE 502
Cdd:PRK10419 102 VNPRKTVREIIREPlRHLLSLDKAERLARASEMLR-AVDLD---DSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDE 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 568932737 503 ATSALDTESEAEVQAALDKAREGRTT--IVIAHRLSTI-RNADVIAGFEDGVIVE 554
Cdd:PRK10419 178 AVSNLDLVLQAGVIRLLKKLQQQFGTacLFITHDLRLVeRFCQRVMVMDNGQIVE 232
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
331-575 |
1.40e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 116.87 E-value: 1.40e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 331 PDNIkgnLEFSDVHFSYPSraNIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQ--DIRNFN 408
Cdd:PRK13636 2 EDYI---LKVEELNYNYSD--GTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpiDYSRKG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 409 VRCLREIIGVVSQEP--VLFSTTIAENIRYGRGNVTM--DEIEKAVKEANAYDFIMKLPQKfdtlvgdRGAQLSGGQKQR 484
Cdd:PRK13636 77 LMKLRESVGMVFQDPdnQLFSASVYQDVSFGAVNLKLpeDEVRKRVDNALKRTGIEHLKDK-------PTHCLSFGQKKR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 485 IAIARALVRNPKILLLDEATSALDTESEAEV-QAALDKAREGRTTIVIA-HRLSTIR-NADVIAGFEDGVIVEQGSHSEL 561
Cdd:PRK13636 150 VAIAGVLVMEPKVLVLDEPTAGLDPMGVSEImKLLVEMQKELGLTIIIAtHDIDIVPlYCDNVFVMKEGRVILQGNPKEV 229
|
250
....*....|....*
gi 568932737 562 M-KKEGIyfRLVNMQ 575
Cdd:PRK13636 230 FaEKEML--RKVNLR 242
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
965-1222 |
1.57e-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: 1.57e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 965 SGEGLWPDKFE---------GSVTFNEVVFNYpTRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAG 1035
Cdd:TIGR00957 615 SHEELEPDSIErrtikpgegNSITVHNATFTW-ARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEG 693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1036 SVLLDGQEAkklnvqwlraqlgIVSQEPILFDCSIAENIAYGDNSRVVPHDEIVRAAKeanIHPFIETLPQKYNTRVGDK 1115
Cdd:TIGR00957 694 HVHMKGSVA-------------YVPQQAWIQNDSLRENILFGKALNEKYYQQVLEACA---LLPDLEILPSGDRTEIGEK 757
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1116 GTQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEAL---DKAREGRTCIVIAHRLSTIQNADLIVVIENG 1192
Cdd:TIGR00957 758 GVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVigpEGVLKNKTRILVTHGISYLPQVDVIIVMSGG 837
|
250 260 270
....*....|....*....|....*....|
gi 568932737 1193 KVKEHGTHQQLLAQKGIYFSMVNIQAGTQN 1222
Cdd:TIGR00957 838 KISEMGSYQELLQRDGAFAEFLRTYAPDEQ 867
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
658-930 |
1.71e-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: 1.71e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 658 GTVCAIANGALQPAFSIILSEMI-AIFGPGDDAVKQQkcnmFSLVFLGLGVL-SFFTFFlQGFTFGKAGEILTTRLRSMA 735
Cdd:cd18576 1 GLILLLLSSAIGLVFPLLAGQLIdAALGGGDTASLNQ----IALLLLGLFLLqAVFSFF-RIYLFARVGERVVADLRKDL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 736 FKAMLRQDMSWFDDHKnsTGALSTRLATDAAQVQGATGTRLALIAQNTANLGTGIIISFIYGWQLTLLLLSVVPFIAVAG 815
Cdd:cd18576 76 YRHLQRLPLSFFHERR--VGELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWKLTLLMLATVPVVVLVA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 816 IVEMKMLAGNAKRDKKEMEAAGKIATEAIENIRTVVSLTQERkFESM-YVEKLHGPYRNSVRKAHIYGITFSISQAFMYF 894
Cdd:cd18576 154 VLFGRRIRKLSKKVQDELAEANTIVEETLQGIRVVKAFTRED-YEIErYRKALERVVKLALKRARIRALFSSFIIFLLFG 232
|
250 260 270
....*....|....*....|....*....|....*...
gi 568932737 895 SYAGCFRFGSYLIVNGHMRFKDVI--LVFSAIVLGAVA 930
Cdd:cd18576 233 AIVAVLWYGGRLVLAGELTAGDLVafLLYTLFIAGSIG 270
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
359-564 |
1.75e-28 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 118.28 E-value: 1.75e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 359 LNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRcLREIIgVVSQEPVLFS-TTIAENIRYG 437
Cdd:PRK11432 25 LNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQ-QRDIC-MVFQSYALFPhMSLGENVGYG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 438 RG--NVTMDEIEKAVKEANAydfimklpqkfdtLV-----GDRGA-QLSGGQKQRIAIARALVRNPKILLLDEATSALDt 509
Cdd:PRK11432 103 LKmlGVPKEERKQRVKEALE-------------LVdlagfEDRYVdQISGGQQQRVALARALILKPKVLLFDEPLSNLD- 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568932737 510 eseAEVQAAL-DKARE-----GRTTIVIAHRLS-TIRNADVIAGFEDGVIVEQGSHSELMKK 564
Cdd:PRK11432 169 ---ANLRRSMrEKIRElqqqfNITSLYVTHDQSeAFAVSDTVIVMNKGKIMQIGSPQELYRQ 227
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
338-567 |
1.95e-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: 1.95e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 338 LEFSDVHFSYPsraNIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNV-RCLREII 416
Cdd:COG0410 4 LEVENLHAGYG---GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPhRIARLGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 417 GVVSQEPVLFST-TIAENIRYGRGNVTMDEIEKAVKEAnAYDFIMKLPQKFDTlvgdRGAQLSGGQKQRIAIARALVRNP 495
Cdd:COG0410 81 GYVPEGRRIFPSlTVEENLLLGAYARRDRAEVRADLER-VYELFPRLKERRRQ----RAGTLSGGEQQMLAIGRALMSRP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 496 KILLLDEATSALdteseA-----EVQAALDKAREGRTTIVI----AHRLSTIrnADVIAGFEDGVIVEQGSHSELMKKEG 566
Cdd:COG0410 156 KLLLLDEPSLGL-----ApliveEIFEIIRRLNREGVTILLveqnARFALEI--ADRAYVLERGRIVLEGTAAELLADPE 228
|
.
gi 568932737 567 I 567
Cdd:COG0410 229 V 229
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
338-564 |
3.07e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 116.03 E-value: 3.07e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 338 LEFSDVHFSYPSRA--NIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDI----RNFNVRC 411
Cdd:PRK13646 3 IRFDNVSYTYQKGTpyEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIthktKDKYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 412 LREIIGVVSQ--EPVLFSTTIAENIRYGRGNVTMDeIEKAvkEANAYDFIMKLPQKFDTLvGDRGAQLSGGQKQRIAIAR 489
Cdd:PRK13646 83 VRKRIGMVFQfpESQLFEDTVEREIIFGPKNFKMN-LDEV--KNYAHRLLMDLGFSRDVM-SQSPFQMSGGQMRKIAIVS 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568932737 490 ALVRNPKILLLDEATSALDTESEAEVQAALDKAR--EGRTTIVIAHRLSTI-RNADVIAGFEDGVIVEQGSHSELMKK 564
Cdd:PRK13646 159 ILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtdENKTIILVSHDMNEVaRYADEVIVMKEGSIVSQTSPKELFKD 236
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
983-1205 |
3.39e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 115.58 E-value: 3.39e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 983 VVFNYPTRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQWLRAQLGIVSQE 1062
Cdd:PRK13642 10 LVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIGMVFQN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1063 P--ILFDCSIAENIAYGDNSRVVPHDEIVRAAKEAnihpFIETLPQKYNTRvgdKGTQLSGGQKQRIAIARALIRQPRVL 1140
Cdd:PRK13642 90 PdnQFVGATVEDDVAFGMENQGIPREEMIKRVDEA----LLAVNMLDFKTR---EPARLSGGQKQRVAVAGIIALRPEII 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568932737 1141 LLDEATSALD----TESEKVVQEALDKARegRTCIVIAHRLSTIQNADLIVVIENGKVKEHGTHQQLLA 1205
Cdd:PRK13642 163 ILDESTSMLDptgrQEIMRVIHEIKEKYQ--LTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFA 229
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
338-562 |
5.30e-28 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 114.30 E-value: 5.30e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 338 LEFSDVHFSYPSRaniKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIR------------ 405
Cdd:PRK10619 6 LNVIDLHKRYGEH---EVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlkva 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 406 -NFNVRCLREIIGVVSQEPVLFS-TTIAENIRygRGNVTMDEIEKAVKEANAYDFIMKLPQKfDTLVGDRGAQLSGGQKQ 483
Cdd:PRK10619 83 dKNQLRLLRTRLTMVFQHFNLWShMTVLENVM--EAPIQVLGLSKQEARERAVKYLAKVGID-ERAQGKYPVHLSGGQQQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 484 RIAIARALVRNPKILLLDEATSALDTESEAEVQAALDK-AREGRTTIVIAHRLSTIRNADVIAGF-EDGVIVEQGSHSEL 561
Cdd:PRK10619 160 RVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQlAEEGKTMVVVTHEMGFARHVSSHVIFlHQGKIEEEGAPEQL 239
|
.
gi 568932737 562 M 562
Cdd:PRK10619 240 F 240
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
995-1206 |
6.59e-28 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 116.74 E-value: 6.59e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 995 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQwlRAQLGIVSQEPILF-DCSIAEN 1073
Cdd:PRK11432 21 VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQ--QRDICMVFQSYALFpHMSLGEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1074 IAYGDNSRVVPHDEIVRAAKEA----NIHPFIEtlpqkyntRVGDkgtQLSGGQKQRIAIARALIRQPRVLLLDEATSAL 1149
Cdd:PRK11432 99 VGYGLKMLGVPKEERKQRVKEAlelvDLAGFED--------RYVD---QISGGQQQRVALARALILKPKVLLFDEPLSNL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568932737 1150 DTESEKVVQEaldKARE-----GRTCIVIAHRLS-TIQNADLIVVIENGKVKEHGTHQQLLAQ 1206
Cdd:PRK11432 168 DANLRRSMRE---KIRElqqqfNITSLYVTHDQSeAFAVSDTVIVMNKGKIMQIGSPQELYRQ 227
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
993-1206 |
1.26e-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: 1.26e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 993 VPVLQGLSLEVKKGQTLALVGSSGCGKS----TVVQLLERFYDPMAGSVLLDGQEAKKLNVQWLRA----QLGIVSQEPI 1064
Cdd:COG4172 23 VEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERELRRirgnRIAMIFQEPM 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1065 -----LFdcSIAENIAygdnSRVVPHDEIVRAAKEANIhpfIETLpqkynTRVG--DKGT-------QLSGGQKQRIAIA 1130
Cdd:COG4172 103 tslnpLH--TIGKQIA----EVLRLHRGLSGAAARARA---LELL-----ERVGipDPERrldayphQLSGGQRQRVMIA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1131 RALIRQPRVLLLDEATSALDTesekVVQ-EALD-----KAREGRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHGTHQQL 1203
Cdd:COG4172 169 MALANEPDLLIADEPTTALDV----TVQaQILDllkdlQRELGMALLLITHDLGVVRRfADRVAVMRQGEIVEQGPTAEL 244
|
...
gi 568932737 1204 LAQ 1206
Cdd:COG4172 245 FAA 247
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
211-534 |
1.34e-27 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 119.53 E-value: 1.34e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 211 IAF-GGQNKELERYQKHLENAKKIgIKKAISANISMGiAFLLIYASYALAFWY--GSTLVISKEYTIGNAMTV--FFSIL 285
Cdd:COG4178 234 IALyRGEAAERRRLRRRFDAVIAN-WRRLIRRQRNLT-FFTTGYGQLAVIFPIlvAAPRYFAGEITLGGLMQAasAFGQV 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 286 IGAFSVgqaapCIDAFAN-ARGAAYVI-----FDIIDNNPKIDSFSERGHKPDNikGNLEFSDVHFSYPSRAniKILKGL 359
Cdd:COG4178 312 QGALSW-----FVDNYQSlAEWRATVDrlagfEEALEAADALPEAASRIETSED--GALALEDLTLRTPDGR--PLLEDL 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 360 NLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISI-DGQDIrnfnvrcLreiigVVSQEPVLFSTTIAENIRY-- 436
Cdd:COG4178 383 SLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpAGARV-------L-----FLPQRPYLPLGTLREALLYpa 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 437 GRGNVTMDEIEKAVKEANaydfIMKLPQKFDTlVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQ 516
Cdd:COG4178 451 TAEAFSDAELREALEAVG----LGHLAERLDE-EADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALY 525
|
330
....*....|....*...
gi 568932737 517 AALDKAREGRTTIVIAHR 534
Cdd:COG4178 526 QLLREELPGTTVISVGHR 543
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
338-556 |
1.40e-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: 1.40e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 338 LEFSDVHF---SYPSRANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLL--QRLYDPTEGKISIDGQDIRNFNVRCl 412
Cdd:cd03213 4 LSFRNLTVtvkSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGRPLDKRSFRK- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 413 reIIGVVSQEPVLFST-TIAENIrygrgnvtmdeiekavkeanayDFIMKLpqkfdtlvgdRGaqLSGGQKQRIAIARAL 491
Cdd:cd03213 83 --IIGYVPQDDILHPTlTVRETL----------------------MFAAKL----------RG--LSGGERKRVSIALEL 126
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568932737 492 VRNPKILLLDEATSALDTESEAEVQAALDK-AREGRTTIVIAHRLSTirnaDVIAGFEDGVIVEQG 556
Cdd:cd03213 127 VSNPSLLFLDEPTSGLDSSSALQVMSLLRRlADTGRTIICSIHQPSS----EIFELFDKLLLLSQG 188
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
338-553 |
1.40e-27 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 119.83 E-value: 1.40e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 338 LEFSDVHFSYPS-RANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCL---- 412
Cdd:PRK10535 5 LELKDIRRSYPSgEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALaqlr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 413 REIIGVVSQEPVLFSTTIAENirygrgNVTMDEI----EKAVKEANAYDFIMKLpqKFDTLVGDRGAQLSGGQKQRIAIA 488
Cdd:PRK10535 85 REHFGFIFQRYHLLSHLTAAQ------NVEVPAVyaglERKQRLLRAQELLQRL--GLEDRVEYQPSQLSGGQQQRVSIA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568932737 489 RALVRNPKILLLDEATSALDTESEAEVQAALDKARE-GRTTIVIAHRLSTIRNADVIAGFEDGVIV 553
Cdd:PRK10535 157 RALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDrGHTVIIVTHDPQVAAQAERVIEIRDGEIV 222
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
999-1207 |
1.48e-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: 1.48e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 999 LSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQ----EAKKLNVQWLRAQLGIVSQEPILF-DCSIAEN 1073
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRtlfdSRKGIFLPPEKRRIGYVFQEARLFpHLSVRGN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1074 IAYGdNSRVVPHDEIVRAAKEA---NIHPFIETLPQKyntrvgdkgtqLSGGQKQRIAIARALIRQPRVLLLDEATSALD 1150
Cdd:TIGR02142 96 LRYG-MKRARPSERRISFERVIellGIGHLLGRLPGR-----------LSGGEKQRVAIGRALLSSPRLLLMDEPLAALD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1151 TESEKVVQEALDKARE--GRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHGTHQQLLAQK 1207
Cdd:TIGR02142 164 DPRKYEILPYLERLHAefGIPILYVSHSLQEVLRlADRVVVLEDGRVAAAGPIAEVWASP 223
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
73-308 |
1.59e-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: 113.73 E-value: 1.59e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 73 VAAYIQVSFWTLAAGRQIKKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDDVSKISEGIGDKVGMFFQAIATFFAGFIV 152
Cdd:cd18576 51 VFSFFRIYLFARVGERVVADLRKDLYRHLQRLPLSFFHERRVGELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 153 GFIRGWKLTLVIMAISPILGLSTAVWAKILSTFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKELERYQKHLENAKK 232
Cdd:cd18576 131 LFFISWKLTLLMLATVPVVVLVAVLFGRRIRKLSKKVQDELAEANTIVEETLQGIRVVKAFTREDYEIERYRKALERVVK 210
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568932737 233 IGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTIGNAMT-VFFSILIGAfSVGQAAPCIDAFANARGAA 308
Cdd:cd18576 211 LALKRARIRALFSSFIIFLLFGAIVAVLWYGGRLVLAGELTAGDLVAfLLYTLFIAG-SIGSLADLYGQLQKALGAS 286
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
356-547 |
1.60e-27 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 113.34 E-value: 1.60e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 356 LKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYD--PT---EGKISIDGQDIRNFNVRC--LREIIGVVSQEPVLFST 428
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDliPGfrvEGKVTFHGKNLYAPDVDPveVRRRIGMVFQKPNPFPK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 429 TIAENIRYG------RGNvtMDE-IEKAVKEANAYDFIM-KLPQKfdtlvgdrGAQLSGGQKQRIAIARALVRNPKILLL 500
Cdd:PRK14243 106 SIYDNIAYGaringyKGD--MDElVERSLRQAALWDEVKdKLKQS--------GLSLSGGQQQRLCIARAIAVQPEVILM 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 568932737 501 DEATSALDTESEAEVQAALDKAREGRTTIVIAHRL-STIRNADVIAGF 547
Cdd:PRK14243 176 DEPCSALDPISTLRIEELMHELKEQYTIIIVTHNMqQAARVSDMTAFF 223
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
338-564 |
1.68e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 113.96 E-value: 1.68e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 338 LEFSDVHFSYPSRANI--KILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDI----RNFNVRC 411
Cdd:PRK13634 3 ITFQKVEHRYQYKTPFerRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVItagkKNKKLKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 412 LREIIGVVSQ--EPVLFSTTIAENIRYGRGNVTMDEiEKAVKEANAYDFIMKLPQKfdtlVGDRGA-QLSGGQKQRIAIA 488
Cdd:PRK13634 83 LRKKVGIVFQfpEHQLFEETVEKDICFGPMNFGVSE-EDAKQKAREMIELVGLPEE----LLARSPfELSGGQMRRVAIA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 489 RALVRNPKILLLDEATSALDTESEAEVQ---AALDKaREGRTTIVIAHRLSTIRN-ADVIAGFEDGVIVEQGSHSELMKK 564
Cdd:PRK13634 158 GVLAMEPEVLVLDEPTAGLDPKGRKEMMemfYKLHK-EKGLTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTPREIFAD 236
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
338-561 |
1.70e-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: 1.70e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 338 LEFSDVHFSYPSRANIK-ILKGLNLKVKSGQTVALVGNSGCGKSTT----VQLLQRLYDPTEGKISIDGQDIRNFNVRCL 412
Cdd:COG4172 7 LSVEDLSVAFGQGGGTVeAVKGVSFDIAAGETLALVGESGSGKSVTalsiLRLLPDPAAHPSGSILFDGQDLLGLSEREL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 413 REI----IGVVSQEPV-----LFS--TTIAENIRYGRGnVTMDEIEKAVKEAnaydfimkLpqkfdTLVGDRGA------ 475
Cdd:COG4172 87 RRIrgnrIAMIFQEPMtslnpLHTigKQIAEVLRLHRG-LSGAAARARALEL--------L-----ERVGIPDPerrlda 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 476 ---QLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALD--KAREGRTTIVIAHRLSTIRN-ADVIAGFED 549
Cdd:COG4172 153 yphQLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKdlQRELGMALLLITHDLGVVRRfADRVAVMRQ 232
|
250
....*....|..
gi 568932737 550 GVIVEQGSHSEL 561
Cdd:COG4172 233 GEIVEQGPTAEL 244
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
976-1210 |
1.71e-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: 113.41 E-value: 1.71e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 976 GSVTFNEVVFNYpTRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDpMAGSVLLDGQEAKKLNVQWLRAQ 1055
Cdd:cd03289 1 GQMTVKDLTAKY-TEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1056 LGIVSQEPILFDCSIAENI-AYGDNSrvvpHDEIVRAAKEANIHPFIETLPQKYNTRVGDKGTQLSGGQKQRIAIARALI 1134
Cdd:cd03289 79 FGVIPQKVFIFSGTFRKNLdPYGKWS----DEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568932737 1135 RQPRVLLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIENGKVKEHGTHQQLLAQKGIY 1210
Cdd:cd03289 155 SKAKILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHF 230
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
992-1205 |
2.02e-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: 2.02e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 992 NVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVqWLRAQLGI--VSQEPILF-DC 1068
Cdd:COG0410 15 GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPP-HRIARLGIgyVPEGRRIFpSL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1069 SIAENIAYGdnSRVVPHDEIVRAAKEA--NIHPFIETlpqkyntRVGDKGTQLSGGQKQRIAIARALIRQPRVLLLDEAT 1146
Cdd:COG0410 94 TVEENLLLG--AYARRDRAEVRADLERvyELFPRLKE-------RRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPS 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568932737 1147 SALdteSEKVVQEALDK----AREGRTCIVI---AHRLSTIqnADLIVVIENGKVKEHGTHQQLLA 1205
Cdd:COG0410 165 LGL---APLIVEEIFEIirrlNREGVTILLVeqnARFALEI--ADRAYVLERGRIVLEGTAAELLA 225
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
996-1177 |
2.66e-27 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 112.57 E-value: 2.66e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 996 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMA-----GSVLLDGQE--AKKLNVQWLRAQLGIVSQEPILFDC 1068
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLIPgfrveGKVTFHGKNlyAPDVDPVEVRRRIGMVFQKPNPFPK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1069 SIAENIAYGD--NSRVVPHDEIV-RAAKEAnihpfieTLPQKYNTRVGDKGTQLSGGQKQRIAIARALIRQPRVLLLDEA 1145
Cdd:PRK14243 106 SIYDNIAYGAriNGYKGDMDELVeRSLRQA-------ALWDEVKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEP 178
|
170 180 190
....*....|....*....|....*....|..
gi 568932737 1146 TSALDTESEKVVQEALDKAREGRTCIVIAHRL 1177
Cdd:PRK14243 179 CSALDPISTLRIEELMHELKEQYTIIIVTHNM 210
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
352-561 |
3.15e-27 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 111.93 E-value: 3.15e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 352 NIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYD-----PTEGKISIDGQDIRNFNVRCLREIIGVVSQEPVLF 426
Cdd:PRK14247 15 QVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDIFKMDVIELRRRVQMVFQIPNPI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 427 ST-TIAENIRYG----RGNVTMDEIEKAVKEAnaydfiMKLPQKFDTlVGDR----GAQLSGGQKQRIAIARALVRNPKI 497
Cdd:PRK14247 95 PNlSIFENVALGlklnRLVKSKKELQERVRWA------LEKAQLWDE-VKDRldapAGKLSGGQQQRLCIARALAFQPEV 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568932737 498 LLLDEATSALDTESEAEVQAALDKAREGRTTIVIAH-RLSTIRNADVIAGFEDGVIVEQGSHSEL 561
Cdd:PRK14247 168 LLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHfPQQAARISDYVAFLYKGQIVEWGPTREV 232
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
351-565 |
3.60e-27 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 112.03 E-value: 3.60e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 351 ANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLREIIGVVSQEPVL-FSTT 429
Cdd:PRK11231 13 GTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHHLTpEGIT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 430 IAENIRYGR-------GNVTMDEiEKAVKEAnaydfiMKLPQkFDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDE 502
Cdd:PRK11231 93 VRELVAYGRspwlslwGRLSAED-NARVNQA------MEQTR-INHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568932737 503 ATSALDTESEAEVQAALDKAR-EGRTTIVIAHRLS-TIRNADVIAGFEDGVIVEQGSHSELMKKE 565
Cdd:PRK11231 165 PTTYLDINHQVELMRLMRELNtQGKTVVTVLHDLNqASRYCDHLVVLANGHVMAQGTPEEVMTPG 229
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
337-559 |
4.13e-27 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 111.26 E-value: 4.13e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 337 NLEFSDVHFSYpsrANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIrNFN-------V 409
Cdd:COG4161 2 SIQLKNINCFY---GSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQF-DFSqkpsekaI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 410 RCLREIIGVVSQE----PVLfstTIAENIRYGRGNVTMDEIEKAVKEANAYDFIMKLPQKFDTLvgdrGAQLSGGQKQRI 485
Cdd:COG4161 78 RLLRQKVGMVFQQynlwPHL---TVMENLIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRF----PLHLSGGQQQRV 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568932737 486 AIARALVRNPKILLLDEATSALDTESEAE-VQAALDKAREGRTTIVIAHRLSTIRN-ADVIAGFEDGVIVEQGSHS 559
Cdd:COG4161 151 AIARALMMEPQVLLFDEPTAALDPEITAQvVEIIRELSQTGITQVIVTHEVEFARKvASQVVYMEKGRIIEQGDAS 226
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
978-1199 |
4.23e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 112.59 E-value: 4.23e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 978 VTFNEVVFNYPTrANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGS---VLLDGQEAKKLNVQWLRA 1054
Cdd:PRK13640 6 VEFKHVSFTYPD-SKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnskITVDGITLTAKTVWDIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1055 QLGIVSQEP--ILFDCSIAENIAYGDNSRVVPHDEIVR----AAKEANIHPFIETLPQkyntrvgdkgtQLSGGQKQRIA 1128
Cdd:PRK13640 85 KVGIVFQNPdnQFVGATVGDDVAFGLENRAVPRPEMIKivrdVLADVGMLDYIDSEPA-----------NLSGGQKQRVA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568932737 1129 IARALIRQPRVLLLDEATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTIQNADLIVVIENGKVKEHGT 1199
Cdd:PRK13640 154 IAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKknNLTVISITHDIDEANMADQVLVLDDGKLLAQGS 226
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
979-1175 |
5.00e-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: 5.00e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 979 TFNEVVFNYP-TRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEakklnVQWLRAQLG 1057
Cdd:COG4525 5 TVRHVSVRYPgGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVP-----VTGPGADRG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1058 IVSQEPILFD-CSIAENIAYGDNSRVVPHDEIVRAAKEanihpfietlpqkYNTRVGDKGT------QLSGGQKQRIAIA 1130
Cdd:COG4525 80 VVFQKDALLPwLNVLDNVAFGLRLRGVPKAERRARAEE-------------LLALVGLADFarrriwQLSGGMRQRVGIA 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 568932737 1131 RALIRQPRVLLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAH 1175
Cdd:COG4525 147 RALAADPRFLLMDEPFGALDALTREQMQELLLDvwQRTGKGVFLITH 193
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
996-1206 |
8.47e-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: 8.47e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 996 LQGLSLEVK-----KGQTlALVGSSGCGKSTVVQL---LERfydPMAGSVLLDGQ----EAKKLNVQWLRAQLGIVSQEP 1063
Cdd:COG4148 11 RGGFTLDVDftlpgRGVT-ALFGPSGSGKTTLLRAiagLER---PDSGRIRLGGEvlqdSARGIFLPPHRRRIGYVFQEA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1064 ILFD-CSIAENIAYG-----DNSRVVPHDEIVRAakeANIHPFIETLPQkyntrvgdkgtQLSGGQKQRIAIARALIRQP 1137
Cdd:COG4148 87 RLFPhLSVRGNLLYGrkrapRAERRISFDEVVEL---LGIGHLLDRRPA-----------TLSGGERQRVAIGRALLSSP 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568932737 1138 RVLLLDEATSALDTESeKvvQEALDK----AREGRTCIV-IAHRLSTIQN-ADLIVVIENGKVKEHGTHQQLLAQ 1206
Cdd:COG4148 153 RLLLMDEPLAALDLAR-K--AEILPYlerlRDELDIPILyVSHSLDEVARlADHVVLLEQGRVVASGPLAEVLSR 224
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
342-567 |
8.59e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 111.33 E-value: 8.59e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 342 DVHFSYPSRANIK---ILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNF-NVRCLREIIG 417
Cdd:PRK13633 9 NVSYKYESNEESTeklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEeNLWDIRNKAG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 418 VVSQEP--VLFSTTIAENIRYGRGN--VTMDEIEKAVKEA----NAYDFIMKLPQkfdtlvgdrgaQLSGGQKQRIAIAR 489
Cdd:PRK13633 89 MVFQNPdnQIVATIVEEDVAFGPENlgIPPEEIRERVDESlkkvGMYEYRRHAPH-----------LLSGGQKQRVAIAG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 490 ALVRNPKILLLDEATSALDTESEAEVQAALDK--AREGRTTIVIAHRLSTIRNADVIAGFEDGVIVEQG------SHSEL 561
Cdd:PRK13633 158 ILAMRPECIIFDEPTAMLDPSGRREVVNTIKElnKKYGITIILITHYMEEAVEADRIIVMDSGKVVMEGtpkeifKEVEM 237
|
....*.
gi 568932737 562 MKKEGI 567
Cdd:PRK13633 238 MKKIGL 243
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
352-556 |
9.35e-27 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 109.23 E-value: 9.35e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 352 NIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNfNVRCLREIiGVVSQEPVLFST-TI 430
Cdd:cd03268 12 KKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQK-NIEALRRI-GALIEAPGFYPNlTA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 431 AENIR-----YGRGNVTMDEIEKAVKEANAYDfimklpqkfdtlvgDRGAQLSGGQKQRIAIARALVRNPKILLLDEATS 505
Cdd:cd03268 90 RENLRllarlLGIRKKRIDEVLDVVGLKDSAK--------------KKVKGFSLGMKQRLGIALALLGNPDLLILDEPTN 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 568932737 506 ALDTESEAEVQAAL-DKAREGRTTIVIAHRLSTIRN-ADVIAGFEDGVIVEQG 556
Cdd:cd03268 156 GLDPDGIKELRELIlSLRDQGITVLISSHLLSEIQKvADRIGIINKGKLIEEG 208
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
991-1206 |
9.95e-27 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 112.37 E-value: 9.95e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 991 ANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLN---VQWLRAQLGIVSQEPilfd 1067
Cdd:PRK11308 26 RLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADpeaQKLLRQKIQIVFQNP---- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1068 csiaeniaYGD-NSR----------VVPHDEIVRAAKEANIHPFIEtlpqkyntRVGDKGTQ-------LSGGQKQRIAI 1129
Cdd:PRK11308 102 --------YGSlNPRkkvgqileepLLINTSLSAAERREKALAMMA--------KVGLRPEHydryphmFSGGQRQRIAI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1130 ARALIRQPRVLLLDEATSALDTESE-KVVQEALDKAREGRTCIV-IAHRLSTIQN-ADLIVVIENGKVKEHGTHQQLLAQ 1206
Cdd:PRK11308 166 ARALMLDPDVVVADEPVSALDVSVQaQVLNLMMDLQQELGLSYVfISHDLSVVEHiADEVMVMYLGRCVEKGTKEQIFNN 245
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
982-1207 |
1.15e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 111.09 E-value: 1.15e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 982 EVVFNYP--TRAnvpvLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQ--EAKKLNVQWLRAQLG 1057
Cdd:PRK13636 10 ELNYNYSdgTHA----LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpiDYSRKGLMKLRESVG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1058 IVSQEP--ILFDCSIAENIAYGDNSRVVPHDEIVRAAKEANIHPFIETLPqkyntrvgDKGTQ-LSGGQKQRIAIARALI 1134
Cdd:PRK13636 86 MVFQDPdnQLFSASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLK--------DKPTHcLSFGQKKRVAIAGVLV 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568932737 1135 RQPRVLLLDEATSALD----TESEKVVQEALDKAreGRTCIVIAHRLSTIQ-NADLIVVIENGKVKEHGTHQQLLAQK 1207
Cdd:PRK13636 158 MEPKVLVLDEPTAGLDpmgvSEIMKLLVEMQKEL--GLTIIIATHDIDIVPlYCDNVFVMKEGRVILQGNPKEVFAEK 233
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
994-1192 |
1.47e-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: 1.47e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 994 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLL-----------ERfydPMAGSVLLdgqeakklnvqwlraqlgiVSQE 1062
Cdd:COG4178 377 PLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIaglwpygsgriAR---PAGARVLF-------------------LPQR 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1063 PILFDCSIAENIAYGDNSRVVPHDEIVRAAKEANIHPFIETLpqkynTRVGDKGTQLSGGQKQRIAIARALIRQPRVLLL 1142
Cdd:COG4178 435 PYLPLGTLREALLYPATAEAFSDAELREALEAVGLGHLAERL-----DEEADWDQVLSLGEQQRLAFARLLLHKPDWLFL 509
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 568932737 1143 DEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIENG 1192
Cdd:COG4178 510 DEATSALDEENEAALYQLLREELPGTTVISVGHRSTLAAFHDRVLELTGD 559
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
338-563 |
1.49e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 111.07 E-value: 1.49e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 338 LEFSDVHFSYP--SRANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIR----NFNVRC 411
Cdd:PRK13641 3 IKFENVDYIYSpgTPMEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgNKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 412 LREIIGVVSQ--EPVLFSTTIAENIRYGRGNVTMDEIEKAVKeanAYDFIMKLPQKfDTLVGDRGAQLSGGQKQRIAIAR 489
Cdd:PRK13641 83 LRKKVSLVFQfpEAQLFENTVLKDVEFGPKNFGFSEDEAKEK---ALKWLKKVGLS-EDLISKSPFELSGGQMRRVAIAG 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568932737 490 ALVRNPKILLLDEATSALDTESEAEV-QAALDKAREGRTTIVIAHrlstirNADVIAGFEDGVIVEQgsHSELMK 563
Cdd:PRK13641 159 VMAYEPEILCLDEPAAGLDPEGRKEMmQLFKDYQKAGHTVILVTH------NMDDVAEYADDVLVLE--HGKLIK 225
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
338-564 |
2.58e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 110.22 E-value: 2.58e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 338 LEFSDVHFSYPS------RAnikiLKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIR----NF 407
Cdd:PRK13649 3 INLQNVSYTYQAgtpfegRA----LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITstskNK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 408 NVRCLREIIGVVSQ--EPVLFSTTIAENIRYGRGN--VTMDEIEKAVKEanaydfimKLpqkfdTLVG------DRGA-Q 476
Cdd:PRK13649 79 DIKQIRKKVGLVFQfpESQLFEETVLKDVAFGPQNfgVSQEEAEALARE--------KL-----ALVGiseslfEKNPfE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 477 LSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIV-IAHRLSTIRN-ADVIAGFEDGVIVE 554
Cdd:PRK13649 146 LSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVlVTHLMDDVANyADFVYVLEKGKLVL 225
|
250
....*....|
gi 568932737 555 QGSHSELMKK 564
Cdd:PRK13649 226 SGKPKDIFQD 235
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
996-1199 |
2.71e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 110.14 E-value: 2.71e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 996 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQE--AKKLNVQWLRAQLGIVSQEP--ILFDCSIA 1071
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDitDKKVKLSDIRKKVGLVFQYPeyQLFEETIE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1072 ENIAYGDNSRVVPHDEIVRAAKEAnihpfIETLPQKYNTrVGDKGT-QLSGGQKQRIAIARALIRQPRVLLLDEATSALD 1150
Cdd:PRK13637 103 KDIAFGPINLGLSEEEIENRVKRA-----MNIVGLDYED-YKDKSPfELSGGQKRRVAIAGVVAMEPKILILDEPTAGLD 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 568932737 1151 TeseKVVQEALDKARE-----GRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHGT 1199
Cdd:PRK13637 177 P---KGRDEILNKIKElhkeyNMTIILVSHSMEDVAKlADRIIVMNKGKCELQGT 228
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
994-1212 |
2.91e-26 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 112.24 E-value: 2.91e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 994 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKklNVQWLRAQLGIVSQEPILF-DCSIAE 1072
Cdd:PRK11607 33 HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLS--HVPPYQRPINMMFQSYALFpHMTVEQ 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1073 NIAYGDNSRVVPHDEIVRAAKE--ANIHpfietlPQKYNTRvgdKGTQLSGGQKQRIAIARALIRQPRVLLLDEATSALD 1150
Cdd:PRK11607 111 NIAFGLKQDKLPKAEIASRVNEmlGLVH------MQEFAKR---KPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALD 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568932737 1151 TESEKVVQ-EALD-KAREGRTCIVIAH-RLSTIQNADLIVVIENGKVKEHGTHQQLLAQKGIYFS 1212
Cdd:PRK11607 182 KKLRDRMQlEVVDiLERVGVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYS 246
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
338-570 |
3.42e-26 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 110.82 E-value: 3.42e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 338 LEFSDVHFSYPSR-------ANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFN-- 408
Cdd:PRK11308 6 LQAIDLKKHYPVKrglfkpeRLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADpe 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 409 -VRCLREIIGVVSQ-----------------EPVLFSTTIAENIRYGRGNVTMDEIEKAVKEANAYdfimklPQKFdtlv 470
Cdd:PRK11308 86 aQKLLRQKIQIVFQnpygslnprkkvgqileEPLLINTSLSAAERREKALAMMAKVGLRPEHYDRY------PHMF---- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 471 gdrgaqlSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAAL-DKAREGRTTIV-IAHRLSTIRN-ADVIAGF 547
Cdd:PRK11308 156 -------SGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMmDLQQELGLSYVfISHDLSVVEHiADEVMVM 228
|
250 260
....*....|....*....|...
gi 568932737 548 EDGVIVEQGShselmkKEGIYFR 570
Cdd:PRK11308 229 YLGRCVEKGT------KEQIFNN 245
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
996-1192 |
4.33e-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: 4.33e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 996 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQWLraqlgIVSQEPILFD-CSIAENI 1074
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM-----VVFQNYSLLPwLTVRENI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1075 AYGDNsRVVPHdeIVRAAKEANIHPFIETLPQkynTRVGDKG-TQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTES 1153
Cdd:TIGR01184 76 ALAVD-RVLPD--LSKSERRAIVEEHIALVGL---TEAADKRpGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALT 149
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 568932737 1154 EKVVQEALDKARE--GRTCIVIAHRL-STIQNADLIVVIENG 1192
Cdd:TIGR01184 150 RGNLQEELMQIWEehRVTVLMVTHDVdEALLLSDRVVMLTNG 191
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
987-1203 |
4.41e-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: 4.41e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 987 YPTRANvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKlNVQWLRAQLGIVSQEPILF 1066
Cdd:cd03263 10 YKKGTK-PAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLGYCPQFDALF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1067 D-CSIAENIAYgdNSRV--VPHDEIvraakEANIHPFIET--LPQKYNTRVGDkgtqLSGGQKQRIAIARALIRQPRVLL 1141
Cdd:cd03263 88 DeLTVREHLRF--YARLkgLPKSEI-----KEEVELLLRVlgLTDKANKRART----LSGGMKRKLSLAIALIGGPSVLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568932737 1142 LDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHGTHQQL 1203
Cdd:cd03263 157 LDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEAlCDRIAIMSDGKLRCIGSPQEL 219
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
338-559 |
4.68e-26 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 108.18 E-value: 4.68e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 338 LEFSDVHFSYPSRaniKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQdirNFN--------- 408
Cdd:PRK11124 3 IQLNGINCFYGAH---QALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGN---HFDfsktpsdka 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 409 VRCLREIIGVVSQEPVLFS-TTIAENIRYGRGNVT-MDEiEKAVKEAnaydfiMKLPQKFD-TLVGDR-GAQLSGGQKQR 484
Cdd:PRK11124 77 IRELRRNVGMVFQQYNLWPhLTVQQNLIEAPCRVLgLSK-DQALARA------EKLLERLRlKPYADRfPLHLSGGQQQR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568932737 485 IAIARALVRNPKILLLDEATSALDTESEAEVQAALDKARE-GRTTIVIAHRLSTIRN-ADVIAGFEDGVIVEQGSHS 559
Cdd:PRK11124 150 VAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAEtGITQVIVTHEVEVARKtASRVVYMENGHIVEQGDAS 226
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
338-561 |
5.35e-26 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 110.57 E-value: 5.35e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 338 LEFSD--VHFSYPSR--------ANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNF 407
Cdd:PRK15079 9 LEVADlkVHFDIKDGkqwfwqppKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGM 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 408 NVRCLREI---IGVVSQEPvLFSTT--------IAENIRYGRGNVTMDEIEKAVKEanaydFIMK---LPQkfdtLVGDR 473
Cdd:PRK15079 89 KDDEWRAVrsdIQMIFQDP-LASLNprmtigeiIAEPLRTYHPKLSRQEVKDRVKA-----MMLKvglLPN----LINRY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 474 GAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDK-ARE-GRTTIVIAHRLSTIRN-ADVIAGFEDG 550
Cdd:PRK15079 159 PHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQlQREmGLSLIFIAHDLAVVKHiSDRVLVMYLG 238
|
250
....*....|.
gi 568932737 551 VIVEQGSHSEL 561
Cdd:PRK15079 239 HAVELGTYDEV 249
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
338-556 |
6.72e-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: 6.72e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 338 LEFSDVHFSYpSRANIKilkgLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRclREIIG 417
Cdd:cd03298 1 VRLDKIRFSY-GEQPMH----FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA--DRPVS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 418 VVSQEPVLFS-TTIAENIRYGRG------NVTMDEIEKAVKEANAYDFIMKLPQkfdtlvgdrgaQLSGGQKQRIAIARA 490
Cdd:cd03298 74 MLFQENNLFAhLTVEQNVGLGLSpglkltAEDRQAIEVALARVGLAGLEKRLPG-----------ELSGGERQRVALARV 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568932737 491 LVRNPKILLLDEATSALDTESEAEVQAALDK--AREGRTTIVIAHRLSTIRN-ADVIAGFEDGVIVEQG 556
Cdd:cd03298 143 LVRDKPVLLLDEPFAALDPALRAEMLDLVLDlhAETKMTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
991-1192 |
6.89e-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: 6.89e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 991 ANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVL----LDGQEAKKLNVQWLRAQLGIVSQEPILF 1066
Cdd:cd03290 12 SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHwsnkNESEPSFEATRSRNRYSVAYAAQKPWLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1067 DCSIAENIAYGDNSRVVPHDEIVRAAkeaNIHPFIETLPQKYNTRVGDKGTQLSGGQKQRIAIARALIRQPRVLLLDEAT 1146
Cdd:cd03290 92 NATVEENITFGSPFNKQRYKAVTDAC---SLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPF 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 568932737 1147 SALDTE-SEKVVQEALDK--AREGRTCIVIAHRLSTIQNADLIVVIENG 1192
Cdd:cd03290 169 SALDIHlSDHLMQEGILKflQDDKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
981-1207 |
7.16e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 108.63 E-value: 7.16e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 981 NEVVFNYPTraNVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQWL--RAQLGI 1058
Cdd:PRK13639 5 RDLKYSYPD--GTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLevRKTVGI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1059 VSQEP--ILFDCSIAENIAYGDNSRVVPHDEIVRAAKEA----NIHPFIETLPQkyntrvgdkgtQLSGGQKQRIAIARA 1132
Cdd:PRK13639 83 VFQNPddQLFAPTVEEDVAFGPLNLGLSKEEVEKRVKEAlkavGMEGFENKPPH-----------HLSGGQKKRVAIAGI 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568932737 1133 LIRQPRVLLLDEATSALDTE-SEKVVQEALDKAREGRTCIVIAHRLSTIQ-NADLIVVIENGKVKEHGTHQQLLAQK 1207
Cdd:PRK13639 152 LAMKPEIIVLDEPTSGLDPMgASQIMKLLYDLNKEGITIIISTHDVDLVPvYADKVYVMSDGKIIKEGTPKEVFSDI 228
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
977-1180 |
7.42e-26 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 108.20 E-value: 7.42e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 977 SVTFNEVVFNYPTRAnvpVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDpMAGSVLLDGQ--------EAKKLN 1048
Cdd:PRK14258 7 AIKVNNLSFYYDTQK---ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNE-LESEVRVEGRveffnqniYERRVN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1049 VQWLRAQLGIVSQEPILFDCSIAENIAYGDN----SRVVPHDEIVRAA-KEANihpfietLPQKYNTRVGDKGTQLSGGQ 1123
Cdd:PRK14258 83 LNRLRRQVSMVHPKPNLFPMSVYDNVAYGVKivgwRPKLEIDDIVESAlKDAD-------LWDEIKHKIHKSALDLSGGQ 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 568932737 1124 KQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEALD--KAREGRTCIVIAHRLSTI 1180
Cdd:PRK14258 156 QQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQslRLRSELTMVIVSHNLHQV 214
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
338-556 |
7.59e-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: 7.59e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 338 LEFSDVHFSYPSRaniKILKGLNLKVKSGQTvALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNfNVRCLREIIG 417
Cdd:cd03264 1 LQLENLTKRYGKK---RALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLRRRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 418 VVSQEPVLFST-TIAENIRY-GRGNVTMD-----EIEKAVKEANAYDFimklpqkfdtlVGDRGAQLSGGQKQRIAIARA 490
Cdd:cd03264 76 YLPQEFGVYPNfTVREFLDYiAWLKGIPSkevkaRVDEVLELVNLGDR-----------AKKKIGSLSGGMRRRVGIAQA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568932737 491 LVRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTIRN-ADVIAGFEDGVIVEQG 556
Cdd:cd03264 145 LVGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
989-1204 |
7.66e-26 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 111.47 E-value: 7.66e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 989 TRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQWLRAQLGIVSQEPIL-FD 1067
Cdd:PRK09536 12 EFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLsFE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1068 CSIAENIAYGDN---SRVVPHDEIVRAAKEanihpfiETLPQKYNTRVGDKG-TQLSGGQKQRIAIARALIRQPRVLLLD 1143
Cdd:PRK09536 92 FDVRQVVEMGRTphrSRFDTWTETDRAAVE-------RAMERTGVAQFADRPvTSLSGGERQRVLLARALAQATPVLLLD 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568932737 1144 EATSALDTESE----KVVQEALDkarEGRTCIVIAHRLS-TIQNADLIVVIENGKVKEHGTHQQLL 1204
Cdd:PRK09536 165 EPTASLDINHQvrtlELVRRLVD---DGKTAVAAIHDLDlAARYCDELVLLADGRVRAAGPPADVL 227
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
995-1205 |
7.86e-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: 7.86e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 995 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSV-----LLDGQE---AKKLNVQWLRAQLGIVSQEPILF 1066
Cdd:PRK11264 18 VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIrvgdiTIDTARslsQQKGLIRQLRQHVGFVFQNFNLF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1067 DC-SIAENIAYGdnSRVV---PHDEIVRAAKEanihpfietlpqkYNTRVGDKGTQ------LSGGQKQRIAIARALIRQ 1136
Cdd:PRK11264 98 PHrTVLENIIEG--PVIVkgePKEEATARARE-------------LLAKVGLAGKEtsyprrLSGGQQQRVAIARALAMR 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568932737 1137 PRVLLLDEATSALDTEsekVVQEALDK----AREGRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHGTHQQLLA 1205
Cdd:PRK11264 163 PEVILFDEPTSALDPE---LVGEVLNTirqlAQEKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKALFA 233
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
978-1206 |
8.48e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 108.64 E-value: 8.48e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 978 VTFNEVVFNY---PTRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQW-LR 1053
Cdd:PRK13633 5 IKCKNVSYKYesnEESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLWdIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1054 AQLGIVSQEPilfDCSIA-----ENIAYGDNSRVVPHDEIVR----AAKEANIHPFIETLPQkyntrvgdkgtQLSGGQK 1124
Cdd:PRK13633 85 NKAGMVFQNP---DNQIVativeEDVAFGPENLGIPPEEIRErvdeSLKKVGMYEYRRHAPH-----------LLSGGQK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1125 QRIAIARALIRQPRVLLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLSTIQNADLIVVIENGKVKEHGTHQQ 1202
Cdd:PRK13633 151 QRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKElnKKYGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKE 230
|
....
gi 568932737 1203 LLAQ 1206
Cdd:PRK13633 231 IFKE 234
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
338-553 |
8.75e-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: 8.75e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 338 LEFSDVHFSYpsrANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRclrEI-- 415
Cdd:cd03219 1 LEVRGLTKRF---GGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPH---EIar 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 416 --IGVVSQEPVLFST-TIAENIRYG-----RGNVTMDEIEKAVKEANAYDF----IMKLPQKFDTLVGDrgaqLSGGQKQ 483
Cdd:cd03219 75 lgIGRTFQIPRLFPElTVLENVMVAaqartGSGLLLARARREEREARERAEelleRVGLADLADRPAGE----LSYGQQR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568932737 484 RIAIARALVRNPKILLLDEATSALdteSEAEVQAALDK----AREGRTTIVIAHRLstirnaDVIAGFEDGVIV 553
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 ... |
995-1198 |
9.38e-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: 9.38e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 995 VLQGLSLEVKKGQTlALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKlNVQWLRAQLGIVSQEPILFD-CSIAEN 1073
Cdd:cd03264 15 ALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLRRRIGYLPQEFGVYPnFTVREF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1074 IAY-----GDNSRVVPHdEIVRAAKEANIHPFietlpqkYNTRVGdkgtQLSGGQKQRIAIARALIRQPRVLLLDEATSA 1148
Cdd:cd03264 93 LDYiawlkGIPSKEVKA-RVDEVLELVNLGDR-------AKKKIG----SLSGGMRRRVGIAQALVGDPSILIVDEPTAG 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 568932737 1149 LDTESEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHG 1198
Cdd:cd03264 161 LDPEERIRFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
338-565 |
9.39e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 108.35 E-value: 9.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 338 LEFSDVHFSYpsRANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLREIIG 417
Cdd:PRK13652 4 IETRDLCYSY--SGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 418 VVSQEP--VLFSTTIAENIRYGRGNVTMDE------IEKAVKEANAYDFIMKLPQkfdtlvgdrgaQLSGGQKQRIAIAR 489
Cdd:PRK13652 82 LVFQNPddQIFSPTVEQDIAFGPINLGLDEetvahrVSSALHMLGLEELRDRVPH-----------HLSGGEKKRVAIAG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568932737 490 ALVRNPKILLLDEATSALDTESEAEVQAALDKARE--GRTTIVIAHRLSTIRN-ADVIAGFEDGVIVEQGSHSELMKKE 565
Cdd:PRK13652 151 VIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPEtyGMTVIFSTHQLDLVPEmADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
337-508 |
1.46e-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: 1.46e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 337 NLEFSDVHFSYPsrANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDI-------RNfnv 409
Cdd:PRK11650 3 GLKLQAVRKSYD--GKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVnelepadRD--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 410 rclreiIGVVSQEPVLFS-TTIAENIRYG---RGnVTMDEIEKAVKEANAydfIMKLpqkfDTLVGDRGAQLSGGQKQRI 485
Cdd:PRK11650 78 ------IAMVFQNYALYPhMSVRENMAYGlkiRG-MPKAEIEERVAEAAR---ILEL----EPLLDRKPRELSGGQRQRV 143
|
170 180
....*....|....*....|...
gi 568932737 486 AIARALVRNPKILLLDEATSALD 508
Cdd:PRK11650 144 AMGRAIVREPAVFLFDEPLSNLD 166
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
990-1207 |
1.52e-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: 1.52e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 990 RANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQWLRA---QLGIVSQepilf 1066
Cdd:TIGR02769 21 KQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQRRAfrrDVQLVFQ----- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1067 DC--------SIAENIA-----YGDNSRVVPHDEIVRAAKEANIHPFI-ETLPQkyntrvgdkgtQLSGGQKQRIAIARA 1132
Cdd:TIGR02769 96 DSpsavnprmTVRQIIGeplrhLTSLDESEQKARIAELLDMVGLRSEDaDKLPR-----------QLSGGQLQRINIARA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568932737 1133 LIRQPRVLLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHGTHQQLLAQK 1207
Cdd:TIGR02769 165 LAVKPKLIVLDEAVSNLDMVLQAVILELLRKlqQAFGTAYLFITHDLRLVQSfCQRVAVMDKGQIVEECDVAQLLSFK 242
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
370-562 |
1.69e-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: 1.69e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 370 ALVGNSGCGKSTTVQLLQRLYDPTEGKISIDG---QDI-RNFNVRCLREIIGVVSQEPVLFST-TIAENIRYGRgnvtmd 444
Cdd:COG4148 29 ALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGevlQDSaRGIFLPPHRRRIGYVFQEARLFPHlSVRGNLLYGR------ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 445 eieKAVKEANAydfimklPQKFDTLVG--------DRG-AQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEV 515
Cdd:COG4148 103 ---KRAPRAER-------RISFDEVVEllgighllDRRpATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEI 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 568932737 516 QAALDK-AREGRTTIV-IAHRLSTI-RNADVIAGFEDGVIVEQGSHSELM 562
Cdd:COG4148 173 LPYLERlRDELDIPILyVSHSLDEVaRLADHVVLLEQGRVVASGPLAEVL 222
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
338-535 |
1.76e-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: 1.76e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 338 LEFSDVHFSYPS-RANikilKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQ--DIRNFNVrCLRE 414
Cdd:COG3845 6 LELRGITKRFGGvVAN----DDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKpvRIRSPRD-AIAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 415 IIGVVSQEPVLFST-TIAENIRYGR-----GNVTMDEIEKAVKE-ANAYDFIMKLpqkfDTLVGDrgaqLSGGQKQRIAI 487
Cdd:COG3845 81 GIGMVHQHFMLVPNlTVAENIVLGLeptkgGRLDRKAARARIRElSERYGLDVDP----DAKVED----LSVGEQQRVEI 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 568932737 488 ARALVRNPKILLLDEATSALdTESEA-EVQAALDK-AREGRTTIVIAHRL 535
Cdd:COG3845 153 LKALYRGARILILDEPTAVL-TPQEAdELFEILRRlAAEGKSIIFITHKL 201
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
990-1204 |
2.02e-25 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 106.78 E-value: 2.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 990 RANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQWLRAQLGIVSQEPIL-FDC 1068
Cdd:PRK13548 12 LGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQHSSLsFPF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1069 SIAENIAYGdnsrVVPHDEIVRAAKEanihpfietLPQKYNTRVGDKG------TQLSGGQKQRIAIARALIR------Q 1136
Cdd:PRK13548 92 TVEEVVAMG----RAPHGLSRAEDDA---------LVAAALAQVDLAHlagrdyPQLSGGEQQRVQLARVLAQlwepdgP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568932737 1137 PRVLLLDEATSALD-TESEKVVQEALDKARE-GRTCIVIAHRLS-TIQNADLIVVIENGKVKEHGTHQQLL 1204
Cdd:PRK13548 159 PRWLLLDEPTSALDlAHQHHVLRLARQLAHErGLAVIVVLHDLNlAARYADRIVLLHQGRLVADGTPAEVL 229
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
993-1196 |
2.33e-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: 2.33e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 993 VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQL---LERfydPMAGSVLLDGQEAKKLN----VQWLRAQLGIVSQE--- 1062
Cdd:COG4181 25 LTILKGISLEVEAGESVAIVGASGSGKSTLLGLlagLDR---PTSGTVRLAGQDLFALDedarARLRARHVGFVFQSfql 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1063 -PILfdcSIAENIAygdnsrvVP-----HDEIVRAAKEAnihpfietLpqkynTRVGDKG------TQLSGGQKQRIAIA 1130
Cdd:COG4181 102 lPTL---TALENVM-------LPlelagRRDARARARAL--------L-----ERVGLGHrldhypAQLSGGEQQRVALA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568932737 1131 RALIRQPRVLLLDEATSALDTESEKVVQEAL-DKARE-GRTCIVIAHRLSTIQNADLIVVIENGKVKE 1196
Cdd:COG4181 159 RAFATEPAILFADEPTGNLDAATGEQIIDLLfELNRErGTTLVLVTHDPALAARCDRVLRLRAGRLVE 226
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
356-561 |
2.60e-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: 105.53 E-value: 2.60e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 356 LKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNfNVRCLREIIGVVSQEPvlfsttIAENIR 435
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREVRRRIGIVFQDL------SVDDEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 436 YGRGNVTM---------DEIEKAVKEANAYdfiMKLPQKFDTLVGdrgaQLSGGQKQRIAIARALVRNPKILLLDEATSA 506
Cdd:cd03265 89 TGWENLYIharlygvpgAERRERIDELLDF---VGLLEAADRLVK----TYSGGMRRRLEIARSLVHRPEVLFLDEPTIG 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 568932737 507 LDTESEAEVQAALDK--AREGRTTIVIAHRLSTIRN-ADVIAGFEDGVIVEQGSHSEL 561
Cdd:cd03265 162 LDPQTRAHVWEYIEKlkEEFGMTILLTTHYMEEAEQlCDRVAIIDHGRIIAEGTPEEL 219
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
999-1198 |
2.68e-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: 2.68e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 999 LSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQwlRAQLGIVSQEPILF-DCSIAENIAYG 1077
Cdd:cd03298 17 FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA--DRPVSMLFQENNLFaHLTVEQNVGLG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1078 DNSRV----VPHDEIVRAAKEANIHPFIETLPQkyntrvgdkgtQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTES 1153
Cdd:cd03298 95 LSPGLkltaEDRQAIEVALARVGLAGLEKRLPG-----------ELSGGERQRVALARVLVRDKPVLLLDEPFAALDPAL 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 568932737 1154 EKVVQEALDK--AREGRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHG 1198
Cdd:cd03298 164 RAEMLDLVLDlhAETKMTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
978-1205 |
3.03e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 107.41 E-value: 3.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 978 VTFNEVVFNYptRANVP----VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLL------DGQEAKKL 1047
Cdd:PRK13634 3 ITFQKVEHRY--QYKTPferrALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIgervitAGKKNKKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1048 NVqwLRAQLGIVSQ--EPILFDCSIAENIAYGDNSRVVPHDEIVRAAKEAnihpfIET--LPQKYNTRvgdKGTQLSGGQ 1123
Cdd:PRK13634 81 KP--LRKKVGIVFQfpEHQLFEETVEKDICFGPMNFGVSEEDAKQKAREM-----IELvgLPEELLAR---SPFELSGGQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1124 KQRIAIARALIRQPRVLLLDEATSALDTESEKVVQE---ALDKaREGRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHGT 1199
Cdd:PRK13634 151 MRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEmfyKLHK-EKGLTTVLVTHSMEDAARyADQIVVMHKGTVFLQGT 229
|
....*.
gi 568932737 1200 HQQLLA 1205
Cdd:PRK13634 230 PREIFA 235
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
352-524 |
3.08e-25 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 108.63 E-value: 3.08e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 352 NIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLReiIGVVSQEPVLFS-TTI 430
Cdd:PRK10851 14 RTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRK--VGFVFQHYALFRhMTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 431 AENIRYG------RGNVTMDEIEKAVkeanaydfiMKLPQ--KFDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDE 502
Cdd:PRK10851 92 FDNIAFGltvlprRERPNAAAIKAKV---------TQLLEmvQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDE 162
|
170 180
....*....|....*....|..
gi 568932737 503 ATSALDTESEAEVQAALDKARE 524
Cdd:PRK10851 163 PFGALDAQVRKELRRWLRQLHE 184
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
996-1186 |
3.20e-25 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 106.01 E-value: 3.20e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 996 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYD-----PMAGSVLLDGQE--AKKLNVQWLRAQLGIVSQEPILFDC 1068
Cdd:PRK14239 21 LNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnpevTITGSIVYNGHNiySPRTDTVDLRKEIGMVFQQPNPFPM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1069 SIAENIAYG-------DNSRVvphDEIV-RAAKEANIHpfietlpQKYNTRVGDKGTQLSGGQKQRIAIARALIRQPRVL 1140
Cdd:PRK14239 101 SIYENVVYGlrlkgikDKQVL---DEAVeKSLKGASIW-------DEVKDRLHDSALGLSGGQQQRVCIARVLATSPKII 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 568932737 1141 LLDEATSALDTESEKVVQEALDKAREGRTCIVIAHrlsTIQNADLI 1186
Cdd:PRK14239 171 LLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTR---SMQQASRI 213
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
336-573 |
4.04e-25 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 113.72 E-value: 4.04e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 336 GNLEFSDVHFSYpsRANIK-ILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLRE 414
Cdd:PTZ00243 1307 GSLVFEGVQMRY--REGLPlVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRR 1384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 415 IIGVVSQEPVLFSTTIAENIRyGRGNVTMDEIEKAVKEANAYDFIMKLPQKFDTLVGDRGAQLSGGQKQRIAIARALV-R 493
Cdd:PTZ00243 1385 QFSMIPQDPVLFDGTVRQNVD-PFLEASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLkK 1463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 494 NPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTIRNADVIAGFEDGVIVEQGSHSEL-MKKEGIYFRLV 572
Cdd:PTZ00243 1464 GSGFILMDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELvMNRQSIFHSMV 1543
|
.
gi 568932737 573 N 573
Cdd:PTZ00243 1544 E 1544
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
992-1198 |
4.26e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 105.77 E-value: 4.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 992 NVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYD-----PMAGSVLLDGQEAKKLNVQWLRAQLGIVSQEP-IL 1065
Cdd:PRK14247 15 QVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDIFKMDVIELRRRVQMVFQIPnPI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1066 FDCSIAENIAYGDN-SRVVPH----DEIVRAAKEAnihpfiETLPQKYNTRVGDKGTQLSGGQKQRIAIARALIRQPRVL 1140
Cdd:PRK14247 95 PNLSIFENVALGLKlNRLVKSkkelQERVRWALEK------AQLWDEVKDRLDAPAGKLSGGQQQRLCIARALAFQPEVL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568932737 1141 LLDEATSALDTESEKVVQEALDKAREGRTCIVIAH------RLStiqnaDLIVVIENGKVKEHG 1198
Cdd:PRK14247 169 LADEPTANLDPENTAKIESLFLELKKDMTIVLVTHfpqqaaRIS-----DYVAFLYKGQIVEWG 227
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
988-1198 |
5.03e-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: 5.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 988 PTRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLL--ERFYDPMAGSVLLDGqeaKKLNVQWLRAQLGIVSQEPIL 1065
Cdd:cd03213 17 PSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLING---RPLDKRSFRKIIGYVPQDDIL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1066 FDC-SIAENIAYgdnsrvvphdeivrAAKeanihpfietLpqkyntrvgdKGtqLSGGQKQRIAIARALIRQPRVLLLDE 1144
Cdd:cd03213 94 HPTlTVRETLMF--------------AAK----------L----------RG--LSGGERKRVSIALELVSNPSLLFLDE 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 568932737 1145 ATSALDTESEKVVQEALDK-AREGRTCIVIAHRLST--IQNADLIVVIENGKVKEHG 1198
Cdd:cd03213 138 PTSGLDSSSALQVMSLLRRlADTGRTIICSIHQPSSeiFELFDKLLLLSQGRVIYFG 194
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
993-1194 |
5.77e-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: 5.77e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 993 VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVqWLRAQLGIVS--QEPILF-DCS 1069
Cdd:COG0411 17 LVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPP-HRIARLGIARtfQNPRLFpELT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1070 IAENIA----YGDNSRVVPH-----------DEIVRAAKEAnihpfIET--LPQKYNTRVGDkgtqLSGGQKQRIAIARA 1132
Cdd:COG0411 96 VLENVLvaahARLGRGLLAAllrlprarreeREARERAEEL-----LERvgLADRADEPAGN----LSYGQQRRLEIARA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568932737 1133 LIRQPRVLLLDEATSAL-DTESEKVVqEALDKARE--GRTCIVIAHRLSTIQN-ADLIVVIENGKV 1194
Cdd:COG0411 167 LATEPKLLLLDEPAAGLnPEETEELA-ELIRRLRDerGITILLIEHDMDLVMGlADRIVVLDFGRV 231
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
355-556 |
5.92e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 105.31 E-value: 5.92e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 355 ILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYD-----PTEGKISIDGQDIRNFNVRCL--REIIGVVSQEPVLFS 427
Cdd:PRK14267 19 VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGRNIYSPDVDPIevRREVGMVFQYPNPFP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 428 -TTIAENIRYG-------RGNVTMDE-IEKAVKEANAYDfimklpqKFDTLVGDRGAQLSGGQKQRIAIARALVRNPKIL 498
Cdd:PRK14267 99 hLTIYDNVAIGvklnglvKSKKELDErVEWALKKAALWD-------EVKDRLNDYPSNLSGGQRQRLVIARALAMKPKIL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 568932737 499 LLDEATSALDTESEAEVQAALDKAREGRTTIVIAHR-LSTIRNADVIAGFEDGVIVEQG 556
Cdd:PRK14267 172 LMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSpAQAARVSDYVAFLYLGKLIEVG 230
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
355-561 |
6.07e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 105.51 E-value: 6.07e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 355 ILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQ------DIRNFNVRCLREIIGVVSQEPVLFS- 427
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkDIFQIDAIKLRKEVGMVFQQPNPFPh 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 428 TTIAENIRY---GRGNVTMDEIEKAVKEANAYDFIMKlpQKFDTLvGDRGAQLSGGQKQRIAIARALVRNPKILLLDEAT 504
Cdd:PRK14246 105 LSIYDNIAYplkSHGIKEKREIKKIVEECLRKVGLWK--EVYDRL-NSPASQLSGGQQQRLTIARALALKPKVLLMDEPT 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 568932737 505 SALDTESEAEVQAALDKAREGRTTIVIAHRLSTI-RNADVIAGFEDGVIVEQGSHSEL 561
Cdd:PRK14246 182 SMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVaRVADYVAFLYNGELVEWGSSNEI 239
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
338-533 |
6.52e-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: 6.52e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 338 LEFSDVHFSYP-SRANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRclReii 416
Cdd:COG4525 4 LTVRHVSVRYPgGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGAD--R--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 417 GVVSQEPVLFS-TTIAENIRYG---RGnvtmdeIEKAVKEANAYDFImklpqkfdTLVGDRGA------QLSGGQKQRIA 486
Cdd:COG4525 79 GVVFQKDALLPwLNVLDNVAFGlrlRG------VPKAERRARAEELL--------ALVGLADFarrriwQLSGGMRQRVG 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 568932737 487 IARALVRNPKILLLDEATSALDTESEAEVQAALDK--AREGRTTIVIAH 533
Cdd:COG4525 145 IARALAADPRFLLMDEPFGALDALTREQMQELLLDvwQRTGKGVFLITH 193
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
354-556 |
6.69e-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: 6.69e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 354 KILKGLNLKVKSGQTVALVGNSGCGKSTTVQLL-QRLYDP--TEGKISIDGQDIRNFNVRclrEIIGVVSQEPVLFST-T 429
Cdd:cd03234 21 RILNDVSLHVESGQVMAILGSSGSGKTTLLDAIsGRVEGGgtTSGQILFNGQPRKPDQFQ---KCVAYVRQDDILLPGlT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 430 IAENIRYGRGNVTMDEIEKAVKEANAYDFIMKlpQKFDTLVGD-RGAQLSGGQKQRIAIARALVRNPKILLLDEATSALD 508
Cdd:cd03234 98 VRETLTYTAILRLPRKSSDAIRKKRVEDVLLR--DLALTRIGGnLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLD 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 568932737 509 TESEAEVQAAL-DKAREGRTTIVIAH--RLSTIRNADVIAGFEDGVIVEQG 556
Cdd:cd03234 176 SFTALNLVSTLsQLARRNRIVILTIHqpRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
977-1200 |
7.21e-25 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 104.71 E-value: 7.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 977 SVTFNEVVFNYptrANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQE---AKKLN---VQ 1050
Cdd:COG4161 2 SIQLKNINCFY---GSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQfdfSQKPSekaIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1051 WLRAQLGIVSQEPILFdcsiaeniaygdnsrvvPH----DEIVRA-------AKEANIHPFIETLPQkynTRVGDKGT-- 1117
Cdd:COG4161 79 LLRQKVGMVFQQYNLW-----------------PHltvmENLIEApckvlglSKEQAREKAMKLLAR---LRLTDKADrf 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1118 --QLSGGQKQRIAIARALIRQPRVLLLDEATSALDTE-SEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVIENGK 1193
Cdd:COG4161 139 plHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEiTAQVVEIIRELSQTGITQVIVTHEVEFARKvASQVVYMEKGR 218
|
....*..
gi 568932737 1194 VKEHGTH 1200
Cdd:COG4161 219 IIEQGDA 225
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
988-1198 |
8.28e-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: 103.99 E-value: 8.28e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 988 PTRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKlNVQWLRAQLGIVSQEPILFD 1067
Cdd:cd03266 13 DVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-EPAEARRRLGFVSDSTGLYD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1068 -CSIAENIAY-GDNSRVVPHDEIVRAAKEANIHPFIETLpqkyNTRVGDkgtqLSGGQKQRIAIARALIRQPRVLLLDEA 1145
Cdd:cd03266 92 rLTARENLEYfAGLYGLKGDELTARLEELADRLGMEELL----DRRVGG----FSTGMRQKVAIARALVHDPPVLLLDEP 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 568932737 1146 TSALDTESEKVVQEALDKAREGRTCIVIA-HRLSTIQN-ADLIVVIENGKVKEHG 1198
Cdd:cd03266 164 TTGLDVMATRALREFIRQLRALGKCILFStHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
338-557 |
8.69e-25 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 110.18 E-value: 8.69e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 338 LEFSDVHFSYPSRANIK--------ILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYdPTEGKISIDGQDIRNFNV 409
Cdd:PRK15134 276 LDVEQLQVAFPIRKGILkrtvdhnvVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLHNLNR 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 410 RCL---REIIGVVSQEP---------VLfsTTIAENIRYGRGNVTMDEIEKAVKEAnaydfiMKlPQKFDTLVGDR-GAQ 476
Cdd:PRK15134 355 RQLlpvRHRIQVVFQDPnsslnprlnVL--QIIEEGLRVHQPTLSAAQREQQVIAV------ME-EVGLDPETRHRyPAE 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 477 LSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKAREGR--TTIVIAHRLSTIRNA--DVIAgFEDGVI 552
Cdd:PRK15134 426 FSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHqlAYLFISHDLHVVRALchQVIV-LRQGEV 504
|
....*
gi 568932737 553 VEQGS 557
Cdd:PRK15134 505 VEQGD 509
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
338-508 |
9.50e-25 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 104.03 E-value: 9.50e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 338 LEFSDVHFSYPSRaniKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLREIIG 417
Cdd:PRK10247 8 LQLQNVGYLAGDA---KILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 418 VVSQEPVLFSTTIAENIRYGRgnvtmdEIEKAVKEANAY-DFIMK--LPqkfDTLVGDRGAQLSGGQKQRIAIARALVRN 494
Cdd:PRK10247 85 YCAQTPTLFGDTVYDNLIFPW------QIRNQQPDPAIFlDDLERfaLP---DTILTKNIAELSGGEKQRISLIRNLQFM 155
|
170
....*....|....
gi 568932737 495 PKILLLDEATSALD 508
Cdd:PRK10247 156 PKVLLLDEITSALD 169
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
359-562 |
1.13e-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: 1.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 359 LNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGqdirnfnvRCL------------REIIGVVSQEPVLF 426
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNG--------RTLfdsrkgiflppeKRRIGYVFQEARLF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 427 S-TTIAENIRYGRGNVTMDEieKAVKEANAYDFImklpqKFDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEATS 505
Cdd:TIGR02142 88 PhLSVRGNLRYGMKRARPSE--RRISFERVIELL-----GIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 506 ALDTESEAEVQAALDK-AREGRTTIV-IAHRLSTI-RNADVIAGFEDGVIVEQGSHSELM 562
Cdd:TIGR02142 161 ALDDPRKYEILPYLERlHAEFGIPILyVSHSLQEVlRLADRVVVLEDGRVAAAGPIAEVW 220
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
73-291 |
1.79e-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: 104.81 E-value: 1.79e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 73 VAAYIQVSFWTLAAGRQIKKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDDVSKISEGIGDKVGMFFQAIATFFAGFIV 152
Cdd:cd18552 54 LASYLQTYLMAYVGQRVVRDLRNDLFDKLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGV 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 153 GFIRGWKLTLVIMAISPILGLSTAVWAKILSTFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKELERYQKHLENAKK 232
Cdd:cd18552 134 LFYLDWKLTLIALVVLPLAALPIRRIGKRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRR 213
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 568932737 233 IGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTIGNamtvFFSILIGAFSV 291
Cdd:cd18552 214 LSMKIARARALSSPLMELLGAIAIALVLWYGGYQVISGELTPGE----FISFITALLLL 268
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
356-583 |
1.88e-24 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 107.43 E-value: 1.88e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 356 LKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLREI----IGVVSQEPVLFS-TTI 430
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVrrkkIAMVFQSFALMPhMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 431 AENIRYGrgnVTMDEIEKAVKEANAYDFIMKLpqKFDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTE 510
Cdd:PRK10070 124 LDNTAFG---MELAGINAEERREKALDALRQV--GLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPL 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 511 SEAEVQAALDK--AREGRTTIVIAHRL-STIRNADVIAGFEDGVIVEQGSHSELMKKEG-----IYFRLVNMqtagSQIL 582
Cdd:PRK10070 199 IRTEMQDELVKlqAKHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEILNNPAndyvrTFFRGVDI----SQVF 274
|
.
gi 568932737 583 S 583
Cdd:PRK10070 275 S 275
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
353-568 |
2.16e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 105.70 E-value: 2.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 353 IKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISID----GQD--------------IRNFnvRCLRE 414
Cdd:PRK13631 39 LVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGdiyiGDKknnhelitnpyskkIKNF--KELRR 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 415 IIGVVSQEP--VLFSTTIAENIRYGRGNVTMDEIEkAVKEANAYDFIMKLpqKFDTLvgDRGA-QLSGGQKQRIAIARAL 491
Cdd:PRK13631 117 RVSMVFQFPeyQLFKDTIEKDIMFGPVALGVKKSE-AKKLAKFYLNKMGL--DDSYL--ERSPfGLSGGQKRRVAIAGIL 191
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568932737 492 VRNPKILLLDEATSALDTESEAE-VQAALDKAREGRTTIVIAHRLSTIRN-ADVIAGFEDGVIVEQGSHSELMKKEGIY 568
Cdd:PRK13631 192 AIQPEILIFDEPTAGLDPKGEHEmMQLILDAKANNKTVFVITHTMEHVLEvADEVIVMDKGKILKTGTPYEIFTDQHII 270
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
995-1206 |
2.68e-24 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 103.51 E-value: 2.68e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 995 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQE-------------AKKLNVQWLRAQLGIVSQ 1061
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTinlvrdkdgqlkvADKNQLRLLRTRLTMVFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1062 EPILFD-CSIAENI--AYGDNSRVVPHDEIVRAAKEANIHPFIETLPQKYNTrvgdkgtQLSGGQKQRIAIARALIRQPR 1138
Cdd:PRK10619 100 HFNLWShMTVLENVmeAPIQVLGLSKQEARERAVKYLAKVGIDERAQGKYPV-------HLSGGQQQRVSIARALAMEPE 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1139 VLLLDEATSALDTESEKVVQEALDK-AREGRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHGTHQQLLAQ 1206
Cdd:PRK10619 173 VLLFDEPTSALDPELVGEVLRIMQQlAEEGKTMVVVTHEMGFARHvSSHVIFLHQGKIEEEGAPEQLFGN 242
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
354-535 |
3.56e-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: 3.56e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 354 KILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNfnvrcLRE-----IIGVVSQEPVL--- 425
Cdd:COG1101 20 RALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTK-----LPEykrakYIGRVFQDPMMgta 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 426 FSTTIAEN--IRYGRGN-------VTMDEIE---KAVKEANaydfiMKLPQKFDTLVGdrgaQLSGGQKQRIAIARALVR 493
Cdd:COG1101 95 PSMTIEENlaLAYRRGKrrglrrgLTKKRRElfrELLATLG-----LGLENRLDTKVG----LLSGGQRQALSLLMATLT 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 568932737 494 NPKILLLDEATSALDTESEAEVQAALDK--AREGRTTIVIAHRL 535
Cdd:COG1101 166 KPKLLLLDEHTAALDPKTAALVLELTEKivEENNLTTLMVTHNM 209
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
993-1192 |
4.20e-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: 4.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 993 VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQE-----AKKLNVQWL---RAQLGIVSQ--- 1061
Cdd:COG4778 24 LPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGgwvdlAQASPREILalrRRTIGYVSQflr 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1062 ------------EPILfdcsiaeniaygdnSRVVPHDEIVRAAKEA----NIHPFIETLPQkyNTrvgdkgtqLSGGQKQ 1125
Cdd:COG4778 104 viprvsaldvvaEPLL--------------ERGVDREEARARARELlarlNLPERLWDLPP--AT--------FSGGEQQ 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568932737 1126 RIAIARALIRQPRVLLLDEATSALDTESEKVVQEALDKAREGRTCIV-IAHRLSTIQN-ADLIVVIENG 1192
Cdd:COG4778 160 RVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIgIFHDEEVREAvADRVVDVTPF 228
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
338-557 |
4.22e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 103.53 E-value: 4.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 338 LEFSDVHFSYPSraNIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFN-VRCLREII 416
Cdd:PRK13644 2 IRLENVSYSYPD--GTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSkLQGIRKLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 417 GVVSQEP--VLFSTTIAENIRYGRGNVTMD--EIEKAVKEANAYDFIMKLPQKfdtlvgdRGAQLSGGQKQRIAIARALV 492
Cdd:PRK13644 80 GIVFQNPetQFVGRTVEEDLAFGPENLCLPpiEIRKRVDRALAEIGLEKYRHR-------SPKTLSGGQGQCVALAGILT 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568932737 493 RNPKILLLDEATSALDTESEAEVQAALDKA-REGRTTIVIAHRLSTIRNADVIAGFEDGVIVEQGS 557
Cdd:PRK13644 153 MEPECLIFDEVTSMLDPDSGIAVLERIKKLhEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGE 218
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
338-550 |
4.56e-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: 4.56e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 338 LEFSDVHFSYPSraNIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKI----------SIDGQDIRNf 407
Cdd:cd03290 1 VQVTNGYFSWGS--GLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsnknesepSFEATRSRN- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 408 nvrclREIIGVVSQEPVLFSTTIAENIRYGrgNVTMDEIEKAVKEANAYD-FIMKLPQKFDTLVGDRGAQLSGGQKQRIA 486
Cdd:cd03290 78 -----RYSVAYAAQKPWLLNATVEENITFG--SPFNKQRYKAVTDACSLQpDIDLLPFGDQTEIGERGINLSGGQRQRIC 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568932737 487 IARALVRNPKILLLDEATSALDTE-SEAEVQAALDK--AREGRTTIVIAHRLSTIRNADVIAGFEDG 550
Cdd:cd03290 151 VARALYQNTNIVFLDDPFSALDIHlSDHLMQEGILKflQDDKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
340-533 |
4.66e-24 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 107.84 E-value: 4.66e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 340 FSDVHFSYPSRaniKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGqdirnfNVRclreiIGVV 419
Cdd:COG0488 1 LENLSKSFGGR---PLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK------GLR-----IGYL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 420 SQEPVLFST-TIAENIRYGRGNVT-----MDEIEKAVK-----------------EANAYDF------IMK---LPQK-F 466
Cdd:COG0488 67 PQEPPLDDDlTVLDTVLDGDAELRaleaeLEELEAKLAepdedlerlaelqeefeALGGWEAearaeeILSglgFPEEdL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568932737 467 DTLVGDrgaqLSGGQKQRIAIARALVRNPKILLLDEATSALDTES----EAEVqaaldKAREGrTTIVIAH 533
Cdd:COG0488 147 DRPVSE----LSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESiewlEEFL-----KNYPG-TVLVVSH 207
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
977-1199 |
5.15e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 103.29 E-value: 5.15e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 977 SVTFNEVVFNYP--TRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQE----AKKLNVQ 1050
Cdd:PRK13649 2 GINLQNVSYTYQagTPFEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLitstSKNKDIK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1051 WLRAQLGIVSQ--EPILFDCSIAENIAYGDNSRVVPHDEIVRAAKEA-NIHPFIETLPQKyntrvgdKGTQLSGGQKQRI 1127
Cdd:PRK13649 82 QIRKKVGLVFQfpESQLFEETVLKDVAFGPQNFGVSQEEAEALAREKlALVGISESLFEK-------NPFELSGGQMRRV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568932737 1128 AIARALIRQPRVLLLDEATSALDTESEKVVQEALDKARE-GRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHGT 1199
Cdd:PRK13649 155 AIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQsGMTIVLVTHLMDDVANyADFVYVLEKGKLVLSGK 228
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
978-1198 |
5.36e-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: 5.36e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 978 VTFNEVVFNYPTRanvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQWlrAQLG 1057
Cdd:cd03268 1 LKTNDLTKTYGKK---RVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEAL--RRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1058 IVSQEPILFD-CSIAENIAYGDNSRVVPHDEIVRAAKEANIHpfietlpqkynTRVGDKGTQLSGGQKQRIAIARALIRQ 1136
Cdd:cd03268 76 ALIEAPGFYPnLTARENLRLLARLLGIRKKRIDEVLDVVGLK-----------DSAKKKVKGFSLGMKQRLGIALALLGN 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568932737 1137 PRVLLLDEATSALDTESEKVVQEAL-DKAREGRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHG 1198
Cdd:cd03268 145 PDLLILDEPTNGLDPDGIKELRELIlSLRDQGITVLISSHLLSEIQKvADRIGIINKGKLIEEG 208
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
348-556 |
7.89e-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: 7.89e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 348 PSRANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIrNFNVRCLREIIGVVSQEPVLFS 427
Cdd:cd03266 13 DVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDV-VKEPAEARRRLGFVSDSTGLYD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 428 -TTIAENIRY--GRGNVTMDEIEKAVKEanaydfimkLPQKFDT--LVGDRGAQLSGGQKQRIAIARALVRNPKILLLDE 502
Cdd:cd03266 92 rLTARENLEYfaGLYGLKGDELTARLEE---------LADRLGMeeLLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDE 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 568932737 503 ATSALDTESEAEVQAALDKAREGRTTIVIA-HRLSTI-RNADVIAGFEDGVIVEQG 556
Cdd:cd03266 163 PTTGLDVMATRALREFIRQLRALGKCILFStHIMQEVeRLCDRVVVLHRGRVVYEG 218
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
338-565 |
8.86e-24 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 102.16 E-value: 8.86e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 338 LEFSDVHFSYPSRAnikILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLREIIG 417
Cdd:PRK13548 3 LEARNLSVRLGGRT---LLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 418 VVSQEPVL-FSTTIAENIRYGRGnvTMDEIEKAVKEanaydfimkLPQKFDTLVG-----DRG-AQLSGGQKQRIAIARA 490
Cdd:PRK13548 80 VLPQHSSLsFPFTVEEVVAMGRA--PHGLSRAEDDA---------LVAAALAQVDlahlaGRDyPQLSGGEQQRVQLARV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 491 LVR------NPKILLLDEATSALDTESEAEV-QAALDKARE-GRTTIVIAHRLS-TIRNADVIAGFEDGVIVEQGSHSEL 561
Cdd:PRK13548 149 LAQlwepdgPPRWLLLDEPTSALDLAHQHHVlRLARQLAHErGLAVIVVLHDLNlAARYADRIVLLHQGRLVADGTPAEV 228
|
....
gi 568932737 562 MKKE 565
Cdd:PRK13548 229 LTPE 232
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
977-1150 |
1.41e-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: 1.41e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 977 SVTFNEVVFNYPtrANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQL---LERFydpMAGSVLLDGQeakklnvqwlr 1053
Cdd:PRK11650 3 GLKLQAVRKSYD--GKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMvagLERI---TSGEIWIGGR----------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1054 aqlgIVSQ-EPILFDC-------------SIAENIAYGDNSRVVPHDEIVR----AAKEANIHPFIETLPQkyntrvgdk 1115
Cdd:PRK11650 67 ----VVNElEPADRDIamvfqnyalyphmSVRENMAYGLKIRGMPKAEIEErvaeAARILELEPLLDRKPR--------- 133
|
170 180 190
....*....|....*....|....*....|....*
gi 568932737 1116 gtQLSGGQKQRIAIARALIRQPRVLLLDEATSALD 1150
Cdd:PRK11650 134 --ELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLD 166
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
996-1194 |
1.65e-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: 1.65e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 996 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEakklnVQW------LRAQLGIVSQEPILFDC- 1068
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKP-----VRIrsprdaIALGIGMVHQHFMLVPNl 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1069 SIAENIAYGDNSRVVPHDEIVRAAKEanihpfIETLPQKY------NTRVGDkgtqLSGGQKQRIAIARALIRQPRVLLL 1142
Cdd:COG3845 96 TVAENIVLGLEPTKGGRLDRKAARAR------IRELSERYgldvdpDAKVED----LSVGEQQRVEILKALYRGARILIL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 568932737 1143 DEATSAL-DTESEKVVqEALDK-AREGRTCIVIAHRLSTI-QNADLIVVIENGKV 1194
Cdd:COG3845 166 DEPTAVLtPQEADELF-EILRRlAAEGKSIIFITHKLREVmAIADRVTVLRRGKV 219
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
994-1175 |
1.68e-23 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 101.31 E-value: 1.68e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 994 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEakklnVQWLRAQLGIVSQ-EPILFDCSIAE 1072
Cdd:PRK11248 15 PALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKP-----VEGPGAERGVVFQnEGLLPWRNVQD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1073 NIAYGDNSRVVPHDEIVRAAKEANIHPFIETLPQKYNTrvgdkgtQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTE 1152
Cdd:PRK11248 90 NVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIW-------QLSGGQRQRVGIARALAANPQLLLLDEPFGALDAF 162
|
170 180
....*....|....*....|....*
gi 568932737 1153 SEKVVQEALDK--AREGRTCIVIAH 1175
Cdd:PRK11248 163 TREQMQTLLLKlwQETGKQVLLITH 187
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
338-565 |
1.69e-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: 1.69e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 338 LEFSDVHFSYPSRaniKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNV-RCLREII 416
Cdd:cd03218 1 LRAENLSKRYGKR---KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMhKRARLGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 417 GVVSQEPVLF-STTIAENIRygrgnVTMDEIEKAVKEANaydfimklpQKFDTLVGD---------RGAQLSGGQKQRIA 486
Cdd:cd03218 78 GYLPQEASIFrKLTVEENIL-----AVLEIRGLSKKERE---------EKLEELLEEfhithlrksKASSLSGGERRRVE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 487 IARALVRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIA-HR----LSTIRNADVIAgfeDGVIVEQGSHSEL 561
Cdd:cd03218 144 IARALATNPKFLLLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITdHNvretLSITDRAYIIY---EGKVLAEGTPEEI 220
|
....
gi 568932737 562 MKKE 565
Cdd:cd03218 221 AANE 224
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
994-1205 |
1.83e-23 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 101.62 E-value: 1.83e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 994 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQ--EAKKLNVQWLRAQLGIVSQEP--ILFDCS 1069
Cdd:PRK13638 15 PVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKplDYSKRGLLALRQQVATVFQDPeqQIFYTD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1070 IAENIAYGDNSRVVPHDEIVRAAKEAnihpfiETLPQKYNTRvgDKGTQ-LSGGQKQRIAIARALIRQPRVLLLDEATSA 1148
Cdd:PRK13638 95 IDSDIAFSLRNLGVPEAEITRRVDEA------LTLVDAQHFR--HQPIQcLSHGQKKRVAIAGALVLQARYLLLDEPTAG 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 568932737 1149 LDTESEKVVQEALDK-AREGRTCIVIAHRLSTI-QNADLIVVIENGKVKEHGTHQQLLA 1205
Cdd:PRK13638 167 LDPAGRTQMIAIIRRiVAQGNHVIISSHDIDLIyEISDAVYVLRQGQILTHGAPGEVFA 225
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
990-1204 |
2.16e-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: 2.16e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 990 RANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAG-SVLLDGQEAKKLNVQWLRAQLGIVS---QEPIL 1065
Cdd:COG1119 13 RGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGEDVWELRKRIGLVSpalQLRFP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1066 FDCSIAENIAYG--DNSRVVPH--DEIVRAAKEAnihpfIETLpqkyntRVGDKG----TQLSGGQKQRIAIARALIRQP 1137
Cdd:COG1119 93 RDETVLDVVLSGffDSIGLYREptDEQRERAREL-----LELL------GLAHLAdrpfGTLSQGEQRRVLIARALVKDP 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568932737 1138 RVLLLDEATSALDTESEKVVQEALDK-AREGRTCIV-IAHRL----STIQNAdliVVIENGKVKEHGTHQQLL 1204
Cdd:COG1119 162 ELLILDEPTAGLDLGARELLLALLDKlAAEGAPTLVlVTHHVeeipPGITHV---LLLKDGRVVAAGPKEEVL 231
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
356-533 |
2.59e-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: 2.59e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 356 LKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLreiigVVSQEPVLFS-TTIAENI 434
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM-----VVFQNYSLLPwLTVRENI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 435 RYGRGNVtMDEIEKAVKEANAYDFImklpqkfdTLVGDRGA------QLSGGQKQRIAIARALVRNPKILLLDEATSALD 508
Cdd:TIGR01184 76 ALAVDRV-LPDLSKSERRAIVEEHI--------ALVGLTEAadkrpgQLSGGMKQRVAIARALSIRPKVLLLDEPFGALD 146
|
170 180
....*....|....*....|....*..
gi 568932737 509 TESEAEVQAALDKARE--GRTTIVIAH 533
Cdd:TIGR01184 147 ALTRGNLQEELMQIWEehRVTVLMVTH 173
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
338-562 |
2.63e-23 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 101.07 E-value: 2.63e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 338 LEFSDVHFSYPSRAN------IKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQ--DIRNFNV 409
Cdd:COG4167 5 LEVRNLSKTFKYRTGlfrrqqFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHklEYGDYKY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 410 RCLReiIGVVSQEPvlfSTTIAENIRYG-------RGNVTMDEIEKAVKeanaydfImklpqkFDTL--VGDRGAQ---- 476
Cdd:COG4167 85 RCKH--IRMIFQDP---NTSLNPRLNIGqileeplRLNTDLTAEEREER-------I------FATLrlVGLLPEHanfy 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 477 ---LSGGQKQRIAIARALVRNPKILLLDEATSALDTESEA-------EVQaaldkAREGRTTIVIAHRLSTIRN-ADVIA 545
Cdd:COG4167 147 phmLSSGQKQRVALARALILQPKIIIADEALAALDMSVRSqiinlmlELQ-----EKLGISYIYVSQHLGIVKHiSDKVL 221
|
250
....*....|....*..
gi 568932737 546 GFEDGVIVEQGSHSELM 562
Cdd:COG4167 222 VMHQGEVVEYGKTAEVF 238
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
995-1194 |
2.64e-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: 2.64e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 995 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMA---GSVLLDGQEAKKlnVQWLRaQLGIVSQEPILFDC-SI 1070
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFNGQPRKP--DQFQK-CVAYVRQDDILLPGlTV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1071 AENIAYGDNSRV-VPHDEIVRAAKEAnihpfIETLPQKYNTRVGDKG-TQLSGGQKQRIAIARALIRQPRVLLLDEATSA 1148
Cdd:cd03234 99 RETLTYTAILRLpRKSSDAIRKKRVE-----DVLLRDLALTRIGGNLvKGISGGERRRVSIAVQLLWDPKVLILDEPTSG 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 568932737 1149 LDTESE-KVVQEALDKAREGRTCIVIAH--RLSTIQNADLIVVIENGKV 1194
Cdd:cd03234 174 LDSFTAlNLVSTLSQLARRNRIVILTIHqpRSDLFRLFDRILLLSSGEI 222
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
991-1207 |
3.15e-23 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 100.47 E-value: 3.15e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 991 ANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQWLRAQLGIVSQEPIL-FDCS 1069
Cdd:PRK11231 13 GTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHHLTpEGIT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1070 IAENIAYGDN------SRVVPHDE-IVRAAKEANihpFIETLPQKyntRVgdkgTQLSGGQKQRIAIARALIRQPRVLLL 1142
Cdd:PRK11231 93 VRELVAYGRSpwlslwGRLSAEDNaRVNQAMEQT---RINHLADR---RL----TDLSGGQRQRAFLAMVLAQDTPVVLL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1143 DEATSALD----TESEKVVQEAldkAREGRTCIVIAHRLS-TIQNADLIVVIENGKVKEHGTHQQLLAQK 1207
Cdd:PRK11231 163 DEPTTYLDinhqVELMRLMREL---NTQGKTVVTVLHDLNqASRYCDHLVVLANGHVMAQGTPEEVMTPG 229
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
995-1204 |
3.47e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 100.51 E-value: 3.47e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 995 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERF---YDP---MAGSVLLDGQEAKKLNVQWLRAQLGIVSQEPILF-D 1067
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLieiYDSkikVDGKVLYFGKDIFQIDAIKLRKEVGMVFQQPNPFpH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1068 CSIAENIAYGDNSRVVPHDEIVRAAKEANIHPFieTLPQKYNTRVGDKGTQLSGGQKQRIAIARALIRQPRVLLLDEATS 1147
Cdd:PRK14246 105 LSIYDNIAYPLKSHGIKEKREIKKIVEECLRKV--GLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTS 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 568932737 1148 ALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHGTHQQLL 1204
Cdd:PRK14246 183 MIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARvADYVAFLYNGELVEWGSSNEIF 240
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
339-565 |
3.53e-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: 3.53e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 339 EFSDVHFSYpsrANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLREIIGV 418
Cdd:COG4604 3 EIKNVSKRY---GGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 419 VSQEPVLFST-TIAENIRYGR-----GNVTmDEIEKAVKEANAYDFIMKLPQKF-DtlvgdrgaQLSGGQKQRIAIARAL 491
Cdd:COG4604 80 LRQENHINSRlTVRELVAFGRfpyskGRLT-AEDREIIDEAIAYLDLEDLADRYlD--------ELSGGQRQRAFIAMVL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 492 VRNPKILLLDEATSALDTESEAEVQAALDK-ARE-GRTTIVIAHRLstirN-----ADVIAGFEDGVIVEQGSHSELMKK 564
Cdd:COG4604 151 AQDTDYVLLDEPLNNLDMKHSVQMMKLLRRlADElGKTVVIVLHDI----NfascyADHIVAMKDGRVVAQGTPEEIITP 226
|
.
gi 568932737 565 E 565
Cdd:COG4604 227 E 227
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
336-594 |
3.80e-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: 3.80e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 336 GNLEFSDVHFSYPSRANiKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDpTEGKISIDGQDIRNFNVRCLREI 415
Cdd:cd03289 1 GQMTVKDLTAKYTEGGN-AVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 416 IGVVSQEPVLFSTTIAENIR-YGRGNvtMDEIEKAVKEANAYDFIMKLPQKFDTLVGDRGAQLSGGQKQRIAIARALVRN 494
Cdd:cd03289 79 FGVIPQKVFIFSGTFRKNLDpYGKWS--DEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 495 PKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRL--------------STIRNADVIAGF--EDGVIVEQGSH 558
Cdd:cd03289 157 AKILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIeamlecqrflvieeNKVRQYDSIQKLlnEKSHFKQAISP 236
|
250 260 270
....*....|....*....|....*....|....*...
gi 568932737 559 SELMKKEGIYFRLVNMQTAGSQI--LSEEFEVELSDEK 594
Cdd:cd03289 237 SDRLKLFPRRNSSKSKRKPRPQIqaLQEETEEEVQDTR 274
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
338-564 |
3.98e-23 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 99.76 E-value: 3.98e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 338 LEFSDVHFSYPSRaniKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLL--QRLYDPTEGKISIDGQDIRNFNV--RClR 413
Cdd:COG0396 1 LEIKNLHVSVEGK---EILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLmgHPKYEVTSGSILLDGEDILELSPdeRA-R 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 414 EIIGVVSQEPV--------LFSTTIAENIRygRGNVTMDEIEKAVKEANAydfIMKLPQKFdtlvGDRG--AQLSGGQKQ 483
Cdd:COG0396 77 AGIFLAFQYPVeipgvsvsNFLRTALNARR--GEELSAREFLKLLKEKMK---ELGLDEDF----LDRYvnEGFSGGEKK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 484 RIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKAR-EGRTTIVIAH--RLSTIRNADVIAGFEDGVIVEQGShSE 560
Cdd:COG0396 148 RNEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRsPDRGILIITHyqRILDYIKPDFVHVLVDGRIVKSGG-KE 226
|
....
gi 568932737 561 LMKK 564
Cdd:COG0396 227 LALE 230
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
338-561 |
4.49e-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: 4.49e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 338 LEFSDVHFSYpsrANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDI-------Rnfnvr 410
Cdd:TIGR03410 1 LEVSNLNVYY---GQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDItklppheR----- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 411 cLREIIGVVSQEPVLFST-TIAENIRYGRGnvTMDEIEKAVKeanayDFIMKL-PQKFDTLvGDRGAQLSGGQKQRIAIA 488
Cdd:TIGR03410 73 -ARAGIAYVPQGREIFPRlTVEENLLTGLA--ALPRRSRKIP-----DEIYELfPVLKEML-GRRGGDLSGGQQQQLAIA 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568932737 489 RALVRNPKILLLDEATSALDTESEAEVQAALDK--AREGRTTIVIAHRLSTIRN-ADVIAGFEDGVIVEQGSHSEL 561
Cdd:TIGR03410 144 RALVTRPKLLLLDEPTEGIQPSIIKDIGRVIRRlrAEGGMAILLVEQYLDFARElADRYYVMERGRVVASGAGDEL 219
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
995-1199 |
7.18e-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: 98.75 E-value: 7.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 995 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQWlRAQLGI--VSQEPILF-DCSIA 1071
Cdd:TIGR03410 15 ILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHE-RARAGIayVPQGREIFpRLTVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1072 ENIAYGDNsrvvphdeiVRAAKEANIHPFIETL-P---QKYNTRVGDkgtqLSGGQKQRIAIARALIRQPRVLLLDEATS 1147
Cdd:TIGR03410 94 ENLLTGLA---------ALPRRSRKIPDEIYELfPvlkEMLGRRGGD----LSGGQQQQLAIARALVTRPKLLLLDEPTE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 568932737 1148 ALDTESEKVVQEALDK--AREGRTCIVIAHRLS-TIQNADLIVVIENGKVKEHGT 1199
Cdd:TIGR03410 161 GIQPSIIKDIGRVIRRlrAEGGMAILLVEQYLDfARELADRYYVMERGRVVASGA 215
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
347-561 |
7.93e-23 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 102.03 E-value: 7.93e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 347 YPSRANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQdiRNFNVRCLREIIGVVSQEPVLF 426
Cdd:PRK11000 10 TKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEK--RMNDVPPAERGVGMVFQSYALY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 427 S-TTIAENIRYGR--GNVTMDEIEKAVKEANAydfIMKLpqkfDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEA 503
Cdd:PRK11000 88 PhLSVAENMSFGLklAGAKKEEINQRVNQVAE---VLQL----AHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568932737 504 TSALDTESEAEVQAALDK--AREGRTTIVIAH-RLSTIRNADVIAGFEDGVIVEQGSHSEL 561
Cdd:PRK11000 161 LSNLDAALRVQMRIEISRlhKRLGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
984-1210 |
8.40e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 100.70 E-value: 8.40e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 984 VFNYPTRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSV---------------LLDGQEAKKL- 1047
Cdd:PRK13631 30 VFDEKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdiyigdkknnheLITNPYSKKIk 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1048 NVQWLRAQLGIVSQEP--ILFDCSIAENIAYGDNSRVVPHDEivrAAKEANIH--------PFIETLPqkyntrvgdkgT 1117
Cdd:PRK13631 110 NFKELRRRVSMVFQFPeyQLFKDTIEKDIMFGPVALGVKKSE---AKKLAKFYlnkmglddSYLERSP-----------F 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1118 QLSGGQKQRIAIARALIRQPRVLLLDEATSALDTESEK-VVQEALDKAREGRTCIVIAHRLSTI-QNADLIVVIENGKVK 1195
Cdd:PRK13631 176 GLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHeMMQLILDAKANNKTVFVITHTMEHVlEVADEVIVMDKGKIL 255
|
250
....*....|....*
gi 568932737 1196 EHGTHQQLLAQKGIY 1210
Cdd:PRK13631 256 KTGTPYEIFTDQHII 270
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
991-1198 |
8.56e-23 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 97.74 E-value: 8.56e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 991 ANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGqeaKKLNVQwLRAQLGIVSQEPILF-DCS 1069
Cdd:cd03269 11 GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDG---KPLDIA-ARNRIGYLPEERGLYpKMK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1070 IAENIAYGDNSRVVPHDEIVRAAKEanihpFIET--LPQKYNTRVgdkgTQLSGGQKQRIAIARALIRQPRVLLLDEATS 1147
Cdd:cd03269 87 VIDQLVYLAQLKGLKKEEARRRIDE-----WLERleLSEYANKRV----EELSKGNQQKVQFIAAVIHDPELLILDEPFS 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 568932737 1148 ALDTESEKVVQEAL-DKAREGRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHG 1198
Cdd:cd03269 158 GLDPVNVELLKDVIrELARAGKTVILSTHQMELVEElCDRVLLLNKGRAVLYG 210
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1000-1207 |
9.31e-23 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 98.50 E-value: 9.31e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1000 SLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQwlRAQLGIVSQEPILFD-CSIAENIAYGD 1078
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS--RRPVSMLFQENNLFShLTVAQNIGLGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1079 NS----RVVPHDEIVRAAKEANIHPFIETLPqkyntrvgdkgTQLSGGQKQRIAIARALIRQPRVLLLDEATSALD---- 1150
Cdd:PRK10771 97 NPglklNAAQREKLHAIARQMGIEDLLARLP-----------GQLSGGQRQRVALARCLVREQPILLLDEPFSALDpalr 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 568932737 1151 TESEKVVQEALDkaREGRTCIVIAHRLS-TIQNADLIVVIENGKVKEHGTHQQLLAQK 1207
Cdd:PRK10771 166 QEMLTLVSQVCQ--ERQLTLLMVSHSLEdAARIAPRSLVVADGRIAWDGPTDELLSGK 221
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
343-561 |
9.70e-23 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 99.55 E-value: 9.70e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 343 VHFSYPSRANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQdirnfnvrclreiIGVVSQE 422
Cdd:cd03291 40 LFFSNLCLVGAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-------------ISFSSQF 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 423 PVLFSTTIAENIRYGrgnVTMDEI--EKAVKEANAYDFIMKLPQKFDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLL 500
Cdd:cd03291 107 SWIMPGTIKENIIFG---VSYDEYryKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLL 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568932737 501 DEATSALDTESEAEV-QAALDKAREGRTTIVIAHRLSTIRNADVIAGFEDGVIVEQGSHSEL 561
Cdd:cd03291 184 DSPFGYLDVFTEKEIfESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSEL 245
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
338-564 |
1.01e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 99.81 E-value: 1.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 338 LEFSDVHFSYPSRANI--KILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDgqDI------RNFNV 409
Cdd:PRK13643 2 IKFEKVNYTYQPNSPFasRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVG--DIvvsstsKQKEI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 410 RCLREIIGVVSQEP--VLFSTTIAENIRYGRGN--VTMDEIEKAVKE-----ANAYDFIMKLPqkfdtlvgdrgAQLSGG 480
Cdd:PRK13643 80 KPVRKKVGVVFQFPesQLFEETVLKDVAFGPQNfgIPKEKAEKIAAEklemvGLADEFWEKSP-----------FELSGG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 481 QKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKARE-GRTTIVIAHRLSTIRN-ADVIAGFEDGVIVEQGSH 558
Cdd:PRK13643 149 QMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQsGQTVVLVTHLMDDVADyADYVYLLEKGHIISCGTP 228
|
....*.
gi 568932737 559 SELMKK 564
Cdd:PRK13643 229 SDVFQE 234
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
359-561 |
1.36e-22 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 101.45 E-value: 1.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 359 LNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNfnVRCLREIIGVVSQEPVLFS-TTIAENIRYG 437
Cdd:PRK11607 38 VSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSH--VPPYQRPINMMFQSYALFPhMTVEQNIAFG 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 438 --RGNVTMDEIEKAVKE----ANAYDFIMKLPQkfdtlvgdrgaQLSGGQKQRIAIARALVRNPKILLLDEATSALDTE- 510
Cdd:PRK11607 116 lkQDKLPKAEIASRVNEmlglVHMQEFAKRKPH-----------QLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKl 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 568932737 511 ---SEAEVQAALDkaREGRTTIVIAH-RLSTIRNADVIAGFEDGVIVEQGSHSEL 561
Cdd:PRK11607 185 rdrMQLEVVDILE--RVGVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
995-1203 |
1.42e-22 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 100.93 E-value: 1.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 995 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQwlRAQLGIVSQEPILF-DCSIAEN 1073
Cdd:PRK10851 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHAR--DRKVGFVFQHYALFrHMTVFDN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1074 IAYGdnSRVVP-HDEIVRAAKEANIHPFIET-----LPQKYNTrvgdkgtQLSGGQKQRIAIARALIRQPRVLLLDEATS 1147
Cdd:PRK10851 95 IAFG--LTVLPrRERPNAAAIKAKVTQLLEMvqlahLADRYPA-------QLSGGQKQRVALARALAVEPQILLLDEPFG 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 568932737 1148 ALDTESEKVVQEALDKARE--GRTCIVIAH-RLSTIQNADLIVVIENGKVKEHGTHQQL 1203
Cdd:PRK10851 166 ALDAQVRKELRRWLRQLHEelKFTSVFVTHdQEEAMEVADRVVVMSQGNIEQAGTPDQV 224
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
349-524 |
1.46e-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: 1.46e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 349 SRANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDP---TEGKISIDGQDIRNFNVRcLREIiGVVSQEPVL 425
Cdd:COG4136 10 TLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALPAE-QRRI-GILFQDDLL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 426 FS-TTIAENIRYG-----RGNVTMDEIEKAVKEANAYDFimklpqkfdtlvGDRG-AQLSGGQKQRIAIARALVRNPKIL 498
Cdd:COG4136 88 FPhLSVGENLAFAlpptiGRAQRRARVEQALEEAGLAGF------------ADRDpATLSGGQRARVALLRALLAEPRAL 155
|
170 180
....*....|....*....|....*..
gi 568932737 499 LLDEATSALDTESEAEVQA-ALDKARE 524
Cdd:COG4136 156 LLDEPFSKLDAALRAQFREfVFEQIRQ 182
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
995-1196 |
1.70e-22 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 98.61 E-value: 1.70e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 995 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLN----------VQWL----------RA 1054
Cdd:PRK10419 27 VLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNraqrkafrrdIQMVfqdsisavnpRK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1055 QLGIVSQEPI--LFDCSIAENIAygdnsRVvphDEIVRAAKEANIHpfIETLPQkyntrvgdkgtQLSGGQKQRIAIARA 1132
Cdd:PRK10419 107 TVREIIREPLrhLLSLDKAERLA-----RA---SEMLRAVDLDDSV--LDKRPP-----------QLSGGQLQRVCLARA 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568932737 1133 LIRQPRVLLLDEATSALDteseKVVQ-EALD-----KAREGRTCIVIAHRLSTIQN-ADLIVVIENGKVKE 1196
Cdd:PRK10419 166 LAVEPKLLILDEAVSNLD----LVLQaGVIRllkklQQQFGTACLFITHDLRLVERfCQRVMVMDNGQIVE 232
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
994-1205 |
2.15e-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: 2.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 994 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVqWLRAQLGI--VSQEPILF-DCSI 1070
Cdd:cd03218 14 KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPM-HKRARLGIgyLPQEASIFrKLTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1071 AENIAYGDNSRVVPHDEIVRAAkEANIHPF-IETLPQKyntrvgdKGTQLSGGQKQRIAIARALIRQPRVLLLDEATSAL 1149
Cdd:cd03218 93 EENILAVLEIRGLSKKEREEKL-EELLEEFhITHLRKS-------KASSLSGGERRRVEIARALATNPKFLLLDEPFAGV 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 568932737 1150 DTESEKVVQEALDKAREGRTCIVIA-HRLS-TIQNADLIVVIENGKVKEHGTHQQLLA 1205
Cdd:cd03218 165 DPIAVQDIQKIIKILKDRGIGVLITdHNVReTLSITDRAYIIYEGKVLAEGTPEEIAA 222
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
995-1198 |
2.15e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 97.99 E-value: 2.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 995 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYD-----PMAGSVLLDGQE--AKKLNVQWLRAQLGIVSQEPILF- 1066
Cdd:PRK14267 19 VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGRNiySPDVDPIEVRREVGMVFQYPNPFp 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1067 DCSIAENIAYGD--NSRVVPH---DEIVR-AAKEAnihpfieTLPQKYNTRVGDKGTQLSGGQKQRIAIARALIRQPRVL 1140
Cdd:PRK14267 99 HLTIYDNVAIGVklNGLVKSKkelDERVEwALKKA-------ALWDEVKDRLNDYPSNLSGGQRQRLVIARALAMKPKIL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568932737 1141 LLDEATSALDTESEKVVQEALDKAREGRTCIVIAHrlSTIQNA---DLIVVIENGKVKEHG 1198
Cdd:PRK14267 172 LMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTH--SPAQAArvsDYVAFLYLGKLIEVG 230
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
360-562 |
2.40e-22 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 97.35 E-value: 2.40e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 360 NLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRclREIIGVVSQEPVLFS-TTIAENIRYG- 437
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS--RRPVSMLFQENNLFShLTVAQNIGLGl 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 438 RGNVTMDEIEKAVKEANAY-----DFIMKLPqkfdtlvgdrgAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESE 512
Cdd:PRK10771 97 NPGLKLNAAQREKLHAIARqmgieDLLARLP-----------GQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALR 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 568932737 513 AEVQAALDKAREGR--TTIVIAHRLS-TIRNAD---VIAgfeDGVIVEQGSHSELM 562
Cdd:PRK10771 166 QEMLTLVSQVCQERqlTLLMVSHSLEdAARIAPrslVVA---DGRIAWDGPTDELL 218
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
55-308 |
2.76e-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: 98.33 E-value: 2.76e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 55 EEMTRYAYYYSGLGGGVLVAAYIQVSFWTLAAGRQIKKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDDVSKISEGIGD 134
Cdd:cd18575 33 ALLNRAFLLLLAVALVLALASALRFYLVSWLGERVVADLRKAVFAHLLRLSPSFFETTRTGEVLSRLTTDTTLIQTVVGS 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 135 KVGMFFQAIATFFAGFIVGFIRGWKLTLVIMAISPILGLSTAVWAKILSTFSDKELAAYAKAGAVAEEALGAIRTVIAFG 214
Cdd:cd18575 113 SLSIALRNLLLLIGGLVMLFITSPKLTLLVLLVIPLVVLPIILFGRRVRRLSRASQDRLADLSAFAEETLSAIKTVQAFT 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 215 GQNKELERYQKHLENAKKIGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTIGN-AMTVFFSILIgAFSVGQ 293
Cdd:cd18575 193 REDAERQRFATAVEAAFAAALRRIRARALLTALVIFLVFGAIVFVLWLGAHDVLAGRMSAGElSQFVFYAVLA-AGSVGA 271
|
250
....*....|....*
gi 568932737 294 AAPCIDAFANARGAA 308
Cdd:cd18575 272 LSEVWGDLQRAAGAA 286
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
996-1207 |
2.83e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 98.36 E-value: 2.83e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 996 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQ----EAKKLNVQWLRAQLGIVSQ--EPILFDCS 1069
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYhitpETGNKNLKKLRKKVSLVFQfpEAQLFENT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1070 IAENIAYGDNSRVVPHDEivraAKEANIhpfietlpqKYNTRVG------DKGT-QLSGGQKQRIAIARALIRQPRVLLL 1142
Cdd:PRK13641 103 VLKDVEFGPKNFGFSEDE----AKEKAL---------KWLKKVGlsedliSKSPfELSGGQMRRVAIAGVMAYEPEILCL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568932737 1143 DEATSALDTESEK-VVQEALDKAREGRTCIVIAHRLSTI-QNADLIVVIENGKVKEHGTHQQLLAQK 1207
Cdd:PRK13641 170 DEPAAGLDPEGRKeMMQLFKDYQKAGHTVILVTHNMDDVaEYADDVLVLEHGKLIKHASPKEIFSDK 236
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
993-1193 |
2.94e-22 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 102.31 E-value: 2.94e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 993 VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYdPMA---GSVLLDGQEAKKLNVQWL-RAQLGIVSQEPILF-D 1067
Cdd:PRK13549 18 VKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHGtyeGEIIFEGEELQASNIRDTeRAGIAIIHQELALVkE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1068 CSIAENIAYGdnSRVVPH-----DEIVRAAKE------ANIHPfietlpqkyNTRVGDkgtqLSGGQKQRIAIARALIRQ 1136
Cdd:PRK13549 97 LSVLENIFLG--NEITPGgimdyDAMYLRAQKllaqlkLDINP---------ATPVGN----LGLGQQQLVEIAKALNKQ 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1137 PRVLLLDEATSALdTESEKVVQEAL--DKAREGRTCIVIAHRLSTIQN-ADLIVVIENGK 1193
Cdd:PRK13549 162 ARLLILDEPTASL-TESETAVLLDIirDLKAHGIACIYISHKLNEVKAiSDTICVIRDGR 220
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
995-1201 |
4.15e-22 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 96.62 E-value: 4.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 995 VLQGLSLEVKKGQTLALVGSSGCGKST---VVQLLErfydpMAGSVLLD--------GQEAKKLNVQWLRAQLGIVSQE- 1062
Cdd:PRK11124 17 ALFDITLDCPQGETLVLLGPSGAGKSSllrVLNLLE-----MPRSGTLNiagnhfdfSKTPSDKAIRELRRNVGMVFQQy 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1063 ---PILfdcSIAENIAYGDnSRV--VPHDEIVRAAKEanihpFIETLpqkyntRVGDKGT----QLSGGQKQRIAIARAL 1133
Cdd:PRK11124 92 nlwPHL---TVQQNLIEAP-CRVlgLSKDQALARAEK-----LLERL------RLKPYADrfplHLSGGQQQRVAIARAL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1134 IRQPRVLLLDEATSALDTE-SEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHGTHQ 1201
Cdd:PRK11124 157 MMEPQVLLFDEPTAALDPEiTAQIVSIIRELAETGITQVIVTHEVEVARKtASRVVYMENGHIVEQGDAS 226
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
994-1187 |
4.31e-22 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 96.32 E-value: 4.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 994 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQWLRAQLGIVSQEPILFDCSIAEN 1073
Cdd:PRK10247 21 KILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTLFGDTVYDN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1074 IAYGDNSRvvpHDEIVRAAKEANIHPFieTLPQKyntrVGDKG-TQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTE 1152
Cdd:PRK10247 101 LIFPWQIR---NQQPDPAIFLDDLERF--ALPDT----ILTKNiAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDES 171
|
170 180 190
....*....|....*....|....*....|....*..
gi 568932737 1153 SEKVVQEALDK-AREGRTCIV-IAHRLSTIQNADLIV 1187
Cdd:PRK10247 172 NKHNVNEIIHRyVREQNIAVLwVTHDKDEINHADKVI 208
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
983-1177 |
5.41e-22 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 97.08 E-value: 5.41e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 983 VVFNYPTRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVqWLRAQL-GIVSQ 1061
Cdd:COG1101 9 KTFNPGTVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPE-YKRAKYiGRVFQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1062 EPILFDC---SIAEN--IAYGDNSRVvphdEIVRAAKEANIHPFIET-------LPQKYNTRVGdkgtQLSGGQKQRIAI 1129
Cdd:COG1101 88 DPMMGTApsmTIEENlaLAYRRGKRR----GLRRGLTKKRRELFRELlatlglgLENRLDTKVG----LLSGGQRQALSL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 568932737 1130 ARALIRQPRVLLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRL 1177
Cdd:COG1101 160 LMATLTKPKLLLLDEHTAALDPKTAALVLELTEKivEENNLTTLMVTHNM 209
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
338-534 |
5.46e-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: 5.46e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 338 LEFSDVhfSYPSRANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISidgqdirnfnvRCLREIIG 417
Cdd:cd03223 1 IELENL--SLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIG-----------MPEGEDLL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 418 VVSQEPVLFSTTIAENIRYGRGNVtmdeiekavkeanaydfimklpqkfdtlvgdrgaqLSGGQKQRIAIARALVRNPKI 497
Cdd:cd03223 68 FLPQRPYLPLGTLREQLIYPWDDV-----------------------------------LSGGEQQRLAFARLLLHKPKF 112
|
170 180 190
....*....|....*....|....*....|....*...
gi 568932737 498 LLLDEATSALDTESEAEVqaaLDKAREGRTTIV-IAHR 534
Cdd:cd03223 113 VFLDEATSALDEESEDRL---YQLLKELGITVIsVGHR 147
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
655-912 |
5.55e-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: 97.50 E-value: 5.55e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 655 FVVGTVCAIANGALQPAFSIILSEMIaifgpgDDAVKQQKCN---MFSLVFLGLGVLSFFTFFLQGFTFGKAGEILTTRL 731
Cdd:cd18542 1 YLLAILALLLATALNLLIPLLIRRII------DSVIGGGLREllwLLALLILGVALLRGVFRYLQGYLAEKASQKVAYDL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 732 RSMAFKAMLRQDMSWFDdhKNSTGALSTRLATDAAQVQGATGTRLALIAQNTANLGTGIIISFIYGWQLTLLLLSVVPFI 811
Cdd:cd18542 75 RNDLYDHLQRLSFSFHD--KARTGDLMSRCTSDVDTIRRFLAFGLVELVRAVLLFIGALIIMFSINWKLTLISLAIIPFI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 812 AVAGIVEMKMLaGNAKRDKKEMEAA-GKIATEAIENIRTVVSLTQErKFESMYVEKLHGPYRN-SVRKAHIYGITFSISQ 889
Cdd:cd18542 153 ALFSYVFFKKV-RPAFEEIREQEGElNTVLQENLTGVRVVKAFARE-DYEIEKFDKENEEYRDlNIKLAKLLAKYWPLMD 230
|
250 260
....*....|....*....|...
gi 568932737 890 AFMYFSYAGCFRFGSYLIVNGHM 912
Cdd:cd18542 231 FLSGLQIVLVLWVGGYLVINGEI 253
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
1000-1204 |
6.50e-22 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 99.72 E-value: 6.50e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1000 SLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQWL----RAQLGIVSQE-PILFDCSIAENI 1074
Cdd:PRK10070 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELrevrRKKIAMVFQSfALMPHMTVLDNT 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1075 AYGDNSRVVPHDEIVRAAKEANIHPFIETLPQKYNtrvgdkgTQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTESE 1154
Cdd:PRK10070 128 AFGMELAGINAEERREKALDALRQVGLENYAHSYP-------DELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIR 200
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 568932737 1155 KVVQEALDK--AREGRTCIVIAHRL-STIQNADLIVVIENGKVKEHGTHQQLL 1204
Cdd:PRK10070 201 TEMQDELVKlqAKHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
987-1206 |
9.41e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 96.80 E-value: 9.41e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 987 YPTRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQWLRAQLGIVSQEP--I 1064
Cdd:PRK13652 11 YSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQNPddQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1065 LFDCSIAENIAYGDNSRVVPHDEIVRAAKEAnihpfIETLP-QKYNTRVGDkgtQLSGGQKQRIAIARALIRQPRVLLLD 1143
Cdd:PRK13652 91 IFSPTVEQDIAFGPINLGLDEETVAHRVSSA-----LHMLGlEELRDRVPH---HLSGGEKKRVAIAGVIAMEPQVLVLD 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568932737 1144 EATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTI-QNADLIVVIENGKVKEHGTHQQLLAQ 1206
Cdd:PRK13652 163 EPTAGLDPQGVKELIDFLNDLPEtyGMTVIFSTHQLDLVpEMADYIYVMDKGRIVAYGTVEEIFLQ 228
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
44-283 |
9.58e-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: 9.58e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 44 LSMLNPG-------RILEEEMTRYAYYYSG--LGGGVL--VAAYIQVSFWTLAAGRQIKKIRQKFFHAILRQEMGWFDIK 112
Cdd:cd18542 14 LNLLIPLlirriidSVIGGGLRELLWLLALliLGVALLrgVFRYLQGYLAEKASQKVAYDLRNDLYDHLQRLSFSFHDKA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 113 GTTELNTRLTDDVSKISEGIGDKVGMFFQAIATFFAGFIVGFIRGWKLTLVIMAISPILGLST--------AVWAKI--- 181
Cdd:cd18542 94 RTGDLMSRCTSDVDTIRRFLAFGLVELVRAVLLFIGALIIMFSINWKLTLISLAIIPFIALFSyvffkkvrPAFEEIreq 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 182 ---LSTFsdkelaayakagavAEEALGAIRTVIAFGGQNKELERYQKHLENAKKIGIKKAISANISMGIAFLLIYASYAL 258
Cdd:cd18542 174 egeLNTV--------------LQENLTGVRVVKAFAREDYEIEKFDKENEEYRDLNIKLAKLLAKYWPLMDFLSGLQIVL 239
|
250 260
....*....|....*....|....*
gi 568932737 259 AFWYGSTLVISKEYTIGNaMTVFFS 283
Cdd:cd18542 240 VLWVGGYLVINGEITLGE-LVAFIS 263
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
652-1207 |
9.75e-22 |
|
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: 9.75e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 652 WPYFVVGTVCAI--ANGALQPafsIILSEMIAIFGPGDDAVKQQKcnmfslVFLGLGVLSFF---TFFLQGFTFG--KAG 724
Cdd:TIGR01271 80 WRFVFYGILLYFgeATKAVQP---LLLGRIIASYDPFNAPEREIA------YYLALGLCLLFivrTLLLHPAIFGlhHLG 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 725 EILTTRLRSMAFKAMLRQDMSWFDdhKNSTGALSTRLATDAAQV-QGATGTRLALIAQNTANLGTGIIISFIYGWQLTLL 803
Cdd:TIGR01271 151 MQMRIALFSLIYKKTLKLSSRVLD--KISTGQLVSLLSNNLNKFdEGLALAHFVWIAPLQVILLMGLIWELLEVNGFCGL 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 804 LLSVVPFIAVAGIVEMKMlagnAKRDKKemeaAGKIA------TEAIENIRTVVSLTQERKFESMyVEKLHGPYRNSVRK 877
Cdd:TIGR01271 229 GFLILLALFQACLGQKMM----PYRDKR----AGKISerlaitSEIIENIQSVKAYCWEEAMEKI-IKNIRQDELKLTRK 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 878 AhiygitfsisqAFMYFSYAGCFRFGSYLIVNG----HMRFKDVIL--VFSA----IVL---------GAVALGHASSFA 938
Cdd:TIGR01271 300 I-----------AYLRYFYSSAFFFSGFFVVFLsvvpYALIKGIILrrIFTTisycIVLrmtvtrqfpGAIQTWYDSLGA 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 939 ----PDYAKAK------------------LSAAY---LFSLFERQPLIDSYSG-----EGLWPDKFEGSVTfnevvfnyp 988
Cdd:TIGR01271 369 itkiQDFLCKEeyktleynltttevemvnVTASWdegIGELFEKIKQNNKARKqpngdDGLFFSNFSLYVT--------- 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 989 tranvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQeakklnvqwlraqLGIVSQEPILFDC 1068
Cdd:TIGR01271 440 -----PVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR-------------ISFSPQTSWIMPG 501
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1069 SIAENIAYGdnsrvVPHDEI--VRAAKEANIHPFIETLPQKYNTRVGDKGTQLSGGQKQRIAIARALIRQPRVLLLDEAT 1146
Cdd:TIGR01271 502 TIKDNIIFG-----LSYDEYryTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPF 576
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568932737 1147 SALDTESEKVVQEA-LDKAREGRTCIVIAHRLSTIQNADLIVVIENGKVKEHGTHQQLLAQK 1207
Cdd:TIGR01271 577 THLDVVTEKEIFEScLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAKR 638
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
355-552 |
9.84e-22 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 96.29 E-value: 9.84e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 355 ILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKIsIDGqdirNFNVRCLREIIGVVSQEPVLFS-TTIAEN 433
Cdd:PRK11247 27 VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAG----TAPLAEAREDTRLMFQDARLLPwKKVIDN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 434 IRYG-RGNVTMDEIE--KAVKEANAydfimklpqkfdtlVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTE 510
Cdd:PRK11247 102 VGLGlKGQWRDAALQalAAVGLADR--------------ANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDAL 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 568932737 511 SEAEVQAALDK--AREGRTTIVIAHRLS-TIRNADVIAGFEDGVI 552
Cdd:PRK11247 168 TRIEMQDLIESlwQQHGFTVLLVTHDVSeAVAMADRVLLIEEGKI 212
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
353-553 |
1.52e-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: 1.52e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 353 IKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRclrEII--GVVS--QEPVLFST 428
Cdd:COG0411 17 LVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPH---RIArlGIARtfQNPRLFPE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 429 -TIAENIRYGRGNVTMDEIEKAV--------KEANAYDFIM------KLPQKFDTLVGDrgaqLSGGQKQRIAIARALVR 493
Cdd:COG0411 94 lTVLENVLVAAHARLGRGLLAALlrlprarrEEREARERAEellervGLADRADEPAGN----LSYGQQRRLEIARALAT 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568932737 494 NPKILLLDEATSALdteSEAEVQAALD-----KAREGRTTIVIAHRLstirnaDVIAGFEDGVIV 553
Cdd:COG0411 170 EPKLLLLDEPAAGL---NPEETEELAElirrlRDERGITILLIEHDM------DLVMGLADRIVV 225
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
992-1199 |
1.68e-21 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 95.13 E-value: 1.68e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 992 NVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLL---ERfYDPMAGSVLLDGQEAKKLNVQwLRAQLGI-VS-QEPI-- 1064
Cdd:COG0396 12 GKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLmghPK-YEVTSGSILLDGEDILELSPD-ERARAGIfLAfQYPVei 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1065 --------LfdcSIAENIAYGDNSRVVP-HDEIVRAAKEANihpfietLPQKYNTR---VGdkgtqLSGGQKQRIAIARA 1132
Cdd:COG0396 90 pgvsvsnfL---RTALNARRGEELSAREfLKLLKEKMKELG-------LDEDFLDRyvnEG-----FSGGEKKRNEILQM 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1133 LIRQPRVLLLDEATSALDTESEKVVQEALDKAR-EGRTCIVIAH--RLSTIQNADLIVVIENGKVKEHGT 1199
Cdd:COG0396 155 LLLEPKLAILDETDSGLDIDALRIVAEGVNKLRsPDRGILIITHyqRILDYIKPDFVHVLVDGRIVKSGG 224
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
647-1219 |
2.27e-21 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 101.59 E-value: 2.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 647 LNKTEWPYFVVGTVCAIANGALQPAFSIILSEMIAIFGPGDDAvkqqkcnmfslvFLGLgVLSFFTFFlqGFTFGKAGEI 726
Cdd:PLN03232 295 LNNSLGGRFWLGGIFKIGHDLSQFVGPVILSHLLQSMQEGDPA------------WVGY-VYAFLIFF--GVTFGVLCES 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 727 --------LTTRLRSMAFKAMLRQDMSWFDD-HKN-STGALSTRLATDAAQVQgatgtrlaLIAQNTANLGTG---IIIS 793
Cdd:PLN03232 360 qyfqnvgrVGFRLRSTLVAAIFHKSLRLTHEaRKNfASGKVTNMITTDANALQ--------QIAEQLHGLWSApfrIIVS 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 794 FIYGWQL--------TLLLLSVVPFIAVAgIVEMKMLA--GNAKRDKKEmeaagKIATEAIENIRTVVSLTQERKFESMy 863
Cdd:PLN03232 432 MVLLYQQlgvaslfgSLILFLLIPLQTLI-VRKMRKLTkeGLQWTDKRV-----GIINEILASMDTVKCYAWEKSFESR- 504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 864 VEKLHGPYRNSVRKAHIygitFSISQAFMYFS---YAGCFRFGSYLIVNGHMRFKDVILVFSAIVLGAVALGHASSFAPD 940
Cdd:PLN03232 505 IQGIRNEELSWFRKAQL----LSAFNSFILNSipvVVTLVSFGVFVLLGGDLTPARAFTSLSLFAVLRSPLNMLPNLLSQ 580
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 941 YAKAKLSAAYLFSLF--ERQPLIDSYSGEGLWPdkfegSVTFNEVVFNYPTRANVPVLQGLSLEVKKGQTLALVGSSGCG 1018
Cdd:PLN03232 581 VVNANVSLQRIEELLlsEERILAQNPPLQPGAP-----AISIKNGYFSWDSKTSKPTLSDINLEIPVGSLVAIVGGTGEG 655
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1019 KSTVVQLLERFYDPMAGSVLLdgqeakklnvqwLRAQLGIVSQEPILFDCSIAENIAYGDNsrvVPHDEIVRAAKEANIH 1098
Cdd:PLN03232 656 KTSLISAMLGELSHAETSSVV------------IRGSVAYVPQVSWIFNATVRENILFGSD---FESERYWRAIDVTALQ 720
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1099 PFIETLPQKYNTRVGDKGTQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTE-SEKVVQEALDKAREGRTCIVIAHRL 1177
Cdd:PLN03232 721 HDLDLLPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHvAHQVFDSCMKDELKGKTRVLVTNQL 800
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 568932737 1178 STIQNADLIVVIENGKVKEHGTHQQlLAQKGIYFSMVNIQAG 1219
Cdd:PLN03232 801 HFLPLMDRIILVSEGMIKEEGTFAE-LSKSGSLFKKLMENAG 841
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
995-1194 |
2.29e-21 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 95.13 E-value: 2.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 995 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDP-----MAGSVLL-DGQEAKKLNVQWLRaqlgivsqepILFDC 1068
Cdd:PRK11247 27 VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPsagelLAGTAPLaEAREDTRLMFQDAR----------LLPWK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1069 SIAENIAYG--DNSRVVPHD--EIVRAAKEANIHPfietlpqkyntrvgdkgTQLSGGQKQRIAIARALIRQPRVLLLDE 1144
Cdd:PRK11247 97 KVIDNVGLGlkGQWRDAALQalAAVGLADRANEWP-----------------AALSGGQKQRVALARALIHRPGLLLLDE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 568932737 1145 ATSALDTESEKVVQEALDK--AREGRTCIVIAHRLS-TIQNADLIVVIENGKV 1194
Cdd:PRK11247 160 PLGALDALTRIEMQDLIESlwQQHGFTVLLVTHDVSeAVAMADRVLLIEEGKI 212
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
342-565 |
2.46e-21 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 95.24 E-value: 2.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 342 DVHFSYPSRAnikILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCL-REIIGVVS 420
Cdd:PRK10575 16 NVSFRVPGRT---LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFaRKVAYLPQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 421 QEPVLFSTTIAENIRYGR-------GNVTMDEIEKaVKEANAYDFIMKLPQKfdtLVGdrgaQLSGGQKQRIAIARALVR 493
Cdd:PRK10575 93 QLPAAEGMTVRELVAIGRypwhgalGRFGAADREK-VEEAISLVGLKPLAHR---LVD----SLSGGERQRAWIAMLVAQ 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568932737 494 NPKILLLDEATSALDTESEAEVQAALDK-ARE-GRTTIVIAHRLS-TIRNADVIAGFEDGVIVEQGSHSELMKKE 565
Cdd:PRK10575 165 DSRCLLLDEPTSALDIAHQVDVLALVHRlSQErGLTVIAVLHDINmAARYCDYLVALRGGEMIAQGTPAELMRGE 239
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
311-535 |
3.14e-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: 3.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 311 IFDIIDNnPKIDSFSERGHKPDNIKGNLEFSDVHFS--YPSRANI--------------KILKGLNLKVKSGQTVALVGN 374
Cdd:TIGR01271 1175 VFKFIDL-PQEEPRPSGGGGKYQLSTVLVIENPHAQkcWPSGGQMdvqgltakyteagrAVLQDLSFSVEGGQRVGLLGR 1253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 375 SGCGKSTTVQLLQRLYDpTEGKISIDGQDIRNFNVRCLREIIGVVSQEPVLFSTTIAENIR-YGRgnVTMDEIEKAVKEA 453
Cdd:TIGR01271 1254 TGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNLDpYEQ--WSDEEIWKVAEEV 1330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 454 NAYDFIMKLPQKFDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAH 533
Cdd:TIGR01271 1331 GLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEH 1410
|
..
gi 568932737 534 RL 535
Cdd:TIGR01271 1411 RV 1412
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
987-1189 |
3.16e-21 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 92.68 E-value: 3.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 987 YPTRanvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQwlraqlgiVSQEPILF 1066
Cdd:NF040873 2 YGGR---PVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQ--------RSEVPDSL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1067 DCSIAENIAYGDNSRVVPHDEIVRAAKEANIHPFietlpqkynTRVGDKG------TQLSGGQKQRIAIARALIRQPRVL 1140
Cdd:NF040873 71 PLTVRDLVAMGRWARRGLWRRLTRDDRAAVDDAL---------ERVGLADlagrqlGELSGGQRQRALLAQGLAQEADLL 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 568932737 1141 LLDEATSALDTESEKVVQEAL-DKAREGRTCIVIAHRLSTIQNADLIVVI 1189
Cdd:NF040873 142 LLDEPTTGLDAESRERIIALLaEEHARGATVVVVTHDLELVRRADPCVLL 191
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
986-1207 |
3.54e-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: 95.31 E-value: 3.54e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 986 NYPTRANvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQWLRAQlgivsqepil 1065
Cdd:cd03291 44 NLCLVGA-PVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRISFSSQFSWIMPG---------- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1066 fdcSIAENIAYGdnsrvVPHDE-----IVRAAK-EANIHPFietlPQKYNTRVGDKGTQLSGGQKQRIAIARALIRQPRV 1139
Cdd:cd03291 113 ---TIKENIIFG-----VSYDEyryksVVKACQlEEDITKF----PEKDNTVLGEGGITLSGGQRARISLARAVYKDADL 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568932737 1140 LLLDEATSALDTESEKVVQEA-LDKAREGRTCIVIAHRLSTIQNADLIVVIENGKVKEHGTHQQLLAQK 1207
Cdd:cd03291 181 YLLDSPFGYLDVFTEKEIFEScVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSLR 249
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
338-567 |
3.97e-21 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 94.69 E-value: 3.97e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 338 LEFSDVHFSYPSRaniKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIrNFNVR---CLRE 414
Cdd:PRK13638 2 LATSDLWFRYQDE---PVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPL-DYSKRgllALRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 415 IIGVVSQEP--VLFSTTIAENIRYGRGN--VTMDEIEKAVKEANaydfimklpqkfdTLVGDRGAQ------LSGGQKQR 484
Cdd:PRK13638 78 QVATVFQDPeqQIFYTDIDSDIAFSLRNlgVPEAEITRRVDEAL-------------TLVDAQHFRhqpiqcLSHGQKKR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 485 IAIARALVRNPKILLLDEATSALDTESEAEVQAALDK-AREGRTTIVIAHRLSTIRN-ADVIAGFEDGVIVEQG------ 556
Cdd:PRK13638 145 VAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRiVAQGNHVIISSHDIDLIYEiSDAVYVLRQGQILTHGapgevf 224
|
250
....*....|.
gi 568932737 557 SHSELMKKEGI 567
Cdd:PRK13638 225 ACTEAMEQAGL 235
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
353-565 |
3.99e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 95.54 E-value: 3.99e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 353 IKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNF------------------------N 408
Cdd:PRK13651 20 LKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKkktkekekvleklviqktrfkkikK 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 409 VRCLREIIGVVSQ--EPVLFSTTIAENIRYGRGNVTMDEiEKAVKEANAYDFIMKLPQKFDtlvgDRGA-QLSGGQKQRI 485
Cdd:PRK13651 100 IKEIRRRVGVVFQfaEYQLFEQTIEKDIIFGPVSMGVSK-EEAKKRAAKYIELVGLDESYL----QRSPfELSGGQKRRV 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 486 AIARALVRNPKILLLDEATSALDTESEAEVQAALDKA-REGRTTIVIAHRLSTI--RNADVIAgFEDGVIVEQGSHSELM 562
Cdd:PRK13651 175 ALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLnKQGKTIILVTHDLDNVleWTKRTIF-FKDGKIIKDGDTYDIL 253
|
...
gi 568932737 563 KKE 565
Cdd:PRK13651 254 SDN 256
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
978-1199 |
5.21e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 94.80 E-value: 5.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 978 VTFNEVvfNYPTRANVP----VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSV----LLDGQEAKKLNV 1049
Cdd:PRK13643 2 IKFEKV--NYTYQPNSPfasrALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVtvgdIVVSSTSKQKEI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1050 QWLRAQLGIVSQEP--ILFDCSIAENIAYGDNSRVVPHDEIVRAAKE-----ANIHPFIETLPqkyntrvgdkgTQLSGG 1122
Cdd:PRK13643 80 KPVRKKVGVVFQFPesQLFEETVLKDVAFGPQNFGIPKEKAEKIAAEklemvGLADEFWEKSP-----------FELSGG 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568932737 1123 QKQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEALDKARE-GRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHGT 1199
Cdd:PRK13643 149 QMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQsGQTVVLVTHLMDDVADyADYVYLLEKGHIISCGT 227
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
995-1205 |
5.23e-21 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 98.62 E-value: 5.23e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 995 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYdPMAGSVLLDGQEAKKLNVQWL---RAQLGIVSQEP---ILFDC 1068
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLHNLNRRQLlpvRHRIQVVFQDPnssLNPRL 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1069 SIAENIAYGDNsrvVPHDEIVRAAKEANIhpfIETLpqkynTRVG-DKGT------QLSGGQKQRIAIARALIRQPRVLL 1141
Cdd:PRK15134 380 NVLQIIEEGLR---VHQPTLSAAQREQQV---IAVM-----EEVGlDPETrhrypaEFSGGQRQRIAIARALILKPSLII 448
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568932737 1142 LDEATSALDteseKVVQE---ALDKAREGR---TCIVIAHRLSTIQN-ADLIVVIENGKVKEHGTHQQLLA 1205
Cdd:PRK15134 449 LDEPTSSLD----KTVQAqilALLKSLQQKhqlAYLFISHDLHVVRAlCHQVIVLRQGEVVEQGDCERVFA 515
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
655-926 |
5.72e-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: 5.72e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 655 FVVGTVCAIANGALQPAFSIILSEMI-AIFGPGDdavkQQKCNMFSLVFLGLGVLSFFTFFLQGFTFGKAGEILTTRLRS 733
Cdd:cd18552 1 LALAILGMILVAATTAALAWLLKPLLdDIFVEKD----LEALLLVPLAIIGLFLLRGLASYLQTYLMAYVGQRVVRDLRN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 734 MAFKAMLRQDMSWFDdhKNSTGALSTRLATDAAQVQGATGTRLALIAQNTANLGTGIIISFIYGWQLTLLLLSVVPFIAV 813
Cdd:cd18552 77 DLFDKLLRLPLSFFD--RNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKLTLIALVVLPLAAL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 814 AgiveMKMLAGNAKRD-KKEMEAAGKIAT---EAIENIRTVVSLTQERKFESMYVEKLHGPYRNSVRKAHIYGITFSISQ 889
Cdd:cd18552 155 P----IRRIGKRLRKIsRRSQESMGDLTSvlqETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIARARALSSPLME 230
|
250 260 270
....*....|....*....|....*....|....*..
gi 568932737 890 AFMYFSYAGCFRFGSYLIVNGHMRFKDVILVFSAIVL 926
Cdd:cd18552 231 LLGAIAIALVLWYGGYQVISGELTPGEFISFITALLL 267
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
73-294 |
6.51e-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: 6.51e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 73 VAAYIQVSFWTLAAGRQIKKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDDVSKISEGIGDKVGMFFQAIATFFAGFIV 152
Cdd:cd18784 51 VAAGIRGGLFTLAMARLNIRIRNLLFRSIVSQEIGFFDTVKTGDITSRLTSDTTTMSDTVSLNLNIFLRSLVKAIGVIVF 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 153 GFIRGWKLTLVIMAISPILGLSTAVWAKILSTFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKELERYQKHLENAKK 232
Cdd:cd18784 131 MFKLSWQLSLVTLIGLPLIAIVSKVYGDYYKKLSKAVQDSLAKANEVAEETISSIRTVRSFANEDGEANRYSEKLKDTYK 210
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568932737 233 IGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTIGNamtvFFSILIGAFSVGQA 294
Cdd:cd18784 211 LKIKEALAYGGYVWSNELTELALTVSTLYYGGHLVITGQISGGN----LISFILYQLELGSC 268
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
346-542 |
8.51e-21 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 91.53 E-value: 8.51e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 346 SYPSRAnikILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISidgqdirnfnVRCLREIIGVV--SQEP 423
Cdd:NF040873 1 GYGGRP---VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVR----------RAGGARVAYVPqrSEVP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 424 VLFSTTIAENIRYGR-------GNVTMDEiEKAVKEAnaydfIMKLpqKFDTLVGDRGAQLSGGQKQRIAIARALVRNPK 496
Cdd:NF040873 68 DSLPLTVRDLVAMGRwarrglwRRLTRDD-RAAVDDA-----LERV--GLADLAGRQLGELSGGQRQRALLAQGLAQEAD 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 568932737 497 ILLLDEATSALDTESEAEVQAAL-DKAREGRTTIVIAHRLSTIRNAD 542
Cdd:NF040873 140 LLLLDEPTTGLDAESRERIIALLaEEHARGATVVVVTHDLELVRRAD 186
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
88-308 |
1.50e-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: 93.27 E-value: 1.50e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 88 RQIKKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDDVSKISEGIGDKVGMFFQAIATFFAGFIVGFIRGWKLTLVIMAI 167
Cdd:cd18551 66 RVVLDLRRRLWRRLLRLPVSFFDRRRSGDLVSRVTNDTTLLRELITSGLPQLVTGVLTVVGAVVLMFLLDWVLTLVTLAV 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 168 SPILGLSTAVWAKILSTFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKELERYQKHLENAKKIGIKKAISANISMGI 247
Cdd:cd18551 146 VPLAFLIILPLGRRIRKASKRAQDALGELSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAKIEALIGPL 225
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568932737 248 AFLLIYASYALAFWYGSTLVISKEYTIGNAMTVFFSILIGAFSVGQAAPCIDAFANARGAA 308
Cdd:cd18551 226 MGLAVQLALLVVLGVGGARVASGALTVGTLVAFLLYLFQLITPLSQLSSFFTQLQKALGAL 286
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
349-556 |
1.50e-20 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 95.68 E-value: 1.50e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 349 SRANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLREIIGVVSQEPVL-FS 427
Cdd:PRK09536 12 EFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLsFE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 428 TTIAENIRYGRGN-----VTMDE-----IEKAVKEANAYDFImklPQKFDTlvgdrgaqLSGGQKQRIAIARALVRNPKI 497
Cdd:PRK09536 92 FDVRQVVEMGRTPhrsrfDTWTEtdraaVERAMERTGVAQFA---DRPVTS--------LSGGERQRVLLARALAQATPV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568932737 498 LLLDEATSALDTESEAE-VQAALDKAREGRTTIVIAHRLS-TIRNADVIAGFEDGVIVEQG 556
Cdd:PRK09536 161 LLLDEPTASLDINHQVRtLELVRRLVDDGKTAVAAIHDLDlAARYCDELVLLADGRVRAAG 221
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
353-552 |
1.74e-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: 1.74e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 353 IKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQD----------IRNFNVRclREIIGVVSQe 422
Cdd:COG4778 24 LPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGgwvdlaqaspREILALR--RRTIGYVSQ- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 423 pvlFSTTI----AENIrygrgnVTMDEIEKAVKEANAYDFIMKLPQKFDtlVGDRGAQL-----SGGQKQRIAIARALVR 493
Cdd:COG4778 101 ---FLRVIprvsALDV------VAEPLLERGVDREEARARARELLARLN--LPERLWDLppatfSGGEQQRVNIARGFIA 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 494 NPKILLLDEATSALDTESEAEVQAALDKAREGRTTIV-IAHrlstirNADVIAGFEDGVI 552
Cdd:COG4778 170 DPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIgIFH------DEEVREAVADRVV 223
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
995-1205 |
1.95e-20 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 93.33 E-value: 1.95e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 995 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGqEAKKLNVQWLRAQLGIVSQ----EPilfDCSI 1070
Cdd:PRK13537 22 VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCG-EPVPSRARHARQRVGVVPQfdnlDP---DFTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1071 AENIA-----YGDNSrvvphdeivrAAKEANIHPFIE--TLPQKYNTRVGDkgtqLSGGQKQRIAIARALIRQPRVLLLD 1143
Cdd:PRK13537 98 RENLLvfgryFGLSA----------AAARALVPPLLEfaKLENKADAKVGE----LSGGMKRRLTLARALVNDPDVLVLD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568932737 1144 EATSALDTESEKVVQEALDK--AReGRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHGTHQQLLA 1205
Cdd:PRK13537 164 EPTTGLDPQARHLMWERLRSllAR-GKTILLTTHFMEEAERlCDRLCVIEEGRKIAEGAPHALIE 227
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
993-1193 |
2.14e-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: 2.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 993 VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFY--DPMAGSVLLDGQEAKKLNVQWL-RAQLGIVSQEPILF-DC 1068
Cdd:TIGR02633 14 VKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYphGTWDGEIYWSGSPLKASNIRDTeRAGIVIIHQELTLVpEL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1069 SIAENIAYGD----NSRVVPHDEIVRAAKEANIHPFIETLPqkyNTR-VGDKGtqlsGGQKQRIAIARALIRQPRVLLLD 1143
Cdd:TIGR02633 94 SVAENIFLGNeitlPGGRMAYNAMYLRAKNLLRELQLDADN---VTRpVGDYG----GGQQQLVEIAKALNKQARLLILD 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 568932737 1144 EATSAL-DTESEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVIENGK 1193
Cdd:TIGR02633 167 EPSSSLtEKETEILLDIIRDLKAHGVACVYISHKLNEVKAvCDTICVIRDGQ 218
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
984-1203 |
2.24e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 93.23 E-value: 2.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 984 VFNYPTRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSV-----------------------LLD 1040
Cdd:PRK13651 11 IFNKKLPTELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknkkktkekekvleklVIQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1041 GQEAKKL-NVQWLRAQLGIVSQ--EPILFDCSIAENIAYGDNSRVVPHDEIVRAAKEanihpFIET--LPQKYNTRvgdK 1115
Cdd:PRK13651 91 KTRFKKIkKIKEIRRRVGVVFQfaEYQLFEQTIEKDIIFGPVSMGVSKEEAKKRAAK-----YIELvgLDESYLQR---S 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1116 GTQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEALDKA-REGRTCIVIAHRL-STIQNADLIVVIENGK 1193
Cdd:PRK13651 163 PFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLnKQGKTIILVTHDLdNVLEWTKRTIFFKDGK 242
|
250
....*....|.
gi 568932737 1194 -VKEHGTHQQL 1203
Cdd:PRK13651 243 iIKDGDTYDIL 253
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
353-550 |
2.57e-20 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 96.15 E-value: 2.57e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 353 IKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYdPT---EGKISIDGQDIRNFNVR-CLREIIGVVSQEPVLFST 428
Cdd:PRK13549 18 VKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHgtyEGEIIFEGEELQASNIRdTERAGIAIIHQELALVKE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 429 -TIAENIRYGRGNVTMDEIEKAVKEANAYDFIMKLpqKFDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEATSAL 507
Cdd:PRK13549 97 lSVLENIFLGNEITPGGIMDYDAMYLRAQKLLAQL--KLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDEPTASL 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 568932737 508 dTESEAEVQAAL--DKAREGRTTIVIAHRLSTIRN-ADVIAGFEDG 550
Cdd:PRK13549 175 -TESETAVLLDIirDLKAHGIACIYISHKLNEVKAiSDTICVIRDG 219
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
355-567 |
3.30e-20 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 91.97 E-value: 3.30e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 355 ILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLREIIGVVSQEPVL-FSTTIAEN 433
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTpGDITVQEL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 434 IRYGRG------NVTMDEIEKAVKEANAYDFIMKLP-QKFDTlvgdrgaqLSGGQKQRIAIARALVRNPKILLLDEATSA 506
Cdd:PRK10253 102 VARGRYphqplfTRWRKEDEEAVTKAMQATGITHLAdQSVDT--------LSGGQRQRAWIAMVLAQETAIMLLDEPTTW 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568932737 507 LDTESEAEVQAALDK--AREGRTTIVIAHRLS-TIRNADVIAGFEDGVIVEQGSHSELMKKEGI 567
Cdd:PRK10253 174 LDISHQIDLLELLSElnREKGYTLAAVLHDLNqACRYASHLIALREGKIVAQGAPKEIVTAELI 237
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
346-502 |
3.58e-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: 3.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 346 SYPSRaniKILKGLNLKVKSGQTVALVGNSGCGKSTT----VQLLQrlydPTEGKISIDGQDIRNF--NVRClREIIGVV 419
Cdd:COG1137 12 SYGKR---TVVKDVSLEVNQGEIVGLLGPNGAGKTTTfymiVGLVK----PDSGRIFLDGEDITHLpmHKRA-RLGIGYL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 420 SQEPVLF-STTIAENIRygrgnvtmdeiekAVKEanaydfIMKLP-----QKFDTLVGD---------RGAQLSGGQKQR 484
Cdd:COG1137 84 PQEASIFrKLTVEDNIL-------------AVLE------LRKLSkkereERLEELLEEfgithlrksKAYSLSGGERRR 144
|
170
....*....|....*...
gi 568932737 485 IAIARALVRNPKILLLDE 502
Cdd:COG1137 145 VEIARALATNPKFILLDE 162
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
338-564 |
3.66e-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: 3.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 338 LEFSDVHFSypsRANIKILKGLNLKVKSGQTVALVGNSGCGKSTtvqLLQRL-----YDPTEGKISIDGQDIRNFNV--R 410
Cdd:cd03217 1 LEIKDLHVS---VGGKEILKGVNLTIKKGEVHALMGPNGSGKST---LAKTImghpkYEVTEGEILFKGEDITDLPPeeR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 411 ClREIIGVVSQEPVLFS-TTIAENIRYgrgnvtmdeiekaVKEAnaydfimklpqkfdtlvgdrgaqLSGGQKQRIAIAR 489
Cdd:cd03217 75 A-RLGIFLAFQYPPEIPgVKNADFLRY-------------VNEG-----------------------FSGGEKKRNEILQ 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 490 ALVRNPKILLLDEATSALDTESEAEVQAALDKAR-EGRTTIVIAH--RLSTIRNADVIAGFEDGVIVEQGSHS---ELMK 563
Cdd:cd03217 118 LLLLEPDLAILDEPDSGLDIDALRLVAEVINKLReEGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVKSGDKElalEIEK 197
|
.
gi 568932737 564 K 564
Cdd:cd03217 198 K 198
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
977-1207 |
4.17e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 92.15 E-value: 4.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 977 SVTFNEVVFNYP--TRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDG----QEAKKLNVQ 1050
Cdd:PRK13646 2 TIRFDNVSYTYQkgTPYEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDititHKTKDKYIR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1051 WLRAQLGIVSQ--EPILFDCSIAENIAYG--------DNSRVVPHDEIVRAAKEANI---HPFietlpqkyntrvgdkgt 1117
Cdd:PRK13646 82 PVRKRIGMVFQfpESQLFEDTVEREIIFGpknfkmnlDEVKNYAHRLLMDLGFSRDVmsqSPF----------------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1118 QLSGGQKQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEALDKAR--EGRTCIVIAHRLSTI-QNADLIVVIENGKV 1194
Cdd:PRK13646 145 QMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtdENKTIILVSHDMNEVaRYADEVIVMKEGSI 224
|
250
....*....|...
gi 568932737 1195 KEHGTHQQLLAQK 1207
Cdd:PRK13646 225 VSQTSPKELFKDK 237
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
974-1205 |
4.75e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 91.70 E-value: 4.75e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 974 FEGSVTFNEVVFNYPTRAnvpvlqglslevkkgqTLALVGSSGCGKSTVVQLLERFYDPMAG-----SVLLDGQEA-KKL 1047
Cdd:PRK14271 31 FAGKTVLDQVSMGFPARA----------------VTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIfNYR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1048 NVQWLRAQLGIVSQEPILFDCSIAENIAYGDNS-RVVPHDEIvRAAKEANIHPFieTLPQKYNTRVGDKGTQLSGGQKQR 1126
Cdd:PRK14271 95 DVLEFRRRVGMLFQRPNPFPMSIMDNVLAGVRAhKLVPRKEF-RGVAQARLTEV--GLWDAVKDRLSDSPFRLSGGQQQL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1127 IAIARALIRQPRVLLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHGTHQQLLA 1205
Cdd:PRK14271 172 LCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARiSDRAALFFDGRLVEEGPTEQLFS 251
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
338-567 |
4.88e-20 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 95.12 E-value: 4.88e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 338 LEFSDVHFSYpsrANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLREI-I 416
Cdd:PRK15439 12 LCARSISKQY---SGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLgI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 417 GVVSQEPVLF-STTIAENIRYG--RGNVTMDEIEKAVKEANAYdfiMKLPQKFDTL-VGDRgaqlsggqkQRIAIARALV 492
Cdd:PRK15439 89 YLVPQEPLLFpNLSVKENILFGlpKRQASMQKMKQLLAALGCQ---LDLDSSAGSLeVADR---------QIVEILRGLM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 493 RNPKILLLDEATSALdTESEAE-----VQAALDKareGRTTIVIAHRLSTIRN-ADVIAGFEDGVIVEQGSHSELMKKEG 566
Cdd:PRK15439 157 RDSRILILDEPTASL-TPAETErlfsrIRELLAQ---GVGIVFISHKLPEIRQlADRISVMRDGTIALSGKTADLSTDDI 232
|
.
gi 568932737 567 I 567
Cdd:PRK15439 233 I 233
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
978-1176 |
6.06e-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: 6.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 978 VTFNEVVFNypTRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGqeakklnvqwlRAQLG 1057
Cdd:cd03223 1 IELENLSLA--TPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPE-----------GEDLL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1058 IVSQEPILFDCSIAENIAYgdnsrvvPHDEIvraakeanihpfietlpqkyntrvgdkgtqLSGGQKQRIAIARALIRQP 1137
Cdd:cd03223 68 FLPQRPYLPLGTLREQLIY-------PWDDV------------------------------LSGGEQQRLAFARLLLHKP 110
|
170 180 190
....*....|....*....|....*....|....*....
gi 568932737 1138 RVLLLDEATSALDTESEKVVQEALDKarEGRTCIVIAHR 1176
Cdd:cd03223 111 KFVFLDEATSALDEESEDRLYQLLKE--LGITVISVGHR 147
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
995-1178 |
6.56e-20 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 90.26 E-value: 6.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 995 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQW---LRAQ-LGIVSQ-EPILFDCS 1069
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAkaeLRNQkLGFIYQfHHLLPDFT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1070 IAENIAYGDNSRVVPHDEIVRAAKEANIHPFIETlpqkyntRVGDKGTQLSGGQKQRIAIARALIRQPRVLLLDEATSAL 1149
Cdd:PRK11629 104 ALENVAMPLLIGKKKPAEINSRALEMLAAVGLEH-------RANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNL 176
|
170 180 190
....*....|....*....|....*....|.
gi 568932737 1150 DTESEKVVQEALDK--AREGRTCIVIAHRLS 1178
Cdd:PRK11629 177 DARNADSIFQLLGElnRLQGTAFLVVTHDLQ 207
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
655-912 |
6.80e-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: 91.34 E-value: 6.80e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 655 FVVGTVCAIANGALQPAFSIILSEMIaifgpgdDAVKQQKCNMFSLVFL-GLGVLSFFTFFLQGFTFGKAGEILTTRLRS 733
Cdd:cd18551 1 LILALLLSLLGTAASLAQPLLVKNLI-------DALSAGGSSGGLLALLvALFLLQAVLSALSSYLLGRTGERVVLDLRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 734 MAFKAMLRQDMSWFDdhKNSTGALSTRLATDAAQVQgatgtrlALIAQNTANLGTGII-------ISFIYGWQLTLLLLS 806
Cdd:cd18551 74 RLWRRLLRLPVSFFD--RRRSGDLVSRVTNDTTLLR-------ELITSGLPQLVTGVLtvvgavvLMFLLDWVLTLVTLA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 807 VVPFIAVAGIVEMKMLAGNAKRDKKEMEAAGKIATEAIENIRTVVSLTQERKFESMYVEKLHGPYRNSVRKAHIYGITFS 886
Cdd:cd18551 145 VVPLAFLIILPLGRRIRKASKRAQDALGELSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAKIEALIGP 224
|
250 260
....*....|....*....|....*.
gi 568932737 887 ISQAFMYFSYAGCFRFGSYLIVNGHM 912
Cdd:cd18551 225 LMGLAVQLALLVVLGVGGARVASGAL 250
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
994-1206 |
6.96e-20 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 94.77 E-value: 6.96e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 994 PVLQGLSLEVKKGQTLALVGSSGCGKS-TVVQLLERFYDP----MAGSVLLDGQEAKKLNVQWLRA----QLGIVSQEPI 1064
Cdd:PRK15134 23 TVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFHGESLLHASEQTLRGvrgnKIAMIFQEPM 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1065 L-------FDCSIAENIAYGDNSRVVP-HDEIVRAAKEANIHpfietlpqKYNTRVGDKGTQLSGGQKQRIAIARALIRQ 1136
Cdd:PRK15134 103 VslnplhtLEKQLYEVLSLHRGMRREAaRGEILNCLDRVGIR--------QAAKRLTDYPHQLSGGERQRVMIAMALLTR 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568932737 1137 PRVLLLDEATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTI-QNADLIVVIENGKVKEHGTHQQLLAQ 1206
Cdd:PRK15134 175 PELLIADEPTTALDVSVQAQILQLLRELQQelNMGLLFITHNLSIVrKLADRVAVMQNGRCVEQNRAATLFSA 247
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
338-565 |
7.12e-20 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 92.59 E-value: 7.12e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 338 LEFSDVHFSYPSRAnikILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNfNVRCLREIIG 417
Cdd:PRK13536 42 IDLAGVSKSYGDKA---VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA-RARLARARIG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 418 VVSQEPVL-FSTTIAEN-IRYGR-GNVTMDEIEKAVkeANAYDFiMKLPQKFDTLVgdrgAQLSGGQKQRIAIARALVRN 494
Cdd:PRK13536 118 VVPQFDNLdLEFTVRENlLVFGRyFGMSTREIEAVI--PSLLEF-ARLESKADARV----SDLSGGMKRRLTLARALIND 190
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568932737 495 PKILLLDEATSALDTESEAEVQAALDK--AReGRTTIVIAHRLSTI-RNADVIAGFEDGVIVEQGSHSELMKKE 565
Cdd:PRK13536 191 PQLLILDEPTTGLDPHARHLIWERLRSllAR-GKTILLTTHFMEEAeRLCDRLCVLEAGRKIAEGRPHALIDEH 263
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
338-554 |
8.28e-20 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 94.75 E-value: 8.28e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 338 LEFSDVHFSYPSRaniKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIdGQdirnfNVRclreiIG 417
Cdd:COG0488 316 LELEGLSKSYGDK---TLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GE-----TVK-----IG 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 418 VVSQEPVLF--STTIAENIRYGRGNVTmdeiekavkEANAYDFIMKL---PQKFDTLVGDrgaqLSGGQKQRIAIARALV 492
Cdd:COG0488 382 YFDQHQEELdpDKTVLDELRDGAPGGT---------EQEVRGYLGRFlfsGDDAFKPVGV----LSGGEKARLALAKLLL 448
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568932737 493 RNPKILLLDEATSALDTESEAEVQAALDkAREGrTTIVIAH-R--LSTIrnADVIAGFEDGVIVE 554
Cdd:COG0488 449 SPPNVLLLDEPTNHLDIETLEALEEALD-DFPG-TVLLVSHdRyfLDRV--ATRILEFEDGGVRE 509
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
338-533 |
8.74e-20 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 90.53 E-value: 8.74e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 338 LEFSDVHFSYPSRaniKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRclReiiG 417
Cdd:PRK11248 2 LQISHLYADYGGK---PALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAE--R---G 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 418 VVSQ-EPVLFSTTIAENIRYGrgnVTMDEIEKAVKEANAYDFIMKlpqkfdtlVGDRGA------QLSGGQKQRIAIARA 490
Cdd:PRK11248 74 VVFQnEGLLPWRNVQDNVAFG---LQLAGVEKMQRLEIAHQMLKK--------VGLEGAekryiwQLSGGQRQRVGIARA 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 568932737 491 LVRNPKILLLDEATSALDTESEAEVQAALDK--AREGRTTIVIAH 533
Cdd:PRK11248 143 LAANPQLLLLDEPFGALDAFTREQMQTLLLKlwQETGKQVLLITH 187
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
999-1206 |
1.07e-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: 1.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 999 LSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQWlRAQLgI--VSQEPilfdcsiaeNIAY 1076
Cdd:COG4167 32 VSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDYKY-RCKH-IrmIFQDP---------NTSL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1077 GDNSRV-----VP---HDEIVRAAKEANIhpfIETLpqkynTRVG-------DKGTQLSGGQKQRIAIARALIRQPRVLL 1141
Cdd:COG4167 101 NPRLNIgqileEPlrlNTDLTAEEREERI---FATL-----RLVGllpehanFYPHMLSSGQKQRVALARALILQPKIII 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568932737 1142 LDEATSALD--TESEKV-----VQEaldkaREGRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHGTHQQLLAQ 1206
Cdd:COG4167 173 ADEALAALDmsVRSQIInlmleLQE-----KLGISYIYVSQHLGIVKHiSDKVLVMHQGEVVEYGKTAEVFAN 240
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
978-1197 |
1.22e-19 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 93.98 E-value: 1.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 978 VTFNEVVFNYPTRanvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLdGQeakklNVQwlraqLG 1057
Cdd:COG0488 316 LELEGLSKSYGDK---TLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GE-----TVK-----IG 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1058 IVSQEPILFDcsiaeniaygDNSRVVphDEIVRAA---KEANIHPFIETL---PQKYNTRVGDkgtqLSGGQKQRIAIAR 1131
Cdd:COG0488 382 YFDQHQEELD----------PDKTVL--DELRDGApggTEQEVRGYLGRFlfsGDDAFKPVGV----LSGGEKARLALAK 445
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568932737 1132 ALIRQPRVLLLDEATSALDTESEKVVQEALDkAREGrTCIVIAH-R--LSTIqnADLIVVIENGKVKEH 1197
Cdd:COG0488 446 LLLSPPNVLLLDEPTNHLDIETLEALEEALD-DFPG-TVLLVSHdRyfLDRV--ATRILEFEDGGVREY 510
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
338-538 |
1.66e-19 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 93.53 E-value: 1.66e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 338 LEFSDVHFSYPSranIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDiRNFN-VRCLREI- 415
Cdd:PRK10762 5 LQLKGIDKAFPG---VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKE-VTFNgPKSSQEAg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 416 IGVVSQEPVLFST-TIAENIRYGRGNVT-MDEIE--KAVKEANAYDFIMKLPQKFDTLVGDrgaqLSGGQKQRIAIARAL 491
Cdd:PRK10762 81 IGIIHQELNLIPQlTIAENIFLGREFVNrFGRIDwkKMYAEADKLLARLNLRFSSDKLVGE----LSIGEQQMVEIAKVL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 568932737 492 VRNPKILLLDEATSAL-DTESEA------EVQAaldkarEGRTTIVIAHRLSTI 538
Cdd:PRK10762 157 SFESKVIIMDEPTDALtDTETESlfrvirELKS------QGRGIVYISHRLKEI 204
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
993-1194 |
1.70e-19 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 94.41 E-value: 1.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 993 VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQWL----RAQLGIVSQE-PILFD 1067
Cdd:PRK10535 21 VEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALaqlrREHFGFIFQRyHLLSH 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1068 CSIAENIAygdnsrvVP--HDEIVRAAKEANIHPFIETLpqKYNTRVGDKGTQLSGGQKQRIAIARALIRQPRVLLLDEA 1145
Cdd:PRK10535 101 LTAAQNVE-------VPavYAGLERKQRLLRAQELLQRL--GLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEP 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 568932737 1146 TSALDTESEKVVQEALDKARE-GRTCIVIAHRLSTIQNADLIVVIENGKV 1194
Cdd:PRK10535 172 TGALDSHSGEEVMAILHQLRDrGHTVIIVTHDPQVAAQAERVIEIRDGEI 221
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
977-1198 |
2.03e-19 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 91.63 E-value: 2.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 977 SVTFNEVVFNYptrANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQ-----EAKKLNVqw 1051
Cdd:PRK11000 3 SVTLRNVTKAY---GDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKrmndvPPAERGV-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1052 lraqlGIVSQEPILF-DCSIAENIAYG----------DNSRVVPHDEIVRAAKeanihpFIETLPQkyntrvgdkgtQLS 1120
Cdd:PRK11000 78 -----GMVFQSYALYpHLSVAENMSFGlklagakkeeINQRVNQVAEVLQLAH------LLDRKPK-----------ALS 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1121 GGQKQRIAIARALIRQPRVLLLDEATSALDTESEkvVQEALDKA----REGRTCIVIAH-RLSTIQNADLIVVIENGKVK 1195
Cdd:PRK11000 136 GGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALR--VQMRIEISrlhkRLGRTMIYVTHdQVEAMTLADKIVVLDAGRVA 213
|
...
gi 568932737 1196 EHG 1198
Cdd:PRK11000 214 QVG 216
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
991-1206 |
2.18e-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: 2.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 991 ANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNvqwlRAQLGIVSQEPILF-DCS 1069
Cdd:COG4152 12 GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPED----RRRIGYLPEERGLYpKMK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1070 IAENIAY-----GdnsrvVPHDEIVRAAKEanihpFIET--LPQKYNTRVGDkgtqLSGGQKQRIAIARALIRQPRVLLL 1142
Cdd:COG4152 88 VGEQLVYlarlkG-----LSKAEAKRRADE-----WLERlgLGDRANKKVEE----LSKGNQQKVQLIAALLHDPELLIL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568932737 1143 DEATSALDTES-EKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHGTHQQLLAQ 1206
Cdd:COG4152 154 DEPFSGLDPVNvELLKDVIRELAAKGTTVIFSSHQMELVEElCDRIVIINKGRKVLSGSVDEIRRQ 219
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
995-1194 |
2.82e-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: 2.82e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 995 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNV-QWLRAQLGIVSQEP----ILFDCS 1069
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPrDAIRAGIAYVPEDRkregLVLDLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1070 IAENIAygdnsrvvphdeivraakeanihpfietLPQkyntrvgdkgtQLSGGQKQRIAIARALIRQPRVLLLDEATSAL 1149
Cdd:cd03215 95 VAENIA----------------------------LSS-----------LLSGGNQQKVVLARWLARDPRVLILDEPTRGV 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 568932737 1150 DTES-EKVVQEALDKAREGRTCIVIahrlST-----IQNADLIVVIENGKV 1194
Cdd:cd03215 136 DVGAkAEIYRLIRELADAGKAVLLI----SSeldelLGLCDRILVMYEGRI 182
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
994-1200 |
4.45e-19 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 90.28 E-value: 4.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 994 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSV-LLDGQEAKKlnVQWLRAQLGIVSQepilFD----- 1067
Cdd:PRK13536 55 AVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKItVLGVPVPAR--ARLARARIGVVPQ----FDnldle 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1068 CSIAEN-IAYGDNSRVVPHDeivraaKEANIHPFIE--TLPQKYNTRVGDkgtqLSGGQKQRIAIARALIRQPRVLLLDE 1144
Cdd:PRK13536 129 FTVRENlLVFGRYFGMSTRE------IEAVIPSLLEfaRLESKADARVSD----LSGGMKRRLTLARALINDPQLLILDE 198
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1145 ATSALDTESEKVVQEALDK--AReGRTCIVIAHRLSTIQN-ADLIVVIENG-KVKEHGTH 1200
Cdd:PRK13536 199 PTTGLDPHARHLIWERLRSllAR-GKTILLTTHFMEEAERlCDRLCVLEAGrKIAEGRPH 257
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
996-1203 |
4.54e-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: 87.43 E-value: 4.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 996 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKlNVQWLRAQLGIVSQEPILFDCSIA-ENI 1074
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREVRRRIGIVFQDLSVDDELTGwENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1075 A-----YGdnsrvVPHDEivRAAKEANIHPFIEtLPQKYNTRVGdkgtQLSGGQKQRIAIARALIRQPRVLLLDEATSAL 1149
Cdd:cd03265 95 YiharlYG-----VPGAE--RRERIDELLDFVG-LLEAADRLVK----TYSGGMRRRLEIARSLVHRPEVLFLDEPTIGL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 568932737 1150 DTESEKVVQEALDK--AREGRTCIVIAHRLSTI-QNADLIVVIENGKVKEHGTHQQL 1203
Cdd:cd03265 163 DPQTRAHVWEYIEKlkEEFGMTILLTTHYMEEAeQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
353-508 |
4.54e-19 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 87.53 E-value: 4.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 353 IKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVR---CLR-EIIGVVSQEPVLFST 428
Cdd:PRK10584 23 LSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEaraKLRaKHVGFVFQSFMLIPT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 429 TIA-ENIRYG---RGNVTMDEIEKAVKEANAydfiMKLPQKFDTLvgdrGAQLSGGQKQRIAIARALVRNPKILLLDEAT 504
Cdd:PRK10584 103 LNAlENVELPallRGESSRQSRNGAKALLEQ----LGLGKRLDHL----PAQLSGGEQQRVALARAFNGRPDVLFADEPT 174
|
....
gi 568932737 505 SALD 508
Cdd:PRK10584 175 GNLD 178
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
993-1206 |
4.92e-19 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 91.90 E-value: 4.92e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 993 VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQ-WLRAQLGIVSQEPILF-DCSI 1070
Cdd:PRK11288 17 VKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTaALAAGVAIIYQELHLVpEMTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1071 AENIAYGD--NSR-VVPHDEIVRAAKEANIHPFIETLPqkyNTRVGDkgtqLSGGQKQRIAIARALIRQPRVLLLDEATS 1147
Cdd:PRK11288 97 AENLYLGQlpHKGgIVNRRLLNYEAREQLEHLGVDIDP---DTPLKY----LSIGQRQMVEIAKALARNARVIAFDEPTS 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1148 ALDT-ESE---KVVQEALDkarEGRTCIVIAHRLSTI-QNADLIVVIENG-KVKEHG-----THQQLLAQ 1206
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 ... |
350-562 |
5.29e-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: 5.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 350 RANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKIS-------IDGQDIRNFNVRCLREIIGVVSQE 422
Cdd:TIGR03269 294 RGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNvrvgdewVDMTKPGPDGRGRAKRYIGILHQE 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 423 PVLFS-TTIAENIRYGRGNVTMDEI--EKAV--------KEANAYDFIMKLPQkfdtlvgdrgaQLSGGQKQRIAIARAL 491
Cdd:TIGR03269 374 YDLYPhRTVLDNLTEAIGLELPDELarMKAVitlkmvgfDEEKAEEILDKYPD-----------ELSEGERHRVALAQVL 442
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568932737 492 VRNPKILLLDEATSALDTESEAEVQAALDKARE--GRTTIVIAHRLSTIRN-ADVIAGFEDGVIVEQGSHSELM 562
Cdd:TIGR03269 443 IKEPRIVILDEPTGTMDPITKVDVTHSILKAREemEQTFIIVSHDMDFVLDvCDRAALMRDGKIVKIGDPEEIV 516
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
338-554 |
9.21e-19 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 91.13 E-value: 9.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 338 LEFSDVHFSYPSranIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVR-CLREII 416
Cdd:PRK11288 5 LSFDGIGKTFPG---VKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTaALAAGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 417 GVVSQE----PVLfstTIAENIRYGRGNVTMDEIEKAVKEANAYDFIMKLPQKFD--TLVGDrgaqLSGGQKQRIAIARA 490
Cdd:PRK11288 82 AIIYQElhlvPEM---TVAENLYLGQLPHKGGIVNRRLLNYEAREQLEHLGVDIDpdTPLKY----LSIGQRQMVEIAKA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568932737 491 LVRNPKILLLDEATSALdTESEAEVQAALDKA--REGRTTIVIAHRLSTI-RNADVIAGFEDGVIVE 554
Cdd:PRK11288 155 LARNARVIAFDEPTSSL-SAREIEQLFRVIRElrAEGRVILYVSHRMEEIfALCDAITVFKDGRYVA 220
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
996-1200 |
1.03e-18 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 86.47 E-value: 1.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 996 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLN---VQWLRAQLGIVSQEP-ILFDCSIA 1071
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKnreVPFLRRQIGMIFQDHhLLMDRTVY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1072 ENIAygdnsrvVPHdeIVRAAKEANIHPFIETLPQKyntrVG--DKG----TQLSGGQKQRIAIARALIRQPRVLLLDEA 1145
Cdd:PRK10908 98 DNVA-------IPL--IIAGASGDDIRRRVSAALDK----VGllDKAknfpIQLSGGEQQRVGIARAVVNKPAVLLADEP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 568932737 1146 TSALDTE-SEKVVQEALDKAREGRTCIVIAHRLSTIQNADL-IVVIENGKVkeHGTH 1200
Cdd:PRK10908 165 TGNLDDAlSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYrMLTLSDGHL--HGGV 219
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
338-565 |
1.05e-18 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 88.32 E-value: 1.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 338 LEFSDVHFSYPSRAnikILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNfNVRCLREIIG 417
Cdd:PRK13537 8 IDFRNVEKRYGDKL---VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPS-RARHARQRVG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 418 VVSQ----EPvlfSTTIAENIR-YGRG-NVTMDEIEKAVkeANAYDFiMKLPQKFDTLVGDrgaqLSGGQKQRIAIARAL 491
Cdd:PRK13537 84 VVPQfdnlDP---DFTVRENLLvFGRYfGLSAAAARALV--PPLLEF-AKLENKADAKVGE----LSGGMKRRLTLARAL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568932737 492 VRNPKILLLDEATSALDTESEAEVQAALDK--AReGRTTIVIAHRLSTI-RNADVIAGFEDGVIVEQGSHSELMKKE 565
Cdd:PRK13537 154 VNDPDVLVLDEPTTGLDPQARHLMWERLRSllAR-GKTILLTTHFMEEAeRLCDRLCVIEEGRKIAEGAPHALIESE 229
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
336-592 |
1.13e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 87.76 E-value: 1.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 336 GNLEFSDVHFSYPSRA--NIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEG-------KISIDGQDIRN 406
Cdd:PRK13645 5 KDIILDNVSYTYAKKTpfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGqtivgdyAIPANLKKIKE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 407 fnVRCLREIIGVVSQEP--VLFSTTIAENIRYGRGNVTMDEiEKAVKEANAYDFIMKLPQKFdtlVGDRGAQLSGGQKQR 484
Cdd:PRK13645 85 --VKRLRKEIGLVFQFPeyQLFQETIEKDIAFGPVNLGENK-QEAYKKVPELLKLVQLPEDY---VKRSPFELSGGQKRR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 485 IAIARALVRNPKILLLDEATSALDTESEAEVQAALDK--AREGRTTIVIAHRLSTI-RNADVIAGFEDGVIVEQG----- 556
Cdd:PRK13645 159 VALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERlnKEYKKRIIMVTHNMDQVlRIADEVIVMHEGKVISIGspfei 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 568932737 557 -SHSELMKKEGI-----YFRLVNMQTAGSQILS------EEFEVELSD 592
Cdd:PRK13645 239 fSNQELLTKIEIdppklYQLMYKLKNKGIDLLNknirtiEEFAKELAK 286
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
338-556 |
1.21e-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: 85.80 E-value: 1.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 338 LEFSDVHFSYpsrANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNvrclREIIG 417
Cdd:cd03269 1 LEVENVTKRF---GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA----RNRIG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 418 VVSQEPVLF-STTIAENIRY-GRgnvtmdeiEKAVKEANAYDFIMKLPQKFDtlVGD----RGAQLSGGQKQRIAIARAL 491
Cdd:cd03269 74 YLPEERGLYpKMKVIDQLVYlAQ--------LKGLKKEEARRRIDEWLERLE--LSEyankRVEELSKGNQQKVQFIAAV 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568932737 492 VRNPKILLLDEATSALDTESeAEV--QAALDKAREGRTTIVIAHRLSTI-RNADVIAGFEDGVIVEQG 556
Cdd:cd03269 144 IHDPELLILDEPFSGLDPVN-VELlkDVIRELARAGKTVILSTHQMELVeELCDRVLLLNKGRAVLYG 210
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
338-599 |
1.44e-18 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 87.86 E-value: 1.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 338 LEFSDVHFSYpsrANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRnfnvRCLREIIG 417
Cdd:COG4152 2 LELKGLTKRF---GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLD----PEDRRRIG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 418 VVSQEPVLF-STTIAENIRY-GR--GnVTMDEIEKAVKEanaydfimkLPQKFDtlVGDRGA----QLSGGQKQRIAIAR 489
Cdd:COG4152 75 YLPEERGLYpKMKVGEQLVYlARlkG-LSKAEAKRRADE---------WLERLG--LGDRANkkveELSKGNQQKVQLIA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 490 ALVRNPKILLLDEATSALDTESeAEV--QAALDKAREGRTTIVIAHRLSTI-RNADVIAGFEDGVIVEQGSHSELMKKEG 566
Cdd:COG4152 143 ALLHDPELLILDEPFSGLDPVN-VELlkDVIRELAAKGTTVIFSSHQMELVeELCDRIVIINKGRKVLSGSVDEIRRQFG 221
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 568932737 567 IYFRLVNMQTAGSQILS-----------EEFEVELSDEKAAGDV 599
Cdd:COG4152 222 RNTLRLEADGDAGWLRAlpgvtvveedgDGAELKLEDGADAQEL 265
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
993-1196 |
1.52e-18 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 90.62 E-value: 1.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 993 VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYdP---MAGSVLLDGQEAKKLNvqwLRA--QLGIV--SQE--- 1062
Cdd:NF040905 14 VKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PhgsYEGEILFDGEVCRFKD---IRDseALGIViiHQElal 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1063 -PILfdcSIAENIAYGdNSR----VVPHDEIVRAAKE------ANIHPfietlpqkyNTRVGDKGTqlsgGQKQRIAIAR 1131
Cdd:NF040905 90 iPYL---SIAENIFLG-NERakrgVIDWNETNRRAREllakvgLDESP---------DTLVTDIGV----GKQQLVEIAK 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568932737 1132 ALIRQPRVLLLDEATSAL-DTESEKVVQEALDKAREGRTCIVIAHRLSTI-QNADLIVVIENGKVKE 1196
Cdd:NF040905 153 ALSKDVKLLILDEPTAALnEEDSAALLDLLLELKAQGITSIIISHKLNEIrRVADSITVLRDGRTIE 219
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
341-561 |
1.73e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 87.07 E-value: 1.73e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 341 SDVHFSYPSRANIKILKGLNLKVKSGQT---------VALVGNSGCGKSTTVQLLQRLYDPTEG-----KISIDGQDIRN 406
Cdd:PRK14271 13 ADVDAAAPAMAAVNLTLGFAGKTVLDQVsmgfparavTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 407 F-NVRCLREIIGVVSQEPVLFSTTIAENIRYG-RGNVTMDEIE-KAVKEANAYDfiMKLPQKFDTLVGDRGAQLSGGQKQ 483
Cdd:PRK14271 93 YrDVLEFRRRVGMLFQRPNPFPMSIMDNVLAGvRAHKLVPRKEfRGVAQARLTE--VGLWDAVKDRLSDSPFRLSGGQQQ 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568932737 484 RIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLS-TIRNADVIAGFEDGVIVEQGSHSEL 561
Cdd:PRK14271 171 LLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAqAARISDRAALFFDGRLVEEGPTEQL 249
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
47-286 |
2.03e-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: 87.08 E-value: 2.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 47 LNPGRILEEEMTRYAYYYSGLGGGVLVAAYIQvSFWTLAAGRQI-KKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDDV 125
Cdd:cd18541 29 LTAGTLTASQLLRYALLILLLALLIGIFRFLW-RYLIFGASRRIeYDLRNDLFAHLLTLSPSFYQKNRTGDLMARATNDL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 126 SKISEGIGDKVGMFFQAIATFFAGFIVGFIRGWKLTLVIMAISPILGLSTAVWAKI-----------LSTFSDKelaaya 194
Cdd:cd18541 108 NAVRMALGPGILYLVDALFLGVLVLVMMFTISPKLTLIALLPLPLLALLVYRLGKKihkrfrkvqeaFSDLSDR------ 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 195 kagavAEEALGAIRTVIAFGGQNKELERYQKHLENAKKIGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTI 274
Cdd:cd18541 182 -----VQESFSGIRVIKAFVQEEAEIERFDKLNEEYVEKNLRLARVDALFFPLIGLLIGLSFLIVLWYGGRLVIRGTITL 256
|
250
....*....|....
gi 568932737 275 GN--AMTVFFSILI 286
Cdd:cd18541 257 GDlvAFNSYLGMLI 270
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
338-567 |
3.01e-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: 3.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 338 LEFSDVHFSYpsrANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNF-NVRCLREII 416
Cdd:PRK11614 6 LSFDKVSAHY---GKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWqTAKIMREAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 417 GVVSQEPVLFS-TTIAENIRYGRGNVTMDEIEKAVKEAnaYDFIMKLPQKfdtlVGDRGAQLSGGQKQRIAIARALVRNP 495
Cdd:PRK11614 83 AIVPEGRRVFSrMTVEENLAMGGFFAERDQFQERIKWV--YELFPRLHER----RIQRAGTMSGGEQQMLAIGRALMSQP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568932737 496 KILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLS--TIRNADVIAGFEDGVIVEQGSHSELMKKEGI 567
Cdd:PRK11614 157 RLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNAnqALKLADRGYVLENGHVVLEDTGDALLANEAV 230
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
998-1203 |
3.04e-18 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 87.45 E-value: 3.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 998 GLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLN-VQWL--RAQLGIVSQEPILF---DCSIA 1071
Cdd:PRK15079 39 GVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKdDEWRavRSDIQMIFQDPLASlnpRMTIG 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1072 ENIA------YGDNSRVVPHDEIVRAAKEANIHP-FIETLPQKYntrvgdkgtqlSGGQKQRIAIARALIRQPRVLLLDE 1144
Cdd:PRK15079 119 EIIAeplrtyHPKLSRQEVKDRVKAMMLKVGLLPnLINRYPHEF-----------SGGQCQRIGIARALILEPKLIICDE 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568932737 1145 ATSALDTESE-KVVQEALDKARE-GRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHGTHQQL 1203
Cdd:PRK15079 188 PVSALDVSIQaQVVNLLQQLQREmGLSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEV 249
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
995-1196 |
3.80e-18 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 84.83 E-value: 3.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 995 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQW---LRAQ-LGIVSQEPILFDCSI 1070
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEArakLRAKhVGFVFQSFMLIPTLN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1071 A-ENIAY-----GDNSRvVPHDEIVRAAKEANIHPFIETLPqkyntrvgdkgTQLSGGQKQRIAIARALIRQPRVLLLDE 1144
Cdd:PRK10584 105 AlENVELpallrGESSR-QSRNGAKALLEQLGLGKRLDHLP-----------AQLSGGEQQRVALARAFNGRPDVLFADE 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 568932737 1145 ATSALDTES-EKVVQEALDKARE-GRTCIVIAHRLSTIQNADLIVVIENGKVKE 1196
Cdd:PRK10584 173 PTGNLDRQTgDKIADLLFSLNREhGTTLILVTHDLQLAARCDRRLRLVNGQLQE 226
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
994-1144 |
3.88e-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: 3.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 994 PVLQGLSLEVKKGQTLALVGSSGCGKSTVvqllerFY------DPMAGSVLLDGQEAKKLNVqWLRAQLGI--VSQEPIL 1065
Cdd:COG1137 17 TVVKDVSLEVNQGEIVGLLGPNGAGKTTT------FYmivglvKPDSGRIFLDGEDITHLPM-HKRARLGIgyLPQEASI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1066 F-DCSIAENIaygdnsRVVPhdEIVRAAKEAnIHPFIETLPQKYN-TRVGD-KGTQLSGGQKQRIAIARALIRQPRVLLL 1142
Cdd:COG1137 90 FrKLTVEDNI------LAVL--ELRKLSKKE-REERLEELLEEFGiTHLRKsKAYSLSGGERRRVEIARALATNPKFILL 160
|
..
gi 568932737 1143 DE 1144
Cdd:COG1137 161 DE 162
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
356-588 |
4.56e-18 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 89.07 E-value: 4.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 356 LKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLREI-IGVVSQE-PVLFSTTIAEN 433
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLgIGIIYQElSVIDELTVLEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 434 IRYGR------GNVTMDEIEKAVKEANAYDFIMKLPQKFDTLVGDrgaqLSGGQKQRIAIARALVRNPKILLLDEATSAL 507
Cdd:PRK09700 101 LYIGRhltkkvCGVNIIDWREMRVRAAMMLLRVGLKVDLDEKVAN----LSISHKQMLEIAKTLMLDAKVIIMDEPTSSL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 508 dTESEAE-VQAALDKAR-EGRTTIVIAHRLSTIRN-ADVIAGFEDGVIVEQGSHSE--------LMKKEGIYFRLVNMQT 576
Cdd:PRK09700 177 -TNKEVDyLFLIMNQLRkEGTAIVYISHKLAEIRRiCDRYTVMKDGSSVCSGMVSDvsnddivrLMVGRELQNRFNAMKE 255
|
250
....*....|...
gi 568932737 577 AGSQILSEE-FEV 588
Cdd:PRK09700 256 NVSNLAHETvFEV 268
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
366-556 |
7.84e-18 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 88.76 E-value: 7.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 366 GQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFN---VRCLREIIGVVSQEPV-------LFSTTIAENIR 435
Cdd:PRK10261 350 GETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSpgkLQALRRDIQFIFQDPYasldprqTVGDSIMEPLR 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 436 YgRGNVTMDEIEKAV---------KEANAYDFimklPQKFdtlvgdrgaqlSGGQKQRIAIARALVRNPKILLLDEATSA 506
Cdd:PRK10261 430 V-HGLLPGKAAAARVawllervglLPEHAWRY----PHEF-----------SGGQRQRICIARALALNPKVIIADEAVSA 493
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 568932737 507 LDTESEAE-VQAALDKARE-GRTTIVIAHRLSTI-RNADVIAGFEDGVIVEQG 556
Cdd:PRK10261 494 LDVSIRGQiINLLLDLQRDfGIAYLFISHDMAVVeRISHRVAVMYLGQIVEIG 546
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
996-1203 |
8.67e-18 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 84.68 E-value: 8.67e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 996 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFY--DPMAGS-VLLDG---QEAKKL--NVQWLRAQLGIVSQEPILFD 1067
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgDKSAGShIELLGrtvQREGRLarDIRKSRANTGYIFQQFNLVN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1068 -CSIAENIAYGDNSRVVPHDEIVRAAKEANIHPFIETLpqkynTRVG------DKGTQLSGGQKQRIAIARALIRQPRVL 1140
Cdd:PRK09984 100 rLSVLENVLIGALGSTPFWRTCFSWFTREQKQRALQAL-----TRVGmvhfahQRVSTLSGGQQQRVAIARALMQQAKVI 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568932737 1141 LLDEATSALDTESEKVVQEALD--KAREGRTCIVIAHRLS-TIQNADLIVVIENGKVKEHGTHQQL 1203
Cdd:PRK09984 175 LADEPIASLDPESARIVMDTLRdiNQNDGITVVVTLHQVDyALRYCERIVALRQGHVFYDGSSQQF 240
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
350-532 |
9.12e-18 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 83.00 E-value: 9.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 350 RANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLREIIGvvSQEPVLFSTT 429
Cdd:PRK13539 12 RGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHYLG--HRNAMKPALT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 430 IAENIR-----YGRGNVTMDEIEKAVKEANAYDfimkLPQKFdtlvgdrgaqLSGGQKQRIAIARALVRNPKILLLDEAT 504
Cdd:PRK13539 90 VAENLEfwaafLGGEELDIAAALEAVGLAPLAH----LPFGY----------LSAGQKRRVALARLLVSNRPIWILDEPT 155
|
170 180
....*....|....*....|....*...
gi 568932737 505 SALDTESEAEVqAALDKAREGRTTIVIA 532
Cdd:PRK13539 156 AALDAAAVALF-AELIRAHLAQGGIVIA 182
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
355-561 |
9.58e-18 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 88.22 E-value: 9.58e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 355 ILKGLNLKVKSGQTVALVGNSGCGKS-TTVQLLQRLYDP----TEGKISIDGQDIRNFNVRCLREI----IGVVSQEPVL 425
Cdd:PRK15134 24 VVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFHGESLLHASEQTLRGVrgnkIAMIFQEPMV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 426 -------FSTTIAENIRYGRGnvtMDeiekavKEANAYDFIMKLPQkfdtlVGDRGA---------QLSGGQKQRIAIAR 489
Cdd:PRK15134 104 slnplhtLEKQLYEVLSLHRG---MR------REAARGEILNCLDR-----VGIRQAakrltdyphQLSGGERQRVMIAM 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568932737 490 ALVRNPKILLLDEATSALDTESEAEVQAALDKARE--GRTTIVIAHRLSTIRN-ADVIAGFEDGVIVEQGSHSEL 561
Cdd:PRK15134 170 ALLTRPELLIADEPTTALDVSVQAQILQLLRELQQelNMGLLFITHNLSIVRKlADRVAVMQNGRCVEQNRAATL 244
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
359-562 |
1.00e-17 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 86.08 E-value: 1.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 359 LNLKVK-----SGQTvALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQ---DIRN-FNVRCLREIIGVVSQEPVLFS-T 428
Cdd:PRK11144 13 LCLTVNltlpaQGIT-AIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRvlfDAEKgICLPPEKRRIGYVFQDARLFPhY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 429 TIAENIRYGrgnvtMDEiekavkeanaydfimKLPQKFDTLVG--------DR-GAQLSGGQKQRIAIARALVRNPKILL 499
Cdd:PRK11144 92 KVRGNLRYG-----MAK---------------SMVAQFDKIVAllgiepllDRyPGSLSGGEKQRVAIGRALLTAPELLL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568932737 500 LDEATSALDTESEAEVQAALDK-AREGRTTIV-IAHRLSTI-RNADVIAGFEDGVIVEQGS-----HSELM 562
Cdd:PRK11144 152 MDEPLASLDLPRKRELLPYLERlAREINIPILyVSHSLDEIlRLADRVVVLEQGKVKAFGPleevwASSAM 222
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
995-1198 |
1.01e-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: 82.96 E-value: 1.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 995 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERF--YDPMAGSVLLDGQEAKKLNVQwLRAQLGI--VSQEPIlfdcsi 1070
Cdd:cd03217 15 ILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPE-ERARLGIflAFQYPP------ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1071 aeniaygdnsrvvphdEI--VRAAKeanihpFIetlpqkyntRVGDKGtqLSGGQKQRIAIARALIRQPRVLLLDEATSA 1148
Cdd:cd03217 88 ----------------EIpgVKNAD------FL---------RYVNEG--FSGGEKKRNEILQLLLLEPDLAILDEPDSG 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 568932737 1149 LDTESEKVVQEALDKAR-EGRTCIVIAH--RLSTIQNADLIVVIENGKVKEHG 1198
Cdd:cd03217 135 LDIDALRLVAEVINKLReEGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVKSG 187
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
993-1198 |
1.03e-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: 1.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 993 VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQeakklnVQW-LRAQLGIVSQ----EPILFD 1067
Cdd:cd03220 35 FWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGR------VSSlLGLGGGFNPEltgrENIYLN 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1068 CSIaeniaYGdnsrvVPHDEIvrAAKEANIHPFIEtLPQKYNTRVGdkgtQLSGGQKQRIAIARALIRQPRVLLLDEATS 1147
Cdd:cd03220 109 GRL-----LG-----LSRKEI--DEKIDEIIEFSE-LGDFIDLPVK----TYSSGMKARLAFAIATALEPDILLIDEVLA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 568932737 1148 ALDTE-SEKVVQEALDKAREGRTCIVIAHRLSTI-QNADLIVVIENGKVKEHG 1198
Cdd:cd03220 172 VGDAAfQEKCQRRLRELLKQGKTVILVSHDPSSIkRLCDRALVLEKGKIRFDG 224
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
344-556 |
1.08e-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: 1.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 344 HFSYPSRANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQdirnfnVRCLREI-IGVvsqE 422
Cdd:cd03220 26 LGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGR------VSSLLGLgGGF---N 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 423 PVLfstTIAENIRYgRG---NVTMDEIEKavKEANAYDFiMKLPQKFDTLVGdrgaQLSGGQKQRIAIARALVRNPKILL 499
Cdd:cd03220 97 PEL---TGRENIYL-NGrllGLSRKEIDE--KIDEIIEF-SELGDFIDLPVK----TYSSGMKARLAFAIATALEPDILL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 568932737 500 LDEATSALDTESEAEVQAALDKAREGRTTIVIA-HRLSTIRN-ADVIAGFEDGVIVEQG 556
Cdd:cd03220 166 IDEVLAVGDAAFQEKCQRRLRELLKQGKTVILVsHDPSSIKRlCDRALVLEKGKIRFDG 224
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
998-1203 |
1.21e-17 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 83.89 E-value: 1.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 998 GLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQWLrAQLGIVS--QEPILF-DCSIAENI 1074
Cdd:PRK11300 23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQI-ARMGVVRtfQHVRLFrEMTVIENL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1075 AygdnsrVVPHDEI--------------VRAAKEA--NIHPFIET--LPQKYNTRVGDkgtqLSGGQKQRIAIARALIRQ 1136
Cdd:PRK11300 102 L------VAQHQQLktglfsgllktpafRRAESEAldRAATWLERvgLLEHANRQAGN----LAYGQQRRLEIARCMVTQ 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1137 PRVLLLDEATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHGTHQQL 1203
Cdd:PRK11300 172 PEILMLDEPAAGLNPKETKELDELIAELRNehNVTVLLIEHDMKLVMGiSDRIYVVNQGTPLANGTPEEI 241
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
359-580 |
1.21e-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: 1.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 359 LNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNfNVRCLREIIGVVSQEPVLFS-TTIAENIRYg 437
Cdd:TIGR01257 949 LNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET-NLDAVRQSLGMCPQHNILFHhLTVAEHILF- 1026
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 438 RGNVTMDEIEKAVKEANAYDFIMKLPQKFDtlvgDRGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQA 517
Cdd:TIGR01257 1027 YAQLKGRSWEEAQLEMEAMLEDTGLHHKRN----EEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWD 1102
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568932737 518 ALDKAREGRTTIVIAHRLStirNADVIAgfEDGVIVEQG----SHSELMKKE----GIYFRLV-NMQTAGSQ 580
Cdd:TIGR01257 1103 LLLKYRSGRTIIMSTHHMD---EADLLG--DRIAIISQGrlycSGTPLFLKNcfgtGFYLTLVrKMKNIQSQ 1169
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
980-1207 |
1.77e-17 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 87.43 E-value: 1.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 980 FNEVVFNYPTRanvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQeakklnvqwlrAQLGIV 1059
Cdd:COG0488 1 LENLSKSFGGR---PLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKG-----------LRIGYL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1060 SQEPILFD-CSIAENIAYGDNSRVVPHDEIVRA-----------AKEANIHPFIETL-------------------PQKY 1108
Cdd:COG0488 67 PQEPPLDDdLTVLDTVLDGDAELRALEAELEELeaklaepdedlERLAELQEEFEALggweaearaeeilsglgfpEEDL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1109 NTRVGDkgtqLSGGQKQRIAIARALIRQPRVLLLDEATSALDTESekvVQ--EALDKAREGrTCIVIAH-R--LSTIqnA 1183
Cdd:COG0488 147 DRPVSE----LSGGWRRRVALARALLSEPDLLLLDEPTNHLDLES---IEwlEEFLKNYPG-TVLVVSHdRyfLDRV--A 216
|
250 260
....*....|....*....|....*
gi 568932737 1184 DLIVVIENGKVKEH-GTHQQLLAQK 1207
Cdd:COG0488 217 TRILELDRGKLTLYpGNYSAYLEQR 241
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
355-536 |
1.81e-17 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 82.94 E-value: 1.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 355 ILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLREI----IGVVSQ-EPVLFSTT 429
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELrnqkLGFIYQfHHLLPDFT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 430 IAENirygrgnVTMDEI--EKAVKEANAYDFIMKLPQKFDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEATSAL 507
Cdd:PRK11629 104 ALEN-------VAMPLLigKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNL 176
|
170 180 190
....*....|....*....|....*....|.
gi 568932737 508 DTESEAEVQAALDK--AREGRTTIVIAHRLS 536
Cdd:PRK11629 177 DARNADSIFQLLGElnRLQGTAFLVVTHDLQ 207
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
354-556 |
2.03e-17 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 83.02 E-value: 2.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 354 KILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIR--NFNVRCLREIiGVVSQEPVLFST-TI 430
Cdd:PRK10895 17 RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISllPLHARARRGI-GYLPQEASIFRRlSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 431 AENIrygrgnVTMDEIEKAVKEANAYDFIMKLPQKFDT--LVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEATSALD 508
Cdd:PRK10895 96 YDNL------MAVLQIRDDLSAEQREDRANELMEEFHIehLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVD 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 568932737 509 TESEAEVQAALDKARE-GRTTIVIAHRLStirnaDVIAGFEDGVIVEQG 556
Cdd:PRK10895 170 PISVIDIKRIIEHLRDsGLGVLITDHNVR-----ETLAVCERAYIVSQG 213
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
974-1206 |
3.20e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 83.52 E-value: 3.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 974 FEGSVTFNEVVFNYPTRA--NVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLdGQEA-----KK 1046
Cdd:PRK13645 3 FSKDIILDNVSYTYAKKTpfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIV-GDYAipanlKK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1047 LN-VQWLRAQLGIVSQEP--ILFDCSIAENIAYGDNSRVVPHDEIVRAAKEAnihPFIETLPQKYNTRvgdKGTQLSGGQ 1123
Cdd:PRK13645 82 IKeVKRLRKEIGLVFQFPeyQLFQETIEKDIAFGPVNLGENKQEAYKKVPEL---LKLVQLPEDYVKR---SPFELSGGQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1124 KQRIAIARALIRQPRVLLLDEATSALDTESEK---VVQEALDKaREGRTCIVIAHRLSTI-QNADLIVVIENGKVKEHG- 1198
Cdd:PRK13645 156 KRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEdfiNLFERLNK-EYKKRIIMVTHNMDQVlRIADEVIVMHEGKVISIGs 234
|
250
....*....|...
gi 568932737 1199 -----THQQLLAQ 1206
Cdd:PRK13645 235 pfeifSNQELLTK 247
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
330-553 |
3.24e-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: 82.38 E-value: 3.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 330 KPDNIKGNLEfsdvHFSYPSRANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNV 409
Cdd:cd03267 15 KEPGLIGSLK----SLFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 410 RCLREIIGVVSQE-------PVLFSTTIAENIrYgrgNVTMDEIEKAVKEANAydfIMKLPQKFDTLVgdrgAQLSGGQK 482
Cdd:cd03267 91 KFLRRIGVVFGQKtqlwwdlPVIDSFYLLAAI-Y---DLPPARFKKRLDELSE---LLDLEELLDTPV----RQLSLGQR 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568932737 483 QRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKA-REGRTTIVIahrlsTIRNADVIAGFEDGVIV 553
Cdd:cd03267 160 MRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYnRERGTTVLL-----TSHYMKDIEALARRVLV 226
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
338-533 |
4.63e-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: 4.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 338 LEFSDVHFSYPSRaniKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIdGQDIRnfnvrclreiIG 417
Cdd:cd03221 1 IELENLSKTYGGK---LLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTW-GSTVK----------IG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 418 VVsqepvlfsttiaenirygrgnvtmdeiekavkeanaydfimklpqkfdtlvgdrgAQLSGGQKQRIAIARALVRNPKI 497
Cdd:cd03221 67 YF-------------------------------------------------------EQLSGGEKMRLALAKLLLENPNL 91
|
170 180 190
....*....|....*....|....*....|....*.
gi 568932737 498 LLLDEATSALDTESEAEVQAALdKAREGrTTIVIAH 533
Cdd:cd03221 92 LLLDEPTNHLDLESIEALEEAL-KEYPG-TVILVSH 125
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
989-1174 |
4.90e-17 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 81.07 E-value: 4.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 989 TRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQWLRAQLGIVSQ-EPILfd 1067
Cdd:PRK13539 11 VRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHYLGHRNAmKPAL-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1068 cSIAENIA-----YGDnsrvvpHDEIVRAAKEA-NIHPfIETLPQKYntrvgdkgtqLSGGQKQRIAIARALIRQPRVLL 1141
Cdd:PRK13539 89 -TVAENLEfwaafLGG------EELDIAAALEAvGLAP-LAHLPFGY----------LSAGQKRRVALARLLVSNRPIWI 150
|
170 180 190
....*....|....*....|....*....|...
gi 568932737 1142 LDEATSALDTESEKVVQEALdKAREGRTCIVIA 1174
Cdd:PRK13539 151 LDEPTAALDAAAVALFAELI-RAHLAQGGIVIA 182
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
353-554 |
5.33e-17 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 85.61 E-value: 5.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 353 IKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYdPT---EGKISIDGQdIRNFnvRCLR--EIIGVV--SQE--- 422
Cdd:NF040905 14 VKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PHgsyEGEILFDGE-VCRF--KDIRdsEALGIViiHQElal 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 423 -PVLfstTIAENIRYG-----RGNVTMDEIEKAVKEanaydfIMK---LPQKFDTLVGDRGAqlsgGQKQRIAIARALVR 493
Cdd:NF040905 90 iPYL---SIAENIFLGnerakRGVIDWNETNRRARE------LLAkvgLDESPDTLVTDIGV----GKQQLVEIAKALSK 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568932737 494 NPKILLLDEATSAL-DTESEAEVQAALDKAREGRTTIVIAHRLSTIRN-ADVIAGFEDGVIVE 554
Cdd:NF040905 157 DVKLLILDEPTAALnEEDSAALLDLLLELKAQGITSIIISHKLNEIRRvADSITVLRDGRTIE 219
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
995-1161 |
5.89e-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: 5.89e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 995 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQWLRAQLGIVSQEPILFDCSIAENI 1074
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSVLENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1075 AY--GDNSRvvphDEIVRAAKEANIHPFiETLPqkyntrvgdkGTQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTE 1152
Cdd:cd03231 95 RFwhADHSD----EQVEEALARVGLNGF-EDRP----------VAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKA 159
|
....*....
gi 568932737 1153 SEKVVQEAL 1161
Cdd:cd03231 160 GVARFAEAM 168
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
985-1205 |
7.01e-17 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 82.14 E-value: 7.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 985 FNYPT----RANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQWLRAQLGIVS 1060
Cdd:PRK15112 14 FRYRTgwfrRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIRMIF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1061 QEPilfdcSIAENiaygDNSRV-----VP---HDEIVRAAKEANIhpfIETLPQkyntrVG---DKGT----QLSGGQKQ 1125
Cdd:PRK15112 94 QDP-----STSLN----PRQRIsqildFPlrlNTDLEPEQREKQI---IETLRQ-----VGllpDHASyyphMLAPGQKQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1126 RIAIARALIRQPRVLLLDEATSALD-TESEKVVQEALD-KAREGRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHGTHQQ 1202
Cdd:PRK15112 157 RLGLARALILRPKVIIADEALASLDmSMRSQLINLMLElQEKQGISYIYVTQHLGMMKHiSDQVLVMHQGEVVERGSTAD 236
|
...
gi 568932737 1203 LLA 1205
Cdd:PRK15112 237 VLA 239
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
356-550 |
8.42e-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: 79.78 E-value: 8.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 356 LKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLREI-IGVVSQEP----VLFSTTI 430
Cdd:cd03215 16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAgIAYVPEDRkregLVLDLSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 431 AENIrygrgnvtmdeiekavkeanaydfimklpqkfdTLvgdrGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTE 510
Cdd:cd03215 96 AENI---------------------------------AL----SSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVG 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 568932737 511 SEAEVQAALDK-AREGRTTIVIahrlST-----IRNADVIAGFEDG 550
Cdd:cd03215 139 AKAEIYRLIRElADAGKAVLLI----SSeldelLGLCDRILVMYEG 180
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
343-538 |
9.26e-17 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 80.69 E-value: 9.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 343 VHFSYPSRANI---KILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDI---RNFNVRCLREII 416
Cdd:PRK10908 2 IRFEHVSKAYLggrQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDItrlKNREVPFLRRQI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 417 GVVSQEP-VLFSTTIAENIRYGR--GNVTMDEIEKAVKEANAYDFIMKLPQKFDTlvgdrgaQLSGGQKQRIAIARALVR 493
Cdd:PRK10908 82 GMIFQDHhLLMDRTVYDNVAIPLiiAGASGDDIRRRVSAALDKVGLLDKAKNFPI-------QLSGGEQQRVGIARAVVN 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 568932737 494 NPKILLLDEATSALDTE-SEAEVQAALDKAREGRTTIVIAHRLSTI 538
Cdd:PRK10908 155 KPAVLLADEPTGNLDDAlSEGILRLFEEFNRVGVTVLMATHDIGLI 200
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
355-563 |
1.06e-16 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 85.10 E-value: 1.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 355 ILKGLNLKVKSGQTVALVGNSGCGKSTtvqLLQRL--YDPT----EGKISIDGQDIrnfNVRCLREIIGVVSQEPVLFST 428
Cdd:TIGR00955 40 LLKNVSGVAKPGELLAVMGSSGAGKTT---LMNALafRSPKgvkgSGSVLLNGMPI---DAKEMRAISAYVQQDDLFIPT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 429 -TIAENI------RYGRgNVTMDEIEKAVKEanaydFI--MKLPQKFDTLVGDRGAQ--LSGGQKQRIAIARALVRNPKI 497
Cdd:TIGR00955 114 lTVREHLmfqahlRMPR-RVTKKEKRERVDE-----VLqaLGLRKCANTRIGVPGRVkgLSGGERKRLAFASELLTDPPL 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568932737 498 LLLDEATSALDTESEAEVQAALDK-AREGRTTIVIAHRLST--IRNADVIAGFEDGVIVEQGSHSELMK 563
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 ... |
687-912 |
1.35e-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: 81.59 E-value: 1.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 687 DDAVKQQKCNMFSLVFLGLGVLSFFTFFLQG-----FTFGKAGeiLTTRLRSMAFKAMLRQDMSWFDdhKNSTGALSTRL 761
Cdd:cd18784 24 DGIVIEKSQDKFSRAIIIMGLLAIASSVAAGirgglFTLAMAR--LNIRIRNLLFRSIVSQEIGFFD--TVKTGDITSRL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 762 ATDAAQVQGATGTRLALIAQNTANLGTGIIISFIYGWQLTLLLLSVVPFIAVAGIVEMKMLAGNAKRDKKEMEAAGKIAT 841
Cdd:cd18784 100 TSDTTTMSDTVSLNLNIFLRSLVKAIGVIVFMFKLSWQLSLVTLIGLPLIAIVSKVYGDYYKKLSKAVQDSLAKANEVAE 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568932737 842 EAIENIRTVVSLTQERKFESMYVEKLHGPYRNSVRKAHIYGITFSISQAFMYFSYAGCFRFGSYLIVNGHM 912
Cdd:cd18784 180 ETISSIRTVRSFANEDGEANRYSEKLKDTYKLKIKEALAYGGYVWSNELTELALTVSTLYYGGHLVITGQI 250
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
993-1199 |
1.36e-16 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 80.90 E-value: 1.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 993 VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGqeakklNVQWLraqLGI-VSQEPILfdcSIA 1071
Cdd:COG1134 39 FWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG------RVSAL---LELgAGFHPEL---TGR 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1072 ENI-----AYGdnsrvVPHDEIVRAAKE----ANIHPFIETlPQKYntrvgdkgtqLSGGQKQRIAIARALIRQPRVLLL 1142
Cdd:COG1134 107 ENIylngrLLG-----LSRKEIDEKFDEivefAELGDFIDQ-PVKT----------YSSGMRARLAFAVATAVDPDILLV 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 568932737 1143 DEATSALDTE-SEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHGT 1199
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 ... |
990-1206 |
2.22e-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: 2.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 990 RANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSV-------LLDGQEAKKLNVQWLRAQLGIVSQE 1062
Cdd:TIGR03269 294 RGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnvrvgdeWVDMTKPGPDGRGRAKRYIGILHQE 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1063 PILF-DCSIAENIAygDNSRVVPHDEIvrAAKEANIHPFIETLPQKYNTRVGDKGT-QLSGGQKQRIAIARALIRQPRVL 1140
Cdd:TIGR03269 374 YDLYpHRTVLDNLT--EAIGLELPDEL--ARMKAVITLKMVGFDEEKAEEILDKYPdELSEGERHRVALAQVLIKEPRIV 449
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568932737 1141 LLDEATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHGTHQQLLAQ 1206
Cdd:TIGR03269 450 ILDEPTGTMDPITKVDVTHSILKAREemEQTFIIVSHDMDFVLDvCDRAALMRDGKIVKIGDPEEIVEE 518
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
978-1209 |
2.50e-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: 2.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 978 VTFNEVVFNYptrANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLerFYDPMA--GSVLLDGQEAkklnVQW---- 1051
Cdd:PRK11614 6 LSFDKVSAHY---GKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTL--CGDPRAtsGRIVFDGKDI----TDWqtak 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1052 -LRAQLGIVSQEPILFD-CSIAENIAYGD--NSRVVPHDEIVRAakeanihpfIETLPQKYNTRVGDKGTqLSGGQKQRI 1127
Cdd:PRK11614 77 iMREAVAIVPEGRRVFSrMTVEENLAMGGffAERDQFQERIKWV---------YELFPRLHERRIQRAGT-MSGGEQQML 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1128 AIARALIRQPRVLLLDEATSALdteSEKVVQEALDKAR----EGRTCIVIAHRLS-TIQNADLIVVIENGKVKEHGTHQQ 1202
Cdd:PRK11614 147 AIGRALMSQPRLLLLDEPSLGL---APIIIQQIFDTIEqlreQGMTIFLVEQNANqALKLADRGYVLENGHVVLEDTGDA 223
|
....*..
gi 568932737 1203 LLAQKGI 1209
Cdd:PRK11614 224 LLANEAV 230
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
994-1194 |
2.50e-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: 2.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 994 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNV-QWLRAQLGIVS----QEPILFDC 1068
Cdd:COG1129 266 GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPrDAIRAGIAYVPedrkGEGLVLDL 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1069 SIAENI---AYGDNSR--VVPHDEIVRAAKEanihpFIETLpqkyNTRVGDKGT---QLSGGQKQRIAIARALIRQPRVL 1140
Cdd:COG1129 346 SIRENItlaSLDRLSRggLLDRRRERALAEE-----YIKRL----RIKTPSPEQpvgNLSGGNQQKVVLAKWLATDPKVL 416
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568932737 1141 LLDEATSALD--TESE--KVVQEAldkAREGRTCIVIahrlST-----IQNADLIVVIENGKV 1194
Cdd:COG1129 417 ILDEPTRGIDvgAKAEiyRLIREL---AAEGKAVIVI----SSelpelLGLSDRILVMREGRI 472
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
994-1218 |
2.60e-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: 2.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 994 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKlNVQWLRAQLGIVSQEPILFD-CSIAE 1072
Cdd:TIGR01257 944 PAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET-NLDAVRQSLGMCPQHNILFHhLTVAE 1022
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1073 NIAYGDNSRVVPHDEiVRAAKEANIHPfiETLPQKYNTRVGDkgtqLSGGQKQRIAIARALIRQPRVLLLDEATSALDTE 1152
Cdd:TIGR01257 1023 HILFYAQLKGRSWEE-AQLEMEAMLED--TGLHHKRNEEAQD----LSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPY 1095
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568932737 1153 SEKVVQEALDKAREGRTCIVIAHRLStiqNADL----IVVIENGKVKEHGTHQQL--LAQKGIYFSMV----NIQA 1218
Cdd:TIGR01257 1096 SRRSIWDLLLKYRSGRTIIMSTHHMD---EADLlgdrIAIISQGRLYCSGTPLFLknCFGTGFYLTLVrkmkNIQS 1168
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
995-1204 |
2.61e-16 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 80.42 E-value: 2.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 995 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQWLRAQLGIVSQEPIL-FDCSIAEN 1073
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTpGDITVQEL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1074 IAYGDnsrvVPHDEIV---RAAKEANIHPFIETlpqkynTRVGDKGTQ----LSGGQKQRIAIARALIRQPRVLLLDEAT 1146
Cdd:PRK10253 102 VARGR----YPHQPLFtrwRKEDEEAVTKAMQA------TGITHLADQsvdtLSGGQRQRAWIAMVLAQETAIMLLDEPT 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568932737 1147 SALDTESEKVVQEALDK--AREGRTCIVIAHRLS-TIQNADLIVVIENGKVKEHGTHQQLL 1204
Cdd:PRK10253 172 TWLDISHQIDLLELLSElnREKGYTLAAVLHDLNqACRYASHLIALREGKIVAQGAPKEIV 232
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
338-569 |
2.80e-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: 2.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 338 LEFSDVHFSYPSRANIK-ILKGLNLKVKSGQTVALVGNSGCGKSTTVQLL-QRLYDPT-EGKISIDGQDIRnfnvRCLRE 414
Cdd:cd03232 4 LTWKNLNYTVPVKGGKRqLLNNISGYVKPGTLTALMGESGAGKTTLLDVLaGRKTAGViTGEILINGRPLD----KNFQR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 415 IIGVVSQEPVLFST-TIAENIRygrgnvtmdeiekavkeanaydFIMKLpqkfdtlvgdRGaqLSGGQKQRIAIARALVR 493
Cdd:cd03232 80 STGYVEQQDVHSPNlTVREALR----------------------FSALL----------RG--LSVEQRKRLTIGVELAA 125
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568932737 494 NPKILLLDEATSALDTESEAEVQAALDK-AREGRTTIVIAHRLStirnADVIAGFeDGVIveqgshseLMKKEG--IYF 569
Cdd:cd03232 126 KPSILFLDEPTSGLDSQAAYNIVRFLKKlADSGQAILCTIHQPS----ASIFEKF-DRLL--------LLKRGGktVYF 191
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
73-290 |
2.83e-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: 2.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 73 VAAYIQVSFWTLAAGRQIKKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDDVSKISEGIGDKVGMFFQAIATFFAGFIV 152
Cdd:cd18564 69 LASYAGTYLTALVGQRVVLDLRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGAIQDLLVSGVLPLLTNLLTLVGMLGV 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 153 GFIRGWKLTLVIMAISPILGLSTAVWAKILSTFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKELERYQKHLENAKK 232
Cdd:cd18564 149 MFWLDWQLALIALAVAPLLLLAARRFSRRIKEASREQRRREGALASVAQESLSAIRVVQAFGREEHEERRFARENRKSLR 228
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 568932737 233 IGIK-KAISANISMGIAfLLIYASYALAFWYGSTLVISKEYTIGnAMTVFFSILIGAFS 290
Cdd:cd18564 229 AGLRaARLQALLSPVVD-VLVAVGTALVLWFGAWLVLAGRLTPG-DLLVFLAYLKNLYK 285
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
984-1198 |
2.85e-16 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 83.75 E-value: 2.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 984 VFNYPTRaNVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLN---VQWLRAQLGIVS 1060
Cdd:PRK10261 329 LLNRVTR-EVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSpgkLQALRRDIQFIF 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1061 QEPIlfdCSIAENIAYGDnSRVVP---HDEIVRAAKEANIHPFIEtlpqkyntRVGDKGT-------QLSGGQKQRIAIA 1130
Cdd:PRK10261 408 QDPY---ASLDPRQTVGD-SIMEPlrvHGLLPGKAAAARVAWLLE--------RVGLLPEhawryphEFSGGQRQRICIA 475
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568932737 1131 RALIRQPRVLLLDEATSALDTE-SEKVVQEALDKARE-GRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHG 1198
Cdd:PRK10261 476 RALALNPKVIIADEAVSALDVSiRGQIINLLLDLQRDfGIAYLFISHDMAVVERiSHRVAVMYLGQIVEIG 546
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
338-553 |
3.34e-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: 3.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 338 LEFSDVhfSYPSRANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLREI-I 416
Cdd:COG3845 258 LEVENL--SVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLgV 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 417 GVVSQEP-----VLfSTTIAENI---RYGRGNVT------MDEIEKAVKEanaydfIMKlpqKFDTLVGDRGA---QLSG 479
Cdd:COG3845 336 AYIPEDRlgrglVP-DMSVAENLilgRYRRPPFSrggfldRKAIRAFAEE------LIE---EFDVRTPGPDTparSLSG 405
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568932737 480 GQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKAR-EGRTTIVIAHRLSTIRN-ADVIAGFEDGVIV 553
Cdd:COG3845 406 GNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRdAGAAVLLISEDLDEILAlSDRIAVMYEGRIV 481
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
989-1203 |
3.67e-16 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 80.19 E-value: 3.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 989 TRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQWL---RAQLGIVSQEPIL 1065
Cdd:PRK11831 16 TRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLytvRKRMSMLFQSGAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1066 F-DCSIAENIAYgdnsrvvPHDEIVRAAkEANIHpfiETLPQKYNTrVGDKG------TQLSGGQKQRIAIARALIRQPR 1138
Cdd:PRK11831 96 FtDMNVFDNVAY-------PLREHTQLP-APLLH---STVMMKLEA-VGLRGaaklmpSELSGGMARRAALARAIALEPD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568932737 1139 VLLLDEATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHGTHQQL 1203
Cdd:PRK11831 164 LIMFDEPFVGQDPITMGVLVKLISELNSalGVTCVVVSHDVPEVLSiADHAYIVADKKIVAHGSAQAL 231
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
353-550 |
3.71e-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: 3.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 353 IKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLY--DPTEGKISIDGQDIRNFNVR-CLREIIGVVSQEPVLF-ST 428
Cdd:TIGR02633 14 VKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYphGTWDGEIYWSGSPLKASNIRdTERAGIVIIHQELTLVpEL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 429 TIAENIRYG-----RGNVTMDEieKAVKEANAYDFIMKLPQKFDTL-VGDRGaqlsGGQKQRIAIARALVRNPKILLLDE 502
Cdd:TIGR02633 94 SVAENIFLGneitlPGGRMAYN--AMYLRAKNLLRELQLDADNVTRpVGDYG----GGQQQLVEIAKALNKQARLLILDE 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 568932737 503 ATSALdTESEAEVQAAL--DKAREGRTTIVIAHRLSTIRN-ADVIAGFEDG 550
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 ... |
995-1205 |
3.89e-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: 3.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 995 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERF--YDPMAGSVL----------------LDGQEAKKLNVQwlraql 1056
Cdd:TIGR03269 15 VLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIyhvalcekcgyverpsKVGEPCPVCGGT------ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1057 gIVSQEPILFDCS------IAENIA---------YGDNsRVVphDEIVRAAKEAN------IHPFIETLPQ-KYNTRVGD 1114
Cdd:TIGR03269 89 -LEPEEVDFWNLSdklrrrIRKRIAimlqrtfalYGDD-TVL--DNVLEALEEIGyegkeaVGRAVDLIEMvQLSHRITH 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1115 KGTQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEALDKA--REGRTCIVIAHRLSTIQN-ADLIVVIEN 1191
Cdd:TIGR03269 165 IARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAvkASGISMVLTSHWPEVIEDlSDKAIWLEN 244
|
250
....*....|....
gi 568932737 1192 GKVKEHGTHQQLLA 1205
Cdd:TIGR03269 245 GEIKEEGTPDEVVA 258
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
349-519 |
3.91e-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: 3.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 349 SRANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLREIIGVVSQEPVLFST 428
Cdd:cd03231 9 ERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 429 TIAENIRYGRGNVTMDEIEKAVKEANAydfimklpqkfdTLVGDRG-AQLSGGQKQRIAIARALVRNPKILLLDEATSAL 507
Cdd:cd03231 89 SVLENLRFWHADHSDEQVEEALARVGL------------NGFEDRPvAQLSAGQQRRVALARLLLSGRPLWILDEPTTAL 156
|
170
....*....|..
gi 568932737 508 DTESEAEVQAAL 519
Cdd:cd03231 157 DKAGVARFAEAM 168
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
355-557 |
5.46e-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: 5.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 355 ILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGqdirnfNVRCLREIIGVVSQEpvlfsTTIAENI 434
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG------RVSALLELGAGFHPE-----LTGRENI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 435 R-----YGrgnVTMDEIEKAVKEANAY----DFImklpqkfDTLVGdrgaQLSGGQKQRIAIARALVRNPKILLLDEATS 505
Cdd:COG1134 110 YlngrlLG---LSRKEIDEKFDEIVEFaelgDFI-------DQPVK----TYSSGMRARLAFAVATAVDPDILLVDEVLA 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 568932737 506 ALDTE----SEAEVQaalDKAREGRTTIVIAHRLSTIRN-ADVIAGFEDGVIVEQGS 557
Cdd:COG1134 176 VGDAAfqkkCLARIR---ELRESGRTVIFVSHSMGAVRRlCDRAIWLEKGRLVMDGD 229
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
350-562 |
9.52e-16 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 78.68 E-value: 9.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 350 RANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDI-------RNFNVRCL---------- 412
Cdd:PRK15112 23 RQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLhfgdysyRSQRIRMIfqdpstslnp 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 413 REIIGVVSQEPVLFSTTIAENIRYGRGNVTMDEIEKAVKEANAYDFImklpqkfdtlvgdrgaqLSGGQKQRIAIARALV 492
Cdd:PRK15112 103 RQRISQILDFPLRLNTDLEPEQREKQIIETLRQVGLLPDHASYYPHM-----------------LAPGQKQRLGLARALI 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568932737 493 RNPKILLLDEATSALDTESEAE-VQAALD-KAREGRTTIVIAHRLSTIRN-ADVIAGFEDGVIVEQGSHSELM 562
Cdd:PRK15112 166 LRPKVIIADEALASLDMSMRSQlINLMLElQEKQGISYIYVTQHLGMMKHiSDQVLVMHQGEVVERGSTADVL 238
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
993-1193 |
1.02e-15 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 81.59 E-value: 1.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 993 VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAK----KLNVQwlrAQLGIVSQEPILFD- 1067
Cdd:PRK10762 17 VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfngpKSSQE---AGIGIIHQELNLIPq 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1068 CSIAENIAYG----------DNSRVvpHDEIVRAAKEANihpfietLPQKYNTRVGDkgtqLSGGQKQRIAIARALIRQP 1137
Cdd:PRK10762 94 LTIAENIFLGrefvnrfgriDWKKM--YAEADKLLARLN-------LRFSSDKLVGE----LSIGEQQMVEIAKVLSFES 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568932737 1138 RVLLLDEATSAL-DTESE---KVVQEALDkarEGRTCIVIAHRLSTI-QNADLIVVIENGK 1193
Cdd:PRK10762 161 KVIIMDEPTDALtDTETEslfRVIRELKS---QGRGIVYISHRLKEIfEICDDVTVFRDGQ 218
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
350-557 |
1.21e-15 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 81.83 E-value: 1.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 350 RANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDI--RNFNVRCLREI------------ 415
Cdd:PRK10261 26 QQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLrrRSRQVIELSEQsaaqmrhvrgad 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 416 IGVVSQEPV-----LFST--TIAENIRYGRGNVTmdeiEKAVKEANAYDFIMKLPQKfDTLVGDRGAQLSGGQKQRIAIA 488
Cdd:PRK10261 106 MAMIFQEPMtslnpVFTVgeQIAESIRLHQGASR----EEAMVEAKRMLDQVRIPEA-QTILSRYPHQLSGGMRQRVMIA 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568932737 489 RALVRNPKILLLDEATSALDTESEAEVQAALDKAREGRT--TIVIAHRLSTIRN-ADVIAGFEDGVIVEQGS 557
Cdd:PRK10261 181 MALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSmgVIFITHDMGVVAEiADRVLVMYQGEAVETGS 252
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
990-1174 |
1.35e-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: 1.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 990 RANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQWLRAQLGIVSQEPILFDCS 1069
Cdd:TIGR01189 10 RGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLPGLKPELS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1070 IAENI----AYGDNSRVVPHDeivrAAKEANIHPFiETLPQKyntrvgdkgtQLSGGQKQRIAIARALIRQPRVLLLDEA 1145
Cdd:TIGR01189 90 ALENLhfwaAIHGGAQRTIED----ALAAVGLTGF-EDLPAA----------QLSAGQQRRLALARLWLSRRPLWILDEP 154
|
170 180
....*....|....*....|....*....
gi 568932737 1146 TSALDTESEKVVQEALDkAREGRTCIVIA 1174
Cdd:TIGR01189 155 TTALDKAGVALLAGLLR-AHLARGGIVLL 182
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
697-930 |
1.36e-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: 78.68 E-value: 1.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 697 MFSLVFLGLGVLSFFTFFLqgftFGKAGEILTTRLRSMAFKAMLRQDMSWFDdhKNSTGALSTRLATDAAQVQGATGTRL 776
Cdd:cd18575 41 LLLAVALVLALASALRFYL----VSWLGERVVADLRKAVFAHLLRLSPSFFE--TTRTGEVLSRLTTDTTLIQTVVGSSL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 777 ALIAQNTANLGTGIIISFIYGWQLTLLLLSVVPFIAVAGIVEMKMLAGNAKRDKKEMEAAGKIATEAIENIRTVVSLTQE 856
Cdd:cd18575 115 SIALRNLLLLIGGLVMLFITSPKLTLLVLLVIPLVVLPIILFGRRVRRLSRASQDRLADLSAFAEETLSAIKTVQAFTRE 194
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568932737 857 RKFESMYVEKLHGPYRNSVRKAHIYGITFSISQAFMYFSYAGCFRFGSYLIVNGHMRFKDVI--LVFSAIVLGAVA 930
Cdd:cd18575 195 DAERQRFATAVEAAFAAALRRIRARALLTALVIFLVFGAIVFVLWLGAHDVLAGRMSAGELSqfVFYAVLAAGSVG 270
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
993-1192 |
1.37e-15 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 81.37 E-value: 1.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 993 VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQwLRAQLG--IVSQEPILFD-CS 1069
Cdd:PRK09700 18 VHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHK-LAAQLGigIIYQELSVIDeLT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1070 IAENIAYGDN-SRVVPHDEIVRAAK---EANIHPFIETLPQKYNTRVGDkgtqLSGGQKQRIAIARALIRQPRVLLLDEA 1145
Cdd:PRK09700 97 VLENLYIGRHlTKKVCGVNIIDWREmrvRAAMMLLRVGLKVDLDEKVAN----LSISHKQMLEIAKTLMLDAKVIIMDEP 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 568932737 1146 TSAL-DTESEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVIENG 1192
Cdd:PRK09700 173 TSSLtNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRiCDRYTVMKDG 221
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
993-1194 |
1.59e-15 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 80.87 E-value: 1.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 993 VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQwLRAQLGI--VSQEPILF-DCS 1069
Cdd:PRK15439 24 VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPA-KAHQLGIylVPQEPLLFpNLS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1070 IAENIAYGDNSRVVPHDEIVRAAKEANIHPFIETlpqkyntrvgdKGTQLSGGQKQRIAIARALIRQPRVLLLDEATSAL 1149
Cdd:PRK15439 103 VKENILFGLPKRQASMQKMKQLLAALGCQLDLDS-----------SAGSLEVADRQIVEILRGLMRDSRILILDEPTASL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 568932737 1150 D-TESEKV---VQEALDKareGRTCIVIAHRLSTI-QNADLIVVIENGKV 1194
Cdd:PRK15439 172 TpAETERLfsrIRELLAQ---GVGIVFISHKLPEIrQLADRISVMRDGTI 218
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
978-1193 |
1.69e-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: 74.79 E-value: 1.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 978 VTFNEVVFNYPTRanvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLerfydpmagsvlldgqeakklnvqwlraqlg 1057
Cdd:cd03221 1 IELENLSKTYGGK---LLLKDISLTINPGDRIGLVGRNGAGKSTLLKLI------------------------------- 46
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1058 ivsqepilfdcsiaeniaygdNSRVVPHDEIVRAAKEANIHPFietlpqkyntrvgdkgTQLSGGQKQRIAIARALIRQP 1137
Cdd:cd03221 47 ---------------------AGELEPDEGIVTWGSTVKIGYF----------------EQLSGGEKMRLALAKLLLENP 89
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 568932737 1138 RVLLLDEATSALDTESEKVVQEALdKAREGrTCIVIAHRLSTIQN-ADLIVVIENGK 1193
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 ... |
354-593 |
1.99e-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: 1.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 354 KILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRL--YDPTEGKI--------SIDGQDIRNFNVRCLREIIGVVSQEP 423
Cdd:TIGR03269 14 EVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIiyhvalceKCGYVERPSKVGEPCPVCGGTLEPEE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 424 VLF---STTIAENIR-------------YGRGNV------TMDEIEKAVKEA--NAYDFI--MKLPQKFDTLVGDrgaqL 477
Cdd:TIGR03269 94 VDFwnlSDKLRRRIRkriaimlqrtfalYGDDTVldnvleALEEIGYEGKEAvgRAVDLIemVQLSHRITHIARD----L 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 478 SGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKA--REGRTTIVIAHRLSTIRN-ADVIAGFEDGVIVE 554
Cdd:TIGR03269 170 SGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAvkASGISMVLTSHWPEVIEDlSDKAIWLENGEIKE 249
|
250 260 270
....*....|....*....|....*....|....*....
gi 568932737 555 QGSHSELMKKegiYFRLVNMqtagsqiLSEEFEVELSDE 593
Cdd:TIGR03269 250 EGTPDEVVAV---FMEGVSE-------VEKECEVEVGEP 278
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
655-912 |
2.06e-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: 2.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 655 FVVGTVCAIANGALQPAFSIILSEMIaifgpgdDAVKQQKCNM-----FSLVFLGLGVLSFFTFFLQGFTFGKAGEILTT 729
Cdd:cd18541 1 YLLGILFLILVDLLQLLIPRIIGRAI-------DALTAGTLTAsqllrYALLILLLALLIGIFRFLWRYLIFGASRRIEY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 730 RLRSMAFKAMLRQDMSWFddHKNSTGALSTRLATDAAQVQGATGTRLALIAQNTANLGTGIIISFIYGWQLTLLLLSVVP 809
Cdd:cd18541 74 DLRNDLFAHLLTLSPSFY--QKNRTGDLMARATNDLNAVRMALGPGILYLVDALFLGVLVLVMMFTISPKLTLIALLPLP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 810 FIAVAGIVEMKMLagnAKRDKKEMEAAGKIATEAIEN---IRTVVSLTQERKFESMYVEKLHGPYRNSVRKAHIYGITFS 886
Cdd:cd18541 152 LLALLVYRLGKKI---HKRFRKVQEAFSDLSDRVQESfsgIRVIKAFVQEEAEIERFDKLNEEYVEKNLRLARVDALFFP 228
|
250 260
....*....|....*....|....*.
gi 568932737 887 ISQAFMYFSYAGCFRFGSYLIVNGHM 912
Cdd:cd18541 229 LIGLLIGLSFLIVLWYGGRLVIRGTI 254
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
655-910 |
3.16e-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: 3.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 655 FVVGTVCAIANGALQPAFSIILSEMIaifgpgDDAVKQQKCNM-----FSLVFLGLGVLSFFTFFLQGFTFGKAGEILTT 729
Cdd:cd18544 1 FILALLLLLLATALELLGPLLIKRAI------DDYIVPGQGDLqglllLALLYLGLLLLSFLLQYLQTYLLQKLGQRIIY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 730 RLRSMAFKAMLRQDMSWFDdhKNSTGALSTRLATDAAQVQGATGTRLALIAQNTANLGTGIIISFIYGWQLTLLLLSVVP 809
Cdd:cd18544 75 DLRRDLFSHIQRLPLSFFD--RTPVGRLVTRVTNDTEALNELFTSGLVTLIGDLLLLIGILIAMFLLNWRLALISLLVLP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 810 FIAVAgIVEMKMLAGNAKRDKKEMEAA--GKIAtEAIENIRTVVSLTQERKFESMYvEKLHGPYRNSVRKA-HIYGITFS 886
Cdd:cd18544 153 LLLLA-TYLFRKKSRKAYREVREKLSRlnAFLQ-ESISGMSVIQLFNREKREFEEF-DEINQEYRKANLKSiKLFALFRP 229
|
250 260
....*....|....*....|....
gi 568932737 887 ISQAFMYFSYAGCFRFGSYLIVNG 910
Cdd:cd18544 230 LVELLSSLALALVLWYGGGQVLSG 253
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
344-567 |
3.34e-15 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 77.17 E-value: 3.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 344 HFSYPSRANIkILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQ-RLYDPTE-------GKISIDGQDIRNFNVR---CL 412
Cdd:PRK13547 6 HLHVARRHRA-ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAgDLTGGGAprgarvtGDVTLNGEPLAAIDAPrlaRL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 413 REIIGVVSQEPVLFSttIAENIRYGR----------GNVTMDEIEKAVKEANAydfimklpqkfDTLVGDRGAQLSGGQK 482
Cdd:PRK13547 85 RAVLPQAAQPAFAFS--AREIVLLGRypharragalTHRDGEIAWQALALAGA-----------TALVGRDVTTLSGGEL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 483 QRIAIARAL---------VRNPKILLLDEATSALDTESEAEVQAAL-DKARE---GRTTIVIAHRLSTiRNADVIAGFED 549
Cdd:PRK13547 152 ARVQFARVLaqlwpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVrRLARDwnlGVLAIVHDPNLAA-RHADRIAMLAD 230
|
250
....*....|....*...
gi 568932737 550 GVIVEQGSHSELMKKEGI 567
Cdd:PRK13547 231 GAIVAHGAPADVLTPAHI 248
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
975-1204 |
3.59e-15 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 77.14 E-value: 3.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 975 EGSVTFNEVVFNYPTRAnvpVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQWLRA 1054
Cdd:PRK10575 9 DTTFALRNVSFRVPGRT---LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFAR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1055 QLGIVSQE-PILFDCSIAENIAYGdnsRVVPHDEIVR--AAKEANIHPFIETLPQK-YNTRVGDkgtQLSGGQKQRIAIA 1130
Cdd:PRK10575 86 KVAYLPQQlPAAEGMTVRELVAIG---RYPWHGALGRfgAADREKVEEAISLVGLKpLAHRLVD---SLSGGERQRAWIA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568932737 1131 RALIRQPRVLLLDEATSALDTESEKVVQEALDKAREGRTCIVIAhRLSTIQNA----DLIVVIENGKVKEHGTHQQLL 1204
Cdd:PRK10575 160 MLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIA-VLHDINMAarycDYLVALRGGEMIAQGTPAELM 236
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
342-553 |
3.70e-15 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 78.23 E-value: 3.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 342 DVHFSYPSrANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDP---TEGKISIDGQDIRNFNVRCLREI--- 415
Cdd:PRK09473 19 RVTFSTPD-GDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAngrIGGSATFNGREILNLPEKELNKLrae 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 416 -IGVVSQEPVlfsTTIAENIRYGRGNVTMDEIEKAVKEANAYDFIMKL----------------PQKFdtlvgdrgaqlS 478
Cdd:PRK09473 98 qISMIFQDPM---TSLNPYMRVGEQLMEVLMLHKGMSKAEAFEESVRMldavkmpearkrmkmyPHEF-----------S 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568932737 479 GGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDK-AREGRTTIV-IAHRLStirnadVIAGFEDGVIV 553
Cdd:PRK09473 164 GGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNElKREFNTAIImITHDLG------VVAGICDKVLV 234
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
65-276 |
3.78e-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: 3.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 65 SGLGGGvlvaayiqvsFWTLAAGRQIKKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDDVSKISEGIGDKVGMFFQAIA 144
Cdd:cd18590 53 AGLRGG----------LFMCTLSRLNLRLRHQLFSSLVQQDIGFFEKTKTGDLTSRLSTDTTLMSRSVALNANVLLRSLV 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 145 TFFAGFIVGFIRGWKLTLVIMAISPILGLSTAVWAKILSTFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKELERYQ 224
Cdd:cd18590 123 KTLGMLGFMLSLSWQLTLLTLIEMPLTAIAQKVYNTYHQKLSQAVQDSIAKAGELAREAVSSIRTVRSFKAEEEEACRYS 202
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 568932737 225 KHLENAKKIGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTIGN 276
Cdd:cd18590 203 EALERTYNLKDRRDTVRAVYLLVRRVLQLGVQVLMLYCGRQLIQSGHLTTGS 254
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
990-1203 |
4.58e-15 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 79.90 E-value: 4.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 990 RANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQWLR--------------AQ 1055
Cdd:PRK10261 26 QQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRSRQVIElseqsaaqmrhvrgAD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1056 LGIVSQEPI-----LFDC--SIAENIAYGDNsrvVPHDEIVRAAK----EANIhPFIETLPQKYNTrvgdkgtQLSGGQK 1124
Cdd:PRK10261 106 MAMIFQEPMtslnpVFTVgeQIAESIRLHQG---ASREEAMVEAKrmldQVRI-PEAQTILSRYPH-------QLSGGMR 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1125 QRIAIARALIRQPRVLLLDEATSALDTESE-------KVVQEALDKAregrtCIVIAHRLSTIQN-ADLIVVIENGKVKE 1196
Cdd:PRK10261 175 QRVMIAMALSCRPAVLIADEPTTALDVTIQaqilqliKVLQKEMSMG-----VIFITHDMGVVAEiADRVLVMYQGEAVE 249
|
....*..
gi 568932737 1197 HGTHQQL 1203
Cdd:PRK10261 250 TGSVEQI 256
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
996-1204 |
4.88e-15 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 76.50 E-value: 4.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 996 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQWL---------RAQLGIVSQEP--- 1063
Cdd:PRK11701 22 CRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALseaerrrllRTEWGFVHQHPrdg 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1064 ILFDCSIAENI-----AYGDNsrvvpHDEIVRAA-----KEANIHPfietlpqkynTRVGDKGTQLSGGQKQRIAIARAL 1133
Cdd:PRK11701 102 LRMQVSAGGNIgerlmAVGAR-----HYGDIRATagdwlERVEIDA----------ARIDDLPTTFSGGMQQRLQIARNL 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568932737 1134 IRQPRVLLLDEATSALDTEsekvVQ-EALDKARE-----GRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHGTHQQLL 1204
Cdd:PRK11701 167 VTHPRLVFMDEPTGGLDVS----VQaRLLDLLRGlvrelGLAVVIVTHDLAVARLlAHRLLVMKQGRVVESGLTDQVL 240
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
986-1194 |
5.96e-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: 5.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 986 NYPTRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLL--ERfyDPMAGSVLLDGQEAKKLNV-QWLRAQLGIVSQE 1062
Cdd:COG3845 264 SVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALagLR--PPASGSIRLDGEDITGLSPrERRRLGVAYIPED 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1063 P-----ILfDCSIAENIA--YGDNSRVVPH-----DEIVRAAKEAnihpfIEtlpqKYNTRVGDKGT---QLSGGQKQRI 1127
Cdd:COG3845 342 RlgrglVP-DMSVAENLIlgRYRRPPFSRGgfldrKAIRAFAEEL-----IE----EFDVRTPGPDTparSLSGGNQQKV 411
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568932737 1128 AIARALIRQPRVLLLDEATSALDTESEKVVQEALDKAR-EGRTCIVIAHRLSTIQN-ADLIVVIENGKV 1194
Cdd:COG3845 412 ILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRdAGAAVLLISEDLDEILAlSDRIAVMYEGRI 480
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
996-1204 |
6.82e-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: 6.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 996 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLErFYDP----MAGSVLLDGqeaKKLNVQWLRAQLGIVSQEPILFDCSIA 1071
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALA-FRSPkgvkGSGSVLLNG---MPIDAKEMRAISAYVQQDDLFIPTLTV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1072 -ENIAYgdNSRVVPHDEIVRAAKEANIHPFIETLPQK--YNTRVGDKGTQ--LSGGQKQRIAIARALIRQPRVLLLDEAT 1146
Cdd:TIGR00955 117 rEHLMF--QAHLRMPRRVTKKEKRERVDEVLQALGLRkcANTRIGVPGRVkgLSGGERKRLAFASELLTDPPLLFCDEPT 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568932737 1147 SALDTES-EKVVQEALDKAREGRTCIVIAHRLST--IQNADLIVVIENGKVKEHGTHQQLL 1204
Cdd:TIGR00955 195 SGLDSFMaYSVVQVLKGLAQKGKTIICTIHQPSSelFELFDKIILMAEGRVAYLGSPDQAV 255
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
988-1194 |
8.86e-15 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 75.06 E-value: 8.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 988 PTRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGqeakklNVQW-----LRAQLGIV--S 1060
Cdd:cd03267 29 RKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAG------LVPWkrrkkFLRRIGVVfgQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1061 QEPILFDCSIAENIAYgdnsrvvpHDEIVR---AAKEANIHPFIETLPQkynTRVGDKGT-QLSGGQKQRIAIARALIRQ 1136
Cdd:cd03267 103 KTQLWWDLPVIDSFYL--------LAAIYDlppARFKKRLDELSELLDL---EELLDTPVrQLSLGQRMRAEIAAALLHE 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568932737 1137 PRVLLLDEATSALDTESEKVVQEALDKAREGR--TCIVIAHRLSTIQN-ADLIVVIENGKV 1194
Cdd:cd03267 172 PEILFLDEPTIGLDVVAQENIRNFLKEYNRERgtTVLLTSHYMKDIEAlARRVLVIDKGRL 232
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
47-275 |
1.05e-14 |
|
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (TrmA) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349988 [Multi-domain] Cd Length: 294 Bit Score: 76.27 E-value: 1.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 47 LNPGRILEEEMTRYAYYYSGLGGGVLVAAYIQVSFWTLAAGRQIKKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDDVS 126
Cdd:cd18544 30 IVPGQGDLQGLLLLALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRDLFSHIQRLPLSFFDRTPVGRLVTRVTNDTE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 127 KISEGIGDKVGMFFQAIATFFAGFIVGFIRGWKLTLVIMAISPILGLSTAVWAKILSTFSDKELAAYAKAGAVAEEALGA 206
Cdd:cd18544 110 ALNELFTSGLVTLIGDLLLLIGILIAMFLLNWRLALISLLVLPLLLLATYLFRKKSRKAYREVREKLSRLNAFLQESISG 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568932737 207 IRTVIAFGGQNKELERYQKHLENAKKIGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTIG 275
Cdd:cd18544 190 MSVIQLFNREKREFEEFDEINQEYRKANLKSIKLFALFRPLVELLSSLALALVLWYGGGQVLSGAVTLG 258
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
348-532 |
1.14e-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: 1.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 348 PSRANIKILKGLNLKVKSGQTVALVGNSGCGKSTtvqLLQRL------YDPTEGKISIDGQDIRNFNVRCLREIIgVVSQ 421
Cdd:cd03233 15 KGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCST---LLKALanrtegNVSVEGDIHYNGIPYKEFAEKYPGEII-YVSE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 422 EPVLFST-TIAEnirygrgnvTMDeiekAVKEANAYDFImklpqkfdtlvgdRGaqLSGGQKQRIAIARALVRNPKILLL 500
Cdd:cd03233 91 EDVHFPTlTVRE---------TLD----FALRCKGNEFV-------------RG--ISGGERKRVSIAEALVSRASVLCW 142
|
170 180 190
....*....|....*....|....*....|...
gi 568932737 501 DEATSALDTESEAE-VQAALDKAREGRTTIVIA 532
Cdd:cd03233 143 DNSTRGLDSSTALEiLKCIRTMADVLKTTTFVS 175
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
992-1199 |
1.22e-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: 1.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 992 NVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQWLRAQLGIVSQEP-ILFDCSI 1070
Cdd:COG4604 13 GKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAILRQENhINSRLTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1071 AENIAYG----DNSRVVPHD-EIVRAAkeanIHPF-IETLPQKYNTrvgdkgtQLSGGQKQRIAIARALIRQPRVLLLDE 1144
Cdd:COG4604 93 RELVAFGrfpySKGRLTAEDrEIIDEA----IAYLdLEDLADRYLD-------ELSGGQRQRAFIAMVLAQDTDYVLLDE 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568932737 1145 ATSALD----TESEKVVQEAldkARE-GRTCIVIAHRLstiqN-----ADLIVVIENGKVKEHGT 1199
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 ... |
70-279 |
1.79e-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: 1.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 70 GVLVAAYIqvSFWTLAAGRQIKKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDDVSK--------ISEGIgdkvgmffQ 141
Cdd:cd18574 56 SLLTFAYI--SLLSVVGERVAARLRNDLFSSLLRQDIAFFDTHRTGELVNRLTADVQEfkssfkqcVSQGL--------R 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 142 AIATFFAGFIVGFIRGWKLTLVIMAISPILGLSTAVWAKILSTFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKELE 221
Cdd:cd18574 126 SVTQTVGCVVSLYLISPKLTLLLLVIVPVVVLVGTLYGSFLRKLSRRAQAQVAKATGVADEALGNIRTVRAFAMEDRELE 205
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568932737 222 RYQKHLENAKK--------IGIKKAISaNISMGIAFLLIYasyalafWYGSTLVISKEYTIGNAMT 279
Cdd:cd18574 206 LYEEEVEKAAKlneklglgIGIFQGLS-NLALNGIVLGVL-------YYGGSLVSRGELTAGDLMS 263
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
356-561 |
2.26e-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: 2.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 356 LKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVR-CLREIIGVVS----QEPVLFSTTI 430
Cdd:COG1129 268 VRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRdAIRAGIAYVPedrkGEGLVLDLSI 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 431 AENI------RYGRGNVtmdeIEKAVKEANAYDFIMKL---PQKFDTLVGdrgaQLSGGQKQRIAIARALVRNPKILLLD 501
Cdd:COG1129 348 RENItlasldRLSRGGL----LDRRRERALAEEYIKRLrikTPSPEQPVG----NLSGGNQQKVVLAKWLATDPKVLILD 419
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568932737 502 EATSALDTESEAEVQAALDK-AREGRTTIVIahrlST-----IRNADVIAGFEDGVIVEQGSHSEL 561
Cdd:COG1129 420 EPTRGIDVGAKAEIYRLIRElAAEGKAVIVI----SSelpelLGLSDRILVMREGRIVGELDREEA 481
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
710-912 |
2.52e-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: 74.89 E-value: 2.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 710 FFTFFLQG-FTF------GKAGEILTTRLRSMAFKAMLRQDMSWFDDHKnsTGALSTRLATDaaqVQGATGTRLALIAQN 782
Cdd:cd18574 49 LGLYLLQSlLTFayisllSVVGERVAARLRNDLFSSLLRQDIAFFDTHR--TGELVNRLTAD---VQEFKSSFKQCVSQG 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 783 TANLG--TGIIISFIY-GWQLTLLLLSVVPFIAVAGIVEMKMLAGNAKRDKKEMEAAGKIATEAIENIRTVVSLTQERKF 859
Cdd:cd18574 124 LRSVTqtVGCVVSLYLiSPKLTLLLLVIVPVVVLVGTLYGSFLRKLSRRAQAQVAKATGVADEALGNIRTVRAFAMEDRE 203
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 568932737 860 ESMYVEKLhgpyrNSVRKAHIY-GITFSISQAFMYFSYAG----CFRFGSYLIVNGHM 912
Cdd:cd18574 204 LELYEEEV-----EKAAKLNEKlGLGIGIFQGLSNLALNGivlgVLYYGGSLVSRGEL 256
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
640-1196 |
2.61e-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: 77.53 E-value: 2.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 640 SFLKVLKlnKTEWPYFVVGTVCAIANGALqpafSIILSEMI--AIFGPGDDAVkqqkcnMFSLVFLGLGVLSFFTFFLQG 717
Cdd:COG4615 2 NLLRLLL--RESRWLLLLALLLGLLSGLA----NAGLIALInqALNATGAALA------RLLLLFAGLLVLLLLSRLASQ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 718 FTFGKAGEILTTRLRSMAFKAMLRQDMSWFDDHknSTGALSTRLATDAAQVQGATGtRLALIAQNTANlgtgIIISFIY- 796
Cdd:COG4615 70 LLLTRLGQHAVARLRLRLSRRILAAPLERLERI--GAARLLAALTEDVRTISQAFV-RLPELLQSVAL----VLGCLAYl 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 797 GWQLTLLLLSVVPFIAVAGIVEMKMLagnaKRDKKEMEAAGKIATEAIENIRTVVS------LTQERKfESMYVEKLHGP 870
Cdd:COG4615 143 AWLSPPLFLLTLVLLGLGVAGYRLLV----RRARRHLRRAREAEDRLFKHFRALLEgfkelkLNRRRR-RAFFDEDLQPT 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 871 ---YRNSVRKAH-IYGITFSISQAFMYFsyagcfrfgsyLIVnghmrfkdvILVFSAIVLGAVALGHASSFA-------- 938
Cdd:COG4615 218 aerYRDLRIRADtIFALANNWGNLLFFA-----------LIG---------LILFLLPALGWADPAVLSGFVlvllflrg 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 939 ---------PDYAKAKLSAAYLFSL---FERQPLIDSYSGEGLWPDKFEgSVTFNEVVFNYPTRANVP--VLQGLSLEVK 1004
Cdd:COG4615 278 plsqlvgalPTLSRANVALRKIEELelaLAAAEPAAADAAAPPAPADFQ-TLELRGVTYRYPGEDGDEgfTLGPIDLTIR 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1005 KGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQWLRAQLGIVSQEPILFDcsiaeniaygdnsRVVP 1084
Cdd:COG4615 357 RGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQLFSAVFSDFHLFD-------------RLLG 423
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1085 HDEIVRAAKeanIHPFIETLPQKYNTRVGDKG---TQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEAL 1161
Cdd:COG4615 424 LDGEADPAR---ARELLERLELDHKVSVEDGRfstTDLSQGQRKRLALLVALLEDRPILVFDEWAADQDPEFRRVFYTEL 500
|
570 580 590
....*....|....*....|....*....|....*..
gi 568932737 1162 --DKAREGRTCIVIAHRLSTIQNADLIVVIENGKVKE 1196
Cdd:COG4615 501 lpELKARGKTVIAISHDDRYFDLADRVLKMDYGKLVE 537
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
1-289 |
2.85e-14 |
|
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm287) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349992 [Multi-domain] Cd Length: 292 Bit Score: 74.74 E-value: 2.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1 MFLGTLMAIAhgsgLPLMMivfGEMTDKFVdNTGNFSLPVNFSLSMLnpgrileeemtryayyysGLGGGVLVAAYIQVS 80
Cdd:cd18548 8 KLLEVLLELL----LPTLM---ADIIDEGI-ANGDLSYILRTGLLML------------------LLALLGLIAGILAGY 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 81 FWTLAAGRQIKKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDDVSKISEGIGDKVGMFFQAIATFFAGFIVGFIRGWKL 160
Cdd:cd18548 62 FAAKASQGFGRDLRKDLFEKIQSFSFAEIDKFGTSSLITRLTNDVTQVQNFVMMLLRMLVRAPIMLIGAIIMAFRINPKL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 161 TLVIMAISPILGLSTAVWAKILSTFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKELERYQKHLENAKKIGIKKAIS 240
Cdd:cd18548 142 ALILLVAIPILALVVFLIMKKAIPLFKKVQKKLDRLNRVVRENLTGIRVIRAFNREDYEEERFDKANDDLTDTSLKAGRL 221
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 568932737 241 ANISMGIAFLLIYASYALAFWYGSTLVISKEYTIGN-------AMTVFFSILIGAF 289
Cdd:cd18548 222 MALLNPLMMLIMNLAIVAILWFGGHLINAGSLQVGDlvafinyLMQILMSLMMLSM 277
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
359-573 |
2.92e-14 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 73.81 E-value: 2.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 359 LNLKVKSGQTVALVGNSGCGKSTtvqLLQRLYD--PTEGKISIDGQDIRNFNVRCLREIIGVVSQE-PVLFSTTIAENI- 434
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKST---LLARMAGllPGSGSIQFAGQPLEAWSAAELARHRAYLSQQqTPPFAMPVFQYLt 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 435 RYGRGNVTMDEIEKAVKE-ANAYDFIMKLPqkfdTLVGdrgaQLSGGQKQRIAIARALVR-----NP--KILLLDEATSA 506
Cdd:PRK03695 92 LHQPDKTRTEAVASALNEvAEALGLDDKLG----RSVN----QLSGGEWQRVRLAAVVLQvwpdiNPagQLLLLDEPMNS 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568932737 507 LDTESeaevQAALDK-----AREGRTTIVIAHRLS-TIRNADVIAGFEDGVIVEQGSHSELMKKE------GIYFRLVN 573
Cdd:PRK03695 164 LDVAQ----QAALDRllselCQQGIAVVMSSHDLNhTLRHADRVWLLKQGKLLASGRRDEVLTPEnlaqvfGVNFRRLD 238
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
999-1198 |
3.45e-14 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 75.68 E-value: 3.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 999 LSLEVK-----KGQTlALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQ----EAKKLNVQWLRAQLGIVSQEPILF-DC 1068
Cdd:PRK11144 13 LCLTVNltlpaQGIT-AIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRvlfdAEKGICLPPEKRRIGYVFQDARLFpHY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1069 SIAENIAYG-DNSRVVPHDEIVRAAkeaNIHPFIETLPqkyntrvgdkgTQLSGGQKQRIAIARALIRQPRVLLLDEATS 1147
Cdd:PRK11144 92 KVRGNLRYGmAKSMVAQFDKIVALL---GIEPLLDRYP-----------GSLSGGEKQRVAIGRALLTAPELLLMDEPLA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 568932737 1148 ALDTESEKVVQEALDK-AREGRTCIV-IAHRLSTI-QNADLIVVIENGKVKEHG 1198
Cdd:PRK11144 158 SLDLPRKRELLPYLERlAREINIPILyVSHSLDEIlRLADRVVVLEQGKVKAFG 211
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
349-532 |
4.33e-14 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 72.39 E-value: 4.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 349 SRANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLREIIGVVSQEPVLFST 428
Cdd:TIGR01189 9 SRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLPGLKPEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 429 TIAENIRYGR--GNVTMDEIEKAVKEANAYDFImklpqkfDTLVgdrgAQLSGGQKQRIAIARALVRNPKILLLDEATSA 506
Cdd:TIGR01189 89 SALENLHFWAaiHGGAQRTIEDALAAVGLTGFE-------DLPA----AQLSAGQQRRLALARLWLSRRPLWILDEPTTA 157
|
170 180
....*....|....*....|....*.
gi 568932737 507 LDTESEAEVQAALDkAREGRTTIVIA 532
Cdd:TIGR01189 158 LDKAGVALLAGLLR-AHLARGGIVLL 182
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
344-534 |
5.94e-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: 5.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 344 HFSYPSRANIK-ILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIrNFNVRClreiigvvsqe 422
Cdd:COG2401 33 AFGVELRVVERyVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDVPDN-QFGREA----------- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 423 pvlfstTIAENIrYGRGNVTMD-EIEKAVKEANAYDFImklpQKFDtlvgdrgaQLSGGQKQRIAIARALVRNPKILLLD 501
Cdd:COG2401 101 ------SLIDAI-GRKGDFKDAvELLNAVGLSDAVLWL----RRFK--------ELSTGQKFRFRLALLLAERPKLLVID 161
|
170 180 190
....*....|....*....|....*....|....*
gi 568932737 502 EATSALDTESEAEVQAALDK-AREGRTTIVIA-HR 534
Cdd:COG2401 162 EFCSHLDRQTAKRVARNLQKlARRAGITLVVAtHH 196
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
980-1206 |
6.32e-14 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 76.16 E-value: 6.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 980 FNEVVFNYPTR--ANVPVlqglSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQWLRAQLG 1057
Cdd:PRK10522 325 LRNVTFAYQDNgfSVGPI----NLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFS 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1058 IVSQEPILFDcsiaeniaygdnsRVV-PHDEivrAAKEANIHPFIETLPQKYNTRVGD---KGTQLSGGQKQRIAIARAL 1133
Cdd:PRK10522 401 AVFTDFHLFD-------------QLLgPEGK---PANPALVEKWLERLKMAHKLELEDgriSNLKLSKGQKKRLALLLAL 464
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568932737 1134 IRQPRVLLLDEATSALDTESEKVV-QEALDKARE-GRTCIVIAHRLSTIQNADLIVVIENGKVKE-HGTHQQLLAQ 1206
Cdd:PRK10522 465 AEERDILLLDEWAADQDPHFRREFyQVLLPLLQEmGKTIFAISHDDHYFIHADRLLEMRNGQLSElTGEERDAASR 540
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
365-556 |
6.75e-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: 70.48 E-value: 6.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 365 SGQTVALVGNSGCGKSTTVQLLQRLYDPTEGK-ISIDGQDIRNFNVRCLREIIgvvsqepvlfsttiaenirygrgnvtm 443
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGvIYIDGEDILEEVLDQLLLII--------------------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 444 deiekavkeanaydfimklpqkfdtlVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALD--- 520
Cdd:smart00382 54 --------------------------VGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElrl 107
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 568932737 521 ----KAREGRTTIVIAHRLSTIRNADVIAGFEDGVIVEQG 556
Cdd:smart00382 108 llllKSEKNLTVILTTNDEKDLGPALLRRRFDRRIVLLLI 147
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
354-508 |
7.67e-14 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 72.84 E-value: 7.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 354 KILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQdirnfnvrcLReiIGVVSQEPVLFST---TI 430
Cdd:PRK09544 18 RVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGK---------LR--IGYVPQKLYLDTTlplTV 86
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568932737 431 AENIRYgRGNVTMDEIEKAVKEANAYDFIMKLPQKfdtlvgdrgaqLSGGQKQRIAIARALVRNPKILLLDEATSALD 508
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 ... |
655-912 |
1.17e-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: 72.90 E-value: 1.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 655 FVVGTVCAIANGALQPAFSIILSEMI--AIFGPGDDAVKqqkcnMFSLVFLGLGVLSFFTFFLQGFTFGKAGEILTTRLR 732
Cdd:cd18543 1 LILALLAALLATLAGLAIPLLTRRAIdgPIAHGDRSALW-----PLVLLLLALGVAEAVLSFLRRYLAGRLSLGVEHDLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 733 SMAFKAMLRQDMSWFDdhKNSTGALSTRLATDAAQVQGATGtRLALIAQNTANLGTGIIISFIYGWQLTLLLLSVVPFIA 812
Cdd:cd18543 76 TDLFAHLQRLDGAFHD--RWQSGQLLSRATSDLSLVQRFLA-FGPFLLGNLLTLVVGLVVMLVLSPPLALVALASLPPLV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 813 VAGIVEMKMLAGNAKRDKkemEAAGKIATEAIEN---IRTVVSLTQERKFESMYVEKLHGPYRNSVRKAHIYGITFSISQ 889
Cdd:cd18543 153 LVARRFRRRYFPASRRAQ---DQAGDLATVVEESvtgIRVVKAFGRERRELDRFEAAARRLRATRLRAARLRARFWPLLE 229
|
250 260
....*....|....*....|...
gi 568932737 890 AFMYFSYAGCFRFGSYLIVNGHM 912
Cdd:cd18543 230 ALPELGLAAVLALGGWLVANGSL 252
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
655-914 |
1.21e-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: 1.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 655 FVVGTVCAIANGALQPAFSIILSemIAIfgpgdDAVKQQKCNMFSLV------------FLGLGVLSFFTF-------FL 715
Cdd:cd18565 1 LVLGLLASILNRLFDLAPPLLIG--VAI-----DAVFNGEASFLPLVpaslgpadprgqLWLLGGLTVAAFlleslfqYL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 716 QGFTFGKAGEILTTRLRSMAFKAMLRQDMSWFDDHknSTGALSTRLATDAAQVQGATGTRLALIAQNTANLGTGIIISFI 795
Cdd:cd18565 74 SGVLWRRFAQRVQHDLRTDTYDHVQRLDMAFFEDR--QTGDLMSVLNNDVNQLERFLDDGANSIIRVVVTVLGIGAILFY 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 796 YGWQLTLLLLSVVPFIAVAGIVEMKMLagnAKRDKKEMEAAGKIAT---EAIENIRTVVSLTQERkFESMYVEKLHGPYR 872
Cdd:cd18565 152 LNWQLALVALLPVPLIIAGTYWFQRRI---EPRYRAVREAVGDLNArleNNLSGIAVIKAFTAED-FERERVADASEEYR 227
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 568932737 873 NSVRKAHIYGITFsisQAFMYF----SYAGCFRFGSYLIVNGHMRF 914
Cdd:cd18565 228 DANWRAIRLRAAF---FPVIRLvagaGFVATFVVGGYWVLDGPPLF 270
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
355-561 |
1.43e-13 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 72.04 E-value: 1.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 355 ILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDP----TEGKISIDGQDIRNFNVRclREIIGVVSQ------EPV 424
Cdd:PRK10418 18 LVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGKPVAPCALR--GRKIATIMQnprsafNPL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 425 LFSTTIAENIRYGRGNVTMDEIEKAVKEANAYDFIMKLPQKFdtlvgdrGAQLSGGQKQRIAIARALVRNPKILLLDEAT 504
Cdd:PRK10418 96 HTMHTHARETCLALGKPADDATLTAALEAVGLENAARVLKLY-------PFEMSGGMLQRMMIALALLCEAPFIIADEPT 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 505 SALDTESEAEVQAALDK--AREGRTTIVIAHRLSTI-RNADVIAGFEDGVIVEQGSHSEL 561
Cdd:PRK10418 169 TDLDVVAQARILDLLESivQKRALGMLLVTHDMGVVaRLADDVAVMSHGRIVEQGDVETL 228
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
1-276 |
1.54e-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: 1.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1 MFLGTLMAIAHGSGLPLMMIVFGEMTDKFVDNTGNfSLPVNFSlsmlnpgrileeEMTRYAYYYSGLGGGVLVAAYIQVS 80
Cdd:cd18547 1 LILVIILAIISTLLSVLGPYLLGKAIDLIIEGLGG-GGGVDFS------------GLLRILLLLLGLYLLSALFSYLQNR 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 81 FWTLAAGRQIKKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDDVSKISEGIGDKVGMFFQAIATFFAGFIVGFIRGWKL 160
Cdd:cd18547 68 LMARVSQRTVYDLRKDLFEKLQRLPLSYFDTHSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPLL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 161 TLVIMAISPILGLSTAVWAKILSTFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKELERYQKHLENAKKIGIKKAIS 240
Cdd:cd18547 148 TLIVLVTVPLSLLVTKFIAKRSQKYFRKQQKALGELNGYIEEMISGQKVVKAFNREEEAIEEFDEINEELYKASFKAQFY 227
|
250 260 270
....*....|....*....|....*....|....*.
gi 568932737 241 ANISMGIAFLLIYASYALAFWYGSTLVISKEYTIGN 276
Cdd:cd18547 228 SGLLMPIMNFINNLGYVLVAVVGGLLVINGALTVGV 263
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
655-912 |
1.78e-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: 72.44 E-value: 1.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 655 FVVGTVCAIANGALQPAFSIILSEMI-AIFGP--GDDAVKQQKCNMFSLVFLGLGVLSFFTFFLQGFTFGKAGEILTTRL 731
Cdd:cd18547 1 LILVIILAIISTLLSVLGPYLLGKAIdLIIEGlgGGGGVDFSGLLRILLLLLGLYLLSALFSYLQNRLMARVSQRTVYDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 732 RSMAFKAMLRQDMSWFDdhKNSTGALSTRLATDAAQVQGATGTRLALIAQNTANLGTGIIISFIYGWQLTLLLLSVVPFI 811
Cdd:cd18547 81 RKDLFEKLQRLPLSYFD--THSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPLLTLIVLVTVPLS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 812 AVAgiveMKMLAGNAKRD-KKEMEAAGKI---ATEAIENIRTVVSLTQERKFESMYvEKLHGPYRNSVRKAHIY-GITFS 886
Cdd:cd18547 159 LLV----TKFIAKRSQKYfRKQQKALGELngyIEEMISGQKVVKAFNREEEAIEEF-DEINEELYKASFKAQFYsGLLMP 233
|
250 260
....*....|....*....|....*.
gi 568932737 887 ISQAFMYFSYAGCFRFGSYLIVNGHM 912
Cdd:cd18547 234 IMNFINNLGYVLVAVVGGLLVINGAL 259
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
55-502 |
1.96e-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: 1.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 55 EEMTRYAYYYSGLGGGVLVAAYI-QVSFWTLAAgRQIKKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDDVSKISEgig 133
Cdd:COG4615 45 AALARLLLLFAGLLVLLLLSRLAsQLLLTRLGQ-HAVARLRLRLSRRILAAPLERLERIGAARLLAALTEDVRTISQ--- 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 134 dkvgmFFQAIATFFAGFIVGFirgwkLTLVIMA-ISPILGLSTAVWAKILSTF---SDKELAAYAKAGAVAEEAL-GAIR 208
Cdd:COG4615 121 -----AFVRLPELLQSVALVL-----GCLAYLAwLSPPLFLLTLVLLGLGVAGyrlLVRRARRHLRRAREAEDRLfKHFR 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 209 TVIafGGqNKEL------------ERYQKHLENAKKIGIKKAISANISMGIAFLLIYASYALAFWYGSTLV-ISKEYTIG 275
Cdd:COG4615 191 ALL--EG-FKELklnrrrrraffdEDLQPTAERYRDLRIRADTIFALANNWGNLLFFALIGLILFLLPALGwADPAVLSG 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 276 NAMTVFFsiLIGAfsVGQAAPCIDAFANARGAAyvifdiidnnPKIDSFSERGHKPDNIKGN------------LEFSDV 343
Cdd:COG4615 268 FVLVLLF--LRGP--LSQLVGALPTLSRANVAL----------RKIEELELALAAAEPAAADaaappapadfqtLELRGV 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 344 HFSYPSRANIK--ILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLREIIGVVSQ 421
Cdd:COG4615 334 TYRYPGEDGDEgfTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQLFSAVFS 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 422 EPVLFSTTiaenirYGRGNVTMDEiekavkEANAYDFIMKLPQK-------FDTLvgdrgaQLSGGQKQRIAIARALVRN 494
Cdd:COG4615 414 DFHLFDRL------LGLDGEADPA------RARELLERLELDHKvsvedgrFSTT------DLSQGQRKRLALLVALLED 475
|
....*...
gi 568932737 495 PKILLLDE 502
Cdd:COG4615 476 RPILVFDE 483
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
337-563 |
2.05e-13 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 72.85 E-value: 2.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 337 NLEFSDVHF---SYPSRANIKIlkglNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYD-P---TEGKISIDGQDIRNFNV 409
Cdd:PRK11022 5 NVDKLSVHFgdeSAPFRAVDRI----SYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDyPgrvMAEKLEFNGQDLQRISE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 410 RCLREIIG----VVSQEPVlfsTTIaeNIRYGRGNVTMDEIE------KAVKEANAYDFImklpqkfdTLVG--DRGA-- 475
Cdd:PRK11022 81 KERRNLVGaevaMIFQDPM---TSL--NPCYTVGFQIMEAIKvhqggnKKTRRQRAIDLL--------NQVGipDPASrl 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 476 -----QLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALD--KAREGRTTIVIAHRLSTI-RNADVIAGF 547
Cdd:PRK11022 148 dvyphQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLelQQKENMALVLITHDLALVaEAAHKIIVM 227
|
250
....*....|....*.
gi 568932737 548 EDGVIVEQGSHSELMK 563
Cdd:PRK11022 228 YAGQVVETGKAHDIFR 243
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
991-1198 |
2.41e-13 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 71.27 E-value: 2.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 991 ANVPVLQGLSLEVKKGQTLALVGSSGCGKS----TVVQLLERFYDPMAGSVLLDGQ--EAKKLN---------------- 1048
Cdd:PRK10418 14 AAQPLVHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDGKpvAPCALRgrkiatimqnprsafn 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1049 -VQWLRA-------QLGIVSQEPILFDCsiAENIAYGDNSRVvphdeivraakeANIHPFietlpqkyntrvgdkgtQLS 1120
Cdd:PRK10418 94 pLHTMHTharetclALGKPADDATLTAA--LEAVGLENAARV------------LKLYPF-----------------EMS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1121 GGQKQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLSTIQN-ADLIVVIENGKVKEH 1197
Cdd:PRK10418 143 GGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESivQKRALGMLLVTHDMGVVARlADDVAVMSHGRIVEQ 222
|
.
gi 568932737 1198 G 1198
Cdd:PRK10418 223 G 223
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
356-538 |
3.12e-13 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 71.45 E-value: 3.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 356 LKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRnfnvRCLRE-IIGVVSQEPVL---FSTTIA 431
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTR----QALQKnLVAYVPQSEEVdwsFPVLVE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 432 ENIRYGR-GNVTMDEIEKA-----VKEANAYDFIMKLPQKfdtlvgdRGAQLSGGQKQRIAIARALVRNPKILLLDEATS 505
Cdd:PRK15056 99 DVVMMGRyGHMGWLRRAKKrdrqiVTAALARVDMVEFRHR-------QIGELSGGQKKRVFLARAIAQQGQVILLDEPFT 171
|
170 180 190
....*....|....*....|....*....|....
gi 568932737 506 ALDTESEAEVQAALDKAR-EGRTTIVIAHRLSTI 538
Cdd:PRK15056 172 GVDVKTEARIISLLRELRdEGKTMLVSTHNLGSV 205
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
338-564 |
4.87e-13 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 70.21 E-value: 4.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 338 LEFSDVHFSYPSRAnikILKGLNLKVKSGQTVALVGNSGCGKSTTVQLL--QRLYDPTEGKISIDGQDIRNFN------- 408
Cdd:PRK09580 2 LSIKDLHVSVEDKA---ILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLagREDYEVTGGTVEFKGKDLLELSpedrage 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 409 -----VRCLREIIGVVSQepvLFSTTIAENIRYGRGNVTMDEIEKAvkeanayDFI------MKLPQkfDTLVGDRGAQL 477
Cdd:PRK09580 79 gifmaFQYPVEIPGVSNQ---FFLQTALNAVRSYRGQEPLDRFDFQ-------DLMeekialLKMPE--DLLTRSVNVGF 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 478 SGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKAREG-RTTIVIAH--RLSTIRNADVIAGFEDGVIVE 554
Cdd:PRK09580 147 SGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGkRSFIIVTHyqRILDYIKPDYVHVLYQGRIVK 226
|
250
....*....|
gi 568932737 555 QGSHSeLMKK 564
Cdd:PRK09580 227 SGDFT-LVKQ 235
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
358-556 |
4.94e-13 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 70.40 E-value: 4.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 358 GLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDI--------------RNF-NVRCLREIIGV---- 418
Cdd:PRK11300 23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIeglpghqiarmgvvRTFqHVRLFREMTVIenll 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 419 VSQEPVLFSTTIAenirygrGNVTMDEIEKAvkEANAYDFIMKLPQKFDTL-VGDRGA-QLSGGQKQRIAIARALVRNPK 496
Cdd:PRK11300 103 VAQHQQLKTGLFS-------GLLKTPAFRRA--ESEALDRAATWLERVGLLeHANRQAgNLAYGQQRRLEIARCMVTQPE 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568932737 497 ILLLDEATSALDTESEAEVQAALDKARE--GRTTIVIAHRLStirnadVIAGFEDGVIV-EQG 556
Cdd:PRK11300 174 ILMLDEPAAGLNPKETKELDELIAELRNehNVTVLLIEHDMK------LVMGISDRIYVvNQG 230
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
70-275 |
5.16e-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: 71.00 E-value: 5.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 70 GVLVAAYIQVSF--W------TLAAGRQIKKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDDVSKISEGIGDKVGMFFQ 141
Cdd:cd18563 47 LGLAGAYVLSALlgIlrgrllARLGERITADLRRDLYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDFLSDGLPDFLT 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 142 AIATFFAGFIVGFIRGWKLTLVIMAISPILGLSTAVWAKILSTFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKELE 221
Cdd:cd18563 127 NILMIIGIGVVLFSLNWKLALLVLIPVPLVVWGSYFFWKKIRRLFHRQWRRWSRLNSVLNDTLPGIRVVKAFGQEKREIK 206
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 568932737 222 RYQKHLENAKKIGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTIG 275
Cdd:cd18563 207 RFDEANQELLDANIRAEKLWATFFPLLTFLTSLGTLIVWYFGGRQVLSGTMTLG 260
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
341-538 |
6.14e-13 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 72.84 E-value: 6.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 341 SDVHFSYPSranIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIrNFNV--RCLREIIGV 418
Cdd:PRK10982 2 SNISKSFPG---VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEI-DFKSskEALENGISM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 419 VSQE-PVLFSTTIAENI---RYGRGNVTMDEiEKAVKEANAYdfimklpqkFDTL-----VGDRGAQLSGGQKQRIAIAR 489
Cdd:PRK10982 78 VHQElNLVLQRSVMDNMwlgRYPTKGMFVDQ-DKMYRDTKAI---------FDELdididPRAKVATLSVSQMQMIEIAK 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 568932737 490 ALVRNPKILLLDEATSALdteSEAEVQ---AALDKARE-GRTTIVIAHRLSTI 538
Cdd:PRK10982 148 AFSYNAKIVIMDEPTSSL---TEKEVNhlfTIIRKLKErGCGIVYISHKMEEI 197
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
994-1176 |
6.20e-13 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 69.60 E-value: 6.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 994 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERfydpmagsVLLDGQEAKKLNVQWLraqlgivsqePILFDCSIAEN 1073
Cdd:COG2401 44 YVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAG--------ALKGTPVAGCVDVPDN----------QFGREASLIDA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1074 IA-YGDNSRVVphdEIVRAAKEANihpfietlPQKYNTRVgdkgTQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTE 1152
Cdd:COG2401 106 IGrKGDFKDAV---ELLNAVGLSD--------AVLWLRRF----KELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQ 170
|
170 180
....*....|....*....|....*.
gi 568932737 1153 SEKVVQEALDKA--REGRTCIVIAHR 1176
Cdd:COG2401 171 TAKRVARNLQKLarRAGITLVVATHH 196
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
355-538 |
9.79e-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: 9.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 355 ILKGLNLKVKSGQTVALVGNSGCGKSTtvqLLQRLYDPTEGKISIDGQDIRNFNVR--CLREIIGVVSQEPV-LFSTTIA 431
Cdd:TIGR00956 778 ILNNVDGWVKPGTLTALMGASGAGKTT---LLNVLAERVTTGVITGGDRLVNGRPLdsSFQRSIGYVQQQDLhLPTSTVR 854
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 432 ENIRYGRGNVTMDEIEKavKEANAY-DFIMKL---PQKFDTLVGDRGAQLSGGQKQRIAIARALVRNPKILL-LDEATSA 506
Cdd:TIGR00956 855 ESLRFSAYLRQPKSVSK--SEKMEYvEEVIKLlemESYADAVVGVPGEGLNVEQRKRLTIGVELVAKPKLLLfLDEPTSG 932
|
170 180 190
....*....|....*....|....*....|...
gi 568932737 507 LDTESEAEVQAALDK-AREGRTTIVIAHRLSTI 538
Cdd:TIGR00956 933 LDSQTAWSICKLMRKlADHGQAILCTIHQPSAI 965
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
655-918 |
1.01e-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: 1.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 655 FVVGTVCAIANGALQPAFSIILSEMIaifgpgDDAVKQQKCNMFSLVFLGLGVLSFFTFFLQgFTFGKAGEILTTR---- 730
Cdd:cd18549 4 FFLDLFCAVLIAALDLVFPLIVRYII------DDLLPSKNLRLILIIGAILLALYILRTLLN-YFVTYWGHVMGARietd 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 731 LRSMAFKAMLRQDMSWFDDHKnsTGALSTRLATDAAQVqgatgTRLA-------LIAqnTANLGTGIIISFIYGWQLTLL 803
Cdd:cd18549 77 MRRDLFEHLQKLSFSFFDNNK--TGQLMSRITNDLFDI-----SELAhhgpedlFIS--IITIIGSFIILLTINVPLTLI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 804 LLSVVPFIAVAGIVEMKMLAGNAKRDKKEMeaaGKI---ATEAIENIRTVVSLTQE----RKFESMYVEklhgpYRNSVR 876
Cdd:cd18549 148 VFALLPLMIIFTIYFNKKMKKAFRRVREKI---GEInaqLEDSLSGIRVVKAFANEeyeiEKFDEGNDR-----FLESKK 219
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 568932737 877 KAHIY-GITFSISQAFMYFSYAGCFRFGSYLIVNGHMRFKDVI 918
Cdd:cd18549 220 KAYKAmAYFFSGMNFFTNLLNLVVLVAGGYFIIKGEITLGDLV 262
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
354-557 |
1.26e-12 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 69.27 E-value: 1.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 354 KILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLY--DPT-EGKISIDGQDIRNF-----NVRCLREIIGVVSQEPVL 425
Cdd:PRK09984 18 QALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgDKSaGSHIELLGRTVQREgrlarDIRKSRANTGYIFQQFNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 426 FST-TIAENIRYGRGNVT------MDEIEKAVKEaNAYDFIMKLPQKFdtLVGDRGAQLSGGQKQRIAIARALVRNPKIL 498
Cdd:PRK09984 98 VNRlSVLENVLIGALGSTpfwrtcFSWFTREQKQ-RALQALTRVGMVH--FAHQRVSTLSGGQQQRVAIARALMQQAKVI 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568932737 499 LLDEATSALDTESEAEVQAALD--KAREGRTTIVIAHRLS-TIRNADVIAGFEDGVIVEQGS 557
Cdd:PRK09984 175 LADEPIASLDPESARIVMDTLRdiNQNDGITVVVTLHQVDyALRYCERIVALRQGHVFYDGS 236
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
351-539 |
1.96e-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: 1.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 351 ANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQ--------RLYDPTEGKISIDGQDiRNFNVRCLREiigvvsqe 422
Cdd:TIGR00954 463 NGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGelwpvyggRLTKPAKGKLFYVPQR-PYMTLGTLRD-------- 533
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 423 PVLFSTTIAENIRYGRGNVTMDEIEKAVKeanaYDFIMKLPQKFDTlVGDRGAQLSGGQKQRIAIARALVRNPKILLLDE 502
Cdd:TIGR00954 534 QIIYPDSSEDMKRRGLSDKDLEQILDNVQ----LTHILEREGGWSA-VQDWMDVLSGGEKQRIAMARLFYHKPQFAILDE 608
|
170 180 190
....*....|....*....|....*....|....*...
gi 568932737 503 ATSALDTESEaevQAALDKARE-GRTTIVIAHRLSTIR 539
Cdd:TIGR00954 609 CTSAVSVDVE---GYMYRLCREfGITLFSVSHRKSLWK 643
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
353-530 |
1.98e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 69.73 E-value: 1.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 353 IKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDI---RNFNVRclreIIGVV----SQ---- 421
Cdd:COG4586 35 VEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPfkrRKEFAR----RIGVVfgqrSQlwwd 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 422 EPVLFSTTIAENIrYGrgnVTMDEIEKAVKEanaYDFIMKLPQKFDTLVgdRgaQLSGGQKQRIAIARALVRNPKILLLD 501
Cdd:COG4586 111 LPAIDSFRLLKAI-YR---IPDAEYKKRLDE---LVELLDLGELLDTPV--R--QLSLGQRMRCELAAALLHRPKILFLD 179
|
170 180 190
....*....|....*....|....*....|
gi 568932737 502 EATSALDTESEAEVQAALDK-AREGRTTIV 530
Cdd:COG4586 180 EPTIGLDVVSKEAIREFLKEyNRERGTTIL 209
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
366-556 |
2.25e-12 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 68.41 E-value: 2.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 366 GQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLREII---------GVVSQEP-------VLFSTT 429
Cdd:PRK11701 32 GEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALSEAErrrllrtewGFVHQHPrdglrmqVSAGGN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 430 IAENI------RYGRGNVT----MDEIEKAVkeanayDFIMKLPQKFdtlvgdrgaqlSGGQKQRIAIARALVRNPKILL 499
Cdd:PRK11701 112 IGERLmavgarHYGDIRATagdwLERVEIDA------ARIDDLPTTF-----------SGGMQQRLQIARNLVTHPRLVF 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568932737 500 LDEATSALDTeseaEVQAA-LDKARE-----GRTTIVIAHRLSTIRN-ADVIAGFEDGVIVEQG 556
Cdd:PRK11701 175 MDEPTGGLDV----SVQARlLDLLRGlvrelGLAVVIVTHDLAVARLlAHRLLVMKQGRVVESG 234
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
358-533 |
2.61e-12 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 67.14 E-value: 2.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 358 GLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRnfnvRClREII-----------GVvsqEPVLf 426
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIR----RQ-RDEYhqdllylghqpGI---KTEL- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 427 stTIAENIRY---GRGNVTMDEIEKAvkeanaydfimkLPQkfdtlVGDRG------AQLSGGQKQRIAIARALVRNPKI 497
Cdd:PRK13538 90 --TALENLRFyqrLHGPGDDEALWEA------------LAQ-----VGLAGfedvpvRQLSAGQQRRVALARLWLTRAPL 150
|
170 180 190
....*....|....*....|....*....|....*..
gi 568932737 498 LLLDEATSALDTESEAEVQAALDK-AREGRTTIVIAH 533
Cdd:PRK13538 151 WILDEPFTAIDKQGVARLEALLAQhAEQGGMVILTTH 187
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
1005-1186 |
2.94e-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: 2.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1005 KGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVlldgqeakklnvqwlraqlgivsqepILFDCSIAeniaygdnsrvvp 1084
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGV--------------------------IYIDGEDI------------- 41
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1085 hdeivraakeanihpFIETLPQKYNTRVGDKGTQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEALD-- 1162
Cdd:smart00382 42 ---------------LEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElr 106
|
170 180
....*....|....*....|....*....
gi 568932737 1163 -----KAREGRTCIVIAHRLSTIQNADLI 1186
Cdd:smart00382 107 lllllKSEKNLTVILTTNDEKDLGPALLR 135
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
992-1199 |
5.22e-12 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 67.36 E-value: 5.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 992 NVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERF--YDPMAGSVLLDGQEAKKLNVQwLRAQLGI----------- 1058
Cdd:CHL00131 19 ENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHpaYKILEGDILFKGESILDLEPE-ERAHLGIflafqypieip 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1059 -VSQEPILfdcsiaeNIAYgdNSRvvphdEIVRAAKEANIHPFIETLPQKYNTrVGDKGTQL--------SGGQKQRIAI 1129
Cdd:CHL00131 98 gVSNADFL-------RLAY--NSK-----RKFQGLPELDPLEFLEIINEKLKL-VGMDPSFLsrnvnegfSGGEKKRNEI 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568932737 1130 ARALIRQPRVLLLDEATSALDTESEKVVQEALDKAREGRTCIV-IAH--RLSTIQNADLIVVIENGKVKEHGT 1199
Cdd:CHL00131 163 LQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIIlITHyqRLLDYIKPDYVHVMQNGKIIKTGD 235
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
978-1177 |
5.26e-12 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 67.45 E-value: 5.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 978 VTFNEVVFNYPTRAnvpVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQeakklnvqwLRaqLG 1057
Cdd:PRK09544 5 VSLENVSVSFGQRR---VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGK---------LR--IG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1058 IVSQEpILFDCSIAENIaygdnSRV------VPHDEIVRAAKEANIHPFIETLPQKyntrvgdkgtqLSGGQKQRIAIAR 1131
Cdd:PRK09544 71 YVPQK-LYLDTTLPLTV-----NRFlrlrpgTKKEDILPALKRVQAGHLIDAPMQK-----------LSGGETQRVLLAR 133
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 568932737 1132 ALIRQPRVLLLDEATSALDTESEKVVQEALDKAREGRTCIV--IAHRL 1177
Cdd:PRK09544 134 ALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVlmVSHDL 181
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
700-861 |
5.69e-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: 5.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 700 LVFLGLGVLSFFTFFLQGFTFGKAGEILTTRLRSMAFKAMLRQDMSWFDDHKnsTGALSTRLATDAAQVQGATGTRLALI 779
Cdd:cd18564 58 AALVGIALLRGLASYAGTYLTALVGQRVVLDLRRDLFAHLQRLSLSFHDRRR--TGDLLSRLTGDVGAIQDLLVSGVLPL 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 780 AQNTANLGTGIIISFIYGWQLTLLLLSVVPFIAVAGIV---EMKMLAGNAKRDKKEMEAagkIATEAIENIRTVVSLTQE 856
Cdd:cd18564 136 LTNLLTLVGMLGVMFWLDWQLALIALAVAPLLLLAARRfsrRIKEASREQRRREGALAS---VAQESLSAIRVVQAFGRE 212
|
....*
gi 568932737 857 RKFES 861
Cdd:cd18564 213 EHEER 217
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
338-502 |
5.87e-12 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 70.00 E-value: 5.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 338 LEFSDVHFSYPSRANIkiLKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLREIIG 417
Cdd:PRK10522 323 LELRNVTFAYQDNGFS--VGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFS 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 418 VVSQEPVLFSTTIAEnirygrgnvtmdeiEKAVKEANAYDF---IMKLPQKFdTLVGDRGA--QLSGGQKQRIAIARALV 492
Cdd:PRK10522 401 AVFTDFHLFDQLLGP--------------EGKPANPALVEKwleRLKMAHKL-ELEDGRISnlKLSKGQKKRLALLLALA 465
|
170
....*....|
gi 568932737 493 RNPKILLLDE 502
Cdd:PRK10522 466 EERDILLLDE 475
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
995-1209 |
5.91e-12 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 66.84 E-value: 5.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 995 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQwLRAQLGI--VSQEPILFD-CSIA 1071
Cdd:PRK10895 18 VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLH-ARARRGIgyLPQEASIFRrLSVY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1072 ENIA-----YGDNSRVVPHDEIVRAAKEANIHPFIETLpqkyntrvgdkGTQLSGGQKQRIAIARALIRQPRVLLLDEAT 1146
Cdd:PRK10895 97 DNLMavlqiRDDLSAEQREDRANELMEEFHIEHLRDSM-----------GQSLSGGERRRVEIARALAANPKFILLDEPF 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568932737 1147 SALDTESEKVVQEALDKARE-GRTCIVIAHRL-STIQNADLIVVIENGKVKEHGTHQQLLAQKGI 1209
Cdd:PRK10895 166 AGVDPISVIDIKRIIEHLRDsGLGVLITDHNVrETLAVCERAYIVSQGHLIAHGTPTEILQDEHV 230
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
338-564 |
6.17e-12 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 66.97 E-value: 6.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 338 LEFSDVHFSYpsrANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLL--QRLYDPTEGKISIDGQDIRNFN--VRCLR 413
Cdd:CHL00131 8 LEIKNLHASV---NENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIagHPAYKILEGDILFKGESILDLEpeERAHL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 414 ----------EIIGVVSQEpvlFSTTIAENIRYGRGNVTMDEIEkavkeanAYDFIM------KLPQKFDTLVGDRGaqL 477
Cdd:CHL00131 85 giflafqypiEIPGVSNAD---FLRLAYNSKRKFQGLPELDPLE-------FLEIINeklklvGMDPSFLSRNVNEG--F 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 478 SGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDK-AREGRTTIVIAH--RLSTIRNADVIAGFEDGVIVE 554
Cdd:CHL00131 153 SGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKlMTSENSIILITHyqRLLDYIKPDYVHVMQNGKIIK 232
|
250
....*....|
gi 568932737 555 QGShSELMKK 564
Cdd:CHL00131 233 TGD-AELAKE 241
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
328-561 |
6.74e-12 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 67.48 E-value: 6.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 328 GHKPDNIkgnLEFSDVHFSypsRANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNF 407
Cdd:PRK11831 1 EQSVANL---VDMRGVSFT---RGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAM 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 408 NVRCL---REIIGVVSQEPVLFS-TTIAENIRYG-RGNVTMDE--IEKAVkeanaydfIMKLPQkfdtlVGDRGA----- 475
Cdd:PRK11831 75 SRSRLytvRKRMSMLFQSGALFTdMNVFDNVAYPlREHTQLPAplLHSTV--------MMKLEA-----VGLRGAaklmp 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 476 -QLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEA-------EVQAALdkareGRTTIVIAHR----LSTIRNADV 543
Cdd:PRK11831 142 sELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGvlvklisELNSAL-----GVTCVVVSHDvpevLSIADHAYI 216
|
250
....*....|....*...
gi 568932737 544 IAgfeDGVIVEQGSHSEL 561
Cdd:PRK11831 217 VA---DKKIVAHGSAQAL 231
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
87-279 |
1.20e-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: 1.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 87 GRQIKKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDDVSKISEGIGDKVGMFFQAIATFFAGFIVGFIRGWKLTLV-IM 165
Cdd:cd18589 65 SRIHSRLQGLVFAAVLRQEIAFFDSNQTGDIVSRVTTDTEDMSESLSENLSLLMWYLARGLFLFIFMLWLSPKLALLtAL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 166 AISPILGLSTAV--WAKILSTFSDKELAAYAKAGAvaeEALGAIRTVIAFGGQNKELERYQKHLENAKKIGIKKAISANI 243
Cdd:cd18589 145 GLPLLLLVPKFVgkFQQSLAVQVQKSLARANQVAV---ETFSAMKTVRSFANEEGEAQRYRQRLQKTYRLNKKEAAAYAV 221
|
170 180 190
....*....|....*....|....*....|....*....
gi 568932737 244 SM---GIAFLLIYASyalAFWYGSTLVISKEYTIGNAMT 279
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 ... |
91-282 |
1.54e-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: 1.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 91 KKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDdVSKISEGIGDKVGMFFQAIATFFAGFIVGFIRGWKLTLVIMAISPI 170
Cdd:cd18570 75 IRLILGYFKHLLKLPLSFFETRKTGEIISRFND-ANKIREAISSTTISLFLDLLMVIISGIILFFYNWKLFLITLLIIPL 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 171 LGLSTAVWAKILSTFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKELERYQKHLENAKKIGIKKAISANISMGIAFL 250
Cdd:cd18570 154 YILIILLFNKPFKKKNREVMESNAELNSYLIESLKGIETIKSLNAEEQFLKKIEKKFSKLLKKSFKLGKLSNLQSSIKGL 233
|
170 180 190
....*....|....*....|....*....|....*..
gi 568932737 251 LIYASYALAFWYGSTLVISKEYTIG-----NAMTVFF 282
Cdd:cd18570 234 ISLIGSLLILWIGSYLVIKGQLSLGqliafNALLGYF 270
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
983-1206 |
1.54e-11 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 67.06 E-value: 1.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 983 VVFNYPTrANVPVLQGLSLEVKKGQTLALVGSSGCGKS-TVVQLLERFYDP--MAGSVLLDGQE-----AKKLNVqwLRA 1054
Cdd:PRK09473 20 VTFSTPD-GDVTAVNDLNFSLRAGETLGIVGESGSGKSqTAFALMGLLAANgrIGGSATFNGREilnlpEKELNK--LRA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1055 -QLGIVSQEP-----------------ILFDCSIAENIAYGDNSRVVPHDEIVRAAKEANIHPFietlpqkyntrvgdkg 1116
Cdd:PRK09473 97 eQISMIFQDPmtslnpymrvgeqlmevLMLHKGMSKAEAFEESVRMLDAVKMPEARKRMKMYPH---------------- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1117 tQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEALDK-AREGRTCIV-IAHRLSTIQN-ADLIVVIENGK 1193
Cdd:PRK09473 161 -EFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNElKREFNTAIImITHDLGVVAGiCDKVLVMYAGR 239
|
250
....*....|...
gi 568932737 1194 VKEHGTHQQLLAQ 1206
Cdd:PRK09473 240 TMEYGNARDVFYQ 252
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
696-912 |
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 568932737 696 NMFSLVFLGLGVLSFFTFFLQG-----FTFgkAGEILTTRLRSMAFKAMLRQDMSWFDdhKNSTGALSTRLATDAAQVQG 770
Cdd:cd18590 33 NAFTSAIGLMCLFSLGSSLSAGlrgglFMC--TLSRLNLRLRHQLFSSLVQQDIGFFE--KTKTGDLTSRLSTDTTLMSR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 771 ATGTRLALIAQNTANlgTGIIISFIYG--WQLTLLLLSVVPFIAVAgiveMKMLAGNAKRDKKEME----AAGKIATEAI 844
Cdd:cd18590 109 SVALNANVLLRSLVK--TLGMLGFMLSlsWQLTLLTLIEMPLTAIA----QKVYNTYHQKLSQAVQdsiaKAGELAREAV 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568932737 845 ENIRTVVSLTQERKFESMYVEKLHGPYRNSVRKAHIYGITFSISQAFMYFSYAGCFRFGSYLIVNGHM 912
Cdd:cd18590 183 SSIRTVRSFKAEEEEACRYSEALERTYNLKDRRDTVRAVYLLVRRVLQLGVQVLMLYCGRQLIQSGHL 250
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
347-560 |
1.87e-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: 1.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 347 YPSRANIKILKGLNLKVKSG-----QTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDirnfnvrclreiigvVSQ 421
Cdd:cd03237 1 YTYPTMKKTLGEFTLEVEGGsisesEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDT---------------VSY 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 422 EPVLFSTTIAENIRYgrgnvTMDEIEKAVKEANAYDF-IMKlPQKFDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLL 500
Cdd:cd03237 66 KPQYIKADYEGTVRD-----LLSSITKDFYTHPYFKTeIAK-PLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLL 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568932737 501 DEATSALDTESEAEVQAALDKAREG--RTTIVIAHrlsTIRNADVIAgfeDGVIVEQGSHSE 560
Cdd:cd03237 140 DEPSAYLDVEQRLMASKVIRRFAENneKTAFVVEH---DIIMIDYLA---DRLIVFEGEPSV 195
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
990-1199 |
2.00e-11 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 66.00 E-value: 2.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 990 RANVpVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLE-RFYDPMA-------GSVLLDGQEAKKLNVQWL---RAQLGI 1058
Cdd:PRK13547 12 RHRA-ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAgDLTGGGAprgarvtGDVTLNGEPLAAIDAPRLarlRAVLPQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1059 VSQEPILFdcSIAENIAYGDnsrvVPHdeiVRAAKEANIHPFiETLPQKY-----NTRVGDKGTQLSGGQKQRIAIARAL 1133
Cdd:PRK13547 91 AAQPAFAF--SAREIVLLGR----YPH---ARRAGALTHRDG-EIAWQALalagaTALVGRDVTTLSGGELARVQFARVL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568932737 1134 ---------IRQPRVLLLDEATSALD-TESEKVVQEALDKAREGRT-CIVIAHRLS-TIQNADLIVVIENGKVKEHGT 1199
Cdd:PRK13547 161 aqlwpphdaAQPPRYLLLDEPTAALDlAHQHRLLDTVRRLARDWNLgVLAIVHDPNlAARHADRIAMLADGAIVAHGA 238
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
363-536 |
3.09e-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: 3.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 363 VKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKIS--IDGQDIrnfnvrcLREIIGVVSQEpvLFSTTIAENIRYGRGN 440
Cdd:cd03236 23 PREGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFDdpPDWDEI-------LDEFRGSELQN--YFTKLLEGDVKVIVKP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 441 VTMDEIEKAVKeANAYDFIMKLPQ--KFDTLVG--------DRG-AQLSGGQKQRIAIARALVRNPKILLLDEATSALDT 509
Cdd:cd03236 94 QYVDLIPKAVK-GKVGELLKKKDErgKLDELVDqlelrhvlDRNiDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDI 172
|
170 180
....*....|....*....|....*...
gi 568932737 510 ESEAEVQAALDK-AREGRTTIVIAHRLS 536
Cdd:cd03236 173 KQRLNAARLIRElAEDDNYVLVVEHDLA 200
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
977-1180 |
3.23e-11 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 65.29 E-value: 3.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 977 SVTFNEVVFNYptRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQWLRAQL 1056
Cdd:PRK15056 6 GIVVNDVTVTW--RNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNLVAYV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1057 GiVSQE-----PILFDcSIAENIAYGDNS---RVVPHD-EIVRAAKEAnihpfIETLPQKYNtRVGdkgtQLSGGQKQRI 1127
Cdd:PRK15056 84 P-QSEEvdwsfPVLVE-DVVMMGRYGHMGwlrRAKKRDrQIVTAALAR-----VDMVEFRHR-QIG----ELSGGQKKRV 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 568932737 1128 AIARALIRQPRVLLLDEATSALDTESEKVVQEALDKAR-EGRTCIVIAHRLSTI 1180
Cdd:PRK15056 152 FLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRdEGKTMLVSTHNLGSV 205
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
989-1194 |
3.99e-11 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 67.06 E-value: 3.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 989 TRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLN-----------VQWLRAQLG 1057
Cdd:PRK10982 257 TSLRQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNaneainhgfalVTEERRSTG 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1058 IVSQEPILFDCSIAENIAYGDNSRVVPHDEIvraakEANIHPFIETLPQK---YNTRVGdkgtQLSGGQKQRIAIARALI 1134
Cdd:PRK10982 337 IYAYLDIGFNSLISNIRNYKNKVGLLDNSRM-----KSDTQWVIDSMRVKtpgHRTQIG----SLSGGNQQKVIIGRWLL 407
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568932737 1135 RQPRVLLLDEATSALDTESE-KVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVIENGKV 1194
Cdd:PRK10982 408 TQPEILMLDEPTRGIDVGAKfEIYQLIAELAKKDKGIIIISSEMPELLGiTDRILVMSNGLV 469
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
994-1194 |
4.79e-11 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 66.90 E-value: 4.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 994 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLerfydpmAGSVLLDG---QEAKKLNVQWL-----RAQLGIVsqepil 1065
Cdd:PRK11147 17 PLLDNAELHIEDNERVCLVGRNGAGKSTLMKIL-------NGEVLLDDgriIYEQDLIVARLqqdppRNVEGTV------ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1066 FDcSIAENIA--------YGDNSRVVPHDE----IVRAAK-------------EANIHPFIETLPQKYNTRVgdkgTQLS 1120
Cdd:PRK11147 84 YD-FVAEGIEeqaeylkrYHDISHLVETDPseknLNELAKlqeqldhhnlwqlENRINEVLAQLGLDPDAAL----SSLS 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568932737 1121 GGQKQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEALdKAREGrTCIVIAHRLSTIQN-ADLIVVIENGKV 1194
Cdd:PRK11147 159 GGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFL-KTFQG-SIIFISHDRSFIRNmATRIVDLDRGKL 231
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
995-1217 |
5.63e-11 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 66.83 E-value: 5.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 995 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLE-RFY-DPMAGSVLLDGqeaKKLNVQWLRaQLGIVSQEPILF-DCSIA 1071
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAgRIQgNNFTGTILANN---RKPTKQILK-RTGFVTQDDILYpHLTVR 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1072 ENIAYGDNSRV---VPHDEIVRAAkEANIHPFieTLPQKYNTRVGDKGTQ-LSGGQKQRIAIARALIRQPRVLLLDEATS 1147
Cdd:PLN03211 159 ETLVFCSLLRLpksLTKQEKILVA-ESVISEL--GLTKCENTIIGNSFIRgISGGERKRVSIAHEMLINPSLLILDEPTS 235
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568932737 1148 ALD-TESEKVVQEALDKAREGRTCIVIAHRLST--IQNADLIVVIENGKVKEHGTHQQLLAqkgiYFSMVNIQ 1217
Cdd:PLN03211 236 GLDaTAAYRLVLTLGSLAQKGKTIVTSMHQPSSrvYQMFDSVLVLSEGRCLFFGKGSDAMA----YFESVGFS 304
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
988-1194 |
6.23e-11 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 65.11 E-value: 6.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 988 PTRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQWLRaQLGIV----SQep 1063
Cdd:COG4586 30 REYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFKRRKEFAR-RIGVVfgqrSQ-- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1064 ILFDCSIAENIA-----YGdnsrvVPHDEIvraakEANIHPFIETL--PQKYNTRVgdkgTQLSGGQKQRIAIARALIRQ 1136
Cdd:COG4586 107 LWWDLPAIDSFRllkaiYR-----IPDAEY-----KKRLDELVELLdlGELLDTPV----RQLSLGQRMRCELAAALLHR 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568932737 1137 PRVLLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLSTIQN-ADLIVVIENGKV 1194
Cdd:COG4586 173 PKILFLDEPTIGLDVVSKEAIREFLKEynRERGTTILLTSHDMDDIEAlCDRVIVIDHGRI 233
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
999-1205 |
6.37e-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: 6.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 999 LSLEVKKGQTLALVGSSGCGKSTVVQLLERFYD-PMAGSVLLDGQEAKKLN-VQWLRAQLGIVSQEP----ILFDCSIAE 1072
Cdd:TIGR02633 279 VSFSLRRGEILGVAGLVGAGRTELVQALFGAYPgKFEGNVFINGKPVDIRNpAQAIRAGIAMVPEDRkrhgIVPILGVGK 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1073 NIAYGDNSRVVPHDEIVRAAKEANIHPFIETLpqKYNTRVGDKG-TQLSGGQKQRIAIARALIRQPRVLLLDEATSALDT 1151
Cdd:TIGR02633 359 NITLSVLKSFCFKMRIDAAAELQIIGSAIQRL--KVKTASPFLPiGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDV 436
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568932737 1152 ESEKVVQEALDK-AREGRTCIVIAHRLSTIQN-ADLIVVIENGKVK----EHG-THQQLLA 1205
Cdd:TIGR02633 437 GAKYEIYKLINQlAQEGVAIIVVSSELAEVLGlSDRVLVIGEGKLKgdfvNHAlTQEQVLA 497
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
978-1178 |
6.43e-11 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 66.70 E-value: 6.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 978 VTFNEVVF-NYP--TRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYdPMAGSVLLDGQEAKklnvqwlra 1054
Cdd:TIGR00954 447 YQDNGIKFeNIPlvTPNGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELW-PVYGGRLTKPAKGK--------- 516
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1055 qLGIVSQEPILFDCSIAENIAYGDNSrvvpHDEIVRAAKEANIHPFIETLPQKYN-TR------VGDKGTQLSGGQKQRI 1127
Cdd:TIGR00954 517 -LFYVPQRPYMTLGTLRDQIIYPDSS----EDMKRRGLSDKDLEQILDNVQLTHIlEReggwsaVQDWMDVLSGGEKQRI 591
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 568932737 1128 AIARALIRQPRVLLLDEATSALDTESEKVVQEALDKAreGRTCIVIAHRLS 1178
Cdd:TIGR00954 592 AMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCREF--GITLFSVSHRKS 640
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
997-1175 |
8.21e-11 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 62.90 E-value: 8.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 997 QGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKL------NVQWLRAQLGIVS----QEPILF 1066
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQrdeyhqDLLYLGHQPGIKTeltaLENLRF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1067 DCSIAEniaygdnsrvVPHDEIVRAAKEA-NIHPFiETLPQKyntrvgdkgtQLSGGQKQRIAIARALIRQPRVLLLDEA 1145
Cdd:PRK13538 98 YQRLHG----------PGDDEALWEALAQvGLAGF-EDVPVR----------QLSAGQQRRVALARLWLTRAPLWILDEP 156
|
170 180 190
....*....|....*....|....*....|.
gi 568932737 1146 TSALDTESEKVVQEALDK-AREGRTCIVIAH 1175
Cdd:PRK13538 157 FTAIDKQGVARLEALLAQhAEQGGMVILTTH 187
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
700-918 |
8.76e-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: 64.34 E-value: 8.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 700 LVFLGLGVLSFFTFFLQGFTFGKAGEILTTRLRSMAFKAMLRQDMSWFDdhKNSTGALSTRLATDAAQVQGA--TGTRLA 777
Cdd:cd18548 43 LLMLLLALLGLIAGILAGYFAAKASQGFGRDLRKDLFEKIQSFSFAEID--KFGTSSLITRLTNDVTQVQNFvmMLLRML 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 778 LIAqnTANLGTGIIISFIYGWQLTLLLLSVVPFIAVAGIVEMKMLAGNAKRDKKEMEAAGKIATEAIENIRTVVSLTQE- 856
Cdd:cd18548 121 VRA--PIMLIGAIIMAFRINPKLALILLVAIPILALVVFLIMKKAIPLFKKVQKKLDRLNRVVRENLTGIRVIRAFNREd 198
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568932737 857 ---RKFESMyVEKLhgpYRNSVRKAHIYGITFSISQAFMYFSYAGCFRFGSYLIVNGHMRFKDVI 918
Cdd:cd18548 199 yeeERFDKA-NDDL---TDTSLKAGRLMALLNPLMMLIMNLAIVAILWFGGHLINAGSLQVGDLV 259
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
993-1193 |
1.48e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 65.14 E-value: 1.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 993 VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAK-KLNVQWLRAQLGIVSQE-PILFDCSI 1070
Cdd:PRK10982 11 VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfKSSKEALENGISMVHQElNLVLQRSV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1071 AENIAYGDNSR---VVPHDEIVRAAKEanihpFIETLPQKYNTRvgDKGTQLSGGQKQRIAIARALIRQPRVLLLDEATS 1147
Cdd:PRK10982 91 MDNMWLGRYPTkgmFVDQDKMYRDTKA-----IFDELDIDIDPR--AKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTS 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 568932737 1148 ALdteSEKVVQ---EALDKAREgRTC--IVIAHRLSTI-QNADLIVVIENGK 1193
Cdd:PRK10982 164 SL---TEKEVNhlfTIIRKLKE-RGCgiVYISHKMEEIfQLCDEITILRDGQ 211
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
982-1184 |
1.83e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 61.89 E-value: 1.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 982 EVVFNYPTRanvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQWlRAQLGIVSQ 1061
Cdd:PRK13540 6 ELDFDYHDQ---PLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTY-QKQLCFVGH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1062 EP-ILFDCSIAENIAYG--DNSRVVPHDEIVRAAKEANIHPFIETLpqkyntrvgdkgtqLSGGQKQRIAIARALIRQPR 1138
Cdd:PRK13540 82 RSgINPYLTLRENCLYDihFSPGAVGITELCRLFSLEHLIDYPCGL--------------LSSGQKRQVALLRLWMSKAK 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 568932737 1139 VLLLDEATSALDTESEKVVQEALDKAR-EGRTCIVIAHRLSTIQNAD 1184
Cdd:PRK13540 148 LWLLDEPLVALDELSLLTIITKIQEHRaKGGAVLLTSHQDLPLNKAD 194
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
57-275 |
1.94e-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: 1.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 57 MTRYAYYYSGLGGGVLVAAYIQVSFWTLAAGRQIKKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDDVSKISEGIGDKV 136
Cdd:cd18545 39 LLIIALLFLALNLVNWVASRLRIYLMAKVGQRILYDLRQDLFSHLQKLSFSFFDSRPVGKILSRVINDVNSLSDLLSNGL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 137 GMFFQAIATFFAGFIVGFIRGWKLTLVIMAISPILGLSTAVWAKILSTFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQ 216
Cdd:cd18545 119 INLIPDLLTLVGIVIIMFSLNVRLALVTLAVLPLLVLVVFLLRRRARKAWQRVRKKISNLNAYLHESISGIRVIQSFARE 198
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 217 NKELERYQKHLENAKKIGIkKAISANISMGIAFLLIYA-SYALAFWYGSTLVISKEYTIG 275
Cdd:cd18545 199 DENEEIFDELNRENRKANM-RAVRLNALFWPLVELISAlGTALVYWYGGKLVLGGAITVG 257
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
671-912 |
2.16e-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: 63.23 E-value: 2.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 671 AFSIILSEMIAIFGPG---------DDAVKQQKCNMFSLVFLGLGVLSFFTF---FLQGFTFGKAGEILTTRLRSMAFKA 738
Cdd:cd18570 5 ILILLLSLLITLLGIAgsfffqiliDDIIPSGDINLLNIISIGLILLYLFQSllsYIRSYLLLKLSQKLDIRLILGYFKH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 739 MLRQDMSWFDDHKnsTGALSTRLaTDAAQVQGA-TGTRLALIAQNTANLGTGIIIsFIYGWQLTLLLLSVVPFIAVAGIV 817
Cdd:cd18570 85 LLKLPLSFFETRK--TGEIISRF-NDANKIREAiSSTTISLFLDLLMVIISGIIL-FFYNWKLFLITLLIIPLYILIILL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 818 EMKMLagnAKRDKKEMEAAGKIAT---EAIENIRTVVSLTQERKFesmyVEKLHGPYRNSVRKAHIYGITFSISQAFM-- 892
Cdd:cd18570 161 FNKPF---KKKNREVMESNAELNSyliESLKGIETIKSLNAEEQF----LKKIEKKFSKLLKKSFKLGKLSNLQSSIKgl 233
|
250 260
....*....|....*....|..
gi 568932737 893 --YFSYAGCFRFGSYLIVNGHM 912
Cdd:cd18570 234 isLIGSLLILWIGSYLVIKGQL 255
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
999-1204 |
2.46e-10 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 62.26 E-value: 2.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 999 LSLEVKKGQTLALVGSSGCGKSTvvqLLERfydpMAG------SVLLDGQ-----EAKKLNVQwlRAQLgiVSQEPILF- 1066
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKST---LLAR----MAGllpgsgSIQFAGQpleawSAAELARH--RAYL--SQQQTPPFa 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1067 -------DCSIAENIAYGDNSRVVphDEIVRAAKeanihpfietLPQKYNTRVGdkgtQLSGGQKQRIAIArALIRQ--- 1136
Cdd:PRK03695 84 mpvfqylTLHQPDKTRTEAVASAL--NEVAEALG----------LDDKLGRSVN----QLSGGEWQRVRLA-AVVLQvwp 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1137 ---P--RVLLLDEATSALDtesekVVQE-ALDK-----AREGRTCIVIAHRLS-TIQNADLIVVIENGKVKEHGTHQQLL 1204
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 ... |
354-533 |
2.61e-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: 64.57 E-value: 2.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 354 KILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDgQDIRnfnvrclreiIGVVSQEPVLFST-TIAE 432
Cdd:TIGR03719 19 EILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQ-PGIK----------VGYLPQEPQLDPTkTVRE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 433 NI-------------------RYGRGNVTMD-------EIEKAVKEANAYDFIMKLPQKFDTL---VGD-RGAQLSGGQK 482
Cdd:TIGR03719 88 NVeegvaeikdaldrfneisaKYAEPDADFDklaaeqaELQEIIDAADAWDLDSQLEIAMDALrcpPWDaDVTKLSGGER 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 568932737 483 QRIAIARALVRNPKILLLDEATSALDTESEAEVQAALdKAREGrTTIVIAH 533
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 ... |
976-1192 |
3.25e-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: 3.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 976 GSVTFNEVVFNYPT-RANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLL-ERFYD-PMAGSVLLDGQEAKKLnvqwL 1052
Cdd:cd03232 2 SVLTWKNLNYTVPVkGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLaGRKTAgVITGEILINGRPLDKN----F 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1053 RAQLGIVSQEPILFDCSiaeniaygdnsrvvphdeIVRaakeanihpfiETLPQKYNTRvgdkgtQLSGGQKQRIAIARA 1132
Cdd:cd03232 78 QRSTGYVEQQDVHSPNL------------------TVR-----------EALRFSALLR------GLSVEQRKRLTIGVE 122
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568932737 1133 LIRQPRVLLLDEATSALDTESEKVVQEALDK-AREGRTCIVIAHRLS--TIQNADLIVVIENG 1192
Cdd:cd03232 123 LAAKPSILFLDEPTSGLDSQAAYNIVRFLKKlADSGQAILCTIHQPSasIFEKFDRLLLLKRG 185
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
338-542 |
3.58e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 60.73 E-value: 3.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 338 LEFSDVHFSYPSRAnikILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLREIIG 417
Cdd:PRK13540 2 LDVIELDFDYHDQP---LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 418 VVSQEPVLFSTTIAEN----IRYGRGNVTMDEIEKAVKEANAYDFIMKLpqkfdtlvgdrgaqLSGGQKQRIAIARALVR 493
Cdd:PRK13540 79 VGHRSGINPYLTLRENclydIHFSPGAVGITELCRLFSLEHLIDYPCGL--------------LSSGQKRQVALLRLWMS 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 568932737 494 NPKILLLDEATSALDTESEAEVQAALDKAR-EGRTTIVIAHRLSTIRNAD 542
Cdd:PRK13540 145 KAKLWLLDEPLVALDELSLLTIITKIQEHRaKGGAVLLTSHQDLPLNKAD 194
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
977-1199 |
4.30e-10 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 62.84 E-value: 4.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 977 SVTFNEVvfNYPTRAnvpvLQGLSLEVKKGQTLALVGSSGCGKS----TVVQLLERFYDPMAGSVLLDGQEAKKLNVQWL 1052
Cdd:PRK11022 10 SVHFGDE--SAPFRA----VDRISYSVKQGEVVGIVGESGSGKSvsslAIMGLIDYPGRVMAEKLEFNGQDLQRISEKER 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1053 R----AQLGIVSQEPI--LFDC-----SIAENI-AYGDNSRVVPHDEIVRAAKEANIHPfietlPQkynTRVGDKGTQLS 1120
Cdd:PRK11022 84 RnlvgAEVAMIFQDPMtsLNPCytvgfQIMEAIkVHQGGNKKTRRQRAIDLLNQVGIPD-----PA---SRLDVYPHQLS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1121 GGQKQRIAIARALIRQPRVLLLDEATSALD-TESEKVVQEALD-KAREGRTCIVIAHRLSTI-QNADLIVVIENGKVKEH 1197
Cdd:PRK11022 156 GGMSQRVMIAMAIACRPKLLIADEPTTALDvTIQAQIIELLLElQQKENMALVLITHDLALVaEAAHKIIVMYAGQVVET 235
|
..
gi 568932737 1198 GT 1199
Cdd:PRK11022 236 GK 237
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
982-1205 |
4.35e-10 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 63.79 E-value: 4.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 982 EVVF---NY----PTRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPM-AGSVLLDGQEAKKLN-VQWL 1052
Cdd:PRK13549 257 EVILevrNLtawdPVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPGRwEGEIFIDGKPVKIRNpQQAI 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1053 RAQLGIVSQEP----ILFDCSIAENIAYGDNSRVVPHDEIVRAAKEANIHPFIETLPQKYNT---RVGdkgtQLSGGQKQ 1125
Cdd:PRK13549 337 AQGIAMVPEDRkrdgIVPVMGVGKNITLAALDRFTGGSRIDDAAELKTILESIQRLKVKTASpelAIA----RLSGGNQQ 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1126 RIAIARALIRQPRVLLLDEATSALDT----ESEKVVQEAldkAREGRTCIVIAHRLSTIQN-ADLIVVIENGKVK----- 1195
Cdd:PRK13549 413 KAVLAKCLLLNPKILILDEPTRGIDVgakyEIYKLINQL---VQQGVAIIVISSELPEVLGlSDRVLVMHEGKLKgdlin 489
|
250
....*....|
gi 568932737 1196 EHGTHQQLLA 1205
Cdd:PRK13549 490 HNLTQEQVME 499
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
697-912 |
6.76e-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: 6.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 697 MFSLVFLGLGVLSFFTFFLQGFTFGKAGEILTTRLRSMAFKAMLRQDMSWFDdhKNSTGALSTRLATDAAQVQG-ATGTR 775
Cdd:cd18563 44 LLVLGLAGAYVLSALLGILRGRLLARLGERITADLRRDLYEHLQRLSLSFFD--KRQTGSLMSRVTSDTDRLQDfLSDGL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 776 LALIAQNTANLGTGIIIsFIYGWQLTLLLLSVVPFIAVAGIVEMKML-AGNAKRDKKEMEAAGKIAtEAIENIRTVVSLT 854
Cdd:cd18563 122 PDFLTNILMIIGIGVVL-FSLNWKLALLVLIPVPLVVWGSYFFWKKIrRLFHRQWRRWSRLNSVLN-DTLPGIRVVKAFG 199
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568932737 855 QErKFESMYVEKLHGPYRNSVRKAH--------IYGITFSISQAFMYFsyagcfrFGSYLIVNGHM 912
Cdd:cd18563 200 QE-KREIKRFDEANQELLDANIRAEklwatffpLLTFLTSLGTLIVWY-------FGGRQVLSGTM 257
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
329-553 |
6.94e-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: 6.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 329 HKPDNIKGN-LEFSDVHFSYPSRANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPT-EGKISIDGQ--DI 404
Cdd:TIGR02633 248 HEPHEIGDViLEARNLTCWDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKpvDI 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 405 RNfnvrCLREII-------------GVVSQEPVLFSTTIAENIRY-GRGNVTMDEIEKAVKEAnaydfIMKLpqKFDTLV 470
Cdd:TIGR02633 328 RN----PAQAIRagiamvpedrkrhGIVPILGVGKNITLSVLKSFcFKMRIDAAAELQIIGSA-----IQRL--KVKTAS 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 471 GDRG-AQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDK-AREGRTTIVIAHRLstirnADVIaGFE 548
Cdd:TIGR02633 397 PFLPiGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQlAQEGVAIIVVSSEL-----AEVL-GLS 470
|
....*
gi 568932737 549 DGVIV 553
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 ... |
699-912 |
1.26e-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: 1.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 699 SLVFLGLGVLSFFTFFLQGFTFGKAGEILTTRLRSMAFKAMLRQDMSWFDDHKnsTGALSTRLATDAAQVQGATGTRLAL 778
Cdd:cd18546 42 AAAYLAVVLAGWVAQRAQTRLTGRTGERLLYDLRLRVFAHLQRLSLDFHERET--SGRIMTRMTSDIDALSELLQTGLVQ 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 779 IAQNTANLGTGIIISFIYGWQLTLLLLSVVPFIAVAGIVEMKmLAGNAKRDKKEmEAAGKIAT--EAIENIRTVVSLTQE 856
Cdd:cd18546 120 LVVSLLTLVGIAVVLLVLDPRLALVALAALPPLALATRWFRR-RSSRAYRRARE-RIAAVNADlqETLAGIRVVQAFRRE 197
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 857 RKFESMYVEkLHGPYRNSVRKAHIYgitFSISQAFMYF----SYAGCFRFGSYLIVNGHM 912
Cdd:cd18546 198 RRNAERFAE-LSDDYRDARLRAQRL---VAIYFPGVELlgnlATAAVLLVGAWRVAAGTL 253
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
348-535 |
1.28e-09 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 62.25 E-value: 1.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 348 PSRANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYD-PTEGKISIDGQ--DIRNfnvrCLREI---IGVVSQ 421
Cdd:PRK13549 270 PVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGKpvKIRN----PQQAIaqgIAMVPE 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 422 E-------PVLfstTIAENI------RYGRGNVtmdeIEKAVKEANAYDFIMKLPQKFDTLVGdRGAQLSGGQKQRIAIA 488
Cdd:PRK13549 346 DrkrdgivPVM---GVGKNItlaaldRFTGGSR----IDDAAELKTILESIQRLKVKTASPEL-AIARLSGGNQQKAVLA 417
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 568932737 489 RALVRNPKILLLDEATSALDTESEAEVQAALDK-AREGRTTIVIAHRL 535
Cdd:PRK13549 418 KCLLLNPKILILDEPTRGIDVGAKYEIYKLINQlVQQGVAIIVISSEL 465
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
65-290 |
1.31e-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: 1.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 65 SGLGGGVLVAA-------YIQVSFWTLAAGRQIKKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDDVSKISEGIGDKVG 137
Cdd:cd18550 39 VLLALGMVAVAvasallgVVQTYLSARIGQGVMYDLRVQLYAHLQRMSLAFFTRTRTGEIQSRLNNDVGGAQSVVTGTLT 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 138 MFFQAIATFFAGFIVGFIRGWKLTLVIMAISPILGLSTAVWAKILSTFSDKELAAYAKAGAVAEEALGA--IRTVIAFGG 215
Cdd:cd18550 119 SVVSNVVTLVATLVAMLALDWRLALLSLVLLPLFVLPTRRVGRRRRKLTREQQEKLAELNSIMQETLSVsgALLVKLFGR 198
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568932737 216 QNKELERYQKHLENAKKIGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTIGN--AMTVFFSILIGAFS 290
Cdd:cd18550 199 EDDEAARFARRSRELRDLGVRQALAGRWFFAALGLFTAIGPALVYWVGGLLVIGGGLTIGTlvAFTALLGRLYGPLT 275
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
994-1206 |
1.34e-09 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 60.19 E-value: 1.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 994 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLL--ERFYDPMAGSVLLDGQEAKKLNVQwLRAQLGI--VSQEPI----- 1064
Cdd:PRK09580 15 AILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLagREDYEVTGGTVEFKGKDLLELSPE-DRAGEGIfmAFQYPVeipgv 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1065 ----LFDCSIAENIAYGDnsrvvpHDEIVRAAKEANIHPFIETL--PQKYNTRVGDKGtqLSGGQKQRIAIARALIRQPR 1138
Cdd:PRK09580 94 snqfFLQTALNAVRSYRG------QEPLDRFDFQDLMEEKIALLkmPEDLLTRSVNVG--FSGGEKKRNDILQMAVLEPE 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568932737 1139 VLLLDEATSALDTESEKVVQEALDKAREG-RTCIVIAH--RLSTIQNADLIVVIENGKVKEHGTH---QQLLAQ 1206
Cdd:PRK09580 166 LCILDESDSGLDIDALKIVADGVNSLRDGkRSFIIVTHyqRILDYIKPDYVHVLYQGRIVKSGDFtlvKQLEEQ 239
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
705-910 |
1.48e-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: 1.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 705 LGVLSFFTFFLQGFTFGKAGEILTTRLRSMAFKAMLRQDMSWFDdhKNSTGALSTRLATDAAQVQGATGTRLALIAQNTA 784
Cdd:cd18589 45 LTIASAVSEFVCDLIYNITMSRIHSRLQGLVFAAVLRQEIAFFD--SNQTGDIVSRVTTDTEDMSESLSENLSLLMWYLA 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 785 NLGTGIIISFIYGWQLTLLLLSVVPFIAVAGIVEMKMLAGNAKRDKKEMEAAGKIATEAIENIRTVVSLTQERKFESMYV 864
Cdd:cd18589 123 RGLFLFIFMLWLSPKLALLTALGLPLLLLVPKFVGKFQQSLAVQVQKSLARANQVAVETFSAMKTVRSFANEEGEAQRYR 202
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 568932737 865 EKLHGPYRNSVRKAHIYGI---TFSISQAFMyfsYAGCFRFGSYLIVNG 910
Cdd:cd18589 203 QRLQKTYRLNKKEAAAYAVsmwTSSFSGLAL---KVGILYYGGQLVTAG 248
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
349-557 |
1.87e-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: 1.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 349 SRANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVqlLQRLYDPTEGKISIDGQDIRNFNV----RCLREIIgVVSQEPV 424
Cdd:cd03271 4 KGARENNLKNIDVDIPLGVLTCVTGVSGSGKSSLI--NDTLYPALARRLHLKKEQPGNHDRieglEHIDKVI-VIDQSPI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 425 -------------LFsTTIAE----------------NIRYgRGNVTMDEIEKAVKEAnaYDFIMKLPQ---KFDTLV-- 470
Cdd:cd03271 81 grtprsnpatytgVF-DEIRElfcevckgkrynretlEVRY-KGKSIADVLDMTVEEA--LEFFENIPKiarKLQTLCdv 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 471 -------GDRGAQLSGGQKQRIAIARALVR---NPKILLLDEATSALDTESEAEVQAALDKARE-GRTTIVIAHRLSTIR 539
Cdd:cd03271 157 glgyiklGQPATTLSGGEAQRIKLAKELSKrstGKTLYILDEPTTGLHFHDVKKLLEVLQRLVDkGNTVVVIEHNLDVIK 236
|
250 260
....*....|....*....|....
gi 568932737 540 NADVI------AGFEDGVIVEQGS 557
Cdd:cd03271 237 CADWIidlgpeGGDGGGQVVASGT 260
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1000-1204 |
3.35e-09 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 60.70 E-value: 3.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1000 SLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGqeaKKLNV----QWLRAqlGIV------SQEPILFDCS 1069
Cdd:PRK11288 273 SFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDG---KPIDIrsprDAIRA--GIMlcpedrKAEGIIPVHS 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1070 IAENIAYGDNSRVVPHDEIVRAAKEA-NIHPFIETLPQKynTRVGD-KGTQLSGGQKQRIAIARALIRQPRVLLLDEATS 1147
Cdd:PRK11288 348 VADNINISARRHHLRAGCLINNRWEAeNADRFIRSLNIK--TPSREqLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTR 425
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568932737 1148 ALDTESEKVVQEAL-DKAREGRTCIVIAHRLSTIQN-ADLIVVIENGKV-----KEHGTHQQLL 1204
Cdd:PRK11288 426 GIDVGAKHEIYNVIyELAAQGVAVLFVSSDLPEVLGvADRIVVMREGRIagelaREQATERQAL 489
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
655-878 |
6.43e-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: 6.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 655 FVVGTVCAIANGALQPAFSIILSEMIAIFGPGDDAVkqQKCNMFSLVFLGLGVLSFFTFFLQGFTFGKAGEILTTRLRSM 734
Cdd:cd18778 1 LILTLLCALLSTLLGLVPPWLIRELVDLVTIGSKSL--GLLLGLALLLLGAYLLRALLNFLRIYLNHVAEQKVVADLRSD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 735 AFKAMLRQDMSWFDDHknSTGALSTRLATDAAQVQgatgtRLAL--IAQNTANLGTGIIIS---FIYGWQLTLLLLSVVP 809
Cdd:cd18778 79 LYDKLQRLSLRYFDDR--QTGDLMSRVINDVANVE-----RLIAdgIPQGITNVLTLVGVAiilFSINPKLALLTLIPIP 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568932737 810 FIAVAGIVEMKMLAGNAKRDKKEMEAAGKIATEAIENIRTVVSLTQERKfESMYVEKLHGPYRNSVRKA 878
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) ... |
981-1178 |
1.00e-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: 57.76 E-value: 1.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 981 NEVVFNYPtrANVPVLQGLSLeVKKGQTLALVGSSGCGKSTVVQLLE--------RFYDP---------MAGSVL----- 1038
Cdd:cd03236 4 DEPVHRYG--PNSFKLHRLPV-PREGQVLGLVGPNGIGKSTALKILAgklkpnlgKFDDPpdwdeildeFRGSELqnyft 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1039 --LDGQEAKKLNVQWlraqlgiVSQEPILFDCSIAENIAYGDNSRVVphDEIVraaKEANIHPFIETlpqkyntrvgdKG 1116
Cdd:cd03236 81 klLEGDVKVIVKPQY-------VDLIPKAVKGKVGELLKKKDERGKL--DELV---DQLELRHVLDR-----------NI 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568932737 1117 TQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTESE----KVVQEAldkAREGRTCIVIAHRLS 1178
Cdd:cd03236 138 DQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRlnaaRLIREL---AEDDNYVLVVEHDLA 200
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
331-516 |
1.42e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 59.10 E-value: 1.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 331 PDNIKGN--LEFSDVHFSYPsrANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKIsidgqdIRNFN 408
Cdd:PLN03073 500 PDDRPGPpiISFSDASFGYP--GGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTV------FRSAK 571
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 409 VRclreiIGVVSQEPV----LFSTTIaenirygrgnVTMDEIEKAVKEanaydfimklpQKFDTLVGDRGAQ-------- 476
Cdd:PLN03073 572 VR-----MAVFSQHHVdgldLSSNPL----------LYMMRCFPGVPE-----------QKLRAHLGSFGVTgnlalqpm 625
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 568932737 477 --LSGGQKQRIAIARALVRNPKILLLDEATSALDTES-EAEVQ 516
Cdd:PLN03073 626 ytLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAvEALIQ 668
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
355-537 |
1.42e-08 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 59.12 E-value: 1.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 355 ILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQ-RLYDPT-EGKISIDGqdiRNFNVRCLREIiGVVSQEPVLFS-TTIA 431
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAgRIQGNNfTGTILANN---RKPTKQILKRT-GFVTQDDILYPhLTVR 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 432 ENIRYGRGNVTMDEIEKAVKEANAYDFI--MKLPQKFDTLVGD---RGaqLSGGQKQRIAIARALVRNPKILLLDEATSA 506
Cdd:PLN03211 159 ETLVFCSLLRLPKSLTKQEKILVAESVIseLGLTKCENTIIGNsfiRG--ISGGERKRVSIAHEMLINPSLLILDEPTSG 236
|
170 180 190
....*....|....*....|....*....|..
gi 568932737 507 LD-TESEAEVQAALDKAREGRTTIVIAHRLST 537
Cdd:PLN03211 237 LDaTAAYRLVLTLGSLAQKGKTIVTSMHQPSS 268
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
69-289 |
2.15e-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: 57.07 E-value: 2.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 69 GGVLVAAYI-------QVSFWTLAAGRQIKK-IRQKFFHAILRQEMGWFDIKGTTELNTRLTDDVSKISE----GIGDkv 136
Cdd:cd18549 45 GAILLALYIlrtllnyFVTYWGHVMGARIETdMRRDLFEHLQKLSFSFFDNNKTGQLMSRITNDLFDISElahhGPED-- 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 137 gmFFQAIATFFAGFIVGFIRGWKLTLVIMAISPILGLST--------AVWAKILSTFSDkelaayakAGAVAEEALGAIR 208
Cdd:cd18549 123 --LFISIITIIGSFIILLTINVPLTLIVFALLPLMIIFTiyfnkkmkKAFRRVREKIGE--------INAQLEDSLSGIR 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 209 TVIAFGGQNKELERYQK---HLENAKKIGIKkaISANISMGIAFL--LIYASyALAFwyGSTLVISKEYTIGNAMTvfFS 283
Cdd:cd18549 193 VVKAFANEEYEIEKFDEgndRFLESKKKAYK--AMAYFFSGMNFFtnLLNLV-VLVA--GGYFIIKGEITLGDLVA--FL 265
|
....*.
gi 568932737 284 ILIGAF 289
Cdd:cd18549 266 LYVNVF 271
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
336-626 |
2.18e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 58.42 E-value: 2.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 336 GNLEFSDvhfsYPsranikILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQR--LYDptEGKISIDgQDIrnfnvrclr 413
Cdd:PRK11147 9 AWLSFSD----AP------LLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGevLLD--DGRIIYE-QDL--------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 414 eiigVVS---QEP------VLFSTtIAENI--------RYGR--GNVTMDEIEKAVKE----------ANAYDFIMKLPQ 464
Cdd:PRK11147 67 ----IVArlqQDPprnvegTVYDF-VAEGIeeqaeylkRYHDisHLVETDPSEKNLNElaklqeqldhHNLWQLENRINE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 465 KFDTLVGDRGAQL---SGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALdKAREGrTTIVIAHRLSTIRN- 540
Cdd:PRK11147 142 VLAQLGLDPDAALsslSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFL-KTFQG-SIIFISHDRSFIRNm 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 541 ADVIAGFEDGVIVE-QGSHSE-LMKKEGiYFRLVNMQTAgsqilseEFEVELSDEKAagdvapngW-----KARIFRNST 613
Cdd:PRK11147 220 ATRIVDLDRGKLVSyPGNYDQyLLEKEE-ALRVEELQNA-------EFDRKLAQEEV--------WirqgiKARRTRNEG 283
|
330
....*....|....*..
gi 568932737 614 K----KSLKSPHQNRLD 626
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) ... |
987-1199 |
3.13e-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: 3.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 987 YPTRANVPVLQGLSLEVKKG-----QTLALVGSSGCGKSTVVQLLerfydpmAGSVLLDGQEAKKLNVQwlraqlgiVSQ 1061
Cdd:cd03237 1 YTYPTMKKTLGEFTLEVEGGsisesEVIGILGPNGIGKTTFIKML-------AGVLKPDEGDIEIELDT--------VSY 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1062 EPilfdcsiaENIAYGDNSRVvpHDEIVRAAKEANIHPFIET-------LPQKYNTRVgdkgTQLSGGQKQRIAIARALI 1134
Cdd:cd03237 66 KP--------QYIKADYEGTV--RDLLSSITKDFYTHPYFKTeiakplqIEQILDREV----PELSGGELQRVAIAACLS 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1135 RQPRVLLLDEATSALDTESE----KVVQEALDKARegRTCIVIAHRLSTIQN-ADLIVVIEnGKVKEHGT 1199
Cdd:cd03237 132 KDADIYLLDEPSAYLDVEQRlmasKVIRRFAENNE--KTAFVVEHDIIMIDYlADRLIVFE-GEPSVNGV 198
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
339-510 |
3.55e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 57.65 E-value: 3.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 339 EFSDVHFSYPSRaniKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQ-DIRNFNVRclREIIg 417
Cdd:PRK11147 321 EMENVNYQIDGK---QLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKlEVAYFDQH--RAEL- 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 418 vvsqEPvlfSTTIAENIRYGRGNVTMDEIEKAVKeanAY--DFIMKlPQKFDTLVgdrgAQLSGGQKQRIAIARALVRNP 495
Cdd:PRK11147 395 ----DP---EKTVMDNLAEGKQEVMVNGRPRHVL---GYlqDFLFH-PKRAMTPV----KALSGGERNRLLLARLFLKPS 459
|
170
....*....|....*
gi 568932737 496 KILLLDEATSALDTE 510
Cdd:PRK11147 460 NLLILDEPTNDLDVE 474
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
323-570 |
3.64e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 57.51 E-value: 3.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 323 SFSERGHKPDnikgnlEFSDVHFSYPSRanIKILKGLNLKVKSGQ-----TVALVGNSGCGKSTTVQLLQRLYDPTEG-- 395
Cdd:PRK13409 325 EFEERPPRDE------SERETLVEYPDL--TKKLGDFSLEVEGGEiyegeVIGIVGPNGIGKTTFAKLLAGVLKPDEGev 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 396 ----KISIDGQDIR-NFNVR---CLREIigvvsqePVLFSTTIAENirygrgnvtmdEIEKAvkeanaydfiMKLPQKFD 467
Cdd:PRK13409 397 dpelKISYKPQYIKpDYDGTvedLLRSI-------TDDLGSSYYKS-----------EIIKP----------LQLERLLD 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 468 TLVGDrgaqLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKAREGR--TTIVIAHRLSTIrnaDVIA 545
Cdd:PRK13409 449 KNVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEEReaTALVVDHDIYMI---DYIS 521
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 568932737 546 gfeDGVIV---EQGSH-------------SELMKKEGIYFR 570
Cdd:PRK13409 522 ---DRLMVfegEPGKHghasgpmdmregmNRFLKELGITFR 559
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
363-548 |
4.44e-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: 4.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 363 VKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGqdirnfnvrclreiigvvsqepvlfsttiaenirygrgnvt 442
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDG----------------------------------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 443 mdeIEKAVKeanaydfimklPQKFDtlvgdrgaqLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKA 522
Cdd:cd03222 61 ---ITPVYK-----------PQYID---------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRL 117
|
170 180
....*....|....*....|....*....
gi 568932737 523 RE--GRTTIVIAHRLSTIRN-ADVIAGFE 548
Cdd:cd03222 118 SEegKKTALVVEHDLAVLDYlSDRIHVFE 146
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
355-532 |
4.53e-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: 4.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 355 ILKGLNLKVKSGQTVALVGNSGCGKST-----TVQLLQRLYDpTEGKISIDG---QDIRNFnvrcLREIIGVVSQEPVLF 426
Cdd:TIGR00956 76 ILKPMDGLIKPGELTVVLGRPGSGCSTllktiASNTDGFHIG-VEGVITYDGitpEEIKKH----YRGDVVYNAETDVHF 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 427 -STTIAENIRYG--------RGNvTMDEIEKAVKEANAYDFIMKLPQKFDTLVGD---RGaqLSGGQKQRIAIARALVRN 494
Cdd:TIGR00956 151 pHLTVGETLDFAarcktpqnRPD-GVSREEYAKHIADVYMATYGLSHTRNTKVGNdfvRG--VSGGERKRVSIAEASLGG 227
|
170 180 190
....*....|....*....|....*....|....*....
gi 568932737 495 PKILLLDEATSALDTESEAEVQAAL-DKAREGRTTIVIA 532
Cdd:TIGR00956 228 AKIQCWDNATRGLDSATALEFIRALkTSANILDTTPLVA 266
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
434-561 |
4.61e-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: 4.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 434 IRYgRGNVTMDEIEKAVKEAnaYDFIMKLP---QKFDTLVgDRGAQ----------LSGGQKQRIAIARALVR---NPKI 497
Cdd:TIGR00630 778 VKY-KGKNIADVLDMTVEEA--YEFFEAVPsisRKLQTLC-DVGLGyirlgqpattLSGGEAQRIKLAKELSKrstGRTL 853
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568932737 498 LLLDEATSALDTESEAE----VQAALDKareGRTTIVIAHRLSTIRNADVI------AGFEDGVIVEQGSHSEL 561
Cdd:TIGR00630 854 YILDEPTTGLHFDDIKKllevLQRLVDK---GNTVVVIEHNLDVIKTADYIidlgpeGGDGGGTVVASGTPEEV 924
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
980-1208 |
4.84e-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: 4.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 980 FNEVVFNYPTRANvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKlNVQWLRAQLGIV 1059
Cdd:TIGR01257 1940 LNELTKVYSGTSS-PAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT-NISDVHQNMGYC 2017
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1060 SQEPILFDCSIA-ENIAYGDNSRVVPHDEIVRAAKEAnihpfIETLPQK-YNTRVGdkGTqLSGGQKQRIAIARALIRQP 1137
Cdd:TIGR01257 2018 PQFDAIDDLLTGrEHLYLYARLRGVPAEEIEKVANWS-----IQSLGLSlYADRLA--GT-YSGGNKRKLSTAIALIGCP 2089
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568932737 1138 RVLLLDEATSALDTESEKVVQEAL-DKAREGRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHGTHQQLLAQKG 1208
Cdd:TIGR01257 2090 PLVLLDEPTTGMDPQARRMLWNTIvSIIREGRAVVLTSHSMEECEAlCTRLAIMVKGAFQCLGTIQHLKSKFG 2162
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
996-1186 |
6.41e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 56.74 E-value: 6.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 996 LQGLSLEV-----KKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLldgqeaKKLNV----QWLRA-QLGIVSQepil 1065
Cdd:PRK13409 350 LGDFSLEVeggeiYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVD------PELKIsykpQYIKPdYDGTVED---- 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1066 FDCSIAENIaygDNSRVVPhdEIVRaakeanihPFieTLPQKYNTRVGDkgtqLSGGQKQRIAIARALIRQPRVLLLDEA 1145
Cdd:PRK13409 420 LLRSITDDL---GSSYYKS--EIIK--------PL--QLERLLDKNVKD----LSGGELQRVAIAACLSRDADLYLLDEP 480
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 568932737 1146 TSALDTESEKVVQEALDKAREGR--TCIVIAHRLSTIqnaDLI 1186
Cdd:PRK13409 481 SAHLDVEQRLAVAKAIRRIAEEReaTALVVDHDIYMI---DYI 520
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
353-558 |
7.34e-08 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 57.16 E-value: 7.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 353 IKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLL--QRLYDPTEGKISIDG-----QDIRNFNVRCLREII---GVVSQE 422
Cdd:PLN03140 893 LQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLagRKTGGYIEGDIRISGfpkkqETFARISGYCEQNDIhspQVTVRE 972
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 423 PVLFSTTIAENIRYGRGNVTM--DEIEKAVKEANAYDFIMKLPqkfdtlvGDRGaqLSGGQKQRIAIARALVRNPKILLL 500
Cdd:PLN03140 973 SLIYSAFLRLPKEVSKEEKMMfvDEVMELVELDNLKDAIVGLP-------GVTG--LSTEQRKRLTIAVELVANPSIIFM 1043
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 568932737 501 DEATSALDTESEAEVQAAL-DKAREGRTTIVIAHRLSTirnaDVIAGFEDGVIVEQGSH 558
Cdd:PLN03140 1044 DEPTSGLDARAAAIVMRTVrNTVDTGRTVVCTIHQPSI----DIFEAFDELLLMKRGGQ 1098
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
1111-1187 |
8.14e-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: 8.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1111 RVGDKGTQLSGGQKQRIAIARALIRQPR---VLLLDEATSALDTESEKVVQEALDKARE-GRTCIVIAHRLSTIQNADLI 1186
Cdd:cd03271 162 KLGQPATTLSGGEAQRIKLAKELSKRSTgktLYILDEPTTGLHFHDVKKLLEVLQRLVDkGNTVVVIEHNLDVIKCADWI 241
|
.
gi 568932737 1187 V 1187
Cdd:cd03271 242 I 242
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
354-511 |
8.40e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 56.28 E-value: 8.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 354 KILKGLNLKVKSGQTVALVGNSGCGKSTtvqLLqrlydptegKIsIDGQDiRNFN--VRCLREI-IGVVSQEPVLFST-T 429
Cdd:PRK11819 21 QILKDISLSFFPGAKIGVLGLNGAGKST---LL---------RI-MAGVD-KEFEgeARPAPGIkVGYLPQEPQLDPEkT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 430 IAENIRYGRGNVT----------------MDEIEKAVKE----------ANAYDFIMKLPQKFDTL---VGDRG-AQLSG 479
Cdd:PRK11819 87 VRENVEEGVAEVKaaldrfneiyaayaepDADFDALAAEqgelqeiidaADAWDLDSQLEIAMDALrcpPWDAKvTKLSG 166
|
170 180 190
....*....|....*....|....*....|..
gi 568932737 480 GQKQRIAIARALVRNPKILLLDEATSALDTES 511
Cdd:PRK11819 167 GERRRVALCRLLLEKPDMLLLDEPTNHLDAES 198
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
67-287 |
1.00e-07 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350055 [Multi-domain] Cd Length: 294 Bit Score: 54.91 E-value: 1.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 67 LGGGVLVAAYIQVSF-------WTLAAGRQIKKIRQKFFHAILRQEMGWFDIKGTTELNTRLtDDVSKISEGIGDkvgmf 139
Cdd:cd18782 44 IGVVMLVAALLEAVLtalrtylFTDTANRIDLELGGTIIDHLLRLPLGFFDKRPVGELSTRI-SELDTIRGFLTG----- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 140 fQAIATFF-AGFIVGFIR-----GWKLTLVIMAISPILGLSTAVWAKILSTFSDKELAAYAKAGAVAEEALGAIRTVIAf 213
Cdd:cd18782 118 -TALTTLLdVLFSVIYIAvlfsySPLLTLVVLATVPLQLLLTFLFGPILRRQIRRRAEASAKTQSYLVESLTGIQTVKA- 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 214 ggQNKEL-------ERYQKHLENAKKIGIKKAISANISMGIAFLliyaSYALAFWYGSTLVISKEYTIGNAMTvfFSILI 286
Cdd:cd18782 196 --QNAELkarwrwqNRYARSLGEGFKLTVLGTTSGSLSQFLNKL----SSLLVLWVGAYLVLRGELTLGQLIA--FRILS 267
|
.
gi 568932737 287 G 287
Cdd:cd18782 268 G 268
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
660-857 |
1.12e-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: 1.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 660 VCAIANGALQPAFSIILSEMIaifgpgDDAVKQQkcNMFSLVFL-----GLGVLSFFTFFLQGFTFGKAGEILTTRLRSM 734
Cdd:cd18550 6 LLILLSALLGLLPPLLLREII------DDALPQG--DLGLLVLLalgmvAVAVASALLGVVQTYLSARIGQGVMYDLRVQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 735 AFKAMLRQDMSWFDDHKnsTGALSTRLATDAAQVQGATGTRLALIAQNTANLGTGIIISFIYGWQLTLLLLSVVP-FIAV 813
Cdd:cd18550 78 LYAHLQRMSLAFFTRTR--TGEIQSRLNNDVGGAQSVVTGTLTSVVSNVVTLVATLVAMLALDWRLALLSLVLLPlFVLP 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 568932737 814 AGIVemkmlaGNAKRdkkemeaagKIATEAIENIRTVVSLTQER 857
Cdd:cd18550 156 TRRV------GRRRR---------KLTREQQEKLAELNSIMQET 184
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
328-535 |
1.19e-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: 1.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 328 GHKPDNIKGNlEFSDVHFSYPSRANIKILKGlnlkVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNf 407
Cdd:TIGR01257 1932 GNKTDILRLN-ELTKVYSGTSSPAVDRLCVG----VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT- 2005
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 408 NVRCLREIIGVVSQ-EPVLFSTTIAENIR-YGR-GNVTMDEIEKAvkeANAYDFIMKLPQKFDTLVGdrgaQLSGGQKQR 484
Cdd:TIGR01257 2006 NISDVHQNMGYCPQfDAIDDLLTGREHLYlYARlRGVPAEEIEKV---ANWSIQSLGLSLYADRLAG----TYSGGNKRK 2078
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 568932737 485 IAIARALVRNPKILLLDEATSALDTESEAEV-QAALDKAREGRTTIVIAHRL 535
Cdd:TIGR01257 2079 LSTAIALIGCPPLVLLDEPTTGMDPQARRMLwNTIVSIIREGRAVVLTSHSM 2130
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
373-508 |
1.33e-07 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 56.29 E-value: 1.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 373 GNSGCGKSTTVQLLQRLYDPTEGKISIDGQ--DIRNFNVRcLReiIGVVSQEpvlFST----TIAENIR-----YGrgnV 441
Cdd:NF033858 299 GSNGCGKSTTMKMLTGLLPASEGEAWLFGQpvDAGDIATR-RR--VGYMSQA---FSLygelTVRQNLElharlFH---L 369
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568932737 442 TMDEIEKAVKEanaydfimkLPQKFD--TLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEATSALD 508
Cdd:NF033858 370 PAAEIAARVAE---------MLERFDlaDVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVD 429
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
363-535 |
1.41e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 55.59 E-value: 1.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 363 VKSGQTVALVGNSGCGKSTTVQLLQrlydptegkisidGQDIRNFnvrclreiiGVVSQEPvlfstTIAENIRYGRGNVT 442
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILS-------------GELIPNL---------GDYEEEP-----SWDEVLKRFRGTEL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 443 MDEIEK----AVKEANAYDFIMKLPQKFDTLVGD-------RGA-------------------QLSGGQKQRIAIARALV 492
Cdd:PRK13409 149 QNYFKKlyngEIKVVHKPQYVDLIPKVFKGKVREllkkvdeRGKldevverlglenildrdisELSGGELQRVAIAAALL 228
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 568932737 493 RNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRL 535
Cdd:PRK13409 229 RDADFYFFDEPTSYLDIRQRLNVARLIRELAEGKYVLVVEHDL 271
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
354-558 |
1.51e-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: 1.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 354 KILKGLNLKVKSGQ-----TVALVGNSGCGKSTTVQLLQRLYDPTEG------KISIDGQDIRNFNVRCLREIIGVVSQE 422
Cdd:COG1245 349 KSYGGFSLEVEGGEiregeVLGIVGPNGIGKTTFAKILAGVLKPDEGevdedlKISYKPQYISPDYDGTVEEFLRSANTD 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 423 PvlFSTTIAENirygrgnvtmdEIEKAvkeanaydfiMKLPQKFDTLVGDrgaqLSGGQKQRIAIARALVRNPKILLLDE 502
Cdd:COG1245 429 D--FGSSYYKT-----------EIIKP----------LGLEKLLDKNVKD----LSGGELQRVAIAACLSRDADLYLLDE 481
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568932737 503 ATSALDTESEAEVQAALDKAREGR--TTIVIAHRLSTIrnaDVIAgfeDGVIV---EQGSH 558
Cdd:COG1245 482 PSAHLDVEQRLAVAKAIRRFAENRgkTAMVVDHDIYLI---DYIS---DRLMVfegEPGVH 536
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
69-289 |
1.66e-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: 1.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 69 GGVLVAAYIQVSFWT--------LAAGRQIKKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDDVSKISEGIGDKVGMFF 140
Cdd:cd18778 43 ALLLLGAYLLRALLNflriylnhVAEQKVVADLRSDLYDKLQRLSLRYFDDRQTGDLMSRVINDVANVERLIADGIPQGI 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 141 QAIATFFAGFIVGFIRGWKLTLVIMAISPILGLSTAVWAKILSTFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKEL 220
Cdd:cd18778 123 TNVLTLVGVAIILFSINPKLALLTLIPIPFLALGAWLYSKKVRPRYRKVREALGELNALLQDNLSGIREIQAFGREEEEA 202
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568932737 221 ERYQKHLENAKkigiKKAISANISMGIAFLLIY----ASYALAFWYGSTLVISKEYTIGNamTVFFSILIGAF 289
Cdd:cd18778 203 KRFEALSRRYR----KAQLRAMKLWAIFHPLMEfltsLGTVLVLGFGGRLVLAGELTIGD--LVAFLLYLGLF 269
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
73-291 |
1.66e-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: 1.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 73 VAAYIQVSFWTLAAGRQIKKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDDVSKISEGIGDKVGMFFQAIATFFAGFIV 152
Cdd:cd18565 69 LFQYLSGVLWRRFAQRVQHDLRTDTYDHVQRLDMAFFEDRQTGDLMSVLNNDVNQLERFLDDGANSIIRVVVTVLGIGAI 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 153 GFIRGWKLTLVIMAISPILGLSTAVWAKILSTFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKELERYQKHLENAKk 232
Cdd:cd18565 149 LFYLNWQLALVALLPVPLIIAGTYWFQRRIEPRYRAVREAVGDLNARLENNLSGIAVIKAFTAEDFERERVADASEEYR- 227
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568932737 233 igiKKAISAnISMGIAF-----LLIYASYALAFWYGSTLVISKEYTIGNAMTVffsiliGAFSV 291
Cdd:cd18565 228 ---DANWRA-IRLRAAFfpvirLVAGAGFVATFVVGGYWVLDGPPLFTGTLTV------GTLVT 281
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
91-289 |
2.12e-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: 2.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 91 KKIRQKFFHAILRQEMGWFDIKGTTELNTRLtDDVSKISEGIGDKVGMFFQAIATFFAGFIVGFIRGWKLTLVIMAISPI 170
Cdd:cd18555 75 KSLMSDFFEHLLKLPYSFFENRSSGDLLFRA-NSNVYIRQILSNQVISLIIDLLLLVIYLIYMLYYSPLLTLIVLLLGLL 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 171 LGLSTAVWAKILSTFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKELERYQKHLENAKKIGIKKAISANISMGIAFL 250
Cdd:cd18555 154 IVLLLLLTRKKIKKLNQEEIVAQTKVQSYLTETLYGIETIKSLGSEKNIYKKWENLFKKQLKAFKKKERLSNILNSISSS 233
|
170 180 190
....*....|....*....|....*....|....*....
gi 568932737 251 LIYASYALAFWYGSTLVISKEYTIGnaMTVFFSILIGAF 289
Cdd:cd18555 234 IQFIAPLLILWIGAYLVINGELTLG--ELIAFSSLAGSF 270
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
360-553 |
2.27e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 54.92 E-value: 2.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 360 NLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRnfnVRCLREII--GVV------SQEPVLFSTTIA 431
Cdd:PRK11288 273 SFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPID---IRSPRDAIraGIMlcpedrKAEGIIPVHSVA 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 432 ENIRYG--RGNVTMDEIEKAVKEA-NAYDFIMKLPQKF---DTLVGdrgaQLSGGQKQRIAIARALVRNPKILLLDEATS 505
Cdd:PRK11288 350 DNINISarRHHLRAGCLINNRWEAeNADRFIRSLNIKTpsrEQLIM----NLSGGNQQKAILGRWLSEDMKVILLDEPTR 425
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 568932737 506 ALDTESEAEVQAAL-DKAREGRTTIVIAHRLstirnADVIaGFEDGVIV 553
Cdd:PRK11288 426 GIDVGAKHEIYNVIyELAAQGVAVLFVSSDL-----PEVL-GVADRIVV 468
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
652-912 |
2.28e-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: 2.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 652 WPYFVVGTVCAIANGALQPAFSIILSEMI-AIFGPGDdavkQQKCNMFSLVFLGLGVLSFFTFFLQGFTFGKAGEILTTR 730
Cdd:cd18540 1 KKLLILLIILMLLVALLDAVFPLLTKYAIdHFITPGT----LDGLTGFILLYLGLILIQALSVFLFIRLAGKIEMGVSYD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 731 LRSMAFKAMLRQDMSWFDdhKNSTGALSTRLATDAAQVQGATGTRLALIAQNTANLGTGIIISFIYGWQLTLLLLSVVPF 810
Cdd:cd18540 77 LRKKAFEHLQTLSFSYFD--KTPVGWIMARVTSDTQRLGEIISWGLVDLVWGITYMIGILIVMLILNWKLALIVLAVVPV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 811 IA-VAGIVEMKMLAGNAKRDKKEMEAAGKIaTEAIENIRTVVSLTQERKFESMYVEKLHGPYRNSVRKAHIYGITFSISQ 889
Cdd:cd18540 155 LAvVSIYFQKKILKAYRKVRKINSRITGAF-NEGITGAKTTKTLVREEKNLREFKELTEEMRRASVRAARLSALFLPIVL 233
|
250 260
....*....|....*....|...
gi 568932737 890 AFMYFSYAGCFRFGSYLIVNGHM 912
Cdd:cd18540 234 FLGSIATALVLWYGGILVLAGAI 256
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
98-287 |
2.59e-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: 53.74 E-value: 2.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 98 FHAILRQEMGWFDIKGTTELNTRLTDdVSKISEgigdkvgmFF--QAIATF----FAG--FIVGFIRGWKLTLVIMAISP 169
Cdd:cd18566 82 FEHLLSLPLSFFEREPSGAHLERLNS-LEQIRE--------FLtgQALLALldlpFVLifLGLIWYLGGKLVLVPLVLLG 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 170 ILglstAVWAKILSTFSDKELAAYAKAGAVAE----EALGAIRTVIAFGGQNKELERYQKHLENAKKIGIKKAISANISM 245
Cdd:cd18566 153 LF----VLVAILLGPILRRALKERSRADERRQnfliETLTGIHTIKAMAMEPQMLRRYERLQANAAYAGFKVAKINAVAQ 228
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 568932737 246 GIAFLLIYASYALAFWYGSTLVISKEYTIGnaMTVFFSILIG 287
Cdd:cd18566 229 TLGQLFSQVSMVAVVAFGALLVINGDLTVG--ALIACTMLSG 268
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
1000-1206 |
2.73e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 54.64 E-value: 2.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1000 SLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGS--------VLLDGQEAKKL-NVQWLRAQLGIVSQEPILFDCSI 1070
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGErqsqfshiTRLSFEQLQKLvSDEWQRNNTDMLSPGEDDTGRTT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1071 AENIAYG--DNSRVVphdeivRAAKEANIHPFIETlPQKYntrvgdkgtqLSGGQKQRIAIARALIRQPRVLLLDEATSA 1148
Cdd:PRK10938 103 AEIIQDEvkDPARCE------QLAQQFGITALLDR-RFKY----------LSTGETRKTLLCQALMSEPDLLILDEPFDG 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1149 LDTESEKVVQEALDK-AREGRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHGTHQQLLAQ 1206
Cdd:PRK10938 166 LDVASRQQLAELLASlHQSGITLVLVLNRFDEIPDfVQFAGVLADCTLAETGEREEILQQ 225
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
994-1205 |
3.82e-07 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 54.24 E-value: 3.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 994 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLDGQEAKKLNVQWLRAQlGIV------SQEPILFD 1067
Cdd:PRK10762 266 PGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDGLAN-GIVyisedrKRDGLVLG 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1068 CSIAENI---AYGDNSRvvPHDEIVRAAKEANIHPFIETLPQKYNTRVGDKGTqLSGGQKQRIAIARALIRQPRVLLLDE 1144
Cdd:PRK10762 345 MSVKENMsltALRYFSR--AGGSLKHADEQQAVSDFIRLFNIKTPSMEQAIGL-LSGGNQQKVAIARGLMTRPKVLILDE 421
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568932737 1145 ATSALDTESEKVVQEALDKAR-EGRTCIVIAHRLSTIQN-ADLIVVIENGKV-----KEHGTHQQLLA 1205
Cdd:PRK10762 422 PTRGVDVGAKKEIYQLINQFKaEGLSIILVSSEMPEVLGmSDRILVMHEGRIsgeftREQATQEKLMA 489
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
364-537 |
5.10e-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: 5.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 364 KSGQTVALVGNSGCGKSTTVQLLQrlydptegkisidGQDIRNFnvrclreiiGVVSQEPvlfstTIAENIRYGRGNVTM 443
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILS-------------GELKPNL---------GDYDEEP-----SWDEVLKRFRGTELQ 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 444 DEIEK----AVKEANAYDFIMKLPQKFDTLVGD-------RGA-------------------QLSGGQKQRIAIARALVR 493
Cdd:COG1245 150 DYFKKlangEIKVAHKPQYVDLIPKVFKGTVREllekvdeRGKldelaeklglenildrdisELSGGELQRVAIAAALLR 229
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 568932737 494 NPKILLLDEATSALDTESEAEVQAAL-DKAREGRTTIVIAHRLST 537
Cdd:COG1245 230 DADFYFFDEPSSYLDIYQRLNVARLIrELAEEGKYVLVVEHDLAI 274
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
1092-1187 |
6.08e-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: 6.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1092 AKEANIHPFIETLPQ---KYnTRVGDKGTQLSGGQKQRIAIARALIRQ---PRVLLLDEATSALDTESEK----VVQEAL 1161
Cdd:TIGR00630 801 EAVPSISRKLQTLCDvglGY-IRLGQPATTLSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLHFDDIKklleVLQRLV 879
|
90 100
....*....|....*....|....*.
gi 568932737 1162 DKareGRTCIVIAHRLSTIQNADLIV 1187
Cdd:TIGR00630 880 DK---GNTVVVIEHNLDVIKTADYII 902
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1117-1153 |
6.58e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 53.58 E-value: 6.58e-07
10 20 30
....*....|....*....|....*....|....*..
gi 568932737 1117 TQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTES 1153
Cdd:PRK11819 162 TKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES 198
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1000-1162 |
6.76e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 53.80 E-value: 6.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1000 SLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVlldgQEAKKLNVQWL---RAQLgivsqEPilfDCSIAENIAY 1076
Cdd:PRK11147 339 SAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI----HCGTKLEVAYFdqhRAEL-----DP---EKTVMDNLAE 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1077 GDNsrvvphdEIVRAAKEANIHPFIETL---PQKYNTRVgdkgTQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTES 1153
Cdd:PRK11147 407 GKQ-------EVMVNGRPRHVLGYLQDFlfhPKRAMTPV----KALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVET 475
|
....*....
gi 568932737 1154 EKVVQEALD 1162
Cdd:PRK11147 476 LELLEELLD 484
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
696-912 |
6.77e-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: 6.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 696 NMFSLVFLGLGVLSFFTFFLQGF---TFGKAGEILTTRLRSMAFKAMLRQDMSWFDdhKNSTGALSTRLAtDAAQVQGAT 772
Cdd:cd18566 39 PTLQVLVIGVVIAILLESLLRLLrsyILAWIGARFDHRLSNAAFEHLLSLPLSFFE--REPSGAHLERLN-SLEQIREFL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 773 GTRLALIAQNTANLGTGIIISFIYGWQLTLLLLSVVPFIAVAGIVEMKMLAGNAKRDKKEMEAAGKIATEAIENIRTVVS 852
Cdd:cd18566 116 TGQALLALLDLPFVLIFLGLIWYLGGKLVLVPLVLLGLFVLVAILLGPILRRALKERSRADERRQNFLIETLTGIHTIKA 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 853 LTQERKFESMYVEKLHGPYRNSVRKAHIYGITFSISQAFMYFSYAGCFRFGSYLIVNGHM 912
Cdd:cd18566 196 MAMEPQMLRRYERLQANAAYAGFKVAKINAVAQTLGQLFSQVSMVAVVAFGALLVINGDL 255
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
994-1209 |
7.58e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 53.36 E-value: 7.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 994 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVlldgqeakklnvQWL-RAQLGIVSQEP--------I 1064
Cdd:PRK15064 333 PLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV------------KWSeNANIGYYAQDHaydfendlT 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1065 LFDCsIAENIAYGDNSRVV---------PHDEIVRAAKeanihpfietlpqkyntrvgdkgtQLSGGQKQRIAIARALIR 1135
Cdd:PRK15064 401 LFDW-MSQWRQEGDDEQAVrgtlgrllfSQDDIKKSVK------------------------VLSGGEKGRMLFGKLMMQ 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1136 QPRVLLLDEATSALDTESEKVVQEALDKArEGrTCIVIAH------RLSTiqnaDLIVVIENGKVKEHGTHQQLLAQKGI 1209
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 ... |
1117-1153 |
9.60e-07 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 53.02 E-value: 9.60e-07
10 20 30
....*....|....*....|....*....|....*..
gi 568932737 1117 TQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTES 1153
Cdd:TIGR03719 160 TKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAES 196
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
360-562 |
1.12e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 52.71 E-value: 1.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 360 NLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVRCLREIigvVSQEPVLFSTTIAENIRYGRG 439
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQLQKL---VSDEWQRNNTDMLSPGEDDTG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 440 NVTMDEIEKAVKEANAydfIMKLPQKF--DTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQA 517
Cdd:PRK10938 100 RTTAEIIQDEVKDPAR---CEQLAQQFgiTALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAE 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 568932737 518 ALDK-AREGRTTIVIAHRLSTIRN-ADVIAGFEDGVIVEQGSHSELM 562
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 ... |
687-912 |
1.42e-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: 51.36 E-value: 1.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 687 DDAVKQQKCNMFSLVFLGLGVLSFFTF---FLQGFTFGKAGEILTTRLRSMAFKAMLRQDMSWFDdhKNSTGALSTRlAT 763
Cdd:cd18555 30 DNVIVPGNLNLLNVLGIGILILFLLYGlfsFLRGYIIIKLQTKLDKSLMSDFFEHLLKLPYSFFE--NRSSGDLLFR-AN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 764 DAAQVQGATGTRLALIAQNTANLGTGIIISFIYGWQLTLLLLSVVPFIAVAGIVEMKMLAgnaKRDKKEMEAAGK---IA 840
Cdd:cd18555 107 SNVYIRQILSNQVISLIIDLLLLVIYLIYMLYYSPLLTLIVLLLGLLIVLLLLLTRKKIK---KLNQEEIVAQTKvqsYL 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568932737 841 TEAIENIRTVVSLTQERKFESMYVEKLHGPYRNSVRKAHIYGITFSISQAFMYFSYAGCFRFGSYLIVNGHM 912
Cdd:cd18555 184 TETLYGIETIKSLGSEKNIYKKWENLFKKQLKAFKKKERLSNILNSISSSIQFIAPLLILWIGAYLVINGEL 255
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
349-556 |
1.62e-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: 1.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 349 SRANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQllQRLYdpTEGKISIDGQDIRNFnvrclREIIGVVSQepvlFST 428
Cdd:cd03238 4 SGANVHNLQNLDVSIPLNVLVVVTGVSGSGKSTLVN--EGLY--ASGKARLISFLPKFS-----RNKLIFIDQ----LQF 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 429 TIAENIRYgrgnvtmdeiekavkeanaydfiMKLPQKFDTLvgdrgaqlSGGQKQRIAIARALVRNPK--ILLLDEATSA 506
Cdd:cd03238 71 LIDVGLGY-----------------------LTLGQKLSTL--------SGGELQRVKLASELFSEPPgtLFILDEPSTG 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 568932737 507 LDTESEAEVQAALDKAR-EGRTTIVIAHRLSTIRNADVI------AGFEDGVIVEQG 556
Cdd:cd03238 120 LHQQDINQLLEVIKGLIdLGNTVILIEHNLDVLSSADWIidfgpgSGKSGGKVVFSG 176
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1003-1189 |
1.87e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 52.12 E-value: 1.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1003 VKKGQTLALVGSSGCGKSTVVQLL---------------------ERFydpmAGSVLLDgqEAKKLNVQWLRAQLGI--V 1059
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILsgelipnlgdyeeepswdevlKRF----RGTELQN--YFKKLYNGEIKVVHKPqyV 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1060 SQEPILFDCSIAENIAYGDNSRVVphDEIVraaKEANIHPFIEtlpQKYNtrvgdkgtQLSGGQKQRIAIARALIRQPRV 1139
Cdd:PRK13409 170 DLIPKVFKGKVRELLKKVDERGKL--DEVV---ERLGLENILD---RDIS--------ELSGGELQRVAIAAALLRDADF 233
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 568932737 1140 LLLDEATSALDtesekvVQEALDKAR------EGRTCIVIAHRLSTIQN-ADLIVVI 1189
Cdd:PRK13409 234 YFFDEPTSYLD------IRQRLNVARlirelaEGKYVLVVEHDLAVLDYlADNVHIA 284
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
1002-1199 |
2.02e-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: 52.09 E-value: 2.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1002 EVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVlldgqeAKKLNV----QWLRAQLGIVSQEpILFDcSIAENIayg 1077
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV------DEDLKIsykpQYISPDYDGTVEE-FLRS-ANTDDF--- 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1078 DNSRVvpHDEIVRaakeanihPF-IETLpqkYNTRVGDkgtqLSGGQKQRIAIARALIRQPRVLLLDEATSALDTESEKV 1156
Cdd:COG1245 431 GSSYY--KTEIIK--------PLgLEKL---LDKNVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLA 493
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 568932737 1157 VQEALDKAREGR--TCIVIAHRLSTIqnaDLI---VVIENGKVKEHGT 1199
Cdd:COG1245 494 VAKAIRRFAENRgkTAMVVDHDIYLI---DYIsdrLMVFEGEPGVHGH 538
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
696-912 |
2.10e-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: 50.93 E-value: 2.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 696 NMFSLVFLGLGVLSFFTFFLQGFTFGKAGEILTTRLRSMAFKAMLRQDMSWFDdhKNSTGALSTRLATDAAQVQGA-TGT 774
Cdd:cd18545 40 LIIALLFLALNLVNWVASRLRIYLMAKVGQRILYDLRQDLFSHLQKLSFSFFD--SRPVGKILSRVINDVNSLSDLlSNG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 775 RLALIAqNTANLGTGIIISFIYGWQLTLLLLSVVPFIAVAgiveMKMLAGNAKRdkKEMEAAGKIAT------EAIENIR 848
Cdd:cd18545 118 LINLIP-DLLTLVGIVIIMFSLNVRLALVTLAVLPLLVLV----VFLLRRRARK--AWQRVRKKISNlnaylhESISGIR 190
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568932737 849 TVVSLTQE----RKFESMYVEKLHGpYRNSVRKAHIYG----ITFSISQAFMYFsyagcfrFGSYLIVNGHM 912
Cdd:cd18545 191 VIQSFAREdeneEIFDELNRENRKA-NMRAVRLNALFWplveLISALGTALVYW-------YGGKLVLGGAI 254
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
1004-1189 |
2.75e-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: 2.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1004 KKGQTLALVGSSGCGKSTVVQLLerfydpmAGSvlldgqeakklnvqwLRAQLGIVSQEPilfdcSIAENIAYGDNSRVV 1083
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKIL-------SGE---------------LKPNLGDYDEEP-----SWDEVLKRFRGTELQ 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1084 PHDEIVRAAK-EANIHP-FIETLPQKYNTRVGD-------KG-------------------TQLSGGQKQRIAIARALIR 1135
Cdd:COG1245 150 DYFKKLANGEiKVAHKPqYVDLIPKVFKGTVREllekvdeRGkldelaeklglenildrdiSELSGGELQRVAIAAALLR 229
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 568932737 1136 QPRVLLLDEATSALD----TESEKVVQEAldkAREGRTCIVIAHRLSTIQN-ADLIVVI 1189
Cdd:COG1245 230 DADFYFFDEPSSYLDiyqrLNVARLIREL---AEEGKYVLVVEHDLAILDYlADYVHIL 285
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
338-567 |
3.18e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 51.43 E-value: 3.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 338 LEFSDVHFSYPSRaniKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKIsidgQDIRNFNvrclreiIG 417
Cdd:PRK15064 320 LEVENLTKGFDNG---PLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV----KWSENAN-------IG 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 418 VVSQEPV--------LFS-----TTIAEN---IR--YGRGNVTMDEIEKAVKeanaydfimklpqkfdtlvgdrgaQLSG 479
Cdd:PRK15064 386 YYAQDHAydfendltLFDwmsqwRQEGDDeqaVRgtLGRLLFSQDDIKKSVK------------------------VLSG 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 480 GQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKArEGrTTIVIAH------RLSTirnaDVIAGFEDGVIV 553
Cdd:PRK15064 442 GEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESIESLNMALEKY-EG-TLIFVSHdrefvsSLAT----RIIEITPDGVVD 515
|
250
....*....|....
gi 568932737 554 EQGSHSELMKKEGI 567
Cdd:PRK15064 516 FSGTYEEYLRSQGI 529
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
93-285 |
3.67e-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: 3.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 93 IRQKFFHAILRQEMGWFDIKGTTELNTRLTDDVSKISEGIGdKVGMFFQAIATFFAGFIVGFIRGWKLTLVIMAISPILG 172
Cdd:cd18543 74 LRTDLFAHLQRLDGAFHDRWQSGQLLSRATSDLSLVQRFLA-FGPFLLGNLLTLVVGLVVMLVLSPPLALVALASLPPLV 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 173 LSTAVWAKILSTFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKELERYQKHLENAKKIGIKKA-ISANISMGIAfLL 251
Cdd:cd18543 153 LVARRFRRRYFPASRRAQDQAGDLATVVEESVTGIRVVKAFGRERRELDRFEAAARRLRATRLRAArLRARFWPLLE-AL 231
|
170 180 190
....*....|....*....|....*....|....
gi 568932737 252 IYASYALAFWYGSTLVISKEYTIGnAMTVFFSIL 285
Cdd:cd18543 232 PELGLAAVLALGGWLVANGSLTLG-TLVAFSAYL 264
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
978-1201 |
5.17e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 51.01 E-value: 5.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 978 VTFNEVVFNYPtraNVPVL-QGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLldgQEAKklnvqwlrAQL 1056
Cdd:PLN03073 509 ISFSDASFGYP---GGPLLfKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVF---RSAK--------VRM 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1057 GIVSQEPIlfdcsiaeniaYGDNSRVVPHDEIVRAakeanihpFIETLPQKYNTRVGDKGTQ----------LSGGQKQR 1126
Cdd:PLN03073 575 AVFSQHHV-----------DGLDLSSNPLLYMMRC--------FPGVPEQKLRAHLGSFGVTgnlalqpmytLSGGQKSR 635
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568932737 1127 IAIARALIRQPRVLLLDEATSALDTESEKVVQEALDKAREGrtCIVIAHRLSTIQNA-DLIVVIENGKVKE-HGTHQ 1201
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 ... |
65-282 |
6.34e-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: 49.41 E-value: 6.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 65 SGLGGGVLVAAYIQVSFWTLAAGRQIKKI----RQKFFHAILRQEMGWFDIKGTTELNTRLTDDVSKISEGIGDKVGMFF 140
Cdd:cd18546 42 AAAYLAVVLAGWVAQRAQTRLTGRTGERLlydlRLRVFAHLQRLSLDFHERETSGRIMTRMTSDIDALSELLQTGLVQLV 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 141 QAIATFFAGFIVGFIRGWKLTLVIMAISPILGLSTAVW---------------AKILSTFSdkelaayakagavaeEALG 205
Cdd:cd18546 122 VSLLTLVGIAVVLLVLDPRLALVALAALPPLALATRWFrrrssrayrrareriAAVNADLQ---------------ETLA 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 206 AIRTVIAFGGQNKELERYQKHLENAKKIGIKkaisANISMGIAF----LLIYASYALAFWYGSTLVISKEYTIGnAMTVF 281
Cdd:cd18546 187 GIRVVQAFRRERRNAERFAELSDDYRDARLR----AQRLVAIYFpgveLLGNLATAAVLLVGAWRVAAGTLTVG-VLVAF 261
|
.
gi 568932737 282 F 282
Cdd:cd18546 262 L 262
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
991-1187 |
6.94e-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: 6.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 991 ANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQllERFYDPMAGSVLLDGQEAKKLNVQWLrAQLGIVsqepilfdcsI 1070
Cdd:cd03238 6 ANVHNLQNLDVSIPLNVLVVVTGVSGSGKSTLVN--EGLYASGKARLISFLPKFSRNKLIFI-DQLQFL----------I 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1071 AENIAYgdnsrvvphdeivraakeanihpfiETLPQKYNTrvgdkgtqLSGGQKQRIAIARALIRQPR--VLLLDEATSA 1148
Cdd:cd03238 73 DVGLGY-------------------------LTLGQKLST--------LSGGELQRVKLASELFSEPPgtLFILDEPSTG 119
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 568932737 1149 LDTESEKVVQEALDKAR-EGRTCIVIAHRLSTIQNADLIV 1187
Cdd:cd03238 120 LHQQDINQLLEVIKGLIdLGNTVILIEHNLDVLSSADWII 159
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
1079-1193 |
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 568932737 1079 NSRVVPHDEIVRAAKEANIHPFIETLPQKYNTRVGD---KGtqLSGGQKQRIAIARALIRQPRVLLLDEATSALDTESek 1155
Cdd:TIGR00956 169 QNRPDGVSREEYAKHIADVYMATYGLSHTRNTKVGNdfvRG--VSGGERKRVSIAEASLGGAKIQCWDNATRGLDSAT-- 244
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 568932737 1156 vvqeALDKAREGRTCIVIAHRLSTI------QNA----DLIVVIENGK 1193
Cdd:TIGR00956 245 ----ALEFIRALKTSANILDTTPLVaiyqcsQDAyelfDKVIVLYEGY 288
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
338-560 |
8.32e-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: 49.93 E-value: 8.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 338 LEFSDVHFSYPSRAnikILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIdGQDIRnfnvrclreiIG 417
Cdd:TIGR03719 323 IEAENLTKAFGDKL---LIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETVK----------LA 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 418 VVSQ--EPVLFSTTIAENIRYGrgnvtMDEIEKAVKEAN--AY----DFIMKLPQKfdtLVGdrgaQLSGGQKQRIAIAR 489
Cdd:TIGR03719 389 YVDQsrDALDPNKTVWEEISGG-----LDIIKLGKREIPsrAYvgrfNFKGSDQQK---KVG----QLSGGERNRVHLAK 456
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568932737 490 ALVRNPKILLLDEATSALDTESEAEVQAALDKAreGRTTIVIAH-RLSTIRNADVIAGFEDGVIVE--QGSHSE 560
Cdd:TIGR03719 457 TLKSGGNVLLLDEPTNDLDVETLRALEEALLNF--AGCAVVISHdRWFLDRIATHILAFEGDSHVEwfEGNFSE 528
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
349-567 |
8.44e-06 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 49.78 E-value: 8.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 349 SRANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIR-NFNVRCLREIIGVVSQ---EPV 424
Cdd:PRK09700 272 TSRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISpRSPLDAVKKGMAYITEsrrDNG 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 425 LFST-TIAENI------RYGRGNVTMDEIEKAVKEANAYDFIMKLPQKFDTlVGDRGAQLSGGQKQRIAIARALVRNPKI 497
Cdd:PRK09700 352 FFPNfSIAQNMaisrslKDGGYKGAMGLFHEVDEQRTAENQRELLALKCHS-VNQNITELSGGNQQKVLISKWLCCCPEV 430
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568932737 498 LLLDEATSALDTESEAEVQAALDK-AREGRTTIVIAHRLSTIRNA-DVIAGFEDGVIVEQGSHSELMKKEGI 567
Cdd:PRK09700 431 IIFDEPTRGIDVGAKAEIYKVMRQlADDGKVILMVSSELPEIITVcDRIAVFCEGRLTQILTNRDDMSEEEI 502
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
150-289 |
1.08e-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: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 150 FIVGFIRGWKLTLVIMAISPILGLSTAVWAKILSTFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKELERYQKHLEN 229
Cdd:cd18568 133 LGLMFYYNLQLTLIVLAFIPLYVLLTLLSSPKLKRNSREIFQANAEQQSFLVEALTGIATIKALAAERPIRWRWENKFAK 212
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568932737 230 AKKIGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTIGN--AMTVFFSILIGAF 289
Cdd:cd18568 213 ALNTRFRGQKLSIVLQLISSLINHLGTIAVLWYGAYLVISGQLTIGQlvAFNMLFGSVINPL 274
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
995-1161 |
1.12e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 49.78 E-value: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 995 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLdgqeAKKLnvqwlraQLGIVSQEPILFdcsiaeni 1074
Cdd:PRK10636 327 ILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL----AKGI-------KLGYFAQHQLEF-------- 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1075 AYGDNSrvvPHDEIVRAAkeanihpfietlPQKYNTRV----------GDKGT----QLSGGQKQRIAIARALIRQPRVL 1140
Cdd:PRK10636 388 LRADES---PLQHLARLA------------PQELEQKLrdylggfgfqGDKVTeetrRFSGGEKARLVLALIVWQRPNLL 452
|
170 180
....*....|....*....|.
gi 568932737 1141 LLDEATSALDTESEKVVQEAL 1161
Cdd:PRK10636 453 LLDEPTNHLDLDMRQALTEAL 473
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
995-1179 |
1.15e-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: 49.55 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 995 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVLLdGQEAKklnvqwlraqLGIVSQ--EPILFDCSIAE 1072
Cdd:TIGR03719 337 LIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETVK----------LAYVDQsrDALDPNKTVWE 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1073 NIAYGdnsrvvpHDEIVRAAKEANIHPFIetlpQKYNTRVGD---KGTQLSGGQKQRIAIARALIRQPRVLLLDEATSAL 1149
Cdd:TIGR03719 406 EISGG-------LDIIKLGKREIPSRAYV----GRFNFKGSDqqkKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDL 474
|
170 180 190
....*....|....*....|....*....|....*.
gi 568932737 1150 DTESEKVVQEALDKAreGRTCIVIAH------RLST 1179
Cdd:TIGR03719 475 DVETLRALEEALLNF--AGCAVVISHdrwfldRIAT 508
|
|
| ABC_6TM_CyaB_HlyB_like |
cd18588 |
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ... |
150-290 |
1.93e-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: 1.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 150 FIVGFIRGWKLTLVIMAISPILGLSTAVWAKILSTFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKELERYQKHLEN 229
Cdd:cd18588 133 LAVMFYYSPTLTLIVLASLPLYALLSLLVTPILRRRLEEKFQRGAENQSFLVETVTGIETVKSLAVEPQFQRRWEELLAR 212
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568932737 230 AKKIGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTIGnaMTVFFSILIGAFS 290
Cdd:cd18588 213 YVKASFKTANLSNLASQIVQLIQKLTTLAILWFGAYLVMDGELTIG--QLIAFNMLAGQVS 271
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
696-918 |
2.04e-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: 2.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 696 NMFSLVFLGLGVLSFFTFFLQGFTFGKAGEILTTRLRSMAFKAMLRQDMSWFDdhKNSTGALSTRLAtDAAQVQG-ATGT 774
Cdd:cd18782 42 YVIGVVMLVAALLEAVLTALRTYLFTDTANRIDLELGGTIIDHLLRLPLGFFD--KRPVGELSTRIS-ELDTIRGfLTGT 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 775 RLALIAqNTANLGTGIIISFIYGWQLTLLLLSVVPFIAVAGIVEMKMLagnAKRDKKEMEAAGKIAT---EAIENIRTVV 851
Cdd:cd18782 119 ALTTLL-DVLFSVIYIAVLFSYSPLLTLVVLATVPLQLLLTFLFGPIL---RRQIRRRAEASAKTQSylvESLTGIQTVK 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568932737 852 SLTQERKFESMYvEKLHGPYRNSVRKAHIYGITFS-ISQAFMYFSYAGCFRFGSYLIVNGHMRFKDVI 918
Cdd:cd18782 195 AQNAELKARWRW-QNRYARSLGEGFKLTVLGTTSGsLSQFLNKLSSLLVLWVGAYLVLRGELTLGQLI 261
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
359-567 |
3.05e-05 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 48.12 E-value: 3.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 359 LNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVR-CLRE----------------------- 414
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAqRLARglvylpedrqssglyldaplawn 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 415 IIGVVSQEPVLFSTTIAENI---RYGRG-NVTMDEIEKAVKeanaydfimklpqkfdtlvgdrgaQLSGGQKQRIAIARA 490
Cdd:PRK15439 362 VCALTHNRRGFWIKPARENAvleRYRRAlNIKFNHAEQAAR------------------------TLSGGNQQKVLIAKC 417
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568932737 491 LVRNPKILLLDEATSALDTESEAEV-QAALDKAREGRTTIVIAHRLstirnaDVIAGFEDGVIV-EQGSHSELMKKEGI 567
Cdd:PRK15439 418 LEASPQLLIVDEPTRGVDVSARNDIyQLIRSIAAQNVAVLFISSDL------EEIEQMADRVLVmHQGEISGALTGAAI 490
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
989-1196 |
3.11e-05 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 48.24 E-value: 3.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 989 TRANVPVLQGLSLEVKKGQTLALVGSSGCGKStvvQLLERFY--DPMA-GSVLLDGQEAK-KLNVQWLRAQLGIVSQ--- 1061
Cdd:PRK09700 272 TSRDRKKVRDISFSVCRGEILGFAGLVGSGRT---ELMNCLFgvDKRAgGEIRLNGKDISpRSPLDAVKKGMAYITEsrr 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1062 EPILF-DCSIAENIA---------YGDNSRVVPHDEIVRAAKEANihpfiETLPQKYNTrVGDKGTQLSGGQKQRIAIAR 1131
Cdd:PRK09700 349 DNGFFpNFSIAQNMAisrslkdggYKGAMGLFHEVDEQRTAENQR-----ELLALKCHS-VNQNITELSGGNQQKVLISK 422
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568932737 1132 ALIRQPRVLLLDEATSALDTESEKVVQEALDK-AREGRTCIVIAHRLSTIQNA-DLIVVIENGKVKE 1196
Cdd:PRK09700 423 WLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQlADDGKVILMVSSELPEIITVcDRIAVFCEGRLTQ 489
|
|
| ABC_6TM_CyaB_HlyB_like |
cd18588 |
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ... |
790-912 |
3.32e-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: 47.11 E-value: 3.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 790 IIISFIYGWQLTLLLLSVVPFIAVAGIVEMKMLagNAKRDKKEMEAAGKIA--TEAIENIRTVVSLTQERKFESMYVEKL 867
Cdd:cd18588 133 LAVMFYYSPTLTLIVLASLPLYALLSLLVTPIL--RRRLEEKFQRGAENQSflVETVTGIETVKSLAVEPQFQRRWEELL 210
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 568932737 868 HGPYRNSVRKAHIYGITFSISQAFMYFSYAGCFRFGSYLIVNGHM 912
Cdd:cd18588 211 ARYVKASFKTANLSNLASQIVQLIQKLTTLAILWFGAYLVMDGEL 255
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
1111-1187 |
3.34e-05 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 48.15 E-value: 3.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1111 RVGDKGTQLSGGQKQRIAIARALIRQP--RVL-LLDEATSALDTES----EKVVQEALDKareGRTCIVIAHRLSTIQNA 1183
Cdd:PRK00349 823 KLGQPATTLSGGEAQRVKLAKELSKRStgKTLyILDEPTTGLHFEDirklLEVLHRLVDK---GNTVVVIEHNLDVIKTA 899
|
....
gi 568932737 1184 DLIV 1187
Cdd:PRK00349 900 DWII 903
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
1002-1190 |
3.58e-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: 3.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1002 EVKKGQTLALVGSSGCGKSTVVQLlerfydpMAGSVLLDGQeakklNVQWlraqlgivsqepilfdcsiaeniaygdnsr 1081
Cdd:cd03222 21 VVKEGEVIGIVGPNGTGKTTAVKI-------LAGQLIPNGD-----NDEW------------------------------ 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1082 vvphDEIVRAAKeanihpfietlPQKyntrvgdkgTQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEAL 1161
Cdd:cd03222 59 ----DGITPVYK-----------PQY---------IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAI 114
|
170 180 190
....*....|....*....|....*....|..
gi 568932737 1162 DKARE--GRTCIVIAHRLSTIQN-ADLIVVIE 1190
Cdd:cd03222 115 RRLSEegKKTALVVEHDLAVLDYlSDRIHVFE 146
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
373-544 |
3.62e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 46.02 E-value: 3.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 373 GNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFnvrclreiigvvsQEPvlFSTTIAENIRYgrgNVTMDEIEKAVKE 452
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNI-------------AKP--YCTYIGHNLGL---KLEMTVFENLKFW 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 453 ANAYDFIMKLPQ-----KFDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALD-KAREGR 526
Cdd:PRK13541 95 SEIYNSAETLYAaihyfKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLIVmKANSGG 174
|
170
....*....|....*...
gi 568932737 527 TTIVIAHRLSTIRNADVI 544
Cdd:PRK13541 175 IVLLSSHLESSIKSAQIL 192
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
356-515 |
3.80e-05 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 47.69 E-value: 3.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 356 LKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQDIRNFNVR-CLREIIGVVSQEP-----VL---- 425
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQdGLANGIVYISEDRkrdglVLgmsv 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 426 ---FSTTIAENIRYGRGNVTMDEIEKAVKeanayDFIM----KLPQKfDTLVGDrgaqLSGGQKQRIAIARALVRNPKIL 498
Cdd:PRK10762 348 kenMSLTALRYFSRAGGSLKHADEQQAVS-----DFIRlfniKTPSM-EQAIGL----LSGGNQQKVAIARGLMTRPKVL 417
|
170
....*....|....*..
gi 568932737 499 LLDEATSALDTESEAEV 515
Cdd:PRK10762 418 ILDEPTRGVDVGAKKEI 434
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
353-554 |
4.03e-05 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 47.42 E-value: 4.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 353 IKILKGLNLKVKSGQTVALVGNSGCGKSTTVqLLQRLYDPTEGKisidgqdiRNF-------NVRCLREIIGVvsQEPVL 425
Cdd:NF000106 26 VKAVDGVDLDVREGTVLGVLGP*GAA**RGA-LPAHV*GPDAGR--------RPWrf*twcaNRRALRRTIG*--HRPVR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 426 FSTTIAENiryGRGNVTMDEIEKAVKEANAYDFIMKLPQKFD--TLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEA 503
Cdd:NF000106 95 *GRRESFS---GRENLYMIGR*LDLSRKDARARADELLERFSltEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEP 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568932737 504 TSALDTESEAEV-QAALDKAREGRTTIV----------IAHRLSTIRNADVIAgfeDGVIVE 554
Cdd:NF000106 172 TTGLDPRTRNEVwDEVRSMVRDGATVLLttqymeeaeqLAHELTVIDRGRVIA---DGKVDE 230
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
356-594 |
4.23e-05 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 46.73 E-value: 4.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 356 LKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGKISIDGQdirnfnVRCLREIIGVVSQepvlfsTTIAENIR 435
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGE------VSVIAISAGLSGQ------LTGIENIE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 436 YGR--GNVTMDEIEKAVKEANAY----DFIMKLPQKFdtlvgdrgaqlSGGQKQRIAIARALVRNPKILLLDEATSALDt 509
Cdd:PRK13546 108 FKMlcMGFKRKEIKAMTPKIIEFselgEFIYQPVKKY-----------SSGMRAKLGFSINITVNPDILVIDEALSVGD- 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 510 esEAEVQAALDKARE----GRTTIVIAHRLSTIRN-ADVIAGFEDGVIVEQGSHSELMKKegiYFRLVNMQTAGSQILSE 584
Cdd:PRK13546 176 --QTFAQKCLDKIYEfkeqNKTIFFVSHNLGQVRQfCTKIAWIEGGKLKDYGELDDVLPK---YEAFLNDFKKKSKAEQK 250
|
250
....*....|
gi 568932737 585 EFEVELSDEK 594
Cdd:PRK13546 251 EFRNKLDESR 260
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
93-289 |
4.95e-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: 4.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 93 IRQKFFHAILRQEMGWFDIKGTTELNTRLTDDVSKISE----GIGDkvgmFFQAIATFFAGFIVGFIRGWKLTLVIMAIS 168
Cdd:cd18540 77 LRKKAFEHLQTLSFSYFDKTPVGWIMARVTSDTQRLGEiiswGLVD----LVWGITYMIGILIVMLILNWKLALIVLAVV 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 169 PILGLsTAVW----------------AKILSTFSdkelaayakagavaeEALGAIRTVIAFGGQNKELERYQKHLENAKK 232
Cdd:cd18540 153 PVLAV-VSIYfqkkilkayrkvrkinSRITGAFN---------------EGITGAKTTKTLVREEKNLREFKELTEEMRR 216
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 568932737 233 IGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTIGnAMTVFFSILIGAF 289
Cdd:cd18540 217 ASVRAARLSALFLPIVLFLGSIATALVLWYGGILVLAGAITIG-TLVAFISYATQFF 272
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
1113-1208 |
5.06e-05 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 47.04 E-value: 5.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1113 GDKGTQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTESE-KVVQEALDKAREGRTCIVIAHRLSTI-QNADLIVVIE 1190
Cdd:NF000106 139 GRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRnEVWDEVRSMVRDGATVLLTTQYMEEAeQLAHELTVID 218
|
90
....*....|....*...
gi 568932737 1191 NGKVKEHGTHQQLLAQKG 1208
Cdd:NF000106 219 RGRVIADGKVDELKTKVG 236
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
319-542 |
5.66e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 47.32 E-value: 5.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 319 PKIDSFSERGHKPDNIKgNLEFSDVHFSYPSRaniKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRlyDPTEG--- 395
Cdd:PRK10938 243 PEPDEPSARHALPANEP-RIVLNNGVVSYNDR---PILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG--DHPQGysn 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 396 KISIDGQ---------DIRNFnvrclreiIGVVSQEPVL---FSTTIAENIRYGrgnvTMDEI--EKAVKEANaydfiMK 461
Cdd:PRK10938 317 DLTLFGRrrgsgetiwDIKKH--------IGYVSSSLHLdyrVSTSVRNVILSG----FFDSIgiYQAVSDRQ-----QK 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 462 LPQKFDTLVG--DRGAQ-----LSGGQkQRIA-IARALVRNPKILLLDEATSALDTESEAEVQAALDK-AREGRTTIV-- 530
Cdd:PRK10938 380 LAQQWLDILGidKRTADapfhsLSWGQ-QRLAlIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVlISEGETQLLfv 458
|
250 260
....*....|....*....|..
gi 568932737 531 ----------IAHRLSTIRNAD 542
Cdd:PRK10938 459 shhaedapacITHRLEFVPDGD 480
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
988-1150 |
5.85e-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: 5.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 988 PTRANVPVLQGLSLEVKKGQTLALVGSSGCGKST----VVQLLERFYDPmAGSVLLDGQEAKKLNVQWlRAQLGIVSQEp 1063
Cdd:cd03233 15 KGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTllkaLANRTEGNVSV-EGDIHYNGIPYKEFAEKY-PGEIIYVSEE- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1064 ilfdcsiaeniaygdnsrvvphdeivraakeaNIHPFIETLPQKYNTRVGDKGTQ----LSGGQKQRIAIARALIRQPRV 1139
Cdd:cd03233 92 --------------------------------DVHFPTLTVRETLDFALRCKGNEfvrgISGGERKRVSIAEALVSRASV 139
|
170
....*....|.
gi 568932737 1140 LLLDEATSALD 1150
Cdd:cd03233 140 LCWDNSTRGLD 150
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
981-1184 |
5.91e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 47.32 E-value: 5.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 981 NEVVFNYPTRanvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYdPMAGS--VLLDGQeakklnvqwlraQLGi 1058
Cdd:PRK10938 264 NNGVVSYNDR---PILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDH-PQGYSndLTLFGR------------RRG- 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1059 vSQEPIlFDcsIAENIAYGDNS-----RVVP----------HDEI--VRAAKEANihpfiETLPQKY------NTRVGDK 1115
Cdd:PRK10938 327 -SGETI-WD--IKKHIGYVSSSlhldyRVSTsvrnvilsgfFDSIgiYQAVSDRQ-----QKLAQQWldilgiDKRTADA 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1116 GTQ-LSGGQkQRIA-IARALIRQPRVLLLDEATSALDTESEKVVQEALDK-AREGRT--------------CivIAHRLS 1178
Cdd:PRK10938 398 PFHsLSWGQ-QRLAlIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVlISEGETqllfvshhaedapaC--ITHRLE 474
|
....*.
gi 568932737 1179 TIQNAD 1184
Cdd:PRK10938 475 FVPDGD 480
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1118-1205 |
6.26e-05 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 46.72 E-value: 6.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1118 QLSGGQKQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTI-QNADLIVVIENGKV 1194
Cdd:PRK15093 158 ELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQnnNTTILLISHDLQMLsQWADKINVLYCGQT 237
|
90
....*....|.
gi 568932737 1195 KEHGTHQQLLA 1205
Cdd:PRK15093 238 VETAPSKELVT 248
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
1118-1175 |
7.67e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 47.16 E-value: 7.67e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 568932737 1118 QLSGGQKQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEALDKARegRTCIVIAH 1175
Cdd:PLN03073 344 TFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWP--KTFIVVSH 399
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
477-532 |
7.78e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 46.65 E-value: 7.78e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 568932737 477 LSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEV-QAALDKAREGRTTIVIA 532
Cdd:PRK10982 392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIyQLIAELAKKDKGIIIIS 448
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
60-177 |
8.40e-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: 45.96 E-value: 8.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 60 YAYYYSGLGGGVLVAAYIQVSFWTLAAGRQIKKIRQKFFHAILRQEMGWFDikgTTE----LNtRLTDDVSKISEGIGDK 135
Cdd:cd18580 41 LGVYAALLVLASVLLVLLRWLLFVLAGLRASRRLHDKLLRSVLRAPMSFFD---TTPsgriLN-RFSKDIGLIDEELPLA 116
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 568932737 136 VGMFFQAIATFFAGFIvgfirgwkltlVIMAISPILGLSTAV 177
Cdd:cd18580 117 LLDFLQSLFSVLGSLI-----------VIAIVSPYFLIVLPP 147
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
1013-1186 |
8.60e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 44.86 E-value: 8.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1013 GSSGCGKSTVVQLLERFYDPMAGSVL---LDGQEAKKLNVQWLRAQLGIVSqepilfDCSIAENIAYGdnSRVVPHDEIV 1089
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGNIYyknCNINNIAKPYCTYIGHNLGLKL------EMTVFENLKFW--SEIYNSAETL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1090 RAAkeanIHPFietlpqKYNTRVGDKGTQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEALD-KAREGR 1168
Cdd:PRK13541 105 YAA----IHYF------KLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLIVmKANSGG 174
|
170
....*....|....*...
gi 568932737 1169 TCIVIAHRLSTIQNADLI 1186
Cdd:PRK13541 175 IVLLSSHLESSIKSAQIL 192
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
472-556 |
8.78e-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: 8.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 472 DRGAQ-LSGGQKQRIAIARALVRNPK--ILLLDEATSALDTESEAEVQAALDKARE-GRTTIVIAHRLSTIRNADVI--- 544
Cdd:cd03270 132 SRSAPtLSGGEAQRIRLATQIGSGLTgvLYVLDEPSIGLHPRDNDRLIETLKRLRDlGNTVLVVEHDEDTIRAADHVidi 211
|
90
....*....|....*
gi 568932737 545 ---AGFEDGVIVEQG 556
Cdd:cd03270 212 gpgAGVHGGEIVAQG 226
|
|
| ABC_6TM_MRP7_D2_like |
cd18605 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ... |
696-867 |
1.05e-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: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 696 NMFSLVFLGLGVL-SFFTFFlQGFTFGKAGEILTTRLRSMAFKAMLRQDMSWFDdhKNSTGALSTRLATDAAQVQGATGT 774
Cdd:cd18605 42 NFFLTVYGFLAGLnSLFTLL-RAFLFAYGGLRAARRLHNKLLSSILFAKMSFFD--KTPVGRILNRFSSDVYTIDDSLPF 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 775 RL-ALIAQNTANLGTGIIISFIYGWqltlLLLSVVPFIAVAGIVEMKMLAGNakRDKKEMEAA--GKIAT---EAIENIR 848
Cdd:cd18605 119 ILnILLAQLFGLLGYLVVICYQLPW----LLLLLLPLAFIYYRIQRYYRATS--RELKRLNSVnlSPLYThfsETLKGLV 192
|
170
....*....|....*....
gi 568932737 849 TVVSLTQERKFESMYVEKL 867
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. ... |
1003-1148 |
1.07e-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: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1003 VKKGQTLaLVGSSGCGKSTVVQLLER-FYDPMAGsvllDGQEakklnvqwlraqlGIVSqepilfdcsiaeniaygDNSR 1081
Cdd:pfam09818 77 IPKGITL-IVGGGFHGKSTLLEALERgVYNHIPG----DGRE-------------FVVT-----------------DPDA 121
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568932737 1082 VVPHDEIVRAAKEANIHPFIETLPQkyntrvGDKGTQL-----SGGQKQRIAIARALIRQPRVLLLDEATSA 1148
Cdd:pfam09818 122 VKIRAEDGRSVHGVDISPFINNLPP------GKDTTDFstedaSGSTSQAANIMEALEAGASLLLIDEDTSA 187
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
476-547 |
1.14e-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: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 476 QLSGGQKQRIAIARAL----VRNPKILLLDEATSALDTEseaEVQAALDKARE----GRTTIVIAHRLSTIRNADVIAGF 547
Cdd:cd03227 77 QLSGGEKELSALALILalasLKPRPLYILDEIDRGLDPR---DGQALAEAILEhlvkGAQVIVITHLPELAELADKLIHI 153
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
476-533 |
1.28e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 46.39 E-value: 1.28e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 568932737 476 QLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKARegRTTIVIAH 533
Cdd:PLN03073 344 TFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWP--KTFIVVSH 399
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
1118-1187 |
1.64e-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: 1.64e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568932737 1118 QLSGGQKQRIAIARALI---RQPRVL-LLDEATSALDTESEKVVQEALDKAR-EGRTCIVIAHRLSTIQNADLIV 1187
Cdd:cd03227 77 QLSGGEKELSALALILAlasLKPRPLyILDEIDRGLDPRDGQALAEAILEHLvKGAQVIVITHLPELAELADKLI 151
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
349-544 |
2.29e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 45.59 E-value: 2.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 349 SRANIKILKGLNLKVKSGQTVALVGNSGCGKSTTV---------QLLQRLYDPT----EGKI----------------SI 399
Cdd:PRK00635 604 SKATKHNLKDLTISLPLGRLTVVTGVSGSGKSSLIndtlvpaveEFIEQGFCSNlsiqWGAIsrlvhitrdlpgrsqrSI 683
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 400 DGQDIRNFN---------VRCLR-----------EIIGVVSQEPVLFSTTIAEN--------------------IRYGRG 439
Cdd:PRK00635 684 PLTYIKAFDdlrelfaeqPRSKRlgltkshfsfnTPLGACAECQGLGSITTTDNrtsipcpsclgkrflpqvleVRYKGK 763
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 440 NVTmDEIEKAVKEANayDFIMKLP---QKFDTL---------VGDRGAQLSGGQKQRIAIARAL---VRNPKILLLDEAT 504
Cdd:PRK00635 764 NIA-DILEMTAYEAE--KFFLDEPsihEKIHALcslgldylpLGRPLSSLSGGEIQRLKLAYELlapSKKPTLYVLDEPT 840
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 568932737 505 SALDTES-EAEVQAALDKAREGRTTIVIAHRLSTIRNADVI 544
Cdd:PRK00635 841 TGLHTHDiKALIYVLQSLTHQGHTVVIIEHNMHVVKVADYV 881
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
989-1208 |
3.92e-04 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 44.73 E-value: 3.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 989 TRAnvpvLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLerfydpmAGsvlldgqeAKKL---NVQWL---------RAQL 1056
Cdd:NF033858 14 TVA----LDDVSLDIPAGCMVGLIGPDGVGKSSLLSLI-------AG--------ARKIqqgRVEVLggdmadarhRRAV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1057 GivsqeP-ILF-----------DCSIAENIAY-GdnsRVVPHDeivRAAKEANI---------HPFIETLPQKyntrvgd 1114
Cdd:NF033858 75 C-----PrIAYmpqglgknlypTLSVFENLDFfG---RLFGQD---AAERRRRIdellratglAPFADRPAGK------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1115 kgtqLSGGQKQRIAIARALIRQPRVLLLDEATSALDTESEKvvQ-----EALDKAREGRTCIViahrlST--IQNA---D 1184
Cdd:NF033858 137 ----LSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLSRR--QfweliDRIRAERPGMSVLV-----ATayMEEAerfD 205
|
250 260
....*....|....*....|....
gi 568932737 1185 LIVVIENGKVKEHGTHQQLLAQKG 1208
Cdd:NF033858 206 WLVAMDAGRVLATGTPAELLARTG 229
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
348-531 |
3.99e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 44.40 E-value: 3.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 348 PSRANIKILKGLNLKVKSGQTVALVGNSGCGKS-TTVQLLQRLYDP-TEGKISIDGQDIRNFNVRCL-----------RE 414
Cdd:NF040905 268 PLHPERKVVDDVSLNVRRGEIVGIAGLMGAGRTeLAMSVFGRSYGRnISGTVFKDGKEVDVSTVSDAidaglayvtedRK 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 415 IIGVVSQEPVLFSTTIAENIRYGRGNVtMDEIEKaVKEANAY--DFIMKLPQKFDTLVgdrgaQLSGGQKQRIAIARALV 492
Cdd:NF040905 348 GYGLNLIDDIKRNITLANLGKVSRRGV-IDENEE-IKVAEEYrkKMNIKTPSVFQKVG-----NLSGGNQQKVVLSKWLF 420
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 568932737 493 RNPKILLLDEATSALDTESEAEVQAALDK-AREGRTTIVI 531
Cdd:NF040905 421 TDPDVLILDEPTRGIDVGAKYEIYTIINElAAEGKGVIVI 460
|
|
| ABC_6TM_CvaB_RaxB_like |
cd18567 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ... |
671-912 |
5.23e-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: 5.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 671 AFSIILsEMIAIFGPG------DDAVKQQKCNMFSLVFLGLGVLSFF---TFFLQGFTFGKAGEILTTRLRSMAFKAMLR 741
Cdd:cd18567 9 LLSLAL-ELFALASPLylqlviDEVIVSGDRDLLTVLAIGFGLLLLLqalLSALRSWLVLYLSTSLNLQWTSNLFRHLLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 742 QDMSWFddHKNSTGALSTRL-ATDAAQ---VQGATGTRL-ALIAqntanLGTGIIIsFIYGWQLTLLllsVVPFIAVAGI 816
Cdd:cd18567 88 LPLSYF--EKRHLGDIVSRFgSLDEIQqtlTTGFVEALLdGLMA-----ILTLVMM-FLYSPKLALI---VLAAVALYAL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 817 VEMKMLAGNAKRDKKEMEAAGKIATEAIENIRTVVSL-------TQERKFESMYVEKLhgpyrNSVRKAHIYGITFS-IS 888
Cdd:cd18567 157 LRLALYPPLRRATEEQIVASAKEQSHFLETIRGIQTIklfgreaEREARWLNLLVDAI-----NADIRLQRLQILFSaAN 231
|
250 260
....*....|....*....|....
gi 568932737 889 QAFMYFSYAGCFRFGSYLIVNGHM 912
Cdd:cd18567 232 GLLFGLENILVIYLGALLVLDGEF 255
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
346-544 |
6.50e-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: 6.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 346 SYPSRANIKILKGLNLkvksgqtvaLVGNSGCGKSTTVQLLqrlydptegKISIDGQDIRNFNVRC-LREIIGVVS---Q 421
Cdd:cd03240 11 SFHERSEIEFFSPLTL---------IVGQNGAGKTTIIEAL---------KYALTGELPPNSKGGAhDPKLIREGEvraQ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 422 EPVLFSTTIAENIrygrgnvtmdeieKAVKEANAYDFIMKLPQ-KFDTLVGDRGAQLSGGQKQ------RIAIARALVRN 494
Cdd:cd03240 73 VKLAFENANGKKY-------------TITRSLAILENVIFCHQgESNWPLLDMRGRCSGGEKVlasliiRLALAETFGSN 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 568932737 495 PKILLLDEATSALDTESEAEVQAALDKAREG---RTTIVIAHRLSTIRNADVI 544
Cdd:cd03240 140 CGILALDEPTTNLDEENIEESLAEIIEERKSqknFQLIVITHDEELVDAADHI 192
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
455-568 |
7.05e-04 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 43.91 E-value: 7.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 455 AYDF---IMKLPQKFDTLV---------GDRGAQLSGGQKQRIAIARALVRNP--KIL-LLDEATSALDTESEA---EV- 515
Cdd:PRK00349 797 ALEFfeaIPKIARKLQTLVdvglgyiklGQPATTLSGGEAQRVKLAKELSKRStgKTLyILDEPTTGLHFEDIRkllEVl 876
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 568932737 516 QAALDKareGRTTIVIAHRLSTIRNADVIA--GFEDGV----IVEQGSHSELMKKEGIY 568
Cdd:PRK00349 877 HRLVDK---GNTVVVIEHNLDVIKTADWIIdlGPEGGDgggeIVATGTPEEVAKVEASY 932
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
476-562 |
7.67e-04 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 43.25 E-value: 7.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 476 QLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKARE--GRTTIVIAHRLSTIRN-ADVIAGFEDGVI 552
Cdd:PRK15093 158 ELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQnnNTTILLISHDLQMLSQwADKINVLYCGQT 237
|
90
....*....|
gi 568932737 553 VEQGSHSELM 562
Cdd:PRK15093 238 VETAPSKELV 247
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1106-1162 |
1.37e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 42.80 E-value: 1.37e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 568932737 1106 QKyntRVGdkgtQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEALD 1162
Cdd:PRK11819 440 QK---KVG----VLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVETLRALEEALL 489
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
790-912 |
1.47e-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: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 790 IIISFIYGWQLTLLLLSVVP-FIAVAGIVEMKMLAGNAKRDKKEMEAAGKIaTEAIENIRTVVSLTQERKFESmYVEKLH 868
Cdd:cd18568 133 LGLMFYYNLQLTLIVLAFIPlYVLLTLLSSPKLKRNSREIFQANAEQQSFL-VEALTGIATIKALAAERPIRW-RWENKF 210
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 568932737 869 GPYRNSVRKAHIYGITFS-ISQAFMYFSYAGCFRFGSYLIVNGHM 912
Cdd:cd18568 211 AKALNTRFRGQKLSIVLQlISSLINHLGTIAVLWYGAYLVISGQL 255
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
1117-1187 |
1.50e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 43.09 E-value: 1.50e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568932737 1117 TQLSGGQKQRIAIARALIR--QPRVL-LLDEATSALDTESEKVVQEALDKARE-GRTCIVIAHRLSTIQNADLIV 1187
Cdd:COG0178 825 TTLSGGEAQRVKLASELSKrsTGKTLyILDEPTTGLHFHDIRKLLEVLHRLVDkGNTVVVIEHNLDVIKTADWII 899
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
477-570 |
1.87e-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: 1.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 477 LSGGQKQRIAIARAL------VrnpkILLLDEATSAL---DTESEAEVqaaLDKARE-GRTTIVIAHRLSTIRNADVI-- 544
Cdd:TIGR00630 489 LSGGEAQRIRLATQIgsgltgV----LYVLDEPSIGLhqrDNRRLINT---LKRLRDlGNTLIVVEHDEDTIRAADYVid 561
|
90 100 110
....*....|....*....|....*....|....
gi 568932737 545 ----AGFEDGVIVEQGSHSELMKKE----GIYFR 570
Cdd:TIGR00630 562 igpgAGEHGGEVVASGTPEEILANPdsltGQYLS 595
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
477-568 |
2.80e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 41.94 E-value: 2.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 477 LSGGQKQRIAIARALVR--NPKIL-LLDEATSALDTEseaEVQ---AALDKARE-GRTTIVIAHRLSTIRNAD-VI---- 544
Cdd:COG0178 827 LSGGEAQRVKLASELSKrsTGKTLyILDEPTTGLHFH---DIRkllEVLHRLVDkGNTVVVIEHNLDVIKTADwIIdlgp 903
|
90 100
....*....|....*....|....*
gi 568932737 545 -AGFEDGVIVEQGSHSELMKKEGIY 568
Cdd:COG0178 904 eGGDGGGEIVAEGTPEEVAKVKASY 928
|
|
| PRK01889 |
PRK01889 |
GTPase RsgA; Reviewed |
996-1026 |
3.55e-03 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234988 [Multi-domain] Cd Length: 356 Bit Score: 41.07 E-value: 3.55e-03
10 20 30
....*....|....*....|....*....|..
gi 568932737 996 LQGLSLEVKKGQTLALVGSSGCGKSTVV-QLL 1026
Cdd:PRK01889 185 LDVLAAWLSGGKTVALLGSSGVGKSTLVnALL 216
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
1112-1198 |
4.98e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 41.35 E-value: 4.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 1112 VGDKGTQLSGGQKQRIAIARALI---RQPRVLLLDEATSALDTESEKVVQEALDK-AREGRTCIVIAHRLSTIQNADLIV 1187
Cdd:PRK00635 1693 LGQNLSSLSLSEKIAIKIAKFLYlppKHPTLFLLDEIATSLDNQQKSALLVQLRTlVSLGHSVIYIDHDPALLKQADYLI 1772
|
90
....*....|.
gi 568932737 1188 VIENGKVKEHG 1198
Cdd:PRK00635 1773 EMGPGSGKTGG 1783
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1117-1187 |
7.28e-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: 40.73 E-value: 7.28e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568932737 1117 TQLSGGQKQRIAIarALI-----RQPRVL-LLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIV 1187
Cdd:pfam02463 1076 DLLSGGEKTLVAL--ALIfaiqkYKPAPFyLLDEIDAALDDQNVSRVANLLKELSKNAQFIVISLREEMLEKADKLV 1150
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
1119-1187 |
7.77e-03 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 39.55 E-value: 7.77e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568932737 1119 LSGGQKQRIAIARALIRQPRVLL--LDEATSALDTESEKVVQEALDKARE-GRTCIVIAHRLSTIQNADLIV 1187
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; ... |
61-227 |
9.07e-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: 9.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 61 AYY---YSGLGGGVLVAAYIQVSFWTLAAGRQIKKIRQKFFHAILRQEMGWFDikgTT---ELNTRLTDDVSKISEGIGD 134
Cdd:cd18604 43 LYYlgiYALISLLSVLLGTLRYLLFFFGSLRASRKLHERLLHSVLRAPLRWLD---TTpvgRILNRFSKDIETIDSELAD 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932737 135 KVGMFFQAIATFFAGFIVGFIRGWKL---TLVIMAISPILG---LSTAVWAK---------ILSTFSdkelaayakagav 199
Cdd:cd18604 120 SLSSLLESTLSLLVILIAIVVVSPAFllpAVVLAALYVYIGrlyLRASRELKrlesvarspILSHFG------------- 186
|
170 180
....*....|....*....|....*...
gi 568932737 200 aeEALGAIRTVIAFGGQnkelERYQKHL 227
Cdd:cd18604 187 --ETLAGLVTIRAFGAE----ERFIEEM 208
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