|
Name |
Accession |
Description |
Interval |
E-value |
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
462-992 |
1.13e-90 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 300.06 E-value: 1.13e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 462 SLAYGAKILLNTATLRLKRGHRYGLCGKNGTGKSTLMRAITnGQVEgfpsPDE--------VRTFYVEHDIDGSEaDTSV 533
Cdd:COG0488 5 SKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILA-GELE----PDSgevsipkgLRIGYLPQEPPLDD-DLTV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 534 LQFILTDKRVL-------------------------------------SSEAEIKEALASVGFNDERQKQAIGSLSGGWK 576
Cdd:COG0488 79 LDTVLDGDAELraleaeleeleaklaepdedlerlaelqeefealggwEAEARAEEILSGLGFPEEDLDRPVSELSGGWR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 577 MKLALARAMLFKADILLLDEPTNHLDVVNVAWLENYLTSLKtCTSIIVSHDSGFLNNTITDVLHLNRFKLRRYRGN---- 652
Cdd:COG0488 159 RRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYP-GTVLVVSHDRYFLDRVATRILELDRGKLTLYPGNysay 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 653 ------------------------LESFV-----------KAVPEAKSYYSLEALE------DYKFKLPDPPLLeGvktk 691
Cdd:COG0488 238 leqraerleqeaaayakqqkkiakEEEFIrrfrakarkakQAQSRIKALEKLEREEpprrdkTVEIRFPPPERL-G---- 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 692 eKSLLKMRKVGFQYPTQAVqqLYDITLQVSLSSRVAILGPNGSGKSTLVKLLIGDMEPNkGGEIWKHPNLVIGYVAQhaf 771
Cdd:COG0488 313 -KKVLELEGLSKSYGDKTL--LDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPD-SGTVKLGETVKIGYFDQ--- 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 772 HHIDHHLDKTPleymlwryqtgedLEEMSKANRQITEAEAqkmkegalivvegqkrlieeiitrkklkqsyeyevsfkgl 851
Cdd:COG0488 386 HQEELDPDKTV-------------LDELRDGAPGGTEQEV---------------------------------------- 412
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 852 ssseniwlprdelvkRGFekkvievdtreaqrLGllrplvrreiekhfaDFGLEPEFVsHNTMRGLSGGQKVKIVLGAAT 931
Cdd:COG0488 413 ---------------RGY--------------LG---------------RFLFSGDDA-FKPVGVLSGGEKARLALAKLL 447
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1933195014 932 WRRPHVICLDEPTNYLDRESLAALIAALKVFEGGVLIITHNRDFSESLCHEVWAMRDGRLE 992
Cdd:COG0488 448 LSPPNVLLLDEPTNHLDIETLEALEEALDDFPGTVLLVSHDRYFLDRVATRILEFEDGGVR 508
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
461-991 |
4.65e-62 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 225.51 E-value: 4.65e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 461 FSLAYGAKILLNTATLRLKRGHRYGLCGKNGTGKSTLMRAITNGQVEGFPSpdEVRTFYVEHDIDGSeaDTSVLQFIL-T 539
Cdd:PLN03073 183 FSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMAMHAIDGIPK--NCQILHVEQEVVGD--DTTALQCVLnT 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 540 D---KRVLSSEAEIKEA----------------------------------------------------LASVGFNDERQ 564
Cdd:PLN03073 259 DierTQLLEEEAQLVAQqrelefetetgkgkgankdgvdkdavsqrleeiykrlelidaytaearaasiLAGLSFTPEMQ 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 565 KQAIGSLSGGWKMKLALARAMLFKADILLLDEPTNHLDVVNVAWLENYLTSLKTcTSIIVSHDSGFLNNTITDVLHLNRF 644
Cdd:PLN03073 339 VKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPK-TFIVVSHAREFLNTVVTDILHLHGQ 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 645 KLRRYRGNLESFVKAVPE-----AKSYYSLE----------------------------ALE------------DYKFKL 679
Cdd:PLN03073 418 KLVTYKGDYDTFERTREEqlknqQKAFESNErsrshmqafidkfrynakraslvqsrikALDrlghvdavvndpDYKFEF 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 680 PDPPLLEGVktkekSLLKMRKVGFQYPTQAVqQLYDITLQVSLSSRVAILGPNGSGKSTLVKLLIGDMEPNKgGEIWKHP 759
Cdd:PLN03073 498 PTPDDRPGP-----PIISFSDASFGYPGGPL-LFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSS-GTVFRSA 570
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 760 NLVIGYVAQhafHHIDH-HLDKTPLEYMLwryqtgedleemskanRQITEAEAQKMKegalivvegqkrlieeiitrkkl 838
Cdd:PLN03073 571 KVRMAVFSQ---HHVDGlDLSSNPLLYMM----------------RCFPGVPEQKLR----------------------- 608
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 839 kqsyeyevsfkglssseniwlprdelvkrgfekkvievdtreaqrlgllrplvrreieKHFADFGLEPEfVSHNTMRGLS 918
Cdd:PLN03073 609 ----------------------------------------------------------AHLGSFGVTGN-LALQPMYTLS 629
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1933195014 919 GGQKVKIVLGAATWRRPHVICLDEPTNYLDRESLAALIAALKVFEGGVLIITHNRDFSESLCHEVWAMRDGRL 991
Cdd:PLN03073 630 GGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGLVLFQGGVLMVSHDEHLISGSVDELWVVSEGKV 702
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
466-1054 |
1.22e-51 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 193.08 E-value: 1.22e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 466 GAKILLNTATLRLKRGHRYGLCGKNGTGKSTLMRAITNG-QVEG--FPSPDEVRTFYVEHDIDGseADTSVLQFILT-DK 541
Cdd:PRK10636 12 GVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEiSADGgsYTFPGNWQLAWVNQETPA--LPQPALEYVIDgDR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 542 RVLSSEAEIKEA-------------------------------LASVGFNDERQKQAIGSLSGGWKMKLALARAMLFKAD 590
Cdd:PRK10636 90 EYRQLEAQLHDAnerndghaiatihgkldaidawtirsraaslLHGLGFSNEQLERPVSDFSGGWRMRLNLAQALICRSD 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 591 ILLLDEPTNHLDVVNVAWLENYLTSLkTCTSIIVSHDSGFLNNTITDVLHLNRFKLRRYRGNLESF-------------- 656
Cdd:PRK10636 170 LLLLDEPTNHLDLDAVIWLEKWLKSY-QGTLILISHDRDFLDPIVDKIIHIEQQSLFEYTGNYSSFevqratrlaqqqam 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 657 -------------------VKAVPEAKSYYSLEALEDYKFKLP---DPPLLEGVKTKE---KSLLKMRKVGFQYPTQAVq 711
Cdd:PRK10636 249 yesqqervahlqsyidrfrAKATKAKQAQSRIKMLERMELIAPahvDNPFHFSFRAPEslpNPLLKMEKVSAGYGDRII- 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 712 qLYDITLQVSLSSRVAILGPNGSGKSTLVKLLIGDMEPnKGGEIWKHPNLVIGYVAQHAFHHIdhHLDKTPLEYmlwryq 791
Cdd:PRK10636 328 -LDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAP-VSGEIGLAKGIKLGYFAQHQLEFL--RADESPLQH------ 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 792 tgedleeMSKANRQITEaeaQKMkegalivvegqkrlieeiitrkklkqsyeyevsfkglssseniwlpRDELvkrgfek 871
Cdd:PRK10636 398 -------LARLAPQELE---QKL----------------------------------------------RDYL------- 414
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 872 kvievdtreaqrlgllrplvrreiekhfADFGLEPEFVSHNTMRgLSGGQKVKIVLGAATWRRPHVICLDEPTNYLDRES 951
Cdd:PRK10636 415 ----------------------------GGFGFQGDKVTEETRR-FSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDM 465
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 952 LAALIAALKVFEGGVLIITHNRDFSESLCHEVWAMRDGRLEASGHNWVEGQGSGPRIDKKDG-EDEDQYDAMGNKVDNKK 1030
Cdd:PRK10636 466 RQALTEALIDFEGALVVVSHDRHLLRSTTDDLYLVHDGKVEPFDGDLEDYQQWLSDVQKQENqTDEAPKENNANSAQARK 545
|
650 660
....*....|....*....|....*...
gi 1933195014 1031 TKKLTSSEARK----LKKERMARKKRGE 1054
Cdd:PRK10636 546 DQKRREAELRTqtqpLRKEIARLEKEME 573
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
456-645 |
7.99e-45 |
|
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: 158.38 E-value: 7.99e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 456 LCNCQFSLAYGAKILLNTATLRLKRGHRYGLCGKNGTGKSTLMRAITNG--QVEGFP-SPDEVRTFYVEHdidgseadts 532
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGElePDEGIVtWGSTVKIGYFEQ---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 533 vlqfiltdkrvlsseaeikealasvgfnderqkqaigsLSGGWKMKLALARAMLFKADILLLDEPTNHLDVVNVAWLENY 612
Cdd:cd03221 71 --------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEA 112
|
170 180 190
....*....|....*....|....*....|...
gi 1933195014 613 LTSLKtCTSIIVSHDSGFLNNTITDVLHLNRFK 645
Cdd:cd03221 113 LKEYP-GTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
460-991 |
3.08e-44 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 168.92 E-value: 3.08e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 460 QFslayGAKILLNTATLRLKRGHRYGLCGKNGTGKSTLMRAI------TNGQVegFPSPDEvRTFYVEHDidgseadtsv 533
Cdd:PRK15064 10 QF----GAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILggdlepSAGNV--SLDPNE-RLGKLRQD---------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 534 lQFILTDKRVL-----------------------------------------------SSEAEIKEALASVGFNDERQKQ 566
Cdd:PRK15064 73 -QFAFEEFTVLdtvimghtelwevkqerdriyalpemseedgmkvadlevkfaemdgyTAEARAGELLLGVGIPEEQHYG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 567 AIGSLSGGWKMKLALARAMLFKADILLLDEPTNHLDVVNVAWLENYLTSLKtCTSIIVSHDSGFLNNTITDVLHLNRFKL 646
Cdd:PRK15064 152 LMSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVLNERN-STMIIISHDRHFLNSVCTHMADLDYGEL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 647 RRYRGNLESFVKAVPE---------AKSYYSLEALEDY--KF--------------KLPDPPLLEGVK-----------T 690
Cdd:PRK15064 231 RVYPGNYDEYMTAATQarerlladnAKKKAQIAELQSFvsRFsanaskakqatsraKQIDKIKLEEVKpssrqnpfirfE 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 691 KEKSL----LKMRKVGFQYPTQAVqqLYDITLQVSLSSRVAILGPNGSGKSTLVKLLIGDMEPNKGGEIWKHpNLVIGYV 766
Cdd:PRK15064 311 QDKKLhrnaLEVENLTKGFDNGPL--FKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSE-NANIGYY 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 767 AQHafHHIDHHLDKTPLEYM-LWRyQTGEDleemskanrqiteaeaQKMKEGALivvegqKRLieeiitrkklkqsyeye 845
Cdd:PRK15064 388 AQD--HAYDFENDLTLFDWMsQWR-QEGDD----------------EQAVRGTL------GRL----------------- 425
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 846 vsfkgLSSSENIwlprdelvkrgfeKKVIEVdtreaqrlgllrplvrreiekhfadfglepefvshntmrgLSGGQKVKI 925
Cdd:PRK15064 426 -----LFSQDDI-------------KKSVKV----------------------------------------LSGGEKGRM 447
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1933195014 926 VLGAATWRRPHVICLDEPTNYLDRESLAALIAALKVFEGGVLIITHNRDFSESLCHEVWAMRDGRL 991
Cdd:PRK15064 448 LFGKLMMQKPNVLVMDEPTNHMDMESIESLNMALEKYEGTLIFVSHDREFVSSLATRIIEITPDGV 513
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
462-1051 |
1.44e-39 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 156.65 E-value: 1.44e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 462 SLAYGAKILLNTATLRLKRGHRYGLCGKNGTGKSTLMRaITNGQV------------------EGFPSPDEVRTFY---- 519
Cdd:PRK11147 10 WLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMK-ILNGEVllddgriiyeqdlivarlQQDPPRNVEGTVYdfva 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 520 --VEHDIDGSEADTSVLQFILTD--KRVLSS----------------EAEIKEALASVGFNDERQkqaIGSLSGGWKMKL 579
Cdd:PRK11147 89 egIEEQAEYLKRYHDISHLVETDpsEKNLNElaklqeqldhhnlwqlENRINEVLAQLGLDPDAA---LSSLSGGWLRKA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 580 ALARAMLFKADILLLDEPTNHLDVVNVAWLENYLTSLKtcTSII-VSHDSGFLNNTITDVLHLNRFKLRRYRGNLESFVK 658
Cdd:PRK11147 166 ALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQ--GSIIfISHDRSFIRNMATRIVDLDRGKLVSYPGNYDQYLL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 659 AVPEAksyYSLEALEDYKF--KLPDPP--LLEGVKTKE-------KSLLKMR---------------------------- 699
Cdd:PRK11147 244 EKEEA---LRVEELQNAEFdrKLAQEEvwIRQGIKARRtrnegrvRALKALRrerserrevmgtakmqveeasrsgkivf 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 700 ---KVGFQYPTQavQQLYDITLQVSLSSRVAILGPNGSGKSTLVKLLIGDMEPNKgGEIWKHPNLVIGYVAQHafhhidh 776
Cdd:PRK11147 321 emeNVNYQIDGK--QLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADS-GRIHCGTKLEVAYFDQH------- 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 777 hldktpleymlwryqtgedleemskanRQITEAEAQKMKEgaliVVEGqkrlieeiitrkklkqsyeyevsfkglsssen 856
Cdd:PRK11147 391 ---------------------------RAELDPEKTVMDN----LAEG-------------------------------- 407
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 857 iwlprdelvkrgfeKKVIEVDTREAQRLGLLRplvrreiekhfaDFGLEPEfVSHNTMRGLSGGQKVKIVLgAATWRRP- 935
Cdd:PRK11147 408 --------------KQEVMVNGRPRHVLGYLQ------------DFLFHPK-RAMTPVKALSGGERNRLLL-ARLFLKPs 459
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 936 HVICLDEPTNYLDRESLAALIAALKVFEGGVLIITHNRDFSESLCHEVWamrdgrleasghnWVEGQGsgpRIDKKDGED 1015
Cdd:PRK11147 460 NLLILDEPTNDLDVETLELLEELLDSYQGTVLLVSHDRQFVDNTVTECW-------------IFEGNG---KIGRYVGGY 523
|
650 660 670
....*....|....*....|....*....|....*.
gi 1933195014 1016 EDQYDAMGNKVDNKKTKKLTSSEARKLKKERMARKK 1051
Cdd:PRK11147 524 HDARQQQAQYLALKQPAVKKKEEAAAPKAETVKRSS 559
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
462-656 |
1.18e-35 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 142.90 E-value: 1.18e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 462 SLAYGAKILLNTATLRLKRGHRYGLCGKNGTGKSTLMRAITnGQVEgfpsPDE--------VRTFYVEHDIDGSEADTSV 533
Cdd:COG0488 322 SKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLA-GELE----PDSgtvklgetVKIGYFDQHQEELDPDKTV 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 534 LQFIlTDKRVLSSEAEIKEALASVGFNDERQKQAIGSLSGGWKMKLALARAMLFKADILLLDEPTNHLDVVNVAWLENYL 613
Cdd:COG0488 397 LDEL-RDGAPGGTEQEVRGYLGRFLFSGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEAL 475
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1933195014 614 TSLKTCTsIIVSHDSGFLNNTITDVLHLNRFKLRRYRGNLESF 656
Cdd:COG0488 476 DDFPGTV-LLVSHDRYFLDRVATRILEFEDGGVREYPGGYDDY 517
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
698-991 |
1.31e-31 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 130.57 E-value: 1.31e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 698 MRKVGFQYPTQAVqqLYDITLQVSLSSRVAILGPNGSGKSTLVKLLIGDMEPNkGGEIWKHPNLVIGYVAQhafhhiDHH 777
Cdd:COG0488 1 LENLSKSFGGRPL--LDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPD-SGEVSIPKGLRIGYLPQ------EPP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 778 LD--KTPLEYMLwryqtgEDLEEMSKANRQITEAEAqKMKEGAlivvEGQKRLiEEIITRKKLKQSYEYEVSFKGLssse 855
Cdd:COG0488 72 LDddLTVLDTVL------DGDAELRALEAELEELEA-KLAEPD----EDLERL-AELQEEFEALGGWEAEARAEEI---- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 856 niwlprdelvkrgfekkvievdtreAQRLGLlrplvrreiekhfadfglePEFVSHNTMRGLSGGQKVKIVLGAATWRRP 935
Cdd:COG0488 136 -------------------------LSGLGF-------------------PEEDLDRPVSELSGGWRRRVALARALLSEP 171
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1933195014 936 HVICLDEPTNYLDRESLAALIAALKVFEGGVLIITHNRDFSESLCHEVWAMRDGRL 991
Cdd:COG0488 172 DLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVATRILELDRGKL 227
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
462-1018 |
3.36e-30 |
|
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: 126.97 E-value: 3.36e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 462 SLAYGAKIllntatlrlkrghryGLCGKNGTGKSTLMRAI----TNGQVEGFPSPDeVRTFYVEHD--IDGS-------E 528
Cdd:TIGR03719 27 SFFPGAKI---------------GVLGLNGAGKSTLLRIMagvdKDFNGEARPQPG-IKVGYLPQEpqLDPTktvrenvE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 529 ADTSVLQFILT--------------DKRVLSSE-AEIKEALASV-GFNDERQ-------------KQAIGSLSGGWKMKL 579
Cdd:TIGR03719 91 EGVAEIKDALDrfneisakyaepdaDFDKLAAEqAELQEIIDAAdAWDLDSQleiamdalrcppwDADVTKLSGGERRRV 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 580 ALARAMLFKADILLLDEPTNHLDVVNVAWLENYLTSLKTcTSIIVSHDSGFLNNTITDVLHLNRFKLRRYRGNLESFVka 659
Cdd:TIGR03719 171 ALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPG-TVVAVTHDRYFLDNVAGWILELDRGRGIPWEGNYSSWL-- 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 660 vpEAKS-YYSLEALEDYKFKLPDPPLLEGVK-------TKEKSLL----KMRKVGFQYPTQaVQQLY------------- 714
Cdd:TIGR03719 248 --EQKQkRLEQEEKEESARQKTLKRELEWVRqspkgrqAKSKARLaryeELLSQEFQKRNE-TAEIYippgprlgdkvie 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 715 ---------------DITLQVSLSSRVAILGPNGSGKSTLVKLLIGDMEPNKgGEIWKHPNLVIGYVAQhafhhIDHHLD 779
Cdd:TIGR03719 325 aenltkafgdkllidDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDS-GTIEIGETVKLAYVDQ-----SRDALD 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 780 --KTpleymLWryqtgedlEEMSkanrqiteaeaqkmkEGALIVVEGQKrlieEIITRkklkqSYEYEVSFKGlssseni 857
Cdd:TIGR03719 399 pnKT-----VW--------EEIS---------------GGLDIIKLGKR----EIPSR-----AYVGRFNFKG------- 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 858 wlpRDElvkrgfEKKVIEvdtreaqrlgllrplvrreiekhfadfglepefvshntmrgLSGGQKVKIVLgAATWRRPH- 936
Cdd:TIGR03719 435 ---SDQ------QKKVGQ-----------------------------------------LSGGERNRVHL-AKTLKSGGn 463
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 937 VICLDEPTNYLDRESLAALIAALKVFEGGVLIITHNRDFSESLCHEVWAMR-DGRLEasghnWVEGQGSGPRIDKKD--G 1013
Cdd:TIGR03719 464 VLLLDEPTNDLDVETLRALEEALLNFAGCAVVISHDRWFLDRIATHILAFEgDSHVE-----WFEGNFSEYEEDKKRrlG 538
|
....*
gi 1933195014 1014 EDEDQ 1018
Cdd:TIGR03719 539 EDADQ 543
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
461-995 |
4.13e-30 |
|
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: 126.17 E-value: 4.13e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 461 FSLAYGAKILLNTATLRLKRGHRYGLCGKNGTGKSTLMRAIT-----NGQVEGFPSPDEVRTFYVEHDIDGS-------E 528
Cdd:COG1123 12 VRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMgllphGGRISGEVLLDGRDLLELSEALRGRrigmvfqD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 529 ADTSV--------LQFILTDKRVLSSEAE--IKEALASVGFnDERQKQAIGSLSGGWKMKLALARAMLFKADILLLDEPT 598
Cdd:COG1123 92 PMTQLnpvtvgdqIAEALENLGLSRAEARarVLELLEAVGL-ERRLDRYPHQLSGGQRQRVAIAMALALDPDLLIADEPT 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 599 NHLDVVNVAWLENYLTSLKT---CTSIIVSHDSGFLNNTITDVLHLNRFKLrryrgnlesfVKAVPEAKSYYSLEALEDY 675
Cdd:COG1123 171 TALDVTTQAEILDLLRELQRergTTVLLITHDLGVVAEIADRVVVMDDGRI----------VEDGPPEEILAAPQALAAV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 676 KFKLPDPPLLEGVKTKEKSLLKMRKVGFQYPTQAVQQLY---DITLQVSLSSRVAILGPNGSGKSTLVKLLIGDMEPNkG 752
Cdd:COG1123 241 PRLGAARGRAAPAAAAAEPLLEVRNLSKRYPVRGKGGVRavdDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPT-S 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 753 GEI---------WKHPNL-----VIGYVAQHAFHHIDHhldktpleymlwRYQTGEDLEEMSKANRQITEAEAqkmkega 818
Cdd:COG1123 320 GSIlfdgkdltkLSRRSLrelrrRVQMVFQDPYSSLNP------------RMTVGDIIAEPLRLHGLLSRAER------- 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 819 livvegqkrlieeiitrkklkqsyeyevsfkglssseniwlprdelvkrgfEKKVIEvdtreaqrlgLLRplvrreiekh 898
Cdd:COG1123 381 ---------------------------------------------------RERVAE----------LLE---------- 389
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 899 faDFGLEPEFVS---HntmrGLSGGQKVKIVLGAATWRRPHVICLDEPTNYLD---RESLAALIAALKV-FEGGVLIITH 971
Cdd:COG1123 390 --RVGLPPDLADrypH----ELSGGQRQRVAIARALALEPKLLILDEPTSALDvsvQAQILNLLRDLQReLGLTYLFISH 463
|
570 580
....*....|....*....|....
gi 1933195014 972 NRDFSESLCHEVWAMRDGRLEASG 995
Cdd:COG1123 464 DLAVVRYIADRVAVMYDGRIVEDG 487
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
462-645 |
3.55e-28 |
|
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: 111.18 E-value: 3.55e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 462 SLAYGAKILLNTATLRLKRGHRYGLCGKNGTGKSTLMRAITngqveGFPSPDEVRTFYVEHDIdgseadtsvlqfiltdk 541
Cdd:cd00267 6 SFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIA-----GLLKPTSGEILIDGKDI----------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 542 rvlsSEAEIKEALASVGFnderqkqaIGSLSGGWKMKLALARAMLFKADILLLDEPTNHLDVVNVAWLENYLTSL--KTC 619
Cdd:cd00267 64 ----AKLPLEELRRRIGY--------VPQLSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLRELaeEGR 131
|
170 180
....*....|....*....|....*.
gi 1933195014 620 TSIIVSHDSGFLNNTITDVLHLNRFK 645
Cdd:cd00267 132 TVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
462-643 |
3.94e-28 |
|
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: 113.01 E-value: 3.94e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 462 SLAYGAKILLNTATLRLKRGHRYGLCGKNGTGKSTLMRAI------TNGQVE--GFPSPDEVRTF-YVE--HDIDgSEAD 530
Cdd:cd03235 6 TVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAIlgllkpTSGSIRvfGKPLEKERKRIgYVPqrRSID-RDFP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 531 TSVLQFILT----DKRVL-----SSEAEIKEALASVGFNDERQKQaIGSLSGGWKMKLALARAMLFKADILLLDEPTNHL 601
Cdd:cd03235 85 ISVRDVVLMglygHKGLFrrlskADKAKVDEALERVGLSELADRQ-IGELSGGQQQRVLLARALVQDPDLLLLDEPFAGV 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1933195014 602 DVVNVAWLENYLTSLK--TCTSIIVSHDSGFLNNTITDVLHLNR 643
Cdd:cd03235 164 DPKTQEDIYELLRELRreGMTILVVTHDLGLVLEYFDRVLLLNR 207
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
460-642 |
2.72e-27 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 110.68 E-value: 2.72e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 460 QFSLAYGAKILLNTATLRLKRGHRYGLCGKNGTGKSTLMRAI------TNGQV--EGFP----SPDEVRT--FYVEHD-- 523
Cdd:COG4619 5 GLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALadldppTSGEIylDGKPlsamPPPEWRRqvAYVPQEpa 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 524 -IDGSEADtsVLQFILTDKRVLSSEAEIKEALASVGFNDERQKQAIGSLSGGWKMKLALARAMLFKADILLLDEPTNHLD 602
Cdd:COG4619 85 lWGGTVRD--NLPFPFQLRERKFDRERALELLERLGLPPDILDKPVERLSGGERQRLALIRALLLQPDVLLLDEPTSALD 162
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1933195014 603 VVNVAWLENYLTSLKTC---TSIIVSHDSGFLNNTITDVLHLN 642
Cdd:COG4619 163 PENTRRVEELLREYLAEegrAVLWVSHDPEQIERVADRVLTLE 205
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
462-645 |
5.75e-27 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 109.49 E-value: 5.75e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 462 SLAYGAKILLNTATLRLKRGHRYGLCGKNGTGKSTLMRAI------TNGQV--EGFPSPDEVRTF-----YVEHDiDGSE 528
Cdd:COG4133 9 SCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILagllppSAGEVlwNGEPIRDAREDYrrrlaYLGHA-DGLK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 529 ADTSV---LQFILTDKRVLSSEAEIKEALASVGFnDERQKQAIGSLSGGWKMKLALARAMLFKADILLLDEPTNHLDVVN 605
Cdd:COG4133 88 PELTVrenLRFWAALYGLRADREAIDEALEAVGL-AGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAG 166
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1933195014 606 VAWLENYLTSLKT--CTSIIVSHDSGFLNNtiTDVLHLNRFK 645
Cdd:COG4133 167 VALLAELIAAHLArgGAVLLTTHQPLELAA--ARVLDLGDFK 206
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
696-990 |
4.40e-26 |
|
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: 104.84 E-value: 4.40e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 696 LKMRKVGFQYPTQAVqqLYDITLQVSLSSRVAILGPNGSGKSTLVKLLIGDMEPNKGgEIWKHPNLVIGYVAQhafhhid 775
Cdd:cd03221 1 IELENLSKTYGGKLL--LKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEG-IVTWGSTVKIGYFEQ------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 776 hhldktpleymlwryqtgedleemskanrqiteaeaqkmkegalivvegqkrlieeiitrkklkqsyeyevsfkglssse 855
Cdd:cd03221 --------------------------------------------------------------------------------
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 856 niwlprdelvkrgfekkvievdtreaqrlgllrplvrreiekhfadfglepefvshntmrgLSGGQKVKIVLGAATWRRP 935
Cdd:cd03221 71 -------------------------------------------------------------LSGGEKMRLALAKLLLENP 89
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1933195014 936 HVICLDEPTNYLDRESLAALIAALKVFEGGVLIITHNRDFSESLCHEVWAMRDGR 990
Cdd:cd03221 90 NLLLLDEPTNHLDLESIEALEEALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| CD_eEF3 |
cd18626 |
chromodomain-like insertion in an ATPase domain of elongation factor eEF3; Eukaryotic ... |
826-881 |
5.28e-26 |
|
chromodomain-like insertion in an ATPase domain of elongation factor eEF3; Eukaryotic elongation factor eEF3 (also known as EF-3, YEF3, and TEF3), a member of the ATP-binding cassette (ABC) family of proteins, is a ribosomal binding ATPase essential for fungal translation machinery. Until recently it was considered fungal-specific and therefore an attractive target for antifungal therapy; however, recent bioinformatics analysis indicates it may be more widely distributed among other unicellular eukaryotes, and translation elongation factor 3 activity has been demonstrated from a non-fungal species, Phytophthora infestans. eEF3 is a soluble factor lacking a transmembrane domain and having two ABC domains arranged in tandem, with a unique chromodomain inserted within the ABC2 domain. Chromodomain mutations in the ABC2 domain of eEF3 have been shown to reduce ATPase activity, but not ribosome binding. Thus, the chromodomain-like insertion is critical to eEF3 function. In addition to its elongation function, eEF3 has been shown to interact with mRNA in a translation independent manner, suggesting an additional, non-elongation function for this factor.
Pssm-ID: 349276 [Multi-domain] Cd Length: 56 Bit Score: 101.52 E-value: 5.28e-26
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1933195014 826 KRLIEEIITRKKLKQSYEYEVSFKGLSSSENIWLPRDELVKRGFEKKVIEVDTREA 881
Cdd:cd18626 1 KRVIEKIVGRRKLKKSYEYEVKWKGMSSKDNSWIPREELEEMGFEKLVQEVDDKEA 56
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
696-995 |
1.09e-25 |
|
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: 106.65 E-value: 1.09e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 696 LKMRKVGFQYPTQaVQQLYDITLQVSLSSRVAILGPNGSGKSTLVKLLIGDMEPNKG-----GEIWKHPNLV-----IGY 765
Cdd:COG1122 1 IELENLSFSYPGG-TPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGevlvdGKDITKKNLRelrrkVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 766 VAQHAFHhidhhldktpleymlwryqtgedleemskanrQITEAeaqkmkegalIVVEgqkrlieeiitrkklkqsyeyE 845
Cdd:COG1122 80 VFQNPDD--------------------------------QLFAP----------TVEE---------------------D 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 846 VSFkGLsssENIWLPRDELVKRgfekkVIEVdtreAQRLGLlrplvrreieKHFADfglepefvsHNTMRgLSGGQKVKI 925
Cdd:COG1122 97 VAF-GP---ENLGLPREEIRER-----VEEA----LELVGL----------EHLAD---------RPPHE-LSGGQKQRV 143
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1933195014 926 VLGAATWRRPHVICLDEPTNYLD---RESLAALIAALKVFEGGVLIITHNRDFSESLCHEVWAMRDGRLEASG 995
Cdd:COG1122 144 AIAGVLAMEPEVLVLDEPTAGLDprgRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADG 216
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
462-643 |
1.45e-25 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 106.71 E-value: 1.45e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 462 SLAYGAKILLNTATLRLKRGHRYGLCGKNGTGKSTLMRAI------TNGQVEGF-PSPDEVRTF--YV--EHDIDGSEAd 530
Cdd:COG1121 13 TVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAIlgllppTSGTVRLFgKPPRRARRRigYVpqRAEVDWDFP- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 531 TSVLQFILT--DKRV-----LSSE--AEIKEALASVGFNDERQKQaIGSLSGGWKMKLALARAMLFKADILLLDEPTNHL 601
Cdd:COG1121 92 ITVRDVVLMgrYGRRglfrrPSRAdrEAVDEALERVGLEDLADRP-IGELSGGQQQRVLLARALAQDPDLLLLDEPFAGV 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1933195014 602 DVVNVAWLENYLTSLKT--CTSIIVSHDSGFLNNTITDVLHLNR 643
Cdd:COG1121 171 DAATEEALYELLRELRRegKTILVVTHDLGAVREYFDRVLLLNR 214
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
465-627 |
4.47e-25 |
|
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: 102.86 E-value: 4.47e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 465 YGAKILLNTATLRLKRGHRYGLCGKNGTGKSTLMRAITngqveGFPSPDEVRTFYVEHDIdgSEADTSVLQFI--LTDKR 542
Cdd:cd03230 10 YGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIIL-----GLLKPDSGEIKVLGKDI--KKEPEEVKRRIgyLPEEP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 543 VLSSEAEIKEALasvgfnderqkqaigSLSGGWKMKLALARAMLFKADILLLDEPTNHLDVVNVAWLENYLTSLKT--CT 620
Cdd:cd03230 83 SLYENLTVRENL---------------KLSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWELLRELKKegKT 147
|
....*..
gi 1933195014 621 SIIVSHD 627
Cdd:cd03230 148 ILLSSHI 154
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
465-627 |
1.04e-24 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 103.99 E-value: 1.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 465 YGAKILLNTATLRLKRGHRYGLCGKNGTGKSTLMRAITN------GQVE--GFP---SPDEVR--------TFYVEHDID 525
Cdd:COG1131 10 YGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGllrptsGEVRvlGEDvarDPAEVRrrigyvpqEPALYPDLT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 526 GSEadtsVLQFI--LTDKRVLSSEAEIKEALASVGFnDERQKQAIGSLSGGWKMKLALARAMLFKADILLLDEPTNHLDV 603
Cdd:COG1131 90 VRE----NLRFFarLYGLPRKEARERIDELLELFGL-TDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDP 164
|
170 180
....*....|....*....|....*.
gi 1933195014 604 VNVAWLENYLTSLKT--CTSIIVSHD 627
Cdd:COG1131 165 EARRELWELLRELAAegKTVLLSTHY 190
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
464-627 |
3.77e-24 |
|
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: 102.63 E-value: 3.77e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 464 AYGAKILLNTATLRLKRGHRYGLCGKNGTGKSTLMRAI------TNG--QVEGFPS---PDEVRT--FYVeHDIDGSEAD 530
Cdd:COG4555 10 KYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLagllkpDSGsiLIDGEDVrkePREARRqiGVL-PDERGLYDR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 531 TSVLQFI-----LTDKRVLSSEAEIKEALASVGFNDERqKQAIGSLSGGWKMKLALARAMLFKADILLLDEPTNHLDVVN 605
Cdd:COG4555 89 LTVRENIryfaeLYGLFDEELKKRIEELIELLGLEEFL-DRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNGLDVMA 167
|
170 180
....*....|....*....|....
gi 1933195014 606 VAWLENYLTSLKTCTSIIV--SHD 627
Cdd:COG4555 168 RRLLREILRALKKEGKTVLfsSHI 191
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
471-599 |
7.56e-24 |
|
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: 98.49 E-value: 7.56e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 471 LNTATLRLKRGHRYGLCGKNGTGKSTLMRAI------TNGQV--EGFPSPDEVRTF------YVEHDiDGSEADTSVLQF 536
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIagllspTEGTIllDGQDLTDDERKSlrkeigYVFQD-PQLFPRLTVREN 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1933195014 537 ILTDKRVLS-----SEAEIKEALASVG---FNDERQKQAIGSLSGGWKMKLALARAMLFKADILLLDEPTN 599
Cdd:pfam00005 80 LRLGLLLKGlskreKDARAEEALEKLGlgdLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
697-990 |
1.31e-23 |
|
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: 99.85 E-value: 1.31e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 697 KMRKVGFQYPTQAVQQLYDITLQVSLSSRVAILGPNGSGKSTLVKLLIGDMEPNKG----------GEIWKHPNLVIGYV 766
Cdd:cd03225 1 ELKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGevlvdgkdltKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 767 AQHAFHHIdhhldktpleymlwryqTGEDLEEmskanrqiteaeaqkmkegalivvegqkrlieeiitrkklkqsyeyEV 846
Cdd:cd03225 81 FQNPDDQF-----------------FGPTVEE----------------------------------------------EV 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 847 SFkGLsssENIWLPRDELVKRgfekkVIEVdtreAQRLGLlrplvrreieKHFADfglepEFVSHntmrgLSGGQKVKIV 926
Cdd:cd03225 98 AF-GL---ENLGLPEEEIEER-----VEEA----LELVGL----------EGLRD-----RSPFT-----LSGGQKQRVA 144
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1933195014 927 LGAATWRRPHVICLDEPTNYLDRESLAALIAALKVF--EG-GVLIITHNRDFSESLCHEVWAMRDGR 990
Cdd:cd03225 145 IAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLkaEGkTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
465-1018 |
3.06e-23 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 105.20 E-value: 3.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 465 YGAKIllntatlrlkrghryGLCGKNGTGKSTLMRAI----TNGQVEGFPSP---------------------------- 512
Cdd:PRK11819 32 PGAKI---------------GVLGLNGAGKSTLLRIMagvdKEFEGEARPAPgikvgylpqepqldpektvrenveegva 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 513 ---------DEVRTFYVEHDIDgseadtsvlqfilTDKrvLSSE-AEIKEALASV-GFNDERQ-KQA------------I 568
Cdd:PRK11819 97 evkaaldrfNEIYAAYAEPDAD-------------FDA--LAAEqGELQEIIDAAdAWDLDSQlEIAmdalrcppwdakV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 569 GSLSGGWKMKLALARAMLFKADILLLDEPTNHLDVVNVAWLENYLTSLKTcTSIIVSHDSGFLNNTITDVLHLNRFKLRR 648
Cdd:PRK11819 162 TKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDYPG-TVVAVTHDRYFLDNVAGWILELDRGRGIP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 649 YRGN----LES------------------------FVKAVP---EAKS------YYSLEAlEDYKFKL-------PDPPL 684
Cdd:PRK11819 241 WEGNysswLEQkakrlaqeekqeaarqkalkreleWVRQSPkarQAKSkarlarYEELLS-EEYQKRNetneifiPPGPR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 685 L-------EGVkTK---EKSLLKmrKVGFQYPTQAVqqlyditlqvslssrVAILGPNGSGKSTLVKLLIGDMEPNKG-- 752
Cdd:PRK11819 320 LgdkvieaENL-SKsfgDRLLID--DLSFSLPPGGI---------------VGIIGPNGAGKSTLFKMITGQEQPDSGti 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 753 --GEIWKhpnlvIGYVAQHAfHHIDHhlDKTpleymLWryqtgedlEEMSkanrqiteaeaqkmkEGALIVVEGQKrlie 830
Cdd:PRK11819 382 kiGETVK-----LAYVDQSR-DALDP--NKT-----VW--------EEIS---------------GGLDIIKVGNR---- 421
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 831 EIITRkklkqSYeyeVS---FKGlssseniwlpRDElvkrgfEKKVievdtreaqrlGLlrplvrreiekhfadfglepe 907
Cdd:PRK11819 422 EIPSR-----AY---VGrfnFKG----------GDQ------QKKV-----------GV--------------------- 445
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 908 fvshntmrgLSGGQKVKIVLgAATWRRPH-VICLDEPTNYLDRESLAALIAALKVFEGGVLIITHNRDFSESLCHEVWAm 986
Cdd:PRK11819 446 ---------LSGGERNRLHL-AKTLKQGGnVLLLDEPTNDLDVETLRALEEALLEFPGCAVVISHDRWFLDRIATHILA- 514
|
650 660 670
....*....|....*....|....*....|....*
gi 1933195014 987 rdgrLEASGH-NWVEGQGSGPRIDKKD--GEDEDQ 1018
Cdd:PRK11819 515 ----FEGDSQvEWFEGNFQEYEEDKKRrlGADAAR 545
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
465-626 |
1.35e-22 |
|
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: 96.90 E-value: 1.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 465 YGAKILLNTATLRLKRGHRYGLCGKNGTGKSTLMRAITngqveGFPSPDEVRTFyvehdIDGSEAD-------------- 530
Cdd:cd03268 10 YGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIIL-----GLIKPDSGEIT-----FDGKSYQkniealrrigalie 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 531 --------TSVLQFILTDKRVLSSEAEIKEALASVGFNDERqKQAIGSLSGGWKMKLALARAMLFKADILLLDEPTNHLD 602
Cdd:cd03268 80 apgfypnlTARENLRLLARLLGIRKKRIDEVLDVVGLKDSA-KKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLD 158
|
170 180
....*....|....*....|....*.
gi 1933195014 603 VVNVAWLENYLTSLKT--CTSIIVSH 626
Cdd:cd03268 159 PDGIKELRELILSLRDqgITVLISSH 184
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
460-643 |
5.88e-22 |
|
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: 95.23 E-value: 5.88e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 460 QFSLAY--GAKILLNTATLRLKRGHRYGLCGKNGTGKSTLMRAItNGQveGFPSPDEVRtfyvehdIDGSEADTSVL--- 534
Cdd:cd03225 4 NLSFSYpdGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLL-NGL--LGPTSGEVL-------VDGKDLTKLSLkel 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 535 -------------QFILTdkRVLS-----------SEAEIK----EALASVGFnDERQKQAIGSLSGGWKMKLALARAML 586
Cdd:cd03225 74 rrkvglvfqnpddQFFGP--TVEEevafglenlglPEEEIEerveEALELVGL-EGLRDRSPFTLSGGQKQRVAIAGVLA 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1933195014 587 FKADILLLDEPTNHLDVVNVAWLENYLTSLKTC--TSIIVSHDSGFLNNTITDVLHLNR 643
Cdd:cd03225 151 MDPDILLLDEPTAGLDPAGRRELLELLKKLKAEgkTIIIVTHDLDLLLELADRVIVLED 209
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
462-627 |
9.08e-22 |
|
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: 93.65 E-value: 9.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 462 SLAYGAKILLNTATLRLKRGHRYGLCGKNGTGKSTLMRAItNGQVEgfPSPDEVRtfyvehdIDGSeaDTSVLQFILTDK 541
Cdd:cd03214 6 SVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTL-AGLLK--PSSGEIL-------LDGK--DLASLSPKELAR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 542 RVlsseAEIKEALASVGFNDERQKQaIGSLSGGWKMKLALARAMLFKADILLLDEPTNHLDVVNVAWLENYLTSLKT--- 618
Cdd:cd03214 74 KI----AYVPQALELLGLAHLADRP-FNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIELLELLRRLARerg 148
|
....*....
gi 1933195014 619 CTSIIVSHD 627
Cdd:cd03214 149 KTVVMVLHD 157
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
465-625 |
1.10e-19 |
|
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: 88.79 E-value: 1.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 465 YGAKILLNTATLRLKRGhRYGLCGKNGTGKSTLMRAI------TNGQVE--GFP---SPDEVRTF--YVEHDIDGSEADT 531
Cdd:cd03264 10 YGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILatltppSSGTIRidGQDvlkQPQKLRRRigYLPQEFGVYPNFT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 532 SV--LQFILTDKRVLSSE--AEIKEALASVGFNDeRQKQAIGSLSGGWKMKLALARAMLFKADILLLDEPTNHLDVVNVA 607
Cdd:cd03264 89 VRefLDYIAWLKGIPSKEvkARVDEVLELVNLGD-RAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPEERI 167
|
170
....*....|....*...
gi 1933195014 608 WLENYLTSLKTCTSIIVS 625
Cdd:cd03264 168 RFRNLLSELGEDRIVILS 185
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
462-643 |
1.83e-19 |
|
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: 88.54 E-value: 1.83e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 462 SLAY-GAKILLNTATLRLKRGHRYGLCGKNGTGKSTLMRAI------TNGQV--EGFP----SPDEVRT----------- 517
Cdd:COG1122 7 SFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLngllkpTSGEVlvDGKDitkkNLRELRRkvglvfqnpdd 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 518 --FY--VEHDI---------DGSEADtsvlqfiltdKRVlsseaeiKEALASVGFnDERQKQAIGSLSGGWKMKLALARA 584
Cdd:COG1122 87 qlFAptVEEDVafgpenlglPREEIR----------ERV-------EEALELVGL-EHLADRPPHELSGGQKQRVAIAGV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1933195014 585 MLFKADILLLDEPTNHLDVVNVAWLENYLTSLKT--CTSIIVSHDSGFLNNTITDVLHLNR 643
Cdd:COG1122 149 LAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKegKTVIIVTHDLDLVAELADRVIVLDD 209
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
462-627 |
2.61e-19 |
|
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: 88.56 E-value: 2.61e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 462 SLAYGAKILLNTATLRLKRGHRYGLCGKNGTGKSTLMRAI------TNGQV--EGFP----SPDEVRTF--YV--EHDID 525
Cdd:COG1120 8 SVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALagllkpSSGEVllDGRDlaslSRRELARRiaYVpqEPPAP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 526 GseaDTSVLQFIL-------TDKRVLSSE--AEIKEALASVGFNDERQKQaIGSLSGGWKMKLALARAMLFKADILLLDE 596
Cdd:COG1120 88 F---GLTVRELVAlgryphlGLFGRPSAEdrEAVEEALERTGLEHLADRP-VDELSGGERQRVLIARALAQEPPLLLLDE 163
|
170 180 190
....*....|....*....|....*....|....*
gi 1933195014 597 PTNHLDVVN-VAWLEnYLTSLKT---CTSIIVSHD 627
Cdd:COG1120 164 PTSHLDLAHqLEVLE-LLRRLARergRTVVMVLHD 197
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
461-627 |
1.28e-18 |
|
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: 86.08 E-value: 1.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 461 FSLAYGAKILLNTATLRLKRGHRYGLCGKNGTGKSTLMRAItNGQVEGFPS-PDEVRTFYVEHDIDGSEADTS------- 532
Cdd:cd03260 6 LNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLL-NRLNDLIPGaPDEGEVLLDGKDIYDLDVDVLelrrrvg 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 533 -VLQ----FILT---------------DKRVLssEAEIKEALASVGFNDE-RQKQAIGSLSGGWKMKLALARAMLFKADI 591
Cdd:cd03260 85 mVFQkpnpFPGSiydnvayglrlhgikLKEEL--DERVEEALRKAALWDEvKDRLHALGLSGGQQQRLCLARALANEPEV 162
|
170 180 190
....*....|....*....|....*....|....*..
gi 1933195014 592 LLLDEPTNHLDVVNVAWLENYLTSLK-TCTSIIVSHD 627
Cdd:cd03260 163 LLLDEPTSALDPISTAKIEELIAELKkEYTIVIVTHN 199
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
696-995 |
1.56e-18 |
|
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: 91.05 E-value: 1.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 696 LKMRKVGFQYPTQAVQQLYDITLQVSLSSRVAILGPNGSGKSTLVKLLIGDMEPNKgGEIwkhpnlvigyvaqhafhHID 775
Cdd:COG2274 474 IELENVSFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTS-GRI-----------------LID 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 776 hhldktpleymlwryqtGEDLEEMSKAN--RQIteaeAQKMKEGALivvegqkrlieeiitrkklkqsyeyevsFKGlSS 853
Cdd:COG2274 536 -----------------GIDLRQIDPASlrRQI----GVVLQDVFL----------------------------FSG-TI 565
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 854 SENIWLPRDELVkrgfEKKVIEVdtreAQRLGLLrplvrREIEKHfaDFGLepefvshNTM-----RGLSGGQKVKIVLG 928
Cdd:COG2274 566 RENITLGDPDAT----DEEIIEA----ARLAGLH-----DFIEAL--PMGY-------DTVvgeggSNLSGGQRQRLAIA 623
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1933195014 929 AATWRRPHVICLDEPTNYLDRESLAALIAALKVFEGG--VLIITHnRDFSESLCHEVWAMRDGRLEASG 995
Cdd:COG2274 624 RALLRNPRILILDEATSALDAETEAIILENLRRLLKGrtVIIIAH-RLSTIRLADRIIVLDKGRIVEDG 691
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
462-626 |
1.60e-18 |
|
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: 83.97 E-value: 1.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 462 SLAYGAKI--LLNTATLRLKRGHRYGLCGKNGTGKSTLMRAITngqveGFPSPDEVRTFYVEHDIdgSEADTSVLQFILT 539
Cdd:cd03228 7 SFSYPGRPkpVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLL-----RLYDPTSGEILIDGVDL--RDLDLESLRKNIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 540 dkrVLSSEAEIKEAlaSVGFNderqkqaIgsLSGGWKMKLALARAMLFKADILLLDEPTNHLDVVN-VAWLENYLTSLKT 618
Cdd:cd03228 80 ---YVPQDPFLFSG--TIREN-------I--LSGGQRQRIAIARALLRDPPILILDEATSALDPETeALILEALRALAKG 145
|
....*...
gi 1933195014 619 CTSIIVSH 626
Cdd:cd03228 146 KTVIVIAH 153
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
462-627 |
1.93e-18 |
|
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: 85.63 E-value: 1.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 462 SLAYGAKILLNTATLRLKRGHRYGLCGKNGTGKSTLMRAITnGQVEgfpsPDEVRTFYVEHDIDG-SEADT--------- 531
Cdd:cd03261 7 TKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIV-GLLR----PDSGEVLIDGEDISGlSEAELyrlrrrmgm 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 532 -----------SVLQ---FILTDKRVLSsEAEI----KEALASVGFNDERQKQAiGSLSGGWKMKLALARAMLFKADILL 593
Cdd:cd03261 82 lfqsgalfdslTVFEnvaFPLREHTRLS-EEEIreivLEKLEAVGLRGAEDLYP-AELSGGMKKRVALARALALDPELLL 159
|
170 180 190
....*....|....*....|....*....|....*..
gi 1933195014 594 LDEPTNHLDVVNVAWLENYLTSLKT---CTSIIVSHD 627
Cdd:cd03261 160 YDEPTAGLDPIASGVIDDLIRSLKKelgLTSIMVTHD 196
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
462-627 |
3.75e-18 |
|
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: 89.89 E-value: 3.75e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 462 SLAYG--AKILLNTATLRLKRGHRYGLCGKNGTGKSTLMRAI------TNGQVE--GFP----SPDEVRTF--YVEHDID 525
Cdd:COG2274 480 SFRYPgdSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLlglyepTSGRILidGIDlrqiDPASLRRQigVVLQDVF 559
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 526 ---GSeadtsVLQFI-LTDKRVlsSEAEIKEALASVGFNDERQKQAIG----------SLSGGWKMKLALARAMLFKADI 591
Cdd:COG2274 560 lfsGT-----IRENItLGDPDA--TDEEIIEAARLAGLHDFIEALPMGydtvvgeggsNLSGGQRQRLAIARALLRNPRI 632
|
170 180 190
....*....|....*....|....*....|....*..
gi 1933195014 592 LLLDEPTNHLDVVNVAWLENYLTSLKT-CTSIIVSHD 627
Cdd:COG2274 633 LILDEATSALDAETEAIILENLRRLLKgRTVIIIAHR 669
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
462-718 |
6.15e-18 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 89.07 E-value: 6.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 462 SLAYGAKILLNTATLRLKRGHRYGLCGKNGTGKSTLMRAITnGQVEgfPSPDEVRT-------FYVEHDIDGSEADTSVL 534
Cdd:PRK10636 319 SAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLA-GELA--PVSGEIGLakgiklgYFAQHQLEFLRADESPL 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 535 QFILtdkRVLSSEAE--IKEALASVGFNDERQKQAIGSLSGGWKMKLALARAMLFKADILLLDEPTNHLDVVNVAWLENY 612
Cdd:PRK10636 396 QHLA---RLAPQELEqkLRDYLGGFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEA 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 613 LTSLKTCTsIIVSHDSGFLNNTITDVLHLNRFKLRRYRGNLESFVK-------------AVPEAKSYYSLEALEDYK--- 676
Cdd:PRK10636 473 LIDFEGAL-VVVSHDRHLLRSTTDDLYLVHDGKVEPFDGDLEDYQQwlsdvqkqenqtdEAPKENNANSAQARKDQKrre 551
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1933195014 677 --FKLPDPPLLEGVKTKEKsllKMRKVGFQYpTQAVQQLYDITL 718
Cdd:PRK10636 552 aeLRTQTQPLRKEIARLEK---EMEKLNAQL-AQAEEKLGDSEL 591
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
458-642 |
9.74e-18 |
|
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: 82.69 E-value: 9.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 458 NCQFSLAYGAKILlNTATLRLKRGHRYGLCGKNGTGKSTLMRAI------TNGQV--EGFPSPDEVRT---FYVEHDIDG 526
Cdd:cd03226 4 NISFSYKKGTEIL-DDLSLDLYAGEIIALTGKNGAGKTTLAKILaglikeSSGSIllNGKPIKAKERRksiGYVMQDVDY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 527 SEADTSV-LQFILTDKRVLSSEAEIKEALASVGFNDERQKQAIgSLSGGWKMKLALARAMLFKADILLLDEPTNHLD--- 602
Cdd:cd03226 83 QLFTDSVrEELLLGLKELDAGNEQAETVLKDLDLYALKERHPL-SLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDykn 161
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1933195014 603 VVNVAWLENYLTSLKTcTSIIVSHDSGFLNNTITDVLHLN 642
Cdd:cd03226 162 MERVGELIRELAAQGK-AVIVITHDYEFLAKVCDRVLLLA 200
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
462-627 |
1.24e-17 |
|
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: 87.89 E-value: 1.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 462 SLAY-GAKILLNTATLRLKRGHRYGLCGKNGTGKSTLMRAITngqveGFPSPD---------EVRTF----------YVE 521
Cdd:COG4988 343 SFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLL-----GFLPPYsgsilingvDLSDLdpaswrrqiaWVP 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 522 HD---IDGSEADTsvlqfiLTDKRVLSSEAEIKEALASVGFND--ERQKQ----AIGS----LSGGWKMKLALARAMLFK 588
Cdd:COG4988 418 QNpylFAGTIREN------LRLGRPDASDEELEAALEAAGLDEfvAALPDgldtPLGEggrgLSGGQAQRLALARALLRD 491
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1933195014 589 ADILLLDEPTNHLDVVNVAWLENYLTSL-KTCTSIIVSHD 627
Cdd:COG4988 492 APLLLLDEPTAHLDAETEAEILQALRRLaKGRTVILITHR 531
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
461-627 |
2.19e-17 |
|
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: 82.93 E-value: 2.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 461 FSLAYGAKILLNTATLRLKRGHRYGLCGKNGTGKSTLMRAI------TNGQV--EGFP-SPDEVRTFY-----VEHDIDG 526
Cdd:COG1124 11 YGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALaglerpWSGEVtfDGRPvTRRRRKAFRrrvqmVFQDPYA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 527 S-EADTSVLQFI---LTDKRVLSSEAEIKEALASVGFNDERQKQAIGSLSGGWKMKLALARAMLFKADILLLDEPTNHLD 602
Cdd:COG1124 91 SlHPRHTVDRILaepLRIHGLPDREERIAELLEQVGLPPSFLDRYPHQLSGGQRQRVAIARALILEPELLLLDEPTSALD 170
|
170 180 190
....*....|....*....|....*....|
gi 1933195014 603 VVNVAWLENYLTSLK-----TCtsIIVSHD 627
Cdd:COG1124 171 VSVQAEILNLLKDLReerglTY--LFVSHD 198
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
696-995 |
2.31e-17 |
|
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: 83.25 E-value: 2.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 696 LKMRKVGFQYPTQAVQQLYDITLQVSLSSRVAILGPNGSGKSTLVKLLIGDMEPNKGgeiwkhpnlvigyvaqhafhhid 775
Cdd:TIGR04520 1 IEVENVSFSYPESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSG----------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 776 hhldktpleymlwryqtgedleemskanrqiteaeaqkmkegaLIVVEGQKRLIEEIIT--RKKL--------KQ----S 841
Cdd:TIGR04520 58 -------------------------------------------KVTVDGLDTLDEENLWeiRKKVgmvfqnpdNQfvgaT 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 842 YEYEVSFkGLsssENIWLPRDELVKRgfekkvieVDtrEA-QRLGLLrplvrreiekHFADFglEPefvsHNtmrgLSGG 920
Cdd:TIGR04520 95 VEDDVAF-GL---ENLGVPREEMRKR--------VD--EAlKLVGME----------DFRDR--EP----HL----LSGG 140
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 921 QKVKIVLGAATWRRPHVICLDEPTNYLD---RESLAALIAALKVFEG-GVLIITHnrDFSE-SLCHEVWAMRDGRLEASG 995
Cdd:TIGR04520 141 QKQRVAIAGVLAMRPDIIILDEATSMLDpkgRKEVLETIRKLNKEEGiTVISITH--DMEEaVLADRVIVMNKGKIVAEG 218
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
696-991 |
4.80e-17 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 81.02 E-value: 4.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 696 LKMRKVGFQYPTQAVqqLYDITLQVSLSSRVAILGPNGSGKSTLVKlLIGDMEPNKGGEIWkhpnlvigyvaqhaFHhid 775
Cdd:COG4619 1 LELEGLSFRVGGKPI--LSPVSLTLEAGECVAITGPSGSGKSTLLR-ALADLDPPTSGEIY--------------LD--- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 776 hhldktpleymlwryqtGEDLEEMSkanrqiteaeaqkmkegalivvegqkrlIEEIitRKKLkqsyeyevsfkGLSSSE 855
Cdd:COG4619 61 -----------------GKPLSAMP----------------------------PPEW--RRQV-----------AYVPQE 82
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 856 NIWLP---RDELvKRGFEKKVIEVDTREAQRLgllrplvrreiekhFADFGLEPEFVSHNTMRgLSGGQKVKIVLGAATW 932
Cdd:COG4619 83 PALWGgtvRDNL-PFPFQLRERKFDRERALEL--------------LERLGLPPDILDKPVER-LSGGERQRLALIRALL 146
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1933195014 933 RRPHVICLDEPTNYLDRES---LAALIAALKVFEG-GVLIITHNRDFSESLCHEVWAMRDGRL 991
Cdd:COG4619 147 LQPDVLLLDEPTSALDPENtrrVEELLREYLAEEGrAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
695-995 |
5.34e-17 |
|
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: 82.01 E-value: 5.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 695 LLKMRKVGFQYPTQAVqqLYDITLQVSLSSRVAILGPNGSGKSTLVKLLIGDMEPnKGGEIWkhpnlvigyvaqhafhhi 774
Cdd:COG1120 1 MLEAENLSVGYGGRPV--LDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKP-SSGEVL------------------ 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 775 dhhLDktpleymlwryqtGEDLEEMSKANRqiteaeAQKMkegALivvegqkrlieeiitrkkLKQSYEYEVSFKGLsss 854
Cdd:COG1120 60 ---LD-------------GRDLASLSRREL------ARRI---AY------------------VPQEPPAPFGLTVR--- 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 855 eniwlprdELVKRGfekkvievdtREAQR--LGLLRPLVRREIEKHFADFGLEpEFvSHNTMRGLSGGQKVKIVLGAATW 932
Cdd:COG1120 94 --------ELVALG----------RYPHLglFGRPSAEDREAVEEALERTGLE-HL-ADRPVDELSGGERQRVLIARALA 153
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1933195014 933 RRPHVICLDEPTNYLD---RESLAALIAALKVFEG-GVLIITHNRDFSESLCHEVWAMRDGRLEASG 995
Cdd:COG1120 154 QEPPLLLLDEPTSHLDlahQLEVLELLRRLARERGrTVVMVLHDLNLAARYADRLVLLKDGRIVAQG 220
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
465-631 |
6.34e-17 |
|
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: 79.54 E-value: 6.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 465 YGAKILLNTATLRLKRGHRYGLCGKNGTGKSTLMRAITngqveGFPSPDEvrtfyvehdidGseadtsvlQFILTDKRVL 544
Cdd:cd03229 10 YGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIA-----GLEEPDS-----------G--------SILIDGEDLT 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 545 SSEAEIKEALASVG--FNDE--------RQKQAIGsLSGGWKMKLALARAMLFKADILLLDEPTNHLDVVNVAWLENYLT 614
Cdd:cd03229 66 DLEDELPPLRRRIGmvFQDFalfphltvLENIALG-LSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRREVRALLK 144
|
170 180
....*....|....*....|
gi 1933195014 615 SLKT---CTSIIVSHDSGFL 631
Cdd:cd03229 145 SLQAqlgITVVLVTHDLDEA 164
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
695-991 |
9.67e-17 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 80.90 E-value: 9.67e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 695 LLKMRKVGFQYPTQAVqqLYDITLQVSLSSRVAILGPNGSGKSTLVKLLIGDMEPNKG-----GEIWKHPNLVIGYVAQH 769
Cdd:COG1121 6 AIELENLTVSYGGRPV--LEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGtvrlfGKPPRRARRRIGYVPQR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 770 afHHIDHHLdktPLeymlwryqTGEDLEEMskanrqiteaeaqkmkeGALivveGQKRLieeiitrkklkqsyeyevsFK 849
Cdd:COG1121 84 --AEVDWDF---PI--------TVRDVVLM-----------------GRY----GRRGL-------------------FR 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 850 GLSSSeniwlprdelvkrgfEKKVIevdtREA-QRLGLLrplvrreiekHFAdfglepefvsHNTMRGLSGGQKVKIVLG 928
Cdd:COG1121 111 RPSRA---------------DREAV----DEAlERVGLE----------DLA----------DRPIGELSGGQQQRVLLA 151
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1933195014 929 AATWRRPHVICLDEPTNYLD---RESLAALIAALKVFEGGVLIITHNRDFSESLCHEVWAMRDGRL 991
Cdd:COG1121 152 RALAQDPDLLLLDEPFAGVDaatEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRGLV 217
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
707-995 |
2.00e-16 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 79.72 E-value: 2.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 707 TQAVQqlyDITLQVSLSSRVAILGPNGSGKSTLVKLLIGDMEPNKG-----GE-IWKHPNLV---IGYVAQHAFhhidhh 777
Cdd:COG1131 13 KTALD---GVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGevrvlGEdVARDPAEVrrrIGYVPQEPA------ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 778 ldktpleymLWRYQTGEDLEEMSKANRQITEAEAqkmkegalivvegqKRLIEEIITRkklkqsyeyevsfkglssseni 857
Cdd:COG1131 84 ---------LYPDLTVRENLRFFARLYGLPRKEA--------------RERIDELLEL---------------------- 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 858 wlprdelvkrgfekkvievdtreaqrlgllrplvrreiekhfadFGLEPefVSHNTMRGLSGGQKVKIVLGAATWRRPHV 937
Cdd:COG1131 119 --------------------------------------------FGLTD--AADRKVGTLSGGMKQRLGLALALLHDPEL 152
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1933195014 938 ICLDEPTNYLD---RESLAALIAALKVFEGGVLIITHNRDFSESLCHEVWAMRDGRLEASG 995
Cdd:COG1131 153 LILDEPTSGLDpeaRRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADG 213
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
465-626 |
4.57e-16 |
|
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: 76.70 E-value: 4.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 465 YGAKILLNTATLRLKRGHRYGLCGKNGTGKSTLMRAITngqveGFPSPDEVRTFyvehdIDGSEadtsvlqfiltdkrvl 544
Cdd:cd03216 10 FGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILS-----GLYKPDSGEIL-----VDGKE---------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 545 sseaeikealasVGFNDERQKQAIG-----SLSGGWKMKLALARAMLFKADILLLDEPTNHLDVVNVAWLENYLTSLKT- 618
Cdd:cd03216 64 ------------VSFASPRDARRAGiamvyQLSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIRRLRAq 131
|
....*....
gi 1933195014 619 -CTSIIVSH 626
Cdd:cd03216 132 gVAVIFISH 140
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
695-995 |
6.76e-16 |
|
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: 78.36 E-value: 6.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 695 LLKMRKVGFQYptQAVQQLYDITLQVSLSSRVAILGPNGSGKSTLVKLLIGDMEPNKGgEIwkhpnlvigyvaqhafhHI 774
Cdd:COG4555 1 MIEVENLSKKY--GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSG-SI-----------------LI 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 775 DhhldktpleymlwryqtGEDLEEMSKANRQiteaeaqkmkegALIVVEGQKRLieeiitrkklkqsyeyevsFKGLSSS 854
Cdd:COG4555 61 D-----------------GEDVRKEPREARR------------QIGVLPDERGL-------------------YDRLTVR 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 855 ENIWLprdelvkrgfekkvievdtreaqrLGLLRPLVRREIEKHFAD----FGLEPefVSHNTMRGLSGGQKVKIVLGAA 930
Cdd:COG4555 93 ENIRY------------------------FAELYGLFDEELKKRIEElielLGLEE--FLDRRVGELSTGMKKKVALARA 146
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1933195014 931 TWRRPHVICLDEPTNYLD---RESLAALIAALKVFEGGVLIITHNRDFSESLCHEVWAMRDGRLEASG 995
Cdd:COG4555 147 LVHDPKVLLLDEPTNGLDvmaRRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQG 214
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
464-639 |
1.72e-15 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 80.93 E-value: 1.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 464 AYGAKILLNTATLRLKRGHRYGLCGKNGTGKSTLMRAITngqveGFPSPDE--------VRTFYVEHDIDGSEADTSV-- 533
Cdd:PRK11819 333 SFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMIT-----GQEQPDSgtikigetVKLAYVDQSRDALDPNKTVwe 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 534 -----LQFILTDKRVLSSEAEIkealASVGFNDERQKQAIGSLSGGWKMKLALARAMLFKADILLLDEPTNHLDVVNVAW 608
Cdd:PRK11819 408 eisggLDIIKVGNREIPSRAYV----GRFNFKGGDQQKKVGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVETLRA 483
|
170 180 190
....*....|....*....|....*....|.
gi 1933195014 609 LENYLTSLKTCtSIIVSHDSGFLNNTITDVL 639
Cdd:PRK11819 484 LEEALLEFPGC-AVVISHDRWFLDRIATHIL 513
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
478-752 |
1.93e-15 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 81.01 E-value: 1.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 478 LKRGHRYGLCGKNGTGKSTLMRA-----ITN-GQVEGFPSPDEV-RTF-------YVEHDIDGsEADTSV-LQFILTDKR 542
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKIlsgelIPNlGDYEEEPSWDEVlKRFrgtelqnYFKKLYNG-EIKVVHkPQYVDLIPK 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 543 VLSseAEIKEALASVgfnDERQK---------------QAIGSLSGGWKMKLALARAMLFKADILLLDEPTNHLDV---V 604
Cdd:PRK13409 175 VFK--GKVRELLKKV---DERGKldevverlglenildRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIrqrL 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 605 NVAWLENYLTSLKTCtsIIVSHDSGFLnNTITDVLHLNRFKLRRYrgNLESFVKAVPEAKSYYsleaLEDY--------- 675
Cdd:PRK13409 250 NVARLIRELAEGKYV--LVVEHDLAVL-DYLADNVHIAYGEPGAY--GVVSKPKGVRVGINEY----LKGYlpeenmrir 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 676 ----KFKLPDPPllegVKTKEKSLLKmrkvgfqYPtQAVQQLYDITLQVS-----LSSRVAILGPNGSGKSTLVKLLIGD 746
Cdd:PRK13409 321 pepiEFEERPPR----DESERETLVE-------YP-DLTKKLGDFSLEVEggeiyEGEVIGIVGPNGIGKTTFAKLLAGV 388
|
....*.
gi 1933195014 747 MEPNKG 752
Cdd:PRK13409 389 LKPDEG 394
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
460-627 |
3.04e-15 |
|
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: 75.63 E-value: 3.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 460 QFSLAYGAKILLNTATLRLKRGHRYGLCGKNGTGKSTLMRAITngqveGFPSPDEVRTFYVEHDIDGSEADT-------- 531
Cdd:cd03259 5 GLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIA-----GLERPDSGEILIDGRDVTGVPPERrnigmvfq 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 532 --------SVLQ---FILTDKRVLSSEAE--IKEALASVGFNDERQKqAIGSLSGGWKMKLALARAMLFKADILLLDEPT 598
Cdd:cd03259 80 dyalfphlTVAEniaFGLKLRGVPKAEIRarVRELLELVGLEGLLNR-YPHELSGGQQQRVALARALAREPSLLLLDEPL 158
|
170 180 190
....*....|....*....|....*....|....
gi 1933195014 599 NHLDvVNVAW-----LENYLTSLKtCTSIIVSHD 627
Cdd:cd03259 159 SALD-AKLREelreeLKELQRELG-ITTIYVTHD 190
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
868-990 |
4.96e-15 |
|
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: 74.15 E-value: 4.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 868 GFEKKV---IEVDTREAQRLGLLRPLVRREIEKHFADFGLEPEF-VSHNTMRGLSGGQKVKIVLGAATWRRPHVICLDEP 943
Cdd:cd03229 48 GLEEPDsgsILIDGEDLTDLEDELPPLRRRIGMVFQDFALFPHLtVLENIALGLSGGQQQRVALARALAMDPDVLLLDEP 127
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1933195014 944 TNYLD---RESLAALIAALKVFEG-GVLIITHNRDFSESLCHEVWAMRDGR 990
Cdd:cd03229 128 TSALDpitRREVRALLKSLQAQLGiTVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
699-995 |
5.72e-15 |
|
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: 75.32 E-value: 5.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 699 RKVGFQYPTQAVQQLYDITLQVSLSSRVAILGPNGSGKSTLVKLLIGDMEPNKGG------EIWK-HPNLV---IGYVAQ 768
Cdd:cd03245 6 RNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSvlldgtDIRQlDPADLrrnIGYVPQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 769 HAfhhidhHLdktpleymlwryqtgedleemskanrqiteaeaqkmkegalivvegqkrlieeiitrkklkqsyeyevsF 848
Cdd:cd03245 86 DV------TL---------------------------------------------------------------------F 90
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 849 KGlSSSENIWLPR----DELVKRgfekkvievdtreAQRLGLLRPLVRReiekHFADFGLEpefVSHNTmRGLSGGQKVK 924
Cdd:cd03245 91 YG-TLRDNITLGApladDERILR-------------AAELAGVTDFVNK----HPNGLDLQ---IGERG-RGLSGGQRQA 148
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1933195014 925 IVLGAATWRRPHVICLDEPTNYLDRESLAALIAALKVFEGG--VLIITHnRDFSESLCHEVWAMRDGRLEASG 995
Cdd:cd03245 149 VALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGDktLIIITH-RPSLLDLVDRIIVMDSGRIVADG 220
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
468-644 |
8.98e-15 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 78.70 E-value: 8.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 468 KILLNTATLRLKRGHRYGLCGKNGTGKSTLMRAI------TNGQVEgFPSPDEVrTF-----YVehdIDGSEADtsVLQF 536
Cdd:COG4178 376 RPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIaglwpyGSGRIA-RPAGARV-LFlpqrpYL---PLGTLRE--ALLY 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 537 ILTDKRVlsSEAEIKEALASVG-------FNDERQKQAIgsLSGGWKMKLALARAMLFKADILLLDEPTNHLDVVNVAWL 609
Cdd:COG4178 449 PATAEAF--SDAELREALEAVGlghlaerLDEEADWDQV--LSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAAL 524
|
170 180 190
....*....|....*....|....*....|....*.
gi 1933195014 610 ENYL-TSLKTCTSIIVSHDSGfLNNTITDVLHLNRF 644
Cdd:COG4178 525 YQLLrEELPGTTVISVGHRST-LAAFHDRVLELTGD 559
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
464-656 |
1.23e-14 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 78.01 E-value: 1.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 464 AYGAKILLNTATLRLKRGHRYGLCGKNGTGKSTLMRAITN------GQVE-------GFPSPDEvrtfyvEHDIDGseaD 530
Cdd:PRK15064 328 GFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGelepdsGTVKwsenaniGYYAQDH------AYDFEN---D 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 531 TSVLQFILTDKRVLSSEAEIKEALASVGFNDERQKQAIGSLSGGWKMKLALARAMLFKADILLLDEPTNHLDV-----VN 605
Cdd:PRK15064 399 LTLFDWMSQWRQEGDDEQAVRGTLGRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMesiesLN 478
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1933195014 606 VAwLENYltslkTCTSIIVSHDSGFLNNTITDVLHLNRFKLRRYRGNLESF 656
Cdd:PRK15064 479 MA-LEKY-----EGTLIFVSHDREFVSSLATRIIEITPDGVVDFSGTYEEY 523
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
696-995 |
1.37e-14 |
|
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: 74.08 E-value: 1.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 696 LKMRKVGFQYPTQAVQQLYDITLQVSLSSRVAILGPNGSGKSTLVKLLIGDMEPNkGGEIW-------KHPNLV---IGY 765
Cdd:cd03263 1 LQIRNLTKTYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPT-SGTAYingysirTDRKAArqsLGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 766 VAQHafhhidhhlDktpleyMLWRYQTGEDLeemskanrqiteaeaqkmkegalivvegqkrLieEIITRkklkqsyeye 845
Cdd:cd03263 80 CPQF---------D------ALFDELTVREH-------------------------------L--RFYAR---------- 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 846 vsFKGLSSSEniwlprdelvkrgfekkvievdtreaqrlgllrplVRREIEKHFADFGLEPefVSHNTMRGLSGGQKVKI 925
Cdd:cd03263 102 --LKGLPKSE-----------------------------------IKEEVELLLRVLGLTD--KANKRARTLSGGMKRKL 142
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1933195014 926 VLGAATWRRPHVICLDEPTNYLD---RESLAALIAALKvfEG-GVLIITHNRDFSESLCHEVWAMRDGRLEASG 995
Cdd:cd03263 143 SLAIALIGGPSVLLLDEPTSGLDpasRRAIWDLILEVR--KGrSIILTTHSMDEAEALCDRIAIMSDGKLRCIG 214
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
462-627 |
1.63e-14 |
|
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: 74.25 E-value: 1.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 462 SLAYGAKILLNTATLRLKRGHRYGLCGKNGTGKSTLMRAITnGQVEgfpsPDEVRTFYVEHDIDGSEADT---------- 531
Cdd:COG1127 12 TKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLII-GLLR----PDSGEILVDGQDITGLSEKElyelrrrigm 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 532 -----------SVLQ---FILTDKRVLSsEAEIKE----ALASVGFNDERQKqAIGSLSGGwkMK--LALARAMLFKADI 591
Cdd:COG1127 87 lfqggalfdslTVFEnvaFPLREHTDLS-EAEIRElvleKLELVGLPGAADK-MPSELSGG--MRkrVALARALALDPEI 162
|
170 180 190
....*....|....*....|....*....|....*....
gi 1933195014 592 LLLDEPTNHLDVVNVAWLENYLTSLKT---CTSIIVSHD 627
Cdd:COG1127 163 LLYDEPTAGLDPITSAVIDELIRELRDelgLTSVVVTHD 201
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
471-627 |
1.68e-14 |
|
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: 74.08 E-value: 1.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 471 LNTATLRLKRGHRYGLCGKNGTGKSTLMRAI------TNGQVEGFP----SPDEVRTFYVEHDID--GSEADTSV----- 533
Cdd:cd03257 21 LDDVSFSIKKGETLGLVGESGSGKSTLARAIlgllkpTSGSIIFDGkdllKLSRRLRKIRRKEIQmvFQDPMSSLnprmt 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 534 ----LQFILTDKRVLSSEAEIKEA----LASVGFNDERQKQAIGSLSGGWKMKLALARAMLFKADILLLDEPTNHLDVVN 605
Cdd:cd03257 101 igeqIAEPLRIHGKLSKKEARKEAvlllLVGVGLPEEVLNRYPHELSGGQRQRVAIARALALNPKLLIADEPTSALDVSV 180
|
170 180
....*....|....*....|....*
gi 1933195014 606 VAWLENYLTSLKT---CTSIIVSHD 627
Cdd:cd03257 181 QAQILDLLKKLQEelgLTLLFITHD 205
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
698-975 |
2.40e-14 |
|
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: 77.28 E-value: 2.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 698 MRKVGFQYPTQAvQQLYDITLQVSLSSRVAILGPNGSGKSTLVKLLIG-DMEPNkgGEIWKHPNLVIGYVAQhafhhiDH 776
Cdd:TIGR03719 7 MNRVSKVVPPKK-EILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGvDKDFN--GEARPQPGIKVGYLPQ------EP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 777 HLDKTpleymlwryqtgedleemsKANRQITEaeaqkmkEGALIVVEGQKRLiEEIitrkklkqsyeyevsfkglssSEN 856
Cdd:TIGR03719 78 QLDPT-------------------KTVRENVE-------EGVAEIKDALDRF-NEI---------------------SAK 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 857 IWLPRDELVKRGFEKKVIE--VDTREAQRLgllrplvRREIEKHFADFGLEPE--FVSHntmrgLSGGQKVKIVLGAATW 932
Cdd:TIGR03719 110 YAEPDADFDKLAAEQAELQeiIDAADAWDL-------DSQLEIAMDALRCPPWdaDVTK-----LSGGERRRVALCRLLL 177
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1933195014 933 RRPHVICLDEPTNYLDRESLAALIAALKVFEGGVLIITHNRDF 975
Cdd:TIGR03719 178 SKPDMLLLDEPTNHLDAESVAWLERHLQEYPGTVVAVTHDRYF 220
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
715-945 |
2.59e-14 |
|
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: 71.14 E-value: 2.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 715 DITLQVSLSSRVAILGPNGSGKSTLVKLLIGDMEPNKG----------GEIWKHPNLVIGYVAQHAFHhidhhldktple 784
Cdd:pfam00005 3 NVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGtilldgqdltDDERKSLRKEIGYVFQDPQL------------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 785 ymlwryqtgedleemskanrqiteaeaqkmkegalivvegqkrlieeiitrkklkqsyeyevsFKGLSSSENIWLPRD-- 862
Cdd:pfam00005 71 ---------------------------------------------------------------FPRLTVRENLRLGLLlk 87
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 863 ELVKRGFEKKVIEVdtreAQRLGLlrplvrreieKHFADFGLepefvsHNTMRGLSGGQKVKIVLGAATWRRPHVICLDE 942
Cdd:pfam00005 88 GLSKREKDARAEEA----LEKLGL----------GDLADRPV------GERPGTLSGGQRQRVAIARALLTKPKLLLLDE 147
|
...
gi 1933195014 943 PTN 945
Cdd:pfam00005 148 PTA 150
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
696-990 |
3.34e-14 |
|
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: 71.65 E-value: 3.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 696 LKMRKVGFQYPTQAVQQLYDITLQVSLSSRVAILGPNGSGKSTLVKLLIGDMEPNKgGEIwkhpnlvigyvaqhafhHID 775
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTS-GEI-----------------LID 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 776 hhldktpleymlwryqtGEDLEEMSKANRQiteaeaqkmkegALIVVEGQKRLIeeiitrkklkqsyeyevsFKGlSSSE 855
Cdd:cd03228 63 -----------------GVDLRDLDLESLR------------KNIAYVPQDPFL------------------FSG-TIRE 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 856 NIwlprdelvkrgfekkvievdtreaqrlgllrplvrreiekhfadfglepefvshntmrgLSGGQKVKIVLGAATWRRP 935
Cdd:cd03228 95 NI-----------------------------------------------------------LSGGQRQRIAIARALLRDP 115
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1933195014 936 HVICLDEPTNYLDRESLAALIAALKVFEGG--VLIITHnRDFSESLCHEVWAMRDGR 990
Cdd:cd03228 116 PILILDEATSALDPETEALILEALRALAKGktVIVIAH-RLSTIRDADRIIVLDDGR 171
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
471-627 |
3.61e-14 |
|
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: 72.91 E-value: 3.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 471 LNTATLRLKRGHRYGLCGKNGTGKSTLMRAITngqveGFPSPDEVRTFYVEHDIDG-SEADTS---------VLQF---- 536
Cdd:cd03255 20 LKGVSLSIEKGEFVAIVGPSGSGKSTLLNILG-----GLDRPTSGEVRVDGTDISKlSEKELAafrrrhigfVFQSfnll 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 537 -------------ILTDKRVLSSEAEIKEALASVGFNDeRQKQAIGSLSGGWKMKLALARAMLFKADILLLDEPTNHLDV 603
Cdd:cd03255 95 pdltalenvelplLLAGVPKKERRERAEELLERVGLGD-RLNHYPSELSGGQQQRVAIARALANDPKIILADEPTGNLDS 173
|
170 180
....*....|....*....|....*..
gi 1933195014 604 VNVAWLENYLTSLKT---CTSIIVSHD 627
Cdd:cd03255 174 ETGKEVMELLRELNKeagTTIVVVTHD 200
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
692-995 |
4.53e-14 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 73.90 E-value: 4.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 692 EKSLLKMRKVGFQYPTQAVQQLYDITLQVSLSSRVAILGPNGSGKSTLVKLLIGDMEPNKGgeiwkhpnlvigyvaqhaf 771
Cdd:PRK13635 2 KEEIIRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAG------------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 772 hhidhhldktpleymlwryqtgedleemskanrqiteaeaqkmkegaLIVVEGQKrLIEEII--TRKKLKQSY------- 842
Cdd:PRK13635 63 -----------------------------------------------TITVGGMV-LSEETVwdVRRQVGMVFqnpdnqf 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 843 -----EYEVSFkGLsssENIWLPRDELVKRgfekkvieVDtrEAQRlgllrpLVRREiekhfadfglepEFVSHNTMRgL 917
Cdd:PRK13635 95 vgatvQDDVAF-GL---ENIGVPREEMVER--------VD--QALR------QVGME------------DFLNREPHR-L 141
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 918 SGGQKVKIVLGAATWRRPHVICLDEPTNYLD---RESLAALIAALKVfEGG--VLIITHnrDFSESL-CHEVWAMRDGRL 991
Cdd:PRK13635 142 SGGQKQRVAIAGVLALQPDIIILDEATSMLDprgRREVLETVRQLKE-QKGitVLSITH--DLDEAAqADRVIVMNKGEI 218
|
....
gi 1933195014 992 EASG 995
Cdd:PRK13635 219 LEEG 222
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
475-632 |
4.83e-14 |
|
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: 72.62 E-value: 4.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 475 TLRLKRGHRYGLCGKNGTGKSTLMRAI------TNGQV--EGFPS----PDEVRTF--YVEHDID---GSEADTsvlqfi 537
Cdd:cd03245 24 SLTIRAGEKVAIIGRVGSGKSTLLKLLaglykpTSGSVllDGTDIrqldPADLRRNigYVPQDVTlfyGTLRDN------ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 538 LTDKRVLSSEAEIKEALASVGFNDERQKQAIG----------SLSGGWKMKLALARAMLFKADILLLDEPTNHLDVVNVA 607
Cdd:cd03245 98 ITLGAPLADDERILRAAELAGVTDFVNKHPNGldlqigergrGLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEE 177
|
170 180
....*....|....*....|....*.
gi 1933195014 608 WL-ENYLTSLKTCTSIIVSHDSGFLN 632
Cdd:cd03245 178 RLkERLRQLLGDKTLIIITHRPSLLD 203
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
462-627 |
5.97e-14 |
|
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: 75.96 E-value: 5.97e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 462 SLAY--GAKILLNTATLRLKRGHRYGLCGKNGTGKSTL----MRAI--TNGQVE--GFP----SPDEVRTF--YVEHDI- 524
Cdd:COG4987 340 SFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLlallLRFLdpQSGSITlgGVDlrdlDEDDLRRRiaVVPQRPh 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 525 --DGSEADTsvLQFILTDkrvlSSEAEIKEALASVGFND--ERQKQ----AIGS----LSGGWKMKLALARAMLFKADIL 592
Cdd:COG4987 420 lfDTTLREN--LRLARPD----ATDEELWAALERVGLGDwlAALPDgldtWLGEggrrLSGGERRRLALARALLRDAPIL 493
|
170 180 190
....*....|....*....|....*....|....*.
gi 1933195014 593 LLDEPTNHLDVVNV-AWLENYLTSLKTCTSIIVSHD 627
Cdd:COG4987 494 LLDEPTEGLDAATEqALLADLLEALAGRTVLLITHR 529
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
693-993 |
7.35e-14 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 72.00 E-value: 7.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 693 KSLLKMRKVGFQYPT--QAVQQLYDITLQVSLSSRVAILGPNGSGKSTLvkL-LIGDMEPNKGGEIWkhpnlvigyvaqh 769
Cdd:COG1136 2 SPLLELRNLTKSYGTgeGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTL--LnILGGLDRPTSGEVL------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 770 afhhIDhhldktpleymlwryqtGEDLEEMSkaNRQITEAEAQKMkegalivveG---QK-RLIEEiitrkklkqsyeye 845
Cdd:COG1136 67 ----ID-----------------GQDISSLS--ERELARLRRRHI---------GfvfQFfNLLPE-------------- 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 846 vsfkgLSSSENIWLPrdeLVKRGFEKKVIEVDTREA-QRLGLlrplvrREIEKHFADfglEpefvshntmrgLSGGQK-- 922
Cdd:COG1136 101 -----LTALENVALP---LLLAGVSRKERRERARELlERVGL------GDRLDHRPS---Q-----------LSGGQQqr 152
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1933195014 923 VKIvlgA-ATWRRPHVICLDEPTNYLDRESLAALIAALK--VFEGG--VLIITHNRDFSeSLCHEVWAMRDGRLEA 993
Cdd:COG1136 153 VAI---ArALVNRPKLILADEPTGNLDSKTGEEVLELLRelNRELGttIVMVTHDPELA-ARADRVIRLRDGRIVS 224
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
693-995 |
7.43e-14 |
|
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: 75.32 E-value: 7.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 693 KSLLKMRKVGFQYPTQAVQQLYDITLQVSLSSRVAILGPNGSGKSTLVKLLIGDMEPN--KGGEIWKHpnlvigyvaqha 770
Cdd:COG1123 2 TPLLEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgrISGEVLLD------------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 771 fhhidhhldktpleymlwryqtGEDLEEMSKANRqiteaeaqkmkeGALIVVEGQkrlieeiitrkklkqsyEYEVSFKG 850
Cdd:COG1123 70 ----------------------GRDLLELSEALR------------GRRIGMVFQ-----------------DPMTQLNP 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 851 LSsseniwlprdelvkrgfekkvIEVDTREAQRLGLL-RPLVRREIEKHFADFGLEpEFVSHNTMRgLSGGQKVKIVLGA 929
Cdd:COG1123 99 VT---------------------VGDQIAEALENLGLsRAEARARVLELLEAVGLE-RRLDRYPHQ-LSGGQRQRVAIAM 155
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 930 ATWRRPHVICLDEPTNYLD---RESLAALIAALKVFEG-GVLIITHNRDFSESLCHEVWAMRDGRLEASG 995
Cdd:COG1123 156 ALALDPDLLIADEPTTALDvttQAEILDLLRELQRERGtTVLLITHDLGVVAEIADRVVVMDDGRIVEDG 225
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
462-695 |
8.12e-14 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 75.76 E-value: 8.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 462 SLAYGAKILLNTATLRLKRGHRYGLCGKNGTGKSTLMRAITnGQVEgfPSPDEVRT-------FYVEH--DIDgseadts 532
Cdd:PRK11147 326 NYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLML-GQLQ--ADSGRIHCgtklevaYFDQHraELD------- 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 533 vlqfilTDKRVLSSEAEIKEALASVG-------------FNDERQKQAIGSLSGGWKMKLALARAMLFKADILLLDEPTN 599
Cdd:PRK11147 396 ------PEKTVMDNLAEGKQEVMVNGrprhvlgylqdflFHPKRAMTPVKALSGGERNRLLLARLFLKPSNLLILDEPTN 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 600 HLDVVNVAWLENYLTSLKTcTSIIVSHDSGFLNNTITDVLhlnrfklrRYRGN--LESFV----KAVPEAKSYYSLEALE 673
Cdd:PRK11147 470 DLDVETLELLEELLDSYQG-TVLLVSHDRQFVDNTVTECW--------IFEGNgkIGRYVggyhDARQQQAQYLALKQPA 540
|
250 260
....*....|....*....|..
gi 1933195014 674 DYKFKLPDPPLLEGVKTKEKSL 695
Cdd:PRK11147 541 VKKKEEAAAPKAETVKRSSKKL 562
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
478-752 |
8.23e-14 |
|
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: 75.59 E-value: 8.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 478 LKRGHRYGLCGKNGTGKSTLMRA-----ITN-GQVEGFPSPDEVRTFYvehdiDGSE--------ADTSV-----LQFIl 538
Cdd:COG1245 96 PKKGKVTGILGPNGIGKSTALKIlsgelKPNlGDYDEEPSWDEVLKRF-----RGTElqdyfkklANGEIkvahkPQYV- 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 539 tDK--RVLSseAEIKEALASVgfnDERQK---------------QAIGSLSGGWKMKLALARAMLFKADILLLDEPTNHL 601
Cdd:COG1245 170 -DLipKVFK--GTVRELLEKV---DERGKldelaeklglenildRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYL 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 602 DV---VNVAWLENYLTSLKTcTSIIVSHDSGFLnNTITDVLHL--------NRFklrryrgnleSFVKAVPEAKSYYsle 670
Cdd:COG1245 244 DIyqrLNVARLIRELAEEGK-YVLVVEHDLAIL-DYLADYVHIlygepgvyGVV----------SKPKSVRVGINQY--- 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 671 aLEDYkfkLPDppllEGVKTKEKSL---------LKMRKVGFQYPtQAVQQLYDITLQVS-----LSSRVAILGPNGSGK 736
Cdd:COG1245 309 -LDGY---LPE----ENVRIRDEPIefevhaprrEKEEETLVEYP-DLTKSYGGFSLEVEggeirEGEVLGIVGPNGIGK 379
|
330
....*....|....*.
gi 1933195014 737 STLVKLLIGDMEPNKG 752
Cdd:COG1245 380 TTFAKILAGVLKPDEG 395
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
696-995 |
1.03e-13 |
|
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: 75.19 E-value: 1.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 696 LKMRKVGFQYPTQAVQQLYDITLQVSLSSRVAILGPNGSGKSTLVKLLIGDMEPNkGGEIWkhpnlvigyvaqhafhhid 775
Cdd:COG4987 334 LELEDVSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQ-SGSIT------------------- 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 776 hhLDKTPLeymlwryqtgedleemskanRQITEAEAQkmkegALIVVEGQKRLIeeiitrkklkqsyeyevsfkgLSSS- 854
Cdd:COG4987 394 --LGGVDL--------------------RDLDEDDLR-----RRIAVVPQRPHL---------------------FDTTl 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 855 -ENIWLPRDELVkrgfEKKVIEVdtreAQRLGlLRPLVRREIEkhfadfGLepefvshNTM-----RGLSGGQKVKIVLG 928
Cdd:COG4987 426 rENLRLARPDAT----DEELWAA----LERVG-LGDWLAALPD------GL-------DTWlgeggRRLSGGERRRLALA 483
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1933195014 929 AATWRRPHVICLDEPTNYLDRESLAALIAALKVFEGG--VLIITHNRDFSEsLCHEVWAMRDGRLEASG 995
Cdd:COG4987 484 RALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGrtVLLITHRLAGLE-RMDRILVLEDGRIVEQG 551
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
697-995 |
1.17e-13 |
|
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: 70.16 E-value: 1.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 697 KMRKVGFQYPTQAVqqLYDITLQVSLSSRVAILGPNGSGKSTLVKLLIGDMEPNKGgEIwkhpnlvigyvaqhafhhidh 776
Cdd:cd03214 1 EVENLSVGYGGRTV--LDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSG-EI--------------------- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 777 HLDktpleymlwryqtGEDLEEMSKANRqiteaeAQKMkegalivvegqkrlieeiitrkklkqSYeyevsfkglsssen 856
Cdd:cd03214 57 LLD-------------GKDLASLSPKEL------ARKI--------------------------AY-------------- 77
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 857 iwLPrdelvkrgfekKVIEvdtreaqRLGLLrplvrreiekHFADfglepEFVSHntmrgLSGGQKVKIVLGAATWRRPH 936
Cdd:cd03214 78 --VP-----------QALE-------LLGLA----------HLAD-----RPFNE-----LSGGERQRVLLARALAQEPP 117
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1933195014 937 VICLDEPTNYLD---RESLAALIAALKVFEG-GVLIITHNRDFSESLCHEVWAMRDGRLEASG 995
Cdd:cd03214 118 ILLLDEPTSHLDiahQIELLELLRRLARERGkTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
713-995 |
1.35e-13 |
|
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: 71.03 E-value: 1.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 713 LYDITLQVSLSSRVAILGPNGSGKSTLVKLLIGDMEPNKG-----GEIWKHPNLVIGYVAQHafhhidHHLDKT-PLeym 786
Cdd:cd03235 15 LEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGsirvfGKPLEKERKRIGYVPQR------RSIDRDfPI--- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 787 lwryqTGEDLEEMskanrqiteaeaqkmkeGALivveGQKRLieeiitrkklkqsyeyevsFKGLSSSeniwlprdelvk 866
Cdd:cd03235 86 -----SVRDVVLM-----------------GLY----GHKGL-------------------FRRLSKA------------ 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 867 rgfEKKVIEvdtrEA-QRLGLLrplvrreiekHFADfglepefvshNTMRGLSGGQKVKIVLGAATWRRPHVICLDEPTN 945
Cdd:cd03235 109 ---DKAKVD----EAlERVGLS----------ELAD----------RQIGELSGGQQQRVLLARALVQDPDLLLLDEPFA 161
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1933195014 946 YLD---RESLAALIAALKVFEGGVLIITHNRDFSESLCHEVwAMRDGRLEASG 995
Cdd:cd03235 162 GVDpktQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRV-LLLNRTVVASG 213
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
463-626 |
1.75e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 71.48 E-value: 1.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 463 LAYGAKILLNTATLRLKRGHRYGLCGKNGTGKSTLMRaITNGQVEGFPSPDEVRTFYVE-HDI---DGSEADTSVlQFI- 537
Cdd:PRK14247 11 VSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLR-VFNRLIELYPEARVSGEVYLDgQDIfkmDVIELRRRV-QMVf 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 538 ------------------LTDKRVLSSEAE----IKEALASVGFNDE---RQKQAIGSLSGGWKMKLALARAMLFKADIL 592
Cdd:PRK14247 89 qipnpipnlsifenvalgLKLNRLVKSKKElqerVRWALEKAQLWDEvkdRLDAPAGKLSGGQQQRLCIARALAFQPEVL 168
|
170 180 190
....*....|....*....|....*....|....*
gi 1933195014 593 LLDEPTNHLDVVNVAWLENYLTSLKT-CTSIIVSH 626
Cdd:PRK14247 169 LADEPTANLDPENTAKIESLFLELKKdMTIVLVTH 203
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
466-627 |
1.78e-13 |
|
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: 74.32 E-value: 1.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 466 GAKILLNTATLRLKRGHRYGLCGKNGTGKSTLMRAITngqveGFPSPDE---VRTFYVEHDIDGSEA------------- 529
Cdd:TIGR02868 346 GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLA-----GLLDPLQgevTLDGVPVSSLDQDEVrrrvsvcaqdahl 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 530 -DTSVLQFILTdKRVLSSEAEIKEALASVGFNDERQKQAIG----------SLSGGWKMKLALARAMLFKADILLLDEPT 598
Cdd:TIGR02868 421 fDTTVRENLRL-ARPDATDEELWAALERVGLADWLRALPDGldtvlgeggaRLSGGERQRLALARALLADAPILLLDEPT 499
|
170 180 190
....*....|....*....|....*....|
gi 1933195014 599 NHLDV-VNVAWLENYLTSLKTCTSIIVSHD 627
Cdd:TIGR02868 500 EHLDAeTADELLEDLLAALSGRTVVLITHH 529
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
456-626 |
1.98e-13 |
|
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: 69.55 E-value: 1.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 456 LCNCQFSLAYGAKILLNTATLRLKRGHRYGLCGKNGTGKSTLMRAITNGQVegfPSPDEVRtfyvehdIDGSEADTSvlq 535
Cdd:cd03246 3 VENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLR---PTSGRVR-------LDGADISQW--- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 536 filtdkrvlsSEAEIKEALASVGFNDERQKQAIGS--LSGGWKMKLALARAMLFKADILLLDEPTNHLDVVNVAWLENYL 613
Cdd:cd03246 70 ----------DPNELGDHVGYLPQDDELFSGSIAEniLSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAI 139
|
170
....*....|....*
gi 1933195014 614 TSLK--TCTSIIVSH 626
Cdd:cd03246 140 AALKaaGATRIVIAH 154
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
458-626 |
1.98e-13 |
|
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: 70.72 E-value: 1.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 458 NCQFSLAYGaKILLNTATLRLKRGHRYGLCGKNGTGKSTLMRAITngqveGFPSPDEVRTFYveHDIDGSEADTS----- 532
Cdd:cd03254 7 NVNFSYDEK-KPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLM-----RFYDPQKGQILI--DGIDIRDISRKslrsm 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 533 ---VLQ--FILTDK--------RVLSSEAEIKEALASVGFNDERQKQAIG----------SLSGGWKMKLALARAMLFKA 589
Cdd:cd03254 79 igvVLQdtFLFSGTimenirlgRPNATDEEVIEAAKEAGAHDFIMKLPNGydtvlgenggNLSQGERQLLAIARAMLRDP 158
|
170 180 190
....*....|....*....|....*....|....*...
gi 1933195014 590 DILLLDEPTNHLDVVNVAWLENYLTSL-KTCTSIIVSH 626
Cdd:cd03254 159 KILILDEATSNIDTETEKLIQEALEKLmKGRTSIIIAH 196
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
464-630 |
2.62e-13 |
|
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: 70.25 E-value: 2.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 464 AYGAKILLNTATLRLKRGHRYGLCGKNGTGKSTLMRAItNGQVEgfpsPDEVRTFYVEHDIDGSEADT------------ 531
Cdd:cd03262 9 SFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCI-NLLEE----PDSGTIIIDGLKLTDDKKNInelrqkvgmvfq 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 532 --------SVLQFI----LTDKRVLSSEAEIK--EALASVGFnDERQKQAIGSLSGGWKMKLALARAMLFKADILLLDEP 597
Cdd:cd03262 84 qfnlfphlTVLENItlapIKVKGMSKAEAEERalELLEKVGL-ADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEP 162
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1933195014 598 TNHLD------VVNVawlenyLTSLKT--CTSIIVSHDSGF 630
Cdd:cd03262 163 TSALDpelvgeVLDV------MKDLAEegMTMVVVTHEMGF 197
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
696-991 |
2.65e-13 |
|
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: 68.96 E-value: 2.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 696 LKMRKVGFQYPTQAVqqLYDITLQVSLSSRVAILGPNGSGKSTLVKLLIGDMEPNKG------GEIWKHPNLV---IGYV 766
Cdd:cd03230 1 IEVRNLSKRYGKKTA--LDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGeikvlgKDIKKEPEEVkrrIGYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 767 AQHAfhhidhhldktpleyMLWRYQTGEDLEEMSKanrqiteaeaqkmkegalivveGQKrlieeiitrkklkqsyeyev 846
Cdd:cd03230 79 PEEP---------------SLYENLTVRENLKLSG----------------------GMK-------------------- 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 847 sfkglssseniwlprdelvkrgfekkvievdtreaQRLGLLRPLVrreiekhfadfglepefvsHNtmrglsggqkvkiv 926
Cdd:cd03230 102 -----------------------------------QRLALAQALL-------------------HD-------------- 113
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1933195014 927 lgaatwrrPHVICLDEPTNYLD---RESLAALIAALKVFEGGVLIITHNRDFSESLCHEVWAMRDGRL 991
Cdd:cd03230 114 --------PELLILDEPTSGLDpesRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
713-995 |
2.96e-13 |
|
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: 70.02 E-value: 2.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 713 LYDITLQVSL---SSRVAILGPNGSGKSTLVKLLIGDMEPNKGgeiwkhpnlvigyvaqhafhHIDhhLDKTPLeymlwr 789
Cdd:cd03297 10 LPDFTLKIDFdlnEEVTGIFGASGAGKSTLLRCIAGLEKPDGG--------------------TIV--LNGTVL------ 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 790 yQTGEDLEEMSKANRQIteaeaqkmkegALIVvegqkrlieeiitrkklkQSYEYevsFKGLSSSENIwlprdELVKRGF 869
Cdd:cd03297 62 -FDSRKKINLPPQQRKI-----------GLVF------------------QQYAL---FPHLNVRENL-----AFGLKRK 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 870 EKKVIEVdtREAQRLGL--LRPLVRREIEKhfadfglepefvshntmrgLSGGQKVKIVLGAATWRRPHVICLDEPTNYL 947
Cdd:cd03297 104 RNREDRI--SVDELLDLlgLDHLLNRYPAQ-------------------LSGGEKQRVALARALAAQPELLLLDEPFSAL 162
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1933195014 948 DRESLAALIAAL----KVFEGGVLIITHNRDFSESLCHEVWAMRDGRLEASG 995
Cdd:cd03297 163 DRALRLQLLPELkqikKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
462-627 |
3.42e-13 |
|
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: 69.81 E-value: 3.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 462 SLAYGAKILLNTA----TLRLKRGHRYGLCGKNGTGKSTLMRAITngqveGFPSPD--EVRTFYVEhdIDGSEADTS-VL 534
Cdd:cd03293 7 SKTYGGGGGAVTAlediSLSVEEGEFVALVGPSGCGKSTLLRIIA-----GLERPTsgEVLVDGEP--VTGPGPDRGyVF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 535 Q---------------FILTDKRVLSSEA--EIKEALASVG---FNDERQKQaigsLSGGWKMKLALARAMLFKADILLL 594
Cdd:cd03293 80 QqdallpwltvldnvaLGLELQGVPKAEAreRAEELLELVGlsgFENAYPHQ----LSGGMRQRVALARALAVDPDVLLL 155
|
170 180 190
....*....|....*....|....*....|....*.
gi 1933195014 595 DEPTNHLDVVNVAWLENYLTSL--KTCTSII-VSHD 627
Cdd:cd03293 156 DEPFSALDALTREQLQEELLDIwrETGKTVLlVTHD 191
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
464-627 |
4.16e-13 |
|
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: 69.96 E-value: 4.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 464 AYGAKILLNTATLRLKRGHRYGLCGKNGTGKSTLMRAITngqveGFPSPDEVRTFYVEHDIDGSEAD----TSVLQ---- 535
Cdd:cd03300 9 FYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIA-----GFETPTSGEILLDGKDITNLPPHkrpvNTVFQnyal 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 536 -----------FILTDKRVlsSEAEIK----EALASVGFNDERQKQaIGSLSGGWKMKLALARAMLFKADILLLDEPTNH 600
Cdd:cd03300 84 fphltvfeniaFGLRLKKL--PKAEIKervaEALDLVQLEGYANRK-PSQLSGGQQQRVAIARALVNEPKVLLLDEPLGA 160
|
170 180 190
....*....|....*....|....*....|
gi 1933195014 601 LDVVNVAWLENYLTSLKT---CTSIIVSHD 627
Cdd:cd03300 161 LDLKLRKDMQLELKRLQKelgITFVFVTHD 190
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
462-643 |
5.81e-13 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 70.14 E-value: 5.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 462 SLAYGAKILLNTATLRLKRGHRYGLCGKNGTGKSTLMRAI------TNGQVEgfpSPDEVRTFYVEHDIdgsEADTSVlq 535
Cdd:PRK09544 11 SVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVlglvapDEGVIK---RNGKLRIGYVPQKL---YLDTTL-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 536 fILTDKRVL-----SSEAEIKEALASVGFNDERQkQAIGSLSGGWKMKLALARAMLFKADILLLDEPTNHLDVVNVAWLE 610
Cdd:PRK09544 83 -PLTVNRFLrlrpgTKKEDILPALKRVQAGHLID-APMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALY 160
|
170 180 190
....*....|....*....|....*....|....*.
gi 1933195014 611 NYLTSLKT---CTSIIVSHDSGFLNNTITDVLHLNR 643
Cdd:PRK09544 161 DLIDQLRReldCAVLMVSHDLHLVMAKTDEVLCLNH 196
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
917-990 |
6.23e-13 |
|
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: 67.66 E-value: 6.23e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1933195014 917 LSGGQKVKIVLGAATWRRPHVICLDEPTNYLD---RESLAALIAALKVFEGGVLIITHNRDFSESLCHEVWAMRDGR 990
Cdd:cd00267 81 LSGGQRQRVALARALLLNPDLLLLDEPTSGLDpasRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
475-626 |
1.67e-12 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 71.35 E-value: 1.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 475 TLRLKRGHRYGLCGKNGTGKSTLMRAITngqveGF--PSPDEVRtfyvehdIDG---SEADTS--------VLQ--FILT 539
Cdd:COG1132 360 SLTIPPGETVALVGPSGSGKSTLVNLLL-----RFydPTSGRIL-------IDGvdiRDLTLEslrrqigvVPQdtFLFS 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 540 DK--------RVLSSEAEIKEALASVGFND--ERQKQ----AIG----SLSGGWKMKLALARAMLFKADILLLDEPTNHL 601
Cdd:COG1132 428 GTirenirygRPDATDEEVEEAAKAAQAHEfiEALPDgydtVVGergvNLSGGQRQRIAIARALLKDPPILILDEATSAL 507
|
170 180
....*....|....*....|....*.
gi 1933195014 602 DVVNVAWLENYLTSL-KTCTSIIVSH 626
Cdd:COG1132 508 DTETEALIQEALERLmKGRTTIVIAH 533
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
461-626 |
2.88e-12 |
|
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: 67.39 E-value: 2.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 461 FSLAYGAKILLNTATLRLKRGHRYGLCGKNGTGKSTLMRAIT--------NGQVEGF---PSPDEV-RTFYVEHDIDGSE 528
Cdd:cd03266 11 FRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAgllepdagFATVDGFdvvKEPAEArRRLGFVSDSTGLY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 529 ADTSVLQFILTDKRVL-----SSEAEIKEALASVGFNDERQKQAiGSLSGGWKMKLALARAMLFKADILLLDEPTNHLDV 603
Cdd:cd03266 91 DRLTARENLEYFAGLYglkgdELTARLEELADRLGMEELLDRRV-GGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDV 169
|
170 180
....*....|....*....|....*
gi 1933195014 604 VNVAWLENYLTSLKT--CTSIIVSH 626
Cdd:cd03266 170 MATRALREFIRQLRAlgKCILFSTH 194
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
464-598 |
2.96e-12 |
|
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: 67.07 E-value: 2.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 464 AYGAKILLNTATLRLKRGHRYGLCGKNGTGKSTLMRAI------TNGQV--EGfpspdevrtfyveHDIDGSEADTSV-- 533
Cdd:cd03224 9 GYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTImgllppRSGSIrfDG-------------RDITGLPPHERAra 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 534 -LQFILTDKRVLSS---------------EAEIKEALASVgFN-----DERQKQAIGSLSGGWKMKLALARAMLFKADIL 592
Cdd:cd03224 76 gIGYVPEGRRIFPEltveenlllgayarrRAKRKARLERV-YElfprlKERRKQLAGTLSGGEQQMLAIARALMSRPKLL 154
|
....*.
gi 1933195014 593 LLDEPT 598
Cdd:cd03224 155 LLDEPS 160
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
679-996 |
3.08e-12 |
|
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: 70.56 E-value: 3.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 679 LPDPPLLEGVKT---KEKSLLKMRKVGFQYPtQAVQQLYDITLQVSLSSRVAILGPNGSGKSTLVKLLIGDMEPNKgGEI 755
Cdd:COG4988 317 APEPAAPAGTAPlpaAGPPSIELEDVSFSYP-GGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYS-GSI 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 756 wkhpnlvigYVAQHAFHHIDHHldktpleymLWRyqtgedleemskanRQIteaeaqkmkegALIvveGQKRLIeeiitr 835
Cdd:COG4988 395 ---------LINGVDLSDLDPA---------SWR--------------RQI-----------AWV---PQNPYL------ 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 836 kklkqsyeyevsFKGlSSSENIWLPRDELvkrgfekkvievdTREAqrlgllrplVRREIEK-HFADF------GLEpef 908
Cdd:COG4988 423 ------------FAG-TIRENLRLGRPDA-------------SDEE---------LEAALEAaGLDEFvaalpdGLD--- 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 909 vshnTM-----RGLSGGQKVKIVLGAATWRRPHVICLDEPTNYLDRESLAALIAALKVFEGG--VLIITHnRDFSESLCH 981
Cdd:COG4988 465 ----TPlgeggRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGrtVILITH-RLALLAQAD 539
|
330
....*....|....*
gi 1933195014 982 EVWAMRDGRLEASGH 996
Cdd:COG4988 540 RILVLDDGRIVEQGT 554
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
460-627 |
3.62e-12 |
|
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: 70.01 E-value: 3.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 460 QFSLAY-GAKILLNTATLRLKRGHRYGLCGKNGTGKSTLMRAITngqveGFPSPDEVRTFYVEHDIDGSEADT------- 531
Cdd:TIGR02857 326 GVSVAYpGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLL-----GFVDPTEGSIAVNGVPLADADADSwrdqiaw 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 532 ----------SVLQFILTDKRVlSSEAEIKEALASVGFNDERQ------KQAIGS----LSGGWKMKLALARAMLFKADI 591
Cdd:TIGR02857 401 vpqhpflfagTIAENIRLARPD-ASDAEIREALERAGLDEFVAalpqglDTPIGEggagLSGGQAQRLALARAFLRDAPL 479
|
170 180 190
....*....|....*....|....*....|....*..
gi 1933195014 592 LLLDEPTNHLDVVNVA-WLENYLTSLKTCTSIIVSHD 627
Cdd:TIGR02857 480 LLLDEPTAHLDAETEAeVLEALRALAQGRTVLLVTHR 516
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
471-640 |
4.00e-12 |
|
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: 67.08 E-value: 4.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 471 LNTATLRLKRGHRYGLCGKNGTGKSTLMRAITngqveGFPSPDEVRTFYVEHDIDGSEAD-------------------T 531
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLIS-----GFLRPTSGSVLFDGEDITGLPPHeiarlgigrtfqiprlfpeL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 532 SVLQFILT-----------DKRVLSSEAEIKE----ALASVGFNDERQKQAiGSLSGGWKMKLALARAMLFKADILLLDE 596
Cdd:cd03219 91 TVLENVMVaaqartgsgllLARARREEREAREraeeLLERVGLADLADRPA-GELSYGQQRRLEIARALATDPKLLLLDE 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1933195014 597 PTNHLDVVNVAWLENYLTSLKT--CTSIIVSHDSGF---LNNTITdVLH 640
Cdd:cd03219 170 PAAGLNPEETEELAELIRELRErgITVLLVEHDMDVvmsLADRVT-VLD 217
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
458-626 |
4.17e-12 |
|
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: 65.80 E-value: 4.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 458 NCQFSLAYGAKILLNTATLRLKRGHRYGLCGKNGTGKSTLMRAITNgqvegfpspdevrtfyvehDIDGSEAdtsvlQFI 537
Cdd:cd03247 5 NVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTG-------------------DLKPQQG-----EIT 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 538 LTDKRVLSSEAEIKEALASVG-----FNDErQKQAIGS-LSGGWKMKLALARAMLFKADILLLDEPTNHLD-VVNVAWLE 610
Cdd:cd03247 61 LDGVPVSDLEKALSSLISVLNqrpylFDTT-LRNNLGRrFSGGERQRLALARILLQDAPIVLLDEPTVGLDpITERQLLS 139
|
170
....*....|....*.
gi 1933195014 611 NYLTSLKTCTSIIVSH 626
Cdd:cd03247 140 LIFEVLKDKTLIWITH 155
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
462-626 |
4.18e-12 |
|
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: 67.42 E-value: 4.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 462 SLAYGAKILLNTATLRLKRGHRYGLCGKNGTGKSTLMRAITN-------------GQVEGFPSPDEVRTF--YVEHDIDG 526
Cdd:COG1119 10 TVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGdlpptygndvrlfGERRGGEDVWELRKRigLVSPALQL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 527 S-EADTSVLQFILT--------DKRVlsSEAEIKEA---LASVGFnDERQKQAIGSLSGGWKMKLALARAMLFKADILLL 594
Cdd:COG1119 90 RfPRDETVLDVVLSgffdsiglYREP--TDEQRERArelLELLGL-AHLADRPFGTLSQGEQRRVLIARALVKDPELLIL 166
|
170 180 190
....*....|....*....|....*....|....*.
gi 1933195014 595 DEPTNHLDVVN----VAWLEnYLTSLKTCTSIIVSH 626
Cdd:COG1119 167 DEPTAGLDLGArellLALLD-KLAAEGAPTLVLVTH 201
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
466-611 |
5.83e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 66.05 E-value: 5.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 466 GAKILLNTATLRLKRGHRYGLCGKNGTGKSTLMRAIT------------NGQVEGFPSPDEVRTfYVEHDiDGSEADTSV 533
Cdd:PRK13539 13 GGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAgllppaagtiklDGGDIDDPDVAEACH-YLGHR-NAMKPALTV 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1933195014 534 LQFILTDKRVL-SSEAEIKEALASVGFNDERQKQAiGSLSGGWKMKLALARAMLFKADILLLDEPTNHLDVVNVAWLEN 611
Cdd:PRK13539 91 AENLEFWAAFLgGEELDIAAALEAVGLAPLAHLPF-GYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFAE 168
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
471-991 |
5.96e-12 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 69.28 E-value: 5.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 471 LNTATLRLKRGHRYGLCGKNGTGKSTLMRAIT------------NGQVEGFPSPDE-----VRTFYVEHDIdgseADT-S 532
Cdd:COG1129 20 LDGVSLELRPGEVHALLGENGAGKSTLMKILSgvyqpdsgeillDGEPVRFRSPRDaqaagIAIIHQELNL----VPNlS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 533 VLQ--FI--------LTDKRVLSSEAEikEALASVGFN-DERQKqaIGSLSGGWKMKLALARAMLFKADILLLDEPTNHL 601
Cdd:COG1129 96 VAEniFLgreprrggLIDWRAMRRRAR--ELLARLGLDiDPDTP--VGDLSVAQQQLVEIARALSRDARVLILDEPTASL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 602 DVVNVAWLENYLTSLKT--CTSIIVSHdsgFLN------NTITdVlhlnrfkLR--RYRGNLEsfVKAVPEAKsyyslea 671
Cdd:COG1129 172 TEREVERLFRIIRRLKAqgVAIIYISH---RLDevfeiaDRVT-V-------LRdgRLVGTGP--VAELTEDE------- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 672 ledykfklpdppllegvktkeksLLKM---RKVGFQYPTQAVQ------QLYDITLQ-----VSLSSR----VAILGPNG 733
Cdd:COG1129 232 -----------------------LVRLmvgRELEDLFPKRAAApgevvlEVEGLSVGgvvrdVSFSVRageiLGIAGLVG 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 734 SGKSTLVKLLIGdMEPNKGGEIWKHpnlvigyvaqhafhhidhhldktpleymlwryqtGEDLEemskaNRQITEAeaqk 813
Cdd:COG1129 289 AGRTELARALFG-ADPADSGEIRLD----------------------------------GKPVR-----IRSPRDA---- 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 814 MKEG-ALIVvegqkrliEEiitRKK--LkqsyeyevsFKGLSSSENIWLPR-DELVKRGFekkvieVDTREAQRlgllrp 889
Cdd:COG1129 325 IRAGiAYVP--------ED---RKGegL---------VLDLSIRENITLASlDRLSRGGL------LDRRRERA------ 372
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 890 LVRREIEKhfadFGLEPEFVsHNTMRGLSGG--QKVkiVLgaATW--RRPHVICLDEPTNYLD---RESLAALIAALKVf 962
Cdd:COG1129 373 LAEEYIKR----LRIKTPSP-EQPVGNLSGGnqQKV--VL--AKWlaTDPKVLILDEPTRGIDvgaKAEIYRLIRELAA- 442
|
570 580 590
....*....|....*....|....*....|....*
gi 1933195014 963 EG-GVLIIThnrdfSE-----SLCHEVWAMRDGRL 991
Cdd:COG1129 443 EGkAVIVIS-----SElpellGLSDRILVMREGRI 472
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
466-615 |
7.28e-12 |
|
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: 65.59 E-value: 7.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 466 GAKILLNTATLRLKRGHRYGLCGKNGTGKSTLMRAIT------------NGQVEGFPSPDEVRTF-YVEHdIDGSEADTS 532
Cdd:cd03231 11 DGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAglspplagrvllNGGPLDFQRDSIARGLlYLGH-APGIKTTLS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 533 VLQFiLTDKRVLSSEAEIKEALASVGFNDeRQKQAIGSLSGGWKMKLALARAMLFKADILLLDEPTNHLDVVNVAWLENY 612
Cdd:cd03231 90 VLEN-LRFWHADHSDEQVEEALARVGLNG-FEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEA 167
|
...
gi 1933195014 613 LTS 615
Cdd:cd03231 168 MAG 170
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
471-598 |
8.37e-12 |
|
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: 66.60 E-value: 8.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 471 LNTATLRLKRGHRYGLCGKNGTGKSTLMRAITngqveGFPSPDEVRTFYVEHDIDG------------------------ 526
Cdd:COG0411 20 VDDVSLEVERGEIVGLIGPNGAGKTTLFNLIT-----GFYRPTSGRILFDGRDITGlpphriarlgiartfqnprlfpel 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 527 -----------SEADTSVLQFILTDKRVLSSEAEIK----EALASVGFNDERQKQAiGSLSGGWKMKLALARAMLFKADI 591
Cdd:COG0411 95 tvlenvlvaahARLGRGLLAALLRLPRARREEREAReraeELLERVGLADRADEPA-GNLSYGQQRRLEIARALATEPKL 173
|
....*..
gi 1933195014 592 LLLDEPT 598
Cdd:COG0411 174 LLLDEPA 180
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
461-627 |
9.78e-12 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 66.65 E-value: 9.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 461 FSLAYGAKILLNTATLRLKRGHRYGLCGKNGTGKSTLMRAITngqveGFPSPDEVRTFYVEHDIDGSEADT--------- 531
Cdd:COG1116 17 FPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIA-----GLEKPTSGEVLVDGKPVTGPGPDRgvvfqepal 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 532 ----SVLQ---FILTDKRVLSSEAE--IKEALASVG---FNDERQKQaigsLSGGWKMKLALARAMLFKADILLLDEPTN 599
Cdd:COG1116 92 lpwlTVLDnvaLGLELRGVPKAERRerARELLELVGlagFEDAYPHQ----LSGGMRQRVAIARALANDPEVLLMDEPFG 167
|
170 180 190
....*....|....*....|....*....|..
gi 1933195014 600 HLDVVNVA----WLENYLTSLKTcTSIIVSHD 627
Cdd:COG1116 168 ALDALTRErlqdELLRLWQETGK-TVLFVTHD 198
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
694-1008 |
1.14e-11 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 66.63 E-value: 1.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 694 SLLKMRKVGFQYPT-------QAVQQLYDITLQVSLSSRVAILGPNGSGKSTLVKLLIGDMEPNKGGEIWKhpnlvigyv 766
Cdd:PRK10419 2 TLLNVSGLSHHYAHgglsgkhQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWR--------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 767 aqhafhhidhhldktpleymlwryqtGEDLEEMSKANRQITEAEAQKMKEGALIVVEGQKRlIEEIItRKKLKQsyeyev 846
Cdd:PRK10419 73 --------------------------GEPLAKLNRAQRKAFRRDIQMVFQDSISAVNPRKT-VREII-REPLRH------ 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 847 sFKGLSSSEniwlprdelvkrgfekkvievdtREAQRLGLLRPLvrreiekhfadfGLEPEFVSHNTMRgLSGGQKVKIV 926
Cdd:PRK10419 119 -LLSLDKAE-----------------------RLARASEMLRAV------------DLDDSVLDKRPPQ-LSGGQLQRVC 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 927 LGAATWRRPHVICLDEPTNYLDRESLAALIAALKV----FEGGVLIITHNRDFSESLCHEVWAMRDGRLeasghnwVEGQ 1002
Cdd:PRK10419 162 LARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKlqqqFGTACLFITHDLRLVERFCQRVMVMDNGQI-------VETQ 234
|
....*.
gi 1933195014 1003 GSGPRI 1008
Cdd:PRK10419 235 PVGDKL 240
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
462-648 |
1.15e-11 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 65.46 E-value: 1.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 462 SLAYGAKIL-LNTATLRLKRGHRYGLCGKNGTGKSTLMRAI------TNGQ--VEGFP----SPDEV----RTFYVehdi 524
Cdd:COG2884 8 SKRYPGGREaLSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLygeerpTSGQvlVNGQDlsrlKRREIpylrRRIGV---- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 525 dgseadtsVLQ-F-ILTDKRVL-----------SSEAEIK----EALASVGFnDERQKQAIGSLSGGWKMKLALARAMLF 587
Cdd:COG2884 84 --------VFQdFrLLPDRTVYenvalplrvtgKSRKEIRrrvrEVLDLVGL-SDKAKALPHELSGGEQQRVAIARALVN 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1933195014 588 KADILLLDEPTNHLDVVNVAWLENYLTSLKT--CTSIIVSHDSGFLNNTITDVLHLNRFKLRR 648
Cdd:COG2884 155 RPELLLADEPTGNLDPETSWEIMELLEEINRrgTTVLIATHDLELVDRMPKRVLELEDGRLVR 217
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
698-975 |
1.18e-11 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 68.61 E-value: 1.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 698 MRKVGFQYPTQAvQQLYDITLQVSLSSRVAILGPNGSGKSTLVKLLIGdMEPNKGGEIWKHPNLVIGYVAQhafhhiDHH 777
Cdd:PRK11819 9 MNRVSKVVPPKK-QILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAG-VDKEFEGEARPAPGIKVGYLPQ------EPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 778 LD--KTPLEymlwryqtgeDLEE-----MSKANR--QITEAEAQKMKEG-ALIvvEGQKRLIEEIitrkklkqsyeyevs 847
Cdd:PRK11819 81 LDpeKTVRE----------NVEEgvaevKAALDRfnEIYAAYAEPDADFdALA--AEQGELQEII--------------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 848 fkglsSSENIWlprdelvkrgfekkviEVDTREAQRLGLLRplvrreiekhfadfgLEP--EFVSHntmrgLSGGQKVKI 925
Cdd:PRK11819 134 -----DAADAW----------------DLDSQLEIAMDALR---------------CPPwdAKVTK-----LSGGERRRV 172
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1933195014 926 VLGAATWRRPHVICLDEPTNYLDRESLAALIAALKVFEGGVLIITHNRDF 975
Cdd:PRK11819 173 ALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDYPGTVVAVTHDRYF 222
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
485-627 |
1.65e-11 |
|
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: 65.01 E-value: 1.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 485 GLCGKNGTGKSTLMRAI------TNGQVEgfpsPDEVRTFYVEHDIDGSEADTSV------------------LQFILTD 540
Cdd:cd03297 27 GIFGASGAGKSTLLRCIaglekpDGGTIV----LNGTVLFDSRKKINLPPQQRKIglvfqqyalfphlnvrenLAFGLKR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 541 KRVLSSEAEIKEALASVGFnDERQKQAIGSLSGGWKMKLALARAMLFKADILLLDEPTNHLDVVNVAWLENYLTSLKT-- 618
Cdd:cd03297 103 KRNREDRISVDELLDLLGL-DHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQIKKnl 181
|
170
....*....|
gi 1933195014 619 -CTSIIVSHD 627
Cdd:cd03297 182 nIPVIFVTHD 191
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
461-626 |
1.69e-11 |
|
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: 68.23 E-value: 1.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 461 FSLAYGAKILLNTaTLRLKRGHRYGLCGKNGTGKSTLMRAITN------GQVE--GFPSPD----EVRTF--YVEHD--- 523
Cdd:TIGR01193 481 YSYGYGSNILSDI-SLTIKMNSKTTIVGMSGSGKSTLAKLLVGffqarsGEILlnGFSLKDidrhTLRQFinYLPQEpyi 559
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 524 IDGSeadtsVLQFILTDKRVLSSEAEIKEALASVGFNDERQKQAIG----------SLSGGWKMKLALARAMLFKADILL 593
Cdd:TIGR01193 560 FSGS-----ILENLLLGAKENVSQDEIWAACEIAEIKDDIENMPLGyqtelseegsSISGGQKQRIALARALLTDSKVLI 634
|
170 180 190
....*....|....*....|....*....|...
gi 1933195014 594 LDEPTNHLDVVNVAWLENYLTSLKTCTSIIVSH 626
Cdd:TIGR01193 635 LDESTSNLDTITEKKIVNNLLNLQDKTIIFVAH 667
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
696-991 |
2.00e-11 |
|
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: 64.82 E-value: 2.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 696 LKMRKVGFQYPTQAVQQ--LYDITLQVSLSSRVAILGPNGSGKSTLVKLLIGDMEPNKGgEIWkhpnlvigyvaqhafhh 773
Cdd:cd03255 1 IELKNLSKTYGGGGEKVqaLKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSG-EVR----------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 774 IDhhldktpleymlwryqtGEDLEEMSKANRqiTEAEAQKMkeGaliVVEGQKRLIEEiitrkklkqsyeyevsfkgLSS 853
Cdd:cd03255 63 VD-----------------GTDISKLSEKEL--AAFRRRHI--G---FVFQSFNLLPD-------------------LTA 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 854 SENIWLPrdeLVKRGFEKKVIEVDTREA-QRLGLlrplvrREIEKHFadfglepefVSHntmrgLSGGQKVKIVLGAATW 932
Cdd:cd03255 100 LENVELP---LLLAGVPKKERRERAEELlERVGL------GDRLNHY---------PSE-----LSGGQQQRVAIARALA 156
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1933195014 933 RRPHVICLDEPTNYLDRESLAALIAALKVF--EGG--VLIITHNRDFsESLCHEVWAMRDGRL 991
Cdd:cd03255 157 NDPKIILADEPTGNLDSETGKEVMELLRELnkEAGttIVVVTHDPEL-AEYADRIIELRDGKI 218
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
694-991 |
2.01e-11 |
|
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: 65.60 E-value: 2.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 694 SLLKMRKVGFQYPT-------QAVQQLYDITLQVSLSSRVAILGPNGSGKSTLVKLLIGDMEPNKGGEIWKhpnlvigyv 766
Cdd:TIGR02769 1 SLLEVRDVTHTYRTgglfgakQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFR--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 767 aqhafhhidhhldktpleymlwryqtGEDLEEMSKANRQITEAEAQKMKEGALIVVEGQKRlIEEIItRKKLKQsyeyev 846
Cdd:TIGR02769 72 --------------------------GQDLYQLDRKQRRAFRRDVQLVFQDSPSAVNPRMT-VRQII-GEPLRH------ 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 847 sFKGLSSSEniwlprdelvkrgfekkvievdtREAQRLGLLRPLvrreiekhfadfGLEPEfVSHNTMRGLSGGQKVKIV 926
Cdd:TIGR02769 118 -LTSLDESE-----------------------QKARIAELLDMV------------GLRSE-DADKLPRQLSGGQLQRIN 160
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1933195014 927 LGAATWRRPHVICLDEPTNYLDRESLAALIAALKVF--EGGV--LIITHNRDFSESLCHEVWAMRDGRL 991
Cdd:TIGR02769 161 IARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLqqAFGTayLFITHDLRLVQSFCQRVAVMDKGQI 229
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
461-649 |
2.47e-11 |
|
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: 64.22 E-value: 2.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 461 FSLAYGAKILLNTATLRLKRGHRYGLCGKNGTGKSTLMRAI------TNGQVEGFPSPdevRTFYVEHDID------GSE 528
Cdd:cd03269 6 VTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMIlgiilpDSGEVLFDGKP---LDIAARNRIGylpeerGLY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 529 ADTSVL-QFI-LTDKRVLSSE---AEIKEALASVGFNdERQKQAIGSLSGGWKMKLALARAMLFKADILLLDEPTNHLDV 603
Cdd:cd03269 83 PKMKVIdQLVyLAQLKGLKKEearRRIDEWLERLELS-EYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDP 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1933195014 604 VNVAWLENYLTSLKT--CTSIIVSHDSGFLNNTITDVLHLNRFKLRRY 649
Cdd:cd03269 162 VNVELLKDVIRELARagKTVILSTHQMELVEELCDRVLLLNKGRAVLY 209
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
715-995 |
2.73e-11 |
|
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: 64.77 E-value: 2.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 715 DITLQVSLSSRVAILGPNGSGKSTLVKLLIGDMEPNKGgEIwkhpnlvigyvaqhafhhidhHLDktpleymlwryqtGE 794
Cdd:cd03219 18 DVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSG-SV---------------------LFD-------------GE 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 795 DleemskanrqITeaeaqkmkegalivvegqkRLIEEIITRKKLKQSYEYEVSFKGLSSSENIwlprdeLVKRGFEKKVI 874
Cdd:cd03219 63 D----------IT-------------------GLPPHEIARLGIGRTFQIPRLFPELTVLENV------MVAAQARTGSG 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 875 EVDTREAQRLGLLRPLVRREIEKhfadFGLEPefVSHNTMRGLSGGQKVKIVLGAATWRRPHVICLDEPT---NYLDRES 951
Cdd:cd03219 108 LLLARARREEREARERAEELLER----VGLAD--LADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAaglNPEETEE 181
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1933195014 952 LAALIAALKVFEGGVLIITHNRDFSESLCHEVWAMRDGRLEASG 995
Cdd:cd03219 182 LAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEG 225
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
694-756 |
3.41e-11 |
|
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: 64.72 E-value: 3.41e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1933195014 694 SLLKMRKVGFQYPTQAVqqLYDITLQVSLSSRVAILGPNGSGKSTLVKLLIGDMEPNKGGEIW 756
Cdd:COG1119 2 PLLELRNVTVRRGGKTI--LDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDVR 62
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
462-658 |
4.05e-11 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 67.19 E-value: 4.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 462 SLAY-GAKILLNTATLRLKRGHRYGLCGKNGTGKSTLMRAI------TNGQVegFPSPDEVRTFYVEHDIDGSEADTSVL 534
Cdd:PLN03073 515 SFGYpGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLIsgelqpSSGTV--FRSAKVRMAVFSQHHVDGLDLSSNPL 592
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 535 QFILtdkRVLSS--EAEIKEALASVGFNDERQKQAIGSLSGGWKMKLALARAMLFKADILLLDEPTNHLDVVNVAWLENY 612
Cdd:PLN03073 593 LYMM---RCFPGvpEQKLRAHLGSFGVTGNLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQG 669
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1933195014 613 LTSLKTCTsIIVSHDSGFLNNTITDVLHLNRFKLRRYRGNLESFVK 658
Cdd:PLN03073 670 LVLFQGGV-LMVSHDEHLISGSVDELWVVSEGKVTPFHGTFHDYKK 714
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
464-602 |
4.38e-11 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 63.02 E-value: 4.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 464 AYGAKILLNTATLRLKRGHRYGLCGKNGTGKSTLMRAI------TNGQVEGfpSPDEVRTFYVEHdidgSEADTSvlqFI 537
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLagvlrpTSGTVRR--AGGARVAYVPQR----SEVPDS---LP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 538 LTDKRVLS----------------SEAEIKEALASVGFNDERqKQAIGSLSGGWKMKLALARAMLFKADILLLDEPTNHL 601
Cdd:NF040873 72 LTVRDLVAmgrwarrglwrrltrdDRAAVDDALERVGLADLA-GRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGL 150
|
.
gi 1933195014 602 D 602
Cdd:NF040873 151 D 151
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
464-995 |
4.50e-11 |
|
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: 66.75 E-value: 4.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 464 AYGAKILLNTATLRLKRGHRYGLCGKNGTGKSTLMRAITNgqVEGFPsPDEVRTFY------------------------ 519
Cdd:TIGR03269 9 KFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRG--MDQYE-PTSGRIIYhvalcekcgyverpskvgepcpvc 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 520 ----VEHDIDGSEADTSV-----------LQ--FIL-TDKRVLSSeaeIKEALASVGFN-DERQKQAIG----------- 569
Cdd:TIGR03269 86 ggtlEPEEVDFWNLSDKLrrrirkriaimLQrtFALyGDDTVLDN---VLEALEEIGYEgKEAVGRAVDliemvqlshri 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 570 -----SLSGGWKMKLALARAMLFKADILLLDEPTNHLDVVNVAWLENYLTSL---KTCTSIIVSHDSGFLNNTITDVLHL 641
Cdd:TIGR03269 163 thiarDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAvkaSGISMVLTSHWPEVIEDLSDKAIWL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 642 NRFKLRRyRGN----LESFVKAVPEAKSYYSLEALEDykfklpdppllegvktkeksLLKMRKVGFQYPT---QAVQQLY 714
Cdd:TIGR03269 243 ENGEIKE-EGTpdevVAVFMEGVSEVEKECEVEVGEP--------------------IIKVRNVSKRYISvdrGVVKAVD 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 715 DITLQVSLSSRVAILGPNGSGKSTLVKLLIGDMEPNKGgEIWkhpnlvigyvaqhafhhidhhldktpleymlwrYQTGE 794
Cdd:TIGR03269 302 NVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSG-EVN---------------------------------VRVGD 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 795 DLEEMSKANrqiteaeaqkmkegalivVEGQKRLIEEIITRKKLKQSYEYEVSFKGLSSSENIWLPrDELVKRG--FEKK 872
Cdd:TIGR03269 348 EWVDMTKPG------------------PDGRGRAKRYIGILHQEYDLYPHRTVLDNLTEAIGLELP-DELARMKavITLK 408
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 873 VIEVDTREAqrlgllrplvrREIEKHFADfglepefvshntmrGLSGGQKVKIVLGAATWRRPHVICLDEPTNYLD---- 948
Cdd:TIGR03269 409 MVGFDEEKA-----------EEILDKYPD--------------ELSEGERHRVALAQVLIKEPRIVILDEPTGTMDpitk 463
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 1933195014 949 RESLAALIAALKVFEGGVLIITHNRDFSESLCHEVWAMRDGRLEASG 995
Cdd:TIGR03269 464 VDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIG 510
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
464-602 |
5.18e-11 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 65.24 E-value: 5.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 464 AYGAKILLNTATLRLKRGHRYGLCGKNGTGKSTLMRAIT--------NGQVEGFPSPDEVRT----FYVEHDIDGSEADT 531
Cdd:PRK13536 50 SYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILgmtspdagKITVLGVPVPARARLararIGVVPQFDNLDLEF 129
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1933195014 532 SVLQFILTDKRVLSSEA-EIKEALASVGFNDERQKQA---IGSLSGGWKMKLALARAMLFKADILLLDEPTNHLD 602
Cdd:PRK13536 130 TVRENLLVFGRYFGMSTrEIEAVIPSLLEFARLESKAdarVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLD 204
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
465-602 |
6.26e-11 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 64.83 E-value: 6.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 465 YGAKILLNTATLRLKRGHRYGLCGKNGTGKSTLMRAITN------GQVE--GFPSPDEVR----TFYVEHDIDGSEADTS 532
Cdd:PRK13537 17 YGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGlthpdaGSISlcGEPVPSRARharqRVGVVPQFDNLDPDFT 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1933195014 533 VLQFILTDKRVLS-SEAEIKEALASV---GFNDERQKQAIGSLSGGWKMKLALARAMLFKADILLLDEPTNHLD 602
Cdd:PRK13537 97 VRENLLVFGRYFGlSAAAARALVPPLlefAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLD 170
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
571-766 |
6.63e-11 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 66.19 E-value: 6.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 571 LSGGWKMKLALARAMLFKADILLLDEPTNHLDVVNVAWLENYLTSLktctsiivsHDSGflnntITDVLHLNRFklrryr 650
Cdd:PRK10938 136 LSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASL---------HQSG-----ITLVLVLNRF------ 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 651 GNLESFV----------------KAVPEAKSYYSL----EALEDYKFKLPDPPLLEGVKTKEKSLLKMRKVGFQYPTQAV 710
Cdd:PRK10938 196 DEIPDFVqfagvladctlaetgeREEILQQALVAQlahsEQLEGVQLPEPDEPSARHALPANEPRIVLNNGVVSYNDRPI 275
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1933195014 711 qqLYDITLQVSLSSRVAILGPNGSGKSTLVKLLIGDmEPN------------KG-GE-IW---KHpnlvIGYV 766
Cdd:PRK10938 276 --LHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGD-HPQgysndltlfgrrRGsGEtIWdikKH----IGYV 341
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
696-995 |
6.85e-11 |
|
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 downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 64.39 E-value: 6.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 696 LKMRKVGFQY------PTQAvqqLYDITLQVSLSSRVAILGPNGSGKSTLVKLLIGDMEPNKGgEIWkhpnlVIGYVAQH 769
Cdd:TIGR04521 1 IKLKNVSYIYqpgtpfEKKA---LDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSG-TVT-----IDGRDITA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 770 afhhidhhldktpleymlwryQTGEDLEEMSKanrqiteaeaqkmKEGaliVV----EGQkrLIEEIItrkklkqsYEyE 845
Cdd:TIGR04521 72 ---------------------KKKKKLKDLRK-------------KVG---LVfqfpEHQ--LFEETV--------YK-D 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 846 VSFkGLSsseNIWLPRDELVKRgfekkvievdtreaqrlgllrplVRREIEKhfadFGLEPEFVSHNTMRgLSGGQK--V 923
Cdd:TIGR04521 104 IAF-GPK---NLGLSEEEAEER-----------------------VKEALEL----VGLDEEYLERSPFE-LSGGQMrrV 151
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1933195014 924 KI--VLgaATwrRPHVICLDEPTNYLD---RESLAALIAALKVFEG-GVLIITHNRDFSESLCHEVWAMRDGRLEASG 995
Cdd:TIGR04521 152 AIagVL--AM--EPEVLILDEPTAGLDpkgRKEILDLFKRLHKEKGlTVILVTHSMEDVAEYADRVIVMHKGKIVLDG 225
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
705-974 |
7.89e-11 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 62.25 E-value: 7.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 705 YPTQAVqqLYDITLQVSLSSRVAILGPNGSGKSTLVKLLIGDMEPnKGGEIWKHPNLVIGYVAQHAfhhidhHLDKT-PL 783
Cdd:NF040873 2 YGGRPV--LHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRP-TSGTVRRAGGARVAYVPQRS------EVPDSlPL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 784 eymlwryqTGEDLEEMSKanrqiteaeaqkmkegalivvegqkrlieeiitrkklkqsyeyevsfkglssseniWlprde 863
Cdd:NF040873 73 --------TVRDLVAMGR--------------------------------------------------------W----- 83
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 864 lvkrgfekkvievdtreaQRLGLLRPLV---RREIEKHFADFGLEpEFvSHNTMRGLSGGQKVKIVLGAATWRRPHVICL 940
Cdd:NF040873 84 ------------------ARRGLWRRLTrddRAAVDDALERVGLA-DL-AGRQLGELSGGQRQRALLAQGLAQEADLLLL 143
|
250 260 270
....*....|....*....|....*....|....*..
gi 1933195014 941 DEPTNYLDRESLAALIAALKVFEG---GVLIITHNRD 974
Cdd:NF040873 144 DEPTTGLDAESRERIIALLAEEHArgaTVVVVTHDLE 180
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
695-995 |
7.92e-11 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 65.81 E-value: 7.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 695 LLKMRKVGFQYPtqAVQQLYDITLQVSLSSRVAILGPNGSGKSTLVKLLIGDMEPNkGGEIWkhpnlvigyvaqhafhhI 774
Cdd:COG1129 4 LLEMRGISKSFG--GVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPD-SGEIL-----------------L 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 775 DhhldktpleymlwryqtGEDLEEMSkanrqITEAEAQkmkeGalIVVEGQkrlieeiitrkklkqsyeyEVS-FKGLSS 853
Cdd:COG1129 64 D-----------------GEPVRFRS-----PRDAQAA----G--IAIIHQ-------------------ELNlVPNLSV 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 854 SENIWLPRdELVKRGFekkvieVDTREaqrlgllrplVRREIEKHFADFGLEpefVSHNT-MRGLSGGQK--VKIVlgAA 930
Cdd:COG1129 97 AENIFLGR-EPRRGGL------IDWRA----------MRRRARELLARLGLD---IDPDTpVGDLSVAQQqlVEIA--RA 154
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1933195014 931 TWRRPHVICLDEPTNYLDR---ESLAALIAALKVfEG-GVLIITHnrDFSE--SLCHEVWAMRDGRLEASG 995
Cdd:COG1129 155 LSRDARVLILDEPTASLTErevERLFRIIRRLKA-QGvAIIYISH--RLDEvfEIADRVTVLRDGRLVGTG 222
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
713-995 |
8.14e-11 |
|
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: 62.92 E-value: 8.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 713 LYDITLQVSLSSRVAILGPNGSGKSTLVKLLIGDMEPNkGGEIWkhpnlvigyvaqhafhhIDhhldktpleymlwryqt 792
Cdd:cd03259 16 LDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPD-SGEIL-----------------ID----------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 793 GEDLEEMSKANRQIteaeAQKMKEGALivvegqkrlieeiitrkklkqsyeyevsFKGLSSSENIWLPrdeLVKRGFEKK 872
Cdd:cd03259 61 GRDVTGVPPERRNI----GMVFQDYAL----------------------------FPHLTVAENIAFG---LKLRGVPKA 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 873 VIEVDTREAQRLGLLRPLVRREIEKhfadfglepefvshntmrgLSGGQKVKIVLGAATWRRPHVICLDEPTNYLD---- 948
Cdd:cd03259 106 EIRARVRELLELVGLEGLLNRYPHE-------------------LSGGQQQRVALARALAREPSLLLLDEPLSALDaklr 166
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1933195014 949 ---RESLAALIAALKVfegGVLIITHNRDFSESLCHEVWAMRDGRLEASG 995
Cdd:cd03259 167 eelREELKELQRELGI---TTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
698-995 |
8.85e-11 |
|
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: 63.29 E-value: 8.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 698 MRKVGFQYPTQAVqqLYDITLQVSLSSRVAILGPNGSGKSTLVKLLIGDMEPNKgGEIWkhpnlvigyvaqhafhhIDhh 777
Cdd:cd03261 3 LRGLTKSFGGRTV--LKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDS-GEVL-----------------ID-- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 778 ldktpleymlwryqtGEDLEEMSKANRQiteAEAQKM----KEGALivvegqkrlieeiitrkklkqsyeyevsFKGLSS 853
Cdd:cd03261 61 ---------------GEDISGLSEAELY---RLRRRMgmlfQSGAL----------------------------FDSLTV 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 854 SENIWLPrdelvkrgfekkvievdTREaqRLGLLRPLVRREIEKHFADFGLEPefvSHNTMRG-LSGGQKVKIVLGAATW 932
Cdd:cd03261 95 FENVAFP-----------------LRE--HTRLSEEEIREIVLEKLEAVGLRG---AEDLYPAeLSGGMKKRVALARALA 152
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1933195014 933 RRPHVICLDEPTNYLD---RESLAALIAALK-VFEGGVLIITHNRDFSESLCHEVWAMRDGRLEASG 995
Cdd:cd03261 153 LDPELLLYDEPTAGLDpiaSGVIDDLIRSLKkELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEG 219
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
466-615 |
9.60e-11 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 62.38 E-value: 9.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 466 GAKILLNTATLRLKRGHRYGLCGKNGTGKSTLMRAIT------NGQVE--GFPSPdEVRTFYVEH-----DIDGSEADTS 532
Cdd:TIGR01189 11 GERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAgllrpdSGEVRwnGTPLA-EQRDEPHENilylgHLPGLKPELS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 533 V---LQFILTDKRvlSSEAEIKEALASVGFNDeRQKQAIGSLSGGWKMKLALARAMLFKADILLLDEPTNHLDVVNVAWL 609
Cdd:TIGR01189 90 AlenLHFWAAIHG--GAQRTIEDALAAVGLTG-FEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVALL 166
|
....*.
gi 1933195014 610 ENYLTS 615
Cdd:TIGR01189 167 AGLLRA 172
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
465-626 |
1.01e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 63.32 E-value: 1.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 465 YGAKILLNTATLRLKRGHRYGLCGKNGTGKSTLMRAIT-------NGQVEGfpspdEVRTF----YVEhDIDGSEADTSV 533
Cdd:PRK14267 14 YGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNrllelneEARVEG-----EVRLFgrniYSP-DVDPIEVRREV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 534 ------------------LQFILTDKRVLSSEAEIKE----ALASVGFNDE---RQKQAIGSLSGGWKMKLALARAMLFK 588
Cdd:PRK14267 88 gmvfqypnpfphltiydnVAIGVKLNGLVKSKKELDErvewALKKAALWDEvkdRLNDYPSNLSGGQRQRLVIARALAMK 167
|
170 180 190
....*....|....*....|....*....|....*....
gi 1933195014 589 ADILLLDEPTNHLDVVNVAWLENYLTSLKT-CTSIIVSH 626
Cdd:PRK14267 168 PKILLMDEPTANIDPVGTAKIEELLFELKKeYTIVLVTH 206
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
466-627 |
1.12e-10 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 65.50 E-value: 1.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 466 GAKILLNTATLRLKRGHRYGLCGKNGTGKST----LMRAI-TNGQV--EGFPS---------PDEVRTFYVEHDIDGS-E 528
Cdd:PRK15134 297 DHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLInSQGEIwfDGQPLhnlnrrqllPVRHRIQVVFQDPNSSlN 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 529 ADTSVLQFILTDKRV----LSS---EAEIKEALASVGFNDERQKQAIGSLSGGWKMKLALARAMLFKADILLLDEPTNHL 601
Cdd:PRK15134 377 PRLNVLQIIEEGLRVhqptLSAaqrEQQVIAVMEEVGLDPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSL 456
|
170 180
....*....|....*....|....*....
gi 1933195014 602 DVVNVAWLENYLTSLKT---CTSIIVSHD 627
Cdd:PRK15134 457 DKTVQAQILALLKSLQQkhqLAYLFISHD 485
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
696-752 |
1.16e-10 |
|
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: 61.56 E-value: 1.16e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1933195014 696 LKMRKVGFQYPTQAVQQLYDITLQVSLSSRVAILGPNGSGKSTLVKLLIGDMEPNKG 752
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQG 57
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
695-995 |
1.60e-10 |
|
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: 62.14 E-value: 1.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 695 LLKMRKVGFQYPTQ--AVQQLYDITLQVSLSSRVAILGPNGSGKSTLVKLLIGdMEPNKGGEIWkhpnlvigyvaqhaFH 772
Cdd:cd03257 1 LLEVKNLSVSFPTGggSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILG-LLKPTSGSII--------------FD 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 773 hidhhldktpleymlwryqtGEDLEEMSKANRQITEAEAQkmkegalivvegqkrlieeIItrkklkqsyeyevsFKGLS 852
Cdd:cd03257 66 --------------------GKDLLKLSRRLRKIRRKEIQ-------------------MV--------------FQDPM 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 853 SSENIWLPRDELVKRGFEKKVIEVDTREAQRLGLLrplvrreiekHFADFGLEPEFVS---HntmrGLSGGQKVKIVLGA 929
Cdd:cd03257 93 SSLNPRMTIGEQIAEPLRIHGKLSKKEARKEAVLL----------LLVGVGLPEEVLNrypH----ELSGGQRQRVAIAR 158
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1933195014 930 ATWRRPHVICLDEPTNYLDReSLAALIAAL-----KVFEGGVLIITHNRDFSESLCHEVWAMRDGRLEASG 995
Cdd:cd03257 159 ALALNPKLLIADEPTSALDV-SVQAQILDLlkklqEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
471-629 |
1.63e-10 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 62.98 E-value: 1.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 471 LNTATLRLKRGHRYGLCGKNGTGKSTLMRAI------TNGQVE--GFPSPDEVRTFYVEHDIDGSEADTSVLqfILTDKR 542
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALmgfvrlASGKISilGQPTRQALQKNLVAYVPQSEEVDWSFP--VLVEDV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 543 VL---------------SSEAEIKEALASVGFNDERQKQaIGSLSGGWKMKLALARAMLFKADILLLDEPTNHLDVVNVA 607
Cdd:PRK15056 101 VMmgryghmgwlrrakkRDRQIVTAALARVDMVEFRHRQ-IGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEA 179
|
170 180
....*....|....*....|....
gi 1933195014 608 WLENYLTSLKT--CTSIIVSHDSG 629
Cdd:PRK15056 180 RIISLLRELRDegKTMLVSTHNLG 203
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
692-979 |
1.63e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 62.85 E-value: 1.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 692 EKSLLKMRKVGFQYPTQAVQQLYDITLQVSLSSRVAILGPNGSGKSTLVKLLIGDMEPNKGGEIWKhpnlvigyvaqhaf 771
Cdd:PRK13648 4 KNSIIVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYN-------------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 772 hhidhhldktpleymlwryqtgedleemskaNRQITEAEAQKMKEGALIVVEG-QKRLIEEIItrkklkqsyEYEVSFkG 850
Cdd:PRK13648 70 -------------------------------NQAITDDNFEKLRKHIGIVFQNpDNQFVGSIV---------KYDVAF-G 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 851 LsssENIWLPRDELVKRgFEKKVIEVDTreaqrlgllrpLVRREIEKHfadfglepefvshntmrGLSGGQKVKIVLGAA 930
Cdd:PRK13648 109 L---ENHAVPYDEMHRR-VSEALKQVDM-----------LERADYEPN-----------------ALSGGQKQRVAIAGV 156
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1933195014 931 TWRRPHVICLDEPTNYLD---RESLAALIAALKVfEGGVLIITHNRDFSESL 979
Cdd:PRK13648 157 LALNPSVIILDEATSMLDpdaRQNLLDLVRKVKS-EHNITIISITHDLSEAM 207
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
465-617 |
2.05e-10 |
|
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: 62.00 E-value: 2.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 465 YGAKILLNTATLRLKRGHRYGLCGKNGTGKSTLMRAITN--------GQVEGFP---SPDEVRTF--YVEHDIDGSEADT 531
Cdd:cd03265 10 YGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTllkptsgrATVAGHDvvrEPREVRRRigIVFQDLSVDDELT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 532 SVLQFILTDK--RVLSSEAE--IKEALASVGFNDERQKQaIGSLSGGWKMKLALARAMLFKADILLLDEPTNHLDVVNVA 607
Cdd:cd03265 90 GWENLYIHARlyGVPGAERRerIDELLDFVGLLEAADRL-VKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRA 168
|
170
....*....|
gi 1933195014 608 WLENYLTSLK 617
Cdd:cd03265 169 HVWEYIEKLK 178
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
462-603 |
2.06e-10 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 64.09 E-value: 2.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 462 SLAYGAKILLNTATLRLKRGHRYGLCGKNGTGKSTLMRAItngqvEGFPSPDEVRTFYVEHDIDGSEA------------ 529
Cdd:PRK09536 10 SVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAI-----NGTLTPTAGTVLVAGDDVEALSAraasrrvasvpq 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 530 DTSvLQFILTDKRVL----------------SSEAEIKEALASVG---FNDerqkQAIGSLSGGWKMKLALARAMLFKAD 590
Cdd:PRK09536 85 DTS-LSFEFDVRQVVemgrtphrsrfdtwteTDRAAVERAMERTGvaqFAD----RPVTSLSGGERQRVLLARALAQATP 159
|
170
....*....|...
gi 1933195014 591 ILLLDEPTNHLDV 603
Cdd:PRK09536 160 VLLLDEPTASLDI 172
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
703-995 |
2.22e-10 |
|
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: 61.61 E-value: 2.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 703 FQYPTQAVQQLYDITLQVSLSSRVAILGPNGSGKSTLVKLLIGDMEPNKGGEiwkhpnLVIGYVAQHAfhhidhhldktP 782
Cdd:cd03266 11 FRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFA------TVDGFDVVKE-----------P 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 783 LEymlwryqtgedleemskANRQITeaeaqkmkegaliVVEGQKRLIEEIITRKKLkqsyEYEVSFKGLSsseniwlpRD 862
Cdd:cd03266 74 AE-----------------ARRRLG-------------FVSDSTGLYDRLTARENL----EYFAGLYGLK--------GD 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 863 ELVKRgfekkVIEVdtreAQRLGLlRPLVRREIEkhfadfglepefvshntmrGLSGGQKVKIVLGAATWRRPHVICLDE 942
Cdd:cd03266 112 ELTAR-----LEEL----ADRLGM-EELLDRRVG-------------------GFSTGMRQKVAIARALVHDPPVLLLDE 162
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1933195014 943 PTNYLDRESLAALIAALKVF-EGG--VLIITHNRDFSESLCHEVWAMRDGRLEASG 995
Cdd:cd03266 163 PTTGLDVMATRALREFIRQLrALGkcILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
466-626 |
2.23e-10 |
|
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: 65.32 E-value: 2.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 466 GAKILLNTATLRLKRGHRYGLCGKNGTGKSTLMRAI-----TNGQVEgfpspdevrtfyvehdIDGSEADTSVLQ----- 535
Cdd:TIGR01271 1230 AGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALlrllsTEGEIQ----------------IDGVSWNSVTLQtwrka 1293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 536 --------FILT-------DKRVLSSEAEIKEALASVG-------FNDERQKQAIGS---LSGGWKMKLALARAMLFKAD 590
Cdd:TIGR01271 1294 fgvipqkvFIFSgtfrknlDPYEQWSDEEIWKVAEEVGlksvieqFPDKLDFVLVDGgyvLSNGHKQLMCLARSILSKAK 1373
|
170 180 190
....*....|....*....|....*....|....*..
gi 1933195014 591 ILLLDEPTNHLDVVNVAWLENYLT-SLKTCTSIIVSH 626
Cdd:TIGR01271 1374 ILLLDEPSAHLDPVTLQIIRKTLKqSFSNCTVILSEH 1410
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
468-627 |
2.38e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 62.37 E-value: 2.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 468 KILLNTATLRLKRGHRYGLCGKNGTGKSTLMRAItNGQVEGFPSPDEV--RTFYVEHDIDGSEA---------------- 529
Cdd:PRK14246 23 KAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVL-NRLIEIYDSKIKVdgKVLYFGKDIFQIDAiklrkevgmvfqqpnp 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 530 --DTSVLQFI--------LTDKRVLSSEAEikEALASVGFNDE---RQKQAIGSLSGGWKMKLALARAMLFKADILLLDE 596
Cdd:PRK14246 102 fpHLSIYDNIayplkshgIKEKREIKKIVE--ECLRKVGLWKEvydRLNSPASQLSGGQQQRLTIARALALKPKVLLMDE 179
|
170 180 190
....*....|....*....|....*....|..
gi 1933195014 597 PTNHLDVVNVAWLENYLTSLKT-CTSIIVSHD 627
Cdd:PRK14246 180 PTSMIDIVNSQAIEKLITELKNeIAIVIVSHN 211
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
708-995 |
2.60e-10 |
|
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: 61.98 E-value: 2.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 708 QAVQqlyDITLQVSLSSRVAILGPNGSGKSTLVKLLIGDMEPNkGGEIwkhpnlvigyvaqhafhhidhHLDktpleyml 787
Cdd:COG0411 18 VAVD---DVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPT-SGRI---------------------LFD-------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 788 wryqtGEDLEEMS--KANR-------QITeaeaqkmkegalivvegqkRLieeiitrkklkqsyeyevsFKGLSSSENIW 858
Cdd:COG0411 65 -----GRDITGLPphRIARlgiartfQNP-------------------RL-------------------FPELTVLENVL 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 859 LPRDELVKRGFEKKVIEVDTREAQrlgllRPLVRREIEKHFADFGLEPefVSHNTMRGLSGGQK--VKIVLGAATwrRPH 936
Cdd:COG0411 102 VAAHARLGRGLLAALLRLPRARRE-----EREARERAEELLERVGLAD--RADEPAGNLSYGQQrrLEIARALAT--EPK 172
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1933195014 937 VICLDEPT---NYLDRESLAALIAALKVFEG-GVLIITHNRDFSESLCHEVWAMRDGRLEASG 995
Cdd:COG0411 173 LLLLDEPAaglNPEETEELAELIRRLRDERGiTILLIEHDMDLVMGLADRIVVLDFGRVIAEG 235
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
464-602 |
2.61e-10 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 63.20 E-value: 2.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 464 AYGAKILLNTATLRLKRGHRYGLCGKNGTGKSTLMRAitngqVEGFPSPDEVRTFyvehdIDGSEADTSVLQ-------- 535
Cdd:PRK11432 15 RFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRL-----VAGLEKPTEGQIF-----IDGEDVTHRSIQqrdicmvf 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 536 ----------------FILTDKRVLSSE--AEIKEALASV---GFNDERQKQaigsLSGGWKMKLALARAMLFKADILLL 594
Cdd:PRK11432 85 qsyalfphmslgenvgYGLKMLGVPKEErkQRVKEALELVdlaGFEDRYVDQ----ISGGQQQRVALARALILKPKVLLF 160
|
....*...
gi 1933195014 595 DEPTNHLD 602
Cdd:PRK11432 161 DEPLSNLD 168
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
462-626 |
3.46e-10 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 61.72 E-value: 3.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 462 SLAYGAKILLNTATLRLKRGHRYGLCGKNGTGKSTLMRAITNgqvEGFPSPDEVRT---FYVEHDIDGSEADTSVLQ--- 535
Cdd:PRK14239 12 SVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINR---MNDLNPEVTITgsiVYNGHNIYSPRTDTVDLRkei 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 536 ---------FILT---------------DKRVLSSEAEIKEALASV--GFNDERQKQAIGsLSGGWKMKLALARAMLFKA 589
Cdd:PRK14239 89 gmvfqqpnpFPMSiyenvvyglrlkgikDKQVLDEAVEKSLKGASIwdEVKDRLHDSALG-LSGGQQQRVCIARVLATSP 167
|
170 180 190
....*....|....*....|....*....|....*...
gi 1933195014 590 DILLLDEPTNHLDVVNVAWLENYLTSLK-TCTSIIVSH 626
Cdd:PRK14239 168 KIILLDEPTSALDPISAGKIEETLLGLKdDYTMLLVTR 205
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
686-986 |
3.64e-10 |
|
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: 63.84 E-value: 3.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 686 EGVKTKEKSLLKMRKVGFQYP--TQAVQQLydiTLQVSLSSRVAILGPNGSGKSTLVKLLIGDMEPNKGGeiwkhpnLVI 763
Cdd:TIGR02857 312 APVTAAPASSLEFSGVSVAYPgrRPALRPV---SFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGS-------IAV 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 764 GyvaqhafhhidhhldktpleymlwryqtgedleemskaNRQITEAEAQKMKEGALIVveGQKRLIeeiitrkklkqsye 843
Cdd:TIGR02857 382 N--------------------------------------GVPLADADADSWRDQIAWV--PQHPFL-------------- 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 844 yevsFKGlSSSENIWLPR----DELVKRGfekkvievdtreAQRLGLLRPLVRREIekhfadfGLEPEFVSHNtmRGLSG 919
Cdd:TIGR02857 408 ----FAG-TIAENIRLARpdasDAEIREA------------LERAGLDEFVAALPQ-------GLDTPIGEGG--AGLSG 461
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1933195014 920 GQKVKIVLGAATWRRPHVICLDEPTNYLDRESLAALIAALKVFEGG--VLIITHnRDFSESLCHEVWAM 986
Cdd:TIGR02857 462 GQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGrtVLLVTH-RLALAALADRIVVL 529
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
465-627 |
3.69e-10 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 62.81 E-value: 3.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 465 YGAKILLNTATLRLKRGHRYGLCGKNGTGKSTLMRAITngqveGFPSPDEVRTFYVEHDIDGSEAD-------------- 530
Cdd:COG3842 15 YGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIA-----GFETPDSGRILLDGRDVTGLPPEkrnvgmvfqdyalf 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 531 --TSVLQ---FILTDKRVlsSEAEIK----EALASVGFnDERQKQAIGSLSGGWKMKLALARAMLFKADILLLDEPTNHL 601
Cdd:COG3842 90 phLTVAEnvaFGLRMRGV--PKAEIRarvaELLELVGL-EGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDEPLSAL 166
|
170 180 190
....*....|....*....|....*....|
gi 1933195014 602 DV---VNV-AWLENYLTSLKTcTSIIVSHD 627
Cdd:COG3842 167 DAklrEEMrEELRRLQRELGI-TFIYVTHD 195
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
464-598 |
3.96e-10 |
|
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: 61.15 E-value: 3.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 464 AYGAKILLNTATLRLKRGHRYGLCGKNGTGKSTLMRAITnGQVEgfPSPDEVRtfYVEHDIDGSEADT------------ 531
Cdd:COG0410 12 GYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAIS-GLLP--PRSGSIR--FDGEDITGLPPHRiarlgigyvpeg 86
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1933195014 532 -------SVLQFILTDKRVLSSEAEIKEALASVgFN-----DERQKQAIGSLSGGWKMKLALARAMLFKADILLLDEPT 598
Cdd:COG0410 87 rrifpslTVEENLLLGAYARRDRAEVRADLERV-YElfprlKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPS 164
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
465-625 |
4.01e-10 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 62.05 E-value: 4.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 465 YGAKILLNTATLRLKRGHRYGLCGKNGTGKSTLMRAITN------GQVE--GFP-SPDEVRTF-Y------------VE- 521
Cdd:COG4152 11 FGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGilapdsGEVLwdGEPlDPEDRRRIgYlpeerglypkmkVGe 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 522 --------HDIDGSEAdtsvlqfiltdkrvlssEAEIKEALASVGFNDeRQKQAIGSLSGGWKMKLALARAMLFKADILL 593
Cdd:COG4152 91 qlvylarlKGLSKAEA-----------------KRRADEWLERLGLGD-RANKKVEELSKGNQQKVQLIAALLHDPELLI 152
|
170 180 190
....*....|....*....|....*....|...
gi 1933195014 594 LDEPTNHLDVVNVAWLENYLTSLK-TCTSIIVS 625
Cdd:COG4152 153 LDEPFSGLDPVNVELLKDVIRELAaKGTTVIFS 185
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
465-627 |
4.21e-10 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 61.62 E-value: 4.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 465 YGAKILLNTATLRLKRGHRYGLCGKNGTGKSTLMR------AITNGQVEGFPSP-DEVRtfyvehdidgseaDTSVLQF- 536
Cdd:PRK11247 22 YGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRllagleTPSAGELLAGTAPlAEAR-------------EDTRLMFq 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 537 ---ILTDKRVLSS---------EAEIKEALASVGFNDeRQKQAIGSLSGGWKMKLALARAMLFKADILLLDEPTNHLD-- 602
Cdd:PRK11247 89 darLLPWKKVIDNvglglkgqwRDAALQALAAVGLAD-RANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDal 167
|
170 180 190
....*....|....*....|....*....|..
gi 1933195014 603 -------VVNVAWLENYLTSLktctsiIVSHD 627
Cdd:PRK11247 168 triemqdLIESLWQQHGFTVL------LVTHD 193
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
693-995 |
5.63e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 61.55 E-value: 5.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 693 KSLLKMRKVGFQYPTQAVQQLYDITLQVSLSSRVAILGPNGSGKSTLVKLLIGDMEPNKGgeiwkhpNLVIgyvaqhafh 772
Cdd:PRK13632 5 SVMIKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSG-------EIKI--------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 773 hidhhldktpleymlwryqtgeDLEEMSKANrqiteaeaqkmkegalivvegqkrlIEEIitRKKL--------KQ---- 840
Cdd:PRK13632 69 ----------------------DGITISKEN-------------------------LKEI--RKKIgiifqnpdNQfiga 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 841 SYEYEVSFkGLsssENIWLPRDELvkrgfeKKVIEvdtREAQRLGLLRPLVRreiekhfadfglEPEFvshntmrgLSGG 920
Cdd:PRK13632 100 TVEDDIAF-GL---ENKKVPPKKM------KDIID---DLAKKVGMEDYLDK------------EPQN--------LSGG 146
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 921 QKVKIVLGAATWRRPHVICLDEPTNYLD---RESLAALIAALKVFEGGVLI-ITHNRDfsES-LCHEVWAMRDGRLEASG 995
Cdd:PRK13632 147 QKQRVAIASVLALNPEIIIFDESTSMLDpkgKREIKKIMVDLRKTRKKTLIsITHDMD--EAiLADKVIVFSEGKLIAQG 224
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
600-1032 |
5.69e-10 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 63.89 E-value: 5.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 600 HLDVVNVAWLENYLTSLKTCTSIIVSH------DSGFLNNTITDVLH---LNRFKLRRYRGNLESFVKAVPEAKSYYSLe 670
Cdd:PTZ00265 283 HIGMINGFILASYAFGFWYGTRIIISDlsnqqpNNDFHGGSVISILLgvlISMFMLTIILPNITEYMKSLEATNSLYEI- 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 671 aledykfkLPDPPLLE----GVKTKEKSLLKMRKVGFQYPTQAVQQLY-DITLQVSLSSRVAILGPNGSGKSTLVKLLIG 745
Cdd:PTZ00265 362 --------INRKPLVEnnddGKKLKDIKKIQFKNVRFHYDTRKDVEIYkDLNFTLTEGKTYAFVGESGCGKSTILKLIER 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 746 DMEPNKGGEI------WKHPNLV-----IGYVAQHAFhhIDHHLDKTPLEYMLWRYQTGEDLEEMSKANRQITEAEAQKM 814
Cdd:PTZ00265 434 LYDPTEGDIIindshnLKDINLKwwrskIGVVSQDPL--LFSNSIKNNIKYSLYSLKDLEALSNYYNEDGNDSQENKNKR 511
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 815 KEGALIVVEGQKRLIEEIITRKKLKQSYEYEVsfkgLSSSENIwlprdelvkrGFEKKVievdtreaqrlgLLRPLVRRE 894
Cdd:PTZ00265 512 NSCRAKCAGDLNDMSNTTDSNELIEMRKNYQT----IKDSEVV----------DVSKKV------------LIHDFVSAL 565
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 895 IEKHfadfglePEFVSHNTMRgLSGGQKVKIVLGAATWRRPHVICLDEPTNYLDRES---LAALIAALKVFEGGVLIITH 971
Cdd:PTZ00265 566 PDKY-------ETLVGSNASK-LSGGQKQRISIARAIIRNPKILILDEATSSLDNKSeylVQKTINNLKGNENRITIIIA 637
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1933195014 972 NRDFSESLCHEVWAMRDgrLEASGHNWVEGQGSGPRIDKKDGEDEDQYDAMGNKVDNKKTK 1032
Cdd:PTZ00265 638 HRLSTIRYANTIFVLSN--RERGSTVDVDIIGEDPTKDNKENNNKNNKDDNNNNNNNNNNK 696
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
462-627 |
6.00e-10 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 61.34 E-value: 6.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 462 SLAYGAKILLNTATLRLKRGHRYGLCGKNGTGKSTLMRAI--TNGQVEGFPSpdEVRTFYVEHDIDGSEAD--------- 530
Cdd:PRK14243 17 NVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFnrLNDLIPGFRV--EGKVTFHGKNLYAPDVDpvevrrrig 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 531 ----------TSVLQFILTDKRVLSSEAEIKE----ALASVGFNDE---RQKQAIGSLSGGWKMKLALARAMLFKADILL 593
Cdd:PRK14243 95 mvfqkpnpfpKSIYDNIAYGARINGYKGDMDElverSLRQAALWDEvkdKLKQSGLSLSGGQQQRLCIARAIAVQPEVIL 174
|
170 180 190
....*....|....*....|....*....|....*
gi 1933195014 594 LDEPTNHLDVVNVAWLENYLTSLK-TCTSIIVSHD 627
Cdd:PRK14243 175 MDEPCSALDPISTLRIEELMHELKeQYTIIIVTHN 209
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
699-995 |
6.77e-10 |
|
type I secretion system ATPase, LssB 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. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 63.35 E-value: 6.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 699 RKVGFQYPTQAVQQLYDITLQVSLSSRVAILGPNGSGKSTLVKLLIGDMEPNKG---------GEIwkHPNLV---IGYV 766
Cdd:TIGR03375 467 RNVSFAYPGQETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGsvlldgvdiRQI--DPADLrrnIGYV 544
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 767 AQhafhhiDHHLdktpleymlwryqtgedleemskanrqiteaeaqkmkegalivvegqkrlieeiitrkklkqsyeyev 846
Cdd:TIGR03375 545 PQ------DPRL-------------------------------------------------------------------- 550
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 847 sFKGlSSSENIwlprdELVKRGFEKKVIevdTREAQRLGLLRpLVRReiekHFADFGLepefvshntM-----RGLSGGQ 921
Cdd:TIGR03375 551 -FYG-TLRDNI-----ALGAPYADDEEI---LRAAELAGVTE-FVRR----HPDGLDM---------QigergRSLSGGQ 606
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1933195014 922 KVKIVLGAATWRRPHVICLDEPTNYLDRESLAALIAALKVFEGG--VLIITHNRDFSEsLCHEVWAMRDGRLEASG 995
Cdd:TIGR03375 607 RQAVALARALLRDPPILLLDEPTSAMDNRSEERFKDRLKRWLAGktLVLVTHRTSLLD-LVDRIIVMDNGRIVADG 681
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
466-602 |
7.38e-10 |
|
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: 60.66 E-value: 7.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 466 GAKILLNTATLRLKRGHRYGLCGKNGTGKSTLMRAI------TNGQVEGFpspDEVRTFYVEHDIDGSEADT-------- 531
Cdd:cd03256 12 NGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLnglvepTSGSVLID---GTDINKLKGKALRQLRRQIgmifqqfn 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 532 -----SVLQFILTDK-------RVLS---SEAEIKEALA---SVGFNDERQKQAiGSLSGGWKMKLALARAMLFKADILL 593
Cdd:cd03256 89 lierlSVLENVLSGRlgrrstwRSLFglfPKEEKQRALAaleRVGLLDKAYQRA-DQLSGGQQQRVAIARALMQQPKLIL 167
|
....*....
gi 1933195014 594 LDEPTNHLD 602
Cdd:cd03256 168 ADEPVASLD 176
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
471-626 |
7.40e-10 |
|
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: 60.20 E-value: 7.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 471 LNTATLRLKRGHRYGLCGKNGTGKSTLMRAI------TNGQVEgfpspdevrtfyvehdIDGseADTSVLQ--------- 535
Cdd:cd03244 20 LKNISFSIKPGEKVGIVGRTGSGKSSLLLALfrlvelSSGSIL----------------IDG--VDISKIGlhdlrsris 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 536 FILTDKRVLS-------------SEAEIKEALASVGFNDERQKQAIG----------SLSGGWKMKLALARAMLFKADIL 592
Cdd:cd03244 82 IIPQDPVLFSgtirsnldpfgeySDEELWQALERVGLKEFVESLPGGldtvveeggeNLSVGQRQLLCLARALLRKSKIL 161
|
170 180 190
....*....|....*....|....*....|....*
gi 1933195014 593 LLDEPTNHLDVVNVAWLENYL-TSLKTCTSIIVSH 626
Cdd:cd03244 162 VLDEATASVDPETDALIQKTIrEAFKDCTVLTIAH 196
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
465-630 |
8.75e-10 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 60.49 E-value: 8.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 465 YGAKILLNTATLRLKRGHRYGLCGKNGTGKSTLMRAI------TNGQ--VEGFPSPDEVRTfyvEHDIDgSEADTSVLQF 536
Cdd:PRK09493 11 FGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCInkleeiTSGDliVDGLKVNDPKVD---ERLIR-QEAGMVFQQF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 537 IL--------------TDKRVLS---SEAEIKEALASVGFnDERQKQAIGSLSGGWKMKLALARAMLFKADILLLDEPTN 599
Cdd:PRK09493 87 YLfphltalenvmfgpLRVRGASkeeAEKQARELLAKVGL-AERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTS 165
|
170 180 190
....*....|....*....|....*....|....*....
gi 1933195014 600 HLD------VVNVawlenyLTSLKT--CTSIIVSHDSGF 630
Cdd:PRK09493 166 ALDpelrheVLKV------MQDLAEegMTMVIVTHEIGF 198
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
478-627 |
8.76e-10 |
|
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: 62.49 E-value: 8.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 478 LKRGHRYGLCGKNGTGKSTLMRaITNGQVEgfpsPDEVRTF----------YVEHDIDGSEADtsVLQFILTDkRVLSS- 546
Cdd:COG1245 363 IREGEVLGIVGPNGIGKTTFAK-ILAGVLK----PDEGEVDedlkisykpqYISPDYDGTVEE--FLRSANTD-DFGSSy 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 547 -EAEIKEALasvGFNDERQKQaIGSLSGGWKMKLALARAMLFKADILLLDEPTNHLDV---VNVAWLENYLTSLKTCTSI 622
Cdd:COG1245 435 yKTEIIKPL---GLEKLLDKN-VKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVeqrLAVAKAIRRFAENRGKTAM 510
|
....*
gi 1933195014 623 IVSHD 627
Cdd:COG1245 511 VVDHD 515
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
688-995 |
9.71e-10 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 60.04 E-value: 9.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 688 VKTKEKSLLKMRKVGFQYPTQAVQQLYDITLQVSLSSRVAILGPNGSGKSTLVKLLIGDMEPNkGGEIwkhpnLVIGYVA 767
Cdd:cd03267 12 VYSKEPGLIGSLKSLFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPT-SGEV-----RVAGLVP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 768 qhafhhidhhldktpleymlWryqtgedlEEMSKANRQITeaeaqkmkegaliVVEGQKrlieeiitrkklkqsyeyevs 847
Cdd:cd03267 86 --------------------W--------KRRKKFLRRIG-------------VVFGQK--------------------- 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 848 fkglssSENIW-LPrdelVKRGFE--KKVIEVDTREAQRlgllrplvRREiekHFADFgLEPEFVSHNTMRGLSGGQKVK 924
Cdd:cd03267 104 ------TQLWWdLP----VIDSFYllAAIYDLPPARFKK--------RLD---ELSEL-LDLEELLDTPVRQLSLGQRMR 161
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1933195014 925 IVLGAATWRRPHVICLDEPTNYLDRESLAALIAALKVF----EGGVLIITHNRDFSESLCHEVWAMRDGRLEASG 995
Cdd:cd03267 162 AEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYnrerGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
917-991 |
1.20e-09 |
|
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: 58.38 E-value: 1.20e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1933195014 917 LSGGQKVKIVLGAATWRRPHVICLDEPTNYLDRE---SLAALIAALKVFEGGVLIITHNRDFSESlCHEVWAMRDGRL 991
Cdd:cd03246 97 LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEgerALNQAIAALKAAGATRIVIAHRPETLAS-ADRILVLEDGRV 173
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
460-627 |
1.23e-09 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 61.32 E-value: 1.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 460 QFSLAYGAKILLNTATLRLKRGHRYGLCGKNGTGKSTLMRAITngqveGFPSPDEVRTFyvehdIDGSEADTS------- 532
Cdd:COG1118 7 NISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIA-----GLETPDSGRIV-----LNGRDLFTNlpprerr 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 533 ---VLQ---------------FILTDKRVlsSEAEIK----EALASV---GFNDERQKQaigsLSGGWKMKLALARAMLF 587
Cdd:COG1118 77 vgfVFQhyalfphmtvaeniaFGLRVRPP--SKAEIRarveELLELVqleGLADRYPSQ----LSGGQRQRVALARALAV 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1933195014 588 KADILLLDEPTNHLDvVNVA-----WLENYLTSLKtCTSIIVSHD 627
Cdd:COG1118 151 EPEVLLLDEPFGALD-AKVRkelrrWLRRLHDELG-GTTVFVTHD 193
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
464-627 |
1.47e-09 |
|
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: 60.20 E-value: 1.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 464 AYGAKILLNTATLRLKRGHRYGLCGKNGTGKSTLMRAI------TNGQV--EGFP----SPDEVRTF-----YVEHDIDG 526
Cdd:TIGR02769 20 AKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLlglekpAQGTVsfRGQDlyqlDRKQRRAFrrdvqLVFQDSPS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 527 S-EADTSVLQFI------LTDKRVLSSEAEIKEALASVGFNDERQKQAIGSLSGGWKMKLALARAMLFKADILLLDEPTN 599
Cdd:TIGR02769 100 AvNPRMTVRQIIgeplrhLTSLDESEQKARIAELLDMVGLRSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVS 179
|
170 180 190
....*....|....*....|....*....|.
gi 1933195014 600 HLDVVNVAWLENYLTSLKTCTSI---IVSHD 627
Cdd:TIGR02769 180 NLDMVLQAVILELLRKLQQAFGTaylFITHD 210
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
712-995 |
1.94e-09 |
|
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: 59.27 E-value: 1.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 712 QLYDITLQVSLSSRVAILGPNGSGKSTLVKLLIGDMEPNKGgeiwkhpnlvigyvaqhafhhidhhldKTPLEymlwryq 791
Cdd:cd03299 14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSG---------------------------KILLN------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 792 tGEDLEEMSKANRQITeaeaqkmkegalIVvegqkrlieeiitrkklkqsYEYEVSFKGLSSSENIWLprdELVKRGFEK 871
Cdd:cd03299 60 -GKDITNLPPEKRDIS------------YV--------------------PQNYALFPHMTVYKNIAY---GLKKRKVDK 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 872 KVIEVDTRE-AQRLGLLRPLVRREiekhfadfglepefvshntmRGLSGGQKVKIVLGAATWRRPHVICLDEPTNYLDRE 950
Cdd:cd03299 104 KEIERKVLEiAEMLGIDHLLNRKP--------------------ETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVR 163
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1933195014 951 SLAALIAALKV----FEGGVLIITHnrDFSE--SLCHEVWAMRDGRLEASG 995
Cdd:cd03299 164 TKEKLREELKKirkeFGVTVLHVTH--DFEEawALADKVAIMLNGKLIQVG 212
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
471-627 |
2.16e-09 |
|
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: 59.02 E-value: 2.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 471 LNTATLRLKRGHRYGLCGKNGTGKSTLMRAI------TNGQV--EG----FPSPDEVRTFY---------VEHDIdgSEA 529
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLIsglaqpTSGGVilEGkqitEPGPDRMVVFQnysllpwltVRENI--ALA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 530 DTSVLQFILTDKRvlssEAEIKEALASVGFNDERQKQaIGSLSGGWKMKLALARAMLFKADILLLDEPTNHLDVVNVAWL 609
Cdd:TIGR01184 79 VDRVLPDLSKSER----RAIVEEHIALVGLTEAADKR-PGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNL 153
|
170 180
....*....|....*....|.
gi 1933195014 610 ENYLTSL---KTCTSIIVSHD 627
Cdd:TIGR01184 154 QEELMQIweeHRVTVLMVTHD 174
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
709-995 |
2.28e-09 |
|
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: 58.45 E-value: 2.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 709 AVQQLYDITLQVSLSSRVAILGPNGSGKSTLVKLLIGDMEPNKGGEIWK-HPnlvIGYVAQHAFHHIdhhldktPLEYML 787
Cdd:cd03269 12 RVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDgKP---LDIAARNRIGYL-------PEERGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 788 WRyqtgedleemskanrqiteaeaqKMKegalivvegqkrLIEEIItrkklkqsyeYEVSFKGLSSSEniwlprdelvkr 867
Cdd:cd03269 82 YP-----------------------KMK------------VIDQLV----------YLAQLKGLKKEE------------ 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 868 gfekkvievdtreaqrlgllrplVRREIEKHFADFGLEPEfvSHNTMRGLSGGQKVKIVLGAATWRRPHVICLDEPTNYL 947
Cdd:cd03269 105 -----------------------ARRRIDEWLERLELSEY--ANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGL 159
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1933195014 948 D---RESLAALIAALKVFEGGVLIITHNRDFSESLCHEVWAMRDGRLEASG 995
Cdd:cd03269 160 DpvnVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
466-603 |
2.91e-09 |
|
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ATP-binding protein components is found as a three gene cassette along with a periplasmic substrate-binding protein (TIGR03868) and a permease (TIGR03869). The organisms containing this cassette are all Actinobacteria and all contain numerous genes requiring the coenzyme F420. This model was defined based on five such organisms, four of which are lacking all F420 biosynthetic capability save the final side-chain polyglutamate attachment step (via the gene cofE: TIGR01916). In Jonesia denitrificans DSM 20603 and marine actinobacterium PHSC20C1 this cassette is in an apparent operon with the cofE gene and, in PHSC20C1, also with a F420-dependent glucose-6-phosphate dehydrogenase (TIGR03554). Based on these observations we propose that this ATP-binding protein is a component of an F420-0 (that is, F420 lacking only the polyglutamate tail) transporter.
Pssm-ID: 163585 [Multi-domain] Cd Length: 256 Bit Score: 59.06 E-value: 2.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 466 GAKILLNTATLRLKRGHRYGLCGKNGTGKSTLMRAITN--GQVEGFPSPD--EVRTF----------YVEHDIDgSEADT 531
Cdd:TIGR03873 12 GGRLIVDGVDVTAPPGSLTGLLGPNGSGKSTLLRLLAGalRPDAGTVDLAgvDLHGLsrrararrvaLVEQDSD-TAVPL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 532 SVLQFIL---TDKRVL-----SSEAEI-KEALASVGFNDERQKqAIGSLSGGWKMKLALARAMLFKADILLLDEPTNHLD 602
Cdd:TIGR03873 91 TVRDVVAlgrIPHRSLwagdsPHDAAVvDRALARTELSHLADR-DMSTLSGGERQRVHVARALAQEPKLLLLDEPTNHLD 169
|
.
gi 1933195014 603 V 603
Cdd:TIGR03873 170 V 170
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
478-627 |
3.01e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 60.98 E-value: 3.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 478 LKRGHRYGLCGKNGTGKSTLMRAITnGQVEgfpsPDEVRTF----------YVEHDIDGSeadtsVLQFILTDKRVLSS- 546
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLA-GVLK----PDEGEVDpelkisykpqYIKPDYDGT-----VEDLLRSITDDLGSs 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 547 --EAEIKEALasvGFNDERQKQaIGSLSGGWKMKLALARAMLFKADILLLDEPTNHLDV---VNVAWLENYLTSLKTCTS 621
Cdd:PRK13409 432 yyKSEIIKPL---QLERLLDKN-VKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVeqrLAVAKAIRRIAEEREATA 507
|
....*.
gi 1933195014 622 IIVSHD 627
Cdd:PRK13409 508 LVVDHD 513
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
713-989 |
3.12e-09 |
|
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: 58.04 E-value: 3.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 713 LYDITLQVSLSSRVAILGPNGSGKSTLVKLLIGDMEPNKGGEIWKHPNL-------VIGYVAQHAfhhidhhldktpley 785
Cdd:cd03226 16 LDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIkakerrkSIGYVMQDV--------------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 786 mlwRYQTGED--LEEMSKANRQITEAEAQkmkegalivvegqkrlIEEIItrKKLKQSYEYEvsfkglssseniWLPRDe 863
Cdd:cd03226 81 ---DYQLFTDsvREELLLGLKELDAGNEQ----------------AETVL--KDLDLYALKE------------RHPLS- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 864 lvkrgfekkvievdtreaqrlgllrplvrreiekhfadfglepefvshntmrgLSGGQKVKIVLGAATWRRPHVICLDEP 943
Cdd:cd03226 127 -----------------------------------------------------LSGGQKQRLAIAAALLSGKDLLIFDEP 153
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1933195014 944 TNYLDR---ESLAALIAALKVFEGGVLIITHNRDFSESLCHEVWAMRDG 989
Cdd:cd03226 154 TSGLDYknmERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANG 202
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
460-641 |
3.91e-09 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 58.84 E-value: 3.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 460 QFSLAYGAKILLNTATLRLKRGHRYGLCGKNGTGKSTLMRAITN-------------GQVEGFPSPDEVRTFYVEHDIDG 526
Cdd:PRK10253 12 QLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRlmtpahghvwldgEHIQHYASKEVARRIGLLAQNAT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 527 SEADTSVLQFI---------LTDKRVLSSEAEIKEALASVGFNDeRQKQAIGSLSGGWKMKLALARAMLFKADILLLDEP 597
Cdd:PRK10253 92 TPGDITVQELVargryphqpLFTRWRKEDEEAVTKAMQATGITH-LADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEP 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1933195014 598 TNHLDV---VNVAWLENYLTSLKTCTSIIVSHDsgfLNNTITDVLHL 641
Cdd:PRK10253 171 TTWLDIshqIDLLELLSELNREKGYTLAAVLHD---LNQACRYASHL 214
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
701-993 |
3.93e-09 |
|
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: 58.66 E-value: 3.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 701 VGFQYPTQAVQQLYDITLQVSLSSRVAILGPNGSGKSTLVKLLIGdMEPNKGGEIWkhpnlvigyvaqhafhhidhhLDK 780
Cdd:COG1124 9 VSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAG-LERPWSGEVT---------------------FDG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 781 TPLEYMLWRyqtgedleemsKANRQIteaeaqKMkegalivvegqkrlieeiitrkkLKQSYEyevsfkglsSSENiwlP 860
Cdd:COG1124 67 RPVTRRRRK-----------AFRRRV------QM-----------------------VFQDPY---------ASLH---P 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 861 RdelvkrgfeKKVIEVdTREAQRLgLLRPLVRREIEKHFADFGLEPEFVsHNTMRGLSGGQKVKIVLGAATWRRPHVICL 940
Cdd:COG1124 95 R---------HTVDRI-LAEPLRI-HGLPDREERIAELLEQVGLPPSFL-DRYPHQLSGGQRQRVAIARALILEPELLLL 162
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1933195014 941 DEPTNYLD---RESLAALIAALKVFEG-GVLIITHNRDFSESLCHEVWAMRDGRLEA 993
Cdd:COG1124 163 DEPTSALDvsvQAEILNLLKDLREERGlTYLFVSHDLAVVAHLCDRVAVMQNGRIVE 219
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
726-1002 |
4.11e-09 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 58.54 E-value: 4.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 726 VAILGPNGSGKSTLVKLLIGDmePN---KGGEIwkhpnlvigyvaqhafhhidhHLDktpleymlwryqtGEDLEEMSka 802
Cdd:COG0396 29 HAIMGPNGSGKSTLAKVLMGH--PKyevTSGSI---------------------LLD-------------GEDILELS-- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 803 nrqiteaeaqkmkegalivvegqkrlIEEIItRKKLKQSYEYEVSFKGLSSSEniwLPRDELVKRGFEkkviEVDTREAq 882
Cdd:COG0396 71 --------------------------PDERA-RAGIFLAFQYPVEIPGVSVSN---FLRTALNARRGE----ELSAREF- 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 883 rlgllrplvRREIEKHFADFGLEPEFVSHNTMRGLSGGQKVKI-VLGAATwRRPHVICLDEPTNYLDRESL---AALIAA 958
Cdd:COG0396 116 ---------LKLLKEKMKELGLDEDFLDRYVNEGFSGGEKKRNeILQMLL-LEPKLAILDETDSGLDIDALrivAEGVNK 185
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1933195014 959 LKVFEGGVLIITHNR---DFSEslCHEVWAMRDGR------------LEASGHNWVEGQ 1002
Cdd:COG0396 186 LRSPDRGILIITHYQrilDYIK--PDFVHVLVDGRivksggkelaleLEEEGYDWLKEE 242
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
466-626 |
4.14e-09 |
|
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: 58.71 E-value: 4.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 466 GAKILLNTATLRLKRGHRYGLCGKNGTGKSTLMRAItngqvegfpspdeVRTFYVEHDI--DGSEADTSVLQ-------- 535
Cdd:cd03289 15 GGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAF-------------LRLLNTEGDIqiDGVSWNSVPLQkwrkafgv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 536 -----FILT-------DKRVLSSEAEIKEALASVG-------FNDERQKQAIGS---LSGGWKMKLALARAMLFKADILL 593
Cdd:cd03289 82 ipqkvFIFSgtfrknlDPYGKWSDEEIWKVAEEVGlksvieqFPGQLDFVLVDGgcvLSHGHKQLMCLARSVLSKAKILL 161
|
170 180 190
....*....|....*....|....*....|....
gi 1933195014 594 LDEPTNHLDVVNVAWLENYLT-SLKTCTSIIVSH 626
Cdd:cd03289 162 LDEPSAHLDPITYQVIRKTLKqAFADCTVILSEH 195
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
466-625 |
4.18e-09 |
|
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: 57.56 E-value: 4.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 466 GAKILLNTATLRLKRGHRYGLCGKNGTGKSTLMRAITN--------GQV--EGFPSPDEV---RTFYV-EHDIdgseadt 531
Cdd:cd03213 20 SGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrrtglgvsGEVliNGRPLDKRSfrkIIGYVpQDDI------- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 532 sVLQFiLTDKRVLSSEAEIKealasvgfnderqkqaigSLSGGWKMKLALARAMLFKADILLLDEPTNHLDVVNVAWLEN 611
Cdd:cd03213 93 -LHPT-LTVRETLMFAAKLR------------------GLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMS 152
|
170
....*....|....*
gi 1933195014 612 YLTSL-KTCTSIIVS 625
Cdd:cd03213 153 LLRRLaDTGRTIICS 167
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
471-602 |
4.56e-09 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 60.22 E-value: 4.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 471 LNTATLRLKRGHRYGLCGKNGTGKSTLMRAITNgqvEGFPSPDEVRtfyvehdIDG------SEAD----TSVL-QFI-- 537
Cdd:PRK11160 356 LKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTR---AWDPQQGEIL-------LNGqpiadySEAAlrqaISVVsQRVhl 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 538 ----LTDKRVL----SSEAEIKEALASVGF-----NDERQKQAIGS----LSGGWKMKLALARAMLFKADILLLDEPTNH 600
Cdd:PRK11160 426 fsatLRDNLLLaapnASDEALIEVLQQVGLeklleDDKGLNAWLGEggrqLSGGEQRRLGIARALLHDAPLLLLDEPTEG 505
|
..
gi 1933195014 601 LD 602
Cdd:PRK11160 506 LD 507
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
696-997 |
4.96e-09 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 57.75 E-value: 4.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 696 LKMRKVGFQYPTQaVQQLYDITLQVSLSSRVAILGPNGSGKSTLVKLLIGDMEPNKgGEIWkhpnlvigyVAqhafhhid 775
Cdd:COG2884 2 IRFENVSKRYPGG-REALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTS-GQVL---------VN-------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 776 hhldktpleymlwryqtGEDLEEMSKAN-----RQIteaeaqkmkeGalIVVEGQkRLIEEiitrkklkqsyeyevsfkg 850
Cdd:COG2884 63 -----------------GQDLSRLKRREipylrRRI----------G--VVFQDF-RLLPD------------------- 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 851 LSSSENIWLPrdeLVKRGFEKKVIEVDTREA-QRLGLLrplvrreiekHFADfglepEFVSHntmrgLSGGQKVKIVLGA 929
Cdd:COG2884 94 RTVYENVALP---LRVTGKSRKEIRRRVREVlDLVGLS----------DKAK-----ALPHE-----LSGGEQQRVAIAR 150
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1933195014 930 ATWRRPHVICLDEPTNYLDRESLAALIAALKVF-EGG--VLIITHNRDFSESLCHEVWAMRDGRLEASGHN 997
Cdd:COG2884 151 ALVNRPELLLADEPTGNLDPETSWEIMELLEEInRRGttVLIATHDLELVDRMPKRVLELEDGRLVRDEAR 221
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
461-626 |
5.96e-09 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 58.12 E-value: 5.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 461 FSLAYGAKILLNTATLRLKRGHRYGLCGKNGTGKSTLMRA-------ITNGQVEGfpspdEVRtfYVEHDIDGSEADTSV 533
Cdd:COG1117 17 LNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRClnrmndlIPGARVEG-----EIL--LDGEDIYDPDVDVVE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 534 L--------Q----F---I------------LTDKRVLsseAEI-KEALASVGFNDE---RQKQAIGSLSGGWKMKLALA 582
Cdd:COG1117 90 LrrrvgmvfQkpnpFpksIydnvayglrlhgIKSKSEL---DEIvEESLRKAALWDEvkdRLKKSALGLSGGQQQRLCIA 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1933195014 583 RAMLFKADILLLDEPTNHLDVVNVAWLENYLTSLKT-CTSIIVSH 626
Cdd:COG1117 167 RALAVEPEVLLMDEPTSALDPISTAKIEELILELKKdYTIVIVTH 211
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
471-626 |
6.11e-09 |
|
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: 57.63 E-value: 6.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 471 LNTATLRLKRGHRYGLCGKNGTGKSTLMRAITNgqvegFPSPDEVRTFYVEHDIDGSEADT------SVLQ--FILTDK- 541
Cdd:cd03251 18 LRDISLDIPAGETVALVGPSGSGKSTLVNLIPR-----FYDVDSGRILIDGHDVRDYTLASlrrqigLVSQdvFLFNDTv 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 542 -------RVLSSEAEIKEALASVGFND------ERQKQAIGS----LSGGWKMKLALARAMLFKADILLLDEPTNHLDVV 604
Cdd:cd03251 93 aeniaygRPGATREEVEEAARAANAHEfimelpEGYDTVIGErgvkLSGGQRQRIAIARALLKDPPILILDEATSALDTE 172
|
170 180
....*....|....*....|...
gi 1933195014 605 NVAWLENYLTSL-KTCTSIIVSH 626
Cdd:cd03251 173 SERLVQAALERLmKNRTTFVIAH 195
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
471-654 |
6.47e-09 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 57.78 E-value: 6.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 471 LNTATLRLKRGHRYGLCGKNGTGKSTLMRAI------TNGQVEgfpspdevrtfyvehdIDGSEA-----------DTSV 533
Cdd:COG1134 42 LKDVSFEVERGESVGIIGRNGAGKSTLLKLIagilepTSGRVE----------------VNGRVSallelgagfhpELTG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 534 LQFILTDKRVLS-SEAEIKEALASV-------GFNDerqkQAIGSLSGGWKMKLALARAMLFKADILLLDEptnhldVVN 605
Cdd:COG1134 106 RENIYLNGRLLGlSRKEIDEKFDEIvefaelgDFID----QPVKTYSSGMRARLAFAVATAVDPDILLVDE------VLA 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1933195014 606 V----------AWLENYLTSlkTCTSIIVSHDSGFLNNTITDVLHLNRFKLRRYrGNLE 654
Cdd:COG1134 176 VgdaafqkkclARIRELRES--GRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMD-GDPE 231
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
464-630 |
8.81e-09 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 57.31 E-value: 8.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 464 AYGAKILLNTATLRLKRGHRYGLCGKNGTGKSTLMRAItNGQVEgfpsPDEVRTFYVEHDIDGSEADT------------ 531
Cdd:COG1126 10 SFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCI-NLLEE----PDSGTITVDGEDLTDSKKDInklrrkvgmvfq 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 532 --------SVLQFI-LTDKRVL---SSEAEIK--EALASVGFNDERQKQAiGSLSGGWKMKLALARAMLFKADILLLDEP 597
Cdd:COG1126 85 qfnlfphlTVLENVtLAPIKVKkmsKAEAEERamELLERVGLADKADAYP-AQLSGGQQQRVAIARALAMEPKVMLFDEP 163
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1933195014 598 TNHLD------VVNVawlenyLTSLKT--CTSIIVSHDSGF 630
Cdd:COG1126 164 TSALDpelvgeVLDV------MRDLAKegMTMVVVTHEMGF 198
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
471-627 |
8.82e-09 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 56.98 E-value: 8.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 471 LNTATLRLKRGHRYGLCGKNGTGKSTLMRAI------TNGQVegfpspdevrtfYVE-HDIDG-SEADTS---------V 533
Cdd:COG1136 24 LRGVSLSIEAGEFVAIVGPSGSGKSTLLNILggldrpTSGEV------------LIDgQDISSlSERELArlrrrhigfV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 534 LQF-----------------ILTDKRVLSSEAEIKEALASVGFnDERQKQAIGSLSGGWKMKLALARAMLFKADILLLDE 596
Cdd:COG1136 92 FQFfnllpeltalenvalplLLAGVSRKERRERARELLERVGL-GDRLDHRPSQLSGGQQQRVAIARALVNRPKLILADE 170
|
170 180 190
....*....|....*....|....*....|....
gi 1933195014 597 PTNHLDVVNVAWLENYLTSLKT---CTSIIVSHD 627
Cdd:COG1136 171 PTGNLDSKTGEEVLELLRELNRelgTTIVMVTHD 204
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
468-626 |
1.03e-08 |
|
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: 55.62 E-value: 1.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 468 KILLNTATLRLKRGHRYGLCGKNGTGKSTLMRAI------TNGQVEgfpSPDEVRTFYVEHD---IDGSEADtsvlQFIL 538
Cdd:cd03223 14 RVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALaglwpwGSGRIG---MPEGEDLLFLPQRpylPLGTLRE----QLIY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 539 TDKRVLSSeaeikealasvgfnDERQkqaigslsggwkmKLALARAMLFKADILLLDEPTNHLDVVNVAWLENYLTSLKT 618
Cdd:cd03223 87 PWDDVLSG--------------GEQQ-------------RLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKELGI 139
|
....*...
gi 1933195014 619 cTSIIVSH 626
Cdd:cd03223 140 -TVISVGH 146
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
462-597 |
1.18e-08 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 56.69 E-value: 1.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 462 SLAYGAKILlnTATLRLKRGHRYGLCGKNGTGKSTLMRAITngqveGFPSPDEVRTFYVEHDIDGSEADT---------- 531
Cdd:COG3840 8 TYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIA-----GFLPPDSGRILWNGQDLTALPPAErpvsmlfqen 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1933195014 532 ------SVLQFI---LTDKRVLSSE--AEIKEALASVGFNDERQKQAiGSLSGGWKMKLALARAMLFKADILLLDEP 597
Cdd:COG3840 81 nlfphlTVAQNIglgLRPGLKLTAEqrAQVEQALERVGLAGLLDRLP-GQLSGGQRQRVALARCLVRKRPILLLDEP 156
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
695-756 |
1.42e-08 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 58.68 E-value: 1.42e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1933195014 695 LLKMRKVGFQYPTQAVQQLYDITLQVSLSSRVAILGPNGSGKSTLVKLLIGDMEPNKgGEIW 756
Cdd:PRK11160 338 SLTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQ-GEIL 398
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
682-995 |
1.43e-08 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 58.97 E-value: 1.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 682 PPLLEGVktkekslLKMRKVGFQYPTQA-VQQLYDITLQVSLSSRVAILGPNGSGKSTLVKLLIGDMEPNkGGEIwkhpn 760
Cdd:TIGR00958 472 PLNLEGL-------IEFQDVSFSYPNRPdVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPT-GGQV----- 538
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 761 LVIGY-VAQHAFHHIDHHLDKTPLEYMLWryqtgedleemskaNRQITE--AEAQKMKEGALIVVEGQKRLIEEIITrkK 837
Cdd:TIGR00958 539 LLDGVpLVQYDHHYLHRQVALVGQEPVLF--------------SGSVREniAYGLTDTPDEEIMAAAKAANAHDFIM--E 602
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 838 LKQSYEYEVSFKGLSsseniwlprdelvkrgfekkvievdtreaqrlgllrplvrreiekhfadfglepefvshntmrgL 917
Cdd:TIGR00958 603 FPNGYDTEVGEKGSQ----------------------------------------------------------------L 618
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1933195014 918 SGGQKVKIVLGAATWRRPHVICLDEPTNYLDRESLAALIAALKVFEGGVLIITHNRDFSESlCHEVWAMRDGRLEASG 995
Cdd:TIGR00958 619 SGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQESRSRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMG 695
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
465-627 |
1.43e-08 |
|
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: 56.58 E-value: 1.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 465 YGAKILLNTATLRLKRGHRYGLCGKNGTGKSTLMRAITngqveGFPSPDEVRTFYveHDIDGSEADTS------VLQ--- 535
Cdd:cd03296 12 FGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIA-----GLERPDSGTILF--GGEDATDVPVQernvgfVFQhya 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 536 ------------FILTDKRVLS--SEAEIKEALASV-------GFNDERQKQaigsLSGGWKMKLALARAMLFKADILLL 594
Cdd:cd03296 85 lfrhmtvfdnvaFGLRVKPRSErpPEAEIRAKVHELlklvqldWLADRYPAQ----LSGGQRQRVALARALAVEPKVLLL 160
|
170 180 190
....*....|....*....|....*....|....*.
gi 1933195014 595 DEPTNHLDVVNVAWLENYLTSLK---TCTSIIVSHD 627
Cdd:cd03296 161 DEPFGALDAKVRKELRRWLRRLHdelHVTTVFVTHD 196
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
465-646 |
1.89e-08 |
|
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: 55.88 E-value: 1.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 465 YGAKIL-LNTATLRLKRGHRYGLCGKNGTGKSTLMRAI------TNGQVE--GFPSPD--EVRTFYVEHDI--------- 524
Cdd:cd03292 10 YPNGTAaLDGINISISAGEFVFLVGPSGAGKSTLLKLIykeelpTSGTIRvnGQDVSDlrGRAIPYLRRKIgvvfqdfrl 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 525 --DGSEADTSVLQFILTDKRVLSSEAEIKEALASVGFNDERQKQAIGsLSGGWKMKLALARAMLFKADILLLDEPTNHLD 602
Cdd:cd03292 90 lpDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAE-LSGGEQQRVAIARAIVNSPTILIADEPTGNLD 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1933195014 603 VVNVAWLENYLTSL-KTCTSIIVS-HDSGFLNNTITDVLHLNRFKL 646
Cdd:cd03292 169 PDTTWEIMNLLKKInKAGTTVVVAtHAKELVDTTRHRVIALERGKL 214
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
475-627 |
1.93e-08 |
|
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: 55.97 E-value: 1.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 475 TLRLKRGHRYGLCGKNGTGKSTLMRAITngqveGFPSPDEVRTFYVEHDI--DGSEADTSV------------------L 534
Cdd:cd03263 22 SLNVYKGEIFGLLGHNGAGKTTTLKMLT-----GELRPTSGTAYINGYSIrtDRKAARQSLgycpqfdalfdeltvrehL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 535 QF--ILTDKRVLSSEAEIKEALASVGFNDERQKQAiGSLSGGWKMKLALARAMLFKADILLLDEPTNHLDVV--NVAWle 610
Cdd:cd03263 97 RFyaRLKGLPKSEIKEEVELLLRVLGLTDKANKRA-RTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPAsrRAIW-- 173
|
170
....*....|....*...
gi 1933195014 611 NYLTSLKTCTSII-VSHD 627
Cdd:cd03263 174 DLILEVRKGRSIIlTTHS 191
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
461-602 |
1.97e-08 |
|
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: 56.05 E-value: 1.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 461 FSLAYGAKILLNTATLRLKRGHRYGLCGKNGTGKSTLMRAI------TNGQVE--GFP----SPDEVRTFyvEHDIDgse 528
Cdd:cd03258 11 FGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCInglerpTSGSVLvdGTDltllSGKELRKA--RRRIG--- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 529 adtSVLQ-F-ILTDKRVL-----------SSEAEIKEA----LASVGFNDERQKQaIGSLSGGWKMKLALARAMLFKADI 591
Cdd:cd03258 86 ---MIFQhFnLLSSRTVFenvalpleiagVPKAEIEERvlelLELVGLEDKADAY-PAQLSGGQKQRVGIARALANNPKV 161
|
170
....*....|.
gi 1933195014 592 LLLDEPTNHLD 602
Cdd:cd03258 162 LLCDEATSALD 172
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
488-632 |
2.29e-08 |
|
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: 55.31 E-value: 2.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 488 GKNGTGKSTLMRAITNGqVEGFPSPDEVRTFYVEHDIDGSEADTSV-LQFILTDKRVLSSEAEIkEALASVGF--NDERQ 564
Cdd:cd03240 29 GQNGAGKTTIIEALKYA-LTGELPPNSKGGAHDPKLIREGEVRAQVkLAFENANGKKYTITRSL-AILENVIFchQGESN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 565 K---QAIGSLSGGWKMK------LALARAMLFKADILLLDEPTNHLDVVNVAW-LENYLTSLKTCTS---IIVSHDSGFL 631
Cdd:cd03240 107 WpllDMRGRCSGGEKVLasliirLALAETFGSNCGILALDEPTTNLDEENIEEsLAEIIEERKSQKNfqlIVITHDEELV 186
|
.
gi 1933195014 632 N 632
Cdd:cd03240 187 D 187
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
465-646 |
2.47e-08 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 56.13 E-value: 2.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 465 YGAKILLNTATLRLKRGHRYGLCGKNGTGKSTLMRAIT--NGQVEGFPSPDEVRTFYVEhDIDGS--EADTSVLQFILT- 539
Cdd:PRK10619 15 YGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINflEKPSEGSIVVNGQTINLVR-DKDGQlkVADKNQLRLLRTr 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 540 -----------------------DKRVLS-SEAEIKEA----LASVGFNDERQKQAIGSLSGGWKMKLALARAMLFKADI 591
Cdd:PRK10619 94 ltmvfqhfnlwshmtvlenvmeaPIQVLGlSKQEARERavkyLAKVGIDERAQGKYPVHLSGGQQQRVSIARALAMEPEV 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1933195014 592 LLLDEPTNHLDVVNVAWLENYLTSL--KTCTSIIVSHDSGFLNNTITDVLHLNRFKL 646
Cdd:PRK10619 174 LLFDEPTSALDPELVGEVLRIMQQLaeEGKTMVVVTHEMGFARHVSSHVIFLHQGKI 230
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
466-627 |
3.62e-08 |
|
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: 55.73 E-value: 3.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 466 GAKILLNTATLRLKRGHRYGLCGKNGTGKSTLMRAItNGQVEgfPSPDEVrtfyvehDIDG------SEADTS------- 532
Cdd:cd03294 35 GQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCI-NRLIE--PTSGKV-------LIDGqdiaamSRKELRelrrkki 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 533 --VLQ-FILTDKR-VLSSEA---EIK------------EALASVGFNDeRQKQAIGSLSGGWKMKLALARAMLFKADILL 593
Cdd:cd03294 105 smVFQsFALLPHRtVLENVAfglEVQgvpraereeraaEALELVGLEG-WEHKYPDELSGGMQQRVGLARALAVDPDILL 183
|
170 180 190
....*....|....*....|....*....|....*..
gi 1933195014 594 LDEPTNHLDVVNVAWLENYLTSLKTC---TSIIVSHD 627
Cdd:cd03294 184 MDEAFSALDPLIRREMQDELLRLQAElqkTIVFITHD 220
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
464-602 |
3.90e-08 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 56.88 E-value: 3.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 464 AYGAKILLNTATLRLKRGHRYGLCGKNGTGKSTLMRAITngqveGFPSPDEVRTFYVEHDIDGSEAD----TSVLQ---- 535
Cdd:PRK09452 23 SFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIA-----GFETPDSGRIMLDGQDITHVPAEnrhvNTVFQsyal 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 536 -----------FILTDKRVlsSEAEIK----EALASV---GFNDERQKQaigsLSGGWKMKLALARAMLFKADILLLDEP 597
Cdd:PRK09452 98 fphmtvfenvaFGLRMQKT--PAAEITprvmEALRMVqleEFAQRKPHQ----LSGGQQQRVAIARAVVNKPKVLLLDES 171
|
....*
gi 1933195014 598 TNHLD 602
Cdd:PRK09452 172 LSALD 176
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
465-617 |
4.01e-08 |
|
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: 55.24 E-value: 4.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 465 YGAKILLNTATLRLKRGHRYGLCGKNGTGKSTLMRAITngqveGFPSPDEVRTFYVEHDIDGS---------------EA 529
Cdd:cd03218 10 YGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIV-----GLVKPDSGKILLDGQDITKLpmhkrarlgigylpqEA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 530 ----DTSVLQFILTdkrVLS----SEAEIKEALASV--GFNDER-QKQAIGSLSGGWKMKLALARAMLFKADILLLDEPT 598
Cdd:cd03218 85 sifrKLTVEENILA---VLEirglSKKEREEKLEELleEFHITHlRKSKASSLSGGERRRVEIARALATNPKFLLLDEPF 161
|
170
....*....|....*....
gi 1933195014 599 NHLDVVNVAWLENYLTSLK 617
Cdd:cd03218 162 AGVDPIAVQDIQKIIKILK 180
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
466-641 |
4.03e-08 |
|
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: 54.46 E-value: 4.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 466 GAKILLNTATLRLKRGHRYGLCGKNGTGKSTLMRAITngqveGFPSPDEV--RTFYVEHDIDGSEADTSVLQFILtdkrv 543
Cdd:cd03217 11 GGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIM-----GHPKYEVTegEILFKGEDITDLPPEERARLGIF----- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 544 LS--SEAEI-----KEALASV--GFnderqkqaigslSGGWKMKLALARAMLFKADILLLDEPTNHLDVVNVAWLENYLT 614
Cdd:cd03217 81 LAfqYPPEIpgvknADFLRYVneGF------------SGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVIN 148
|
170 180
....*....|....*....|....*....
gi 1933195014 615 SLKT--CTSIIVSHDSGFLNNTITDVLHL 641
Cdd:cd03217 149 KLREegKSVLIITHYQRLLDYIKPDRVHV 177
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
651-995 |
4.33e-08 |
|
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: 56.97 E-value: 4.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 651 GNLESFVKAvpeAKSYYSL-EALEDYKFK-----LPDPpllEGVktkekslLKMRKVGFQYPTQAVQQLYDITLQVSLSS 724
Cdd:TIGR01842 279 GGWKQFSGA---RQAYKRLnELLANYPSRdpampLPEP---EGH-------LSVENVTIVPPGGKKPTLRGISFSLQAGE 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 725 RVAILGPNGSGKSTLVKLLIGDMEPNKG------GEI--WKHPNL--VIGYVAQhafhhidhhldktpleymlwryqtge 794
Cdd:TIGR01842 346 ALAIIGPSGSGKSTLARLIVGIWPPTSGsvrldgADLkqWDRETFgkHIGYLPQ-------------------------- 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 795 DLEEMS---KAN--RQITEAEAQKMKEGAliVVEGqkrlIEEIITRkkLKQSYEYEVSFKGlssseniwlprdelvkrgf 869
Cdd:TIGR01842 400 DVELFPgtvAENiaRFGENADPEKIIEAA--KLAG----VHELILR--LPDGYDTVIGPGG------------------- 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 870 ekkvievdtreaqrlgllrplvrreiekhfadfglepefvshntmRGLSGGQKVKIVLGAATWRRPHVICLDEPTNYLDR 949
Cdd:TIGR01842 453 ---------------------------------------------ATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDE 487
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1933195014 950 ESLAALIAA---LKVFEGGVLIITHnRDFSESLCHEVWAMRDGRLEASG 995
Cdd:TIGR01842 488 EGEQALANAikaLKARGITVVVITH-RPSLLGCVDKILVLQDGRIARFG 535
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
458-631 |
4.34e-08 |
|
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: 54.85 E-value: 4.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 458 NCQFSLAYGAKILLNTATLRLKRGHRYGLCGKNGTGKSTLMRAITngqveGFPSPDEvRTFYVEHDID-------GSEAD 530
Cdd:cd03220 25 ILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLA-----GIYPPDS-GTVTVRGRVSsllglggGFNPE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 531 TSVLQFI--------LTDKRVLSSEAEIKEaLASVGfndERQKQAIGSLSGGWKMKLALARAMLFKADILLLDEPtnhLD 602
Cdd:cd03220 99 LTGRENIylngrllgLSRKEIDEKIDEIIE-FSELG---DFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEV---LA 171
|
170 180 190
....*....|....*....|....*....|....
gi 1933195014 603 VVNVAWLE---NYLTSL--KTCTSIIVSHDSGFL 631
Cdd:cd03220 172 VGDAAFQEkcqRRLRELlkQGKTVILVSHDPSSI 205
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
460-646 |
4.37e-08 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 54.88 E-value: 4.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 460 QFSLAY-GAKILLNTATLRLKRGHRYGLCGKNGTGKSTLMRAITngqveGFPSPDEVRTFYVEHDIdgSEADTSVLQFI- 537
Cdd:PRK10908 6 HVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLIC-----GIERPSAGKIWFSGHDI--TRLKNREVPFLr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 538 ------------LTDKRVL-----------SSEAEIKE----ALASVGFNDERQKQAIgSLSGGWKMKLALARAMLFKAD 590
Cdd:PRK10908 79 rqigmifqdhhlLMDRTVYdnvaipliiagASGDDIRRrvsaALDKVGLLDKAKNFPI-QLSGGEQQRVGIARAVVNKPA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1933195014 591 ILLLDEPTNHLDvvnVAWLENYLTSLKT-----CTSIIVSHDSGFLNNTITDVLHLNRFKL 646
Cdd:PRK10908 158 VLLADEPTGNLD---DALSEGILRLFEEfnrvgVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
696-771 |
4.38e-08 |
|
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: 54.40 E-value: 4.38e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1933195014 696 LKMRKVGFQYP---TQAVQQLYDITLQVSLSSRVAILGPNGSGKSTLVKLLIGDMEPNKgGEIWKHPNlvIGYVAQHAF 771
Cdd:cd03250 1 ISVEDASFTWDsgeQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLS-GSVSVPGS--IAYVSQEPW 76
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
460-598 |
4.47e-08 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 55.27 E-value: 4.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 460 QFSLAYGAKILLNTATLRLKRGHRYGLCGKNGTGKSTLMraitnGQVEGFPSPDEVRTFYVEHDIDGSEADTSVLQ--FI 537
Cdd:PRK11614 10 KVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLL-----GTLCGDPRATSGRIVFDGKDITDWQTAKIMREavAI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 538 LTDKRVLSSEAEIKEALASVGFNDERQK--------------------QAIGSLSGGWKMKLALARAMLFKADILLLDEP 597
Cdd:PRK11614 85 VPEGRRVFSRMTVEENLAMGGFFAERDQfqerikwvyelfprlherriQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEP 164
|
.
gi 1933195014 598 T 598
Cdd:PRK11614 165 S 165
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
692-990 |
4.69e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 55.62 E-value: 4.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 692 EKSLLKMRKVGFQYPtQAVQQLYDITLQVSLSSRVAILGPNGSGKSTLVKLLIGDMEPNKGgEIWKhpnlvigyvaqhaf 771
Cdd:PRK13636 2 EDYILKVEELNYNYS-DGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSG-RILF-------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 772 hhidhhlDKTPLEYmlwryqTGEDLEEMSKANRQITEAEAQKMKEGALivvegqkrlieeiitrkklkqsYEyEVSFKGL 851
Cdd:PRK13636 66 -------DGKPIDY------SRKGLMKLRESVGMVFQDPDNQLFSASV----------------------YQ-DVSFGAV 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 852 ssseNIWLPRDELVKRgfekkvievdtreaqrlgllrplVRREIEKHfadfGLEPefVSHNTMRGLSGGQKVKIVLGAAT 931
Cdd:PRK13636 110 ----NLKLPEDEVRKR-----------------------VDNALKRT----GIEH--LKDKPTHCLSFGQKKRVAIAGVL 156
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1933195014 932 WRRPHVICLDEPTNYLD----RESLAALIAALKVFEGGVLIITHNRDFSESLCHEVWAMRDGR 990
Cdd:PRK13636 157 VMEPKVLVLDEPTAGLDpmgvSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGR 219
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
480-609 |
4.90e-08 |
|
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: 53.15 E-value: 4.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 480 RGHRYGLCGKNGTGKSTLMRAITNgqvegfpspdevrtfyvehdidgseadtsvlQFILTDKRVLSSEAEIKEALASVGF 559
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALAR-------------------------------ELGPPGGGVIYIDGEDILEEVLDQL 49
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1933195014 560 NDERQKQAIGSLSGGWKMKLALARAMLFKADILLLDEPTNHLDVVNVAWL 609
Cdd:smart00382 50 LLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALL 99
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
713-752 |
7.17e-08 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 54.78 E-value: 7.17e-08
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1933195014 713 LYDITLQVSLSSRVAILGPNGSGKSTLVKLLIGDMEPNKG 752
Cdd:PRK13548 18 LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSG 57
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
571-989 |
7.29e-08 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 56.25 E-value: 7.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 571 LSGGWKMKLALARAMLFKADILLLDEPTNHLDVVNVAWLENYLTSLK---TCTSIIVSHDsgfLNntITDVLHLNRFKLR 647
Cdd:PRK15134 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQqelNMGLLFITHN---LS--IVRKLADRVAVMQ 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 648 RYRGNLESFVKAVPEAKSY-YSLEAL----EDYKFKLP--DPPLLE----GVKTKEKSLLKMRKVGFQYptqAVQQLyDI 716
Cdd:PRK15134 232 NGRCVEQNRAATLFSAPTHpYTQKLLnsepSGDPVPLPepASPLLDveqlQVAFPIRKGILKRTVDHNV---VVKNI-SF 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 717 TLQVSLSsrVAILGPNGSGKST----LVKLLigdmepNKGGEIWkhpnlvigyvaqhafhhidhhLDKTPLEyMLWRYQt 792
Cdd:PRK15134 308 TLRPGET--LGLVGESGSGKSTtglaLLRLI------NSQGEIW---------------------FDGQPLH-NLNRRQ- 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 793 gedleeMSKANRQIteaeaqkmkegalivvegqkrlieeiitrkklkqsyeyEVSFKGLSSSENIWLPRDELVKRGFE-- 870
Cdd:PRK15134 357 ------LLPVRHRI--------------------------------------QVVFQDPNSSLNPRLNVLQIIEEGLRvh 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 871 KKVIEVDTREAQrlgllrplVRREIEkhfaDFGLEPEfVSHNTMRGLSGGQKVKIVLGAATWRRPHVICLDEPTNYLDRE 950
Cdd:PRK15134 393 QPTLSAAQREQQ--------VIAVME----EVGLDPE-TRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKT 459
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1933195014 951 SLAALIAALKVFEG----GVLIITHNRDFSESLCHEVWAMRDG 989
Cdd:PRK15134 460 VQAQILALLKSLQQkhqlAYLFISHDLHVVRALCHQVIVLRQG 502
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
460-627 |
7.32e-08 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 54.63 E-value: 7.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 460 QFSLAYGAKILLNTATLRLKRGHRYGLCGKNGTGKSTLMRAI------TNGQVE-------GFPSPDEVRTFYVEHDIDG 526
Cdd:PRK11231 7 NLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFarlltpQSGTVFlgdkpisMLSSRQLARRLALLPQHHL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 527 SEADTSVLQFI-------------LTDKrvlsSEAEIKEALASVGFnDERQKQAIGSLSGGWKMKLALARAMLFKADILL 593
Cdd:PRK11231 87 TPEGITVRELVaygrspwlslwgrLSAE----DNARVNQAMEQTRI-NHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVL 161
|
170 180 190
....*....|....*....|....*....|....*.
gi 1933195014 594 LDEPTNHLDVVNVAWLENYLTSLKTC--TSIIVSHD 627
Cdd:PRK11231 162 LDEPTTYLDINHQVELMRLMRELNTQgkTVVTVLHD 197
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
471-602 |
7.70e-08 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 55.02 E-value: 7.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 471 LNTATLRLKRGHRYGLCGKNGTGKSTLMRAITnGQVEGFPSPDE---------VRTFYVEHDIDGSEADTSVL--QFILT 539
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLS-GLITGDKSAGShiellgrtvQREGRLARDIRKSRANTGYIfqQFNLV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 540 DkRVLSSEAEIKEALASVGF---------NDERQK---------------QAIGSLSGGWKMKLALARAMLFKADILLLD 595
Cdd:PRK09984 99 N-RLSVLENVLIGALGSTPFwrtcfswftREQKQRalqaltrvgmvhfahQRVSTLSGGQQQRVAIARALMQQAKVILAD 177
|
....*..
gi 1933195014 596 EPTNHLD 602
Cdd:PRK09984 178 EPIASLD 184
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
462-602 |
8.00e-08 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 54.78 E-value: 8.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 462 SLAYGAKILLNTATLRLKRGHRYGLCGKNGTGKSTLMRAITngqveGFPSPDEVRTFYVEHDIDGSEADT---------- 531
Cdd:PRK13548 9 SVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALS-----GELSPDSGEVRLNGRPLADWSPAElarrravlpq 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 532 -SVLQFILTDKRVLS------------SEAEIKEALASVGFND--ERQKQAigsLSGGWKMKLALARAM--LFKAD---- 590
Cdd:PRK13548 84 hSSLSFPFTVEEVVAmgraphglsraeDDALVAAALAQVDLAHlaGRDYPQ---LSGGEQQRVQLARVLaqLWEPDgppr 160
|
170
....*....|..
gi 1933195014 591 ILLLDEPTNHLD 602
Cdd:PRK13548 161 WLLLDEPTSALD 172
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
471-602 |
8.03e-08 |
|
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: 56.26 E-value: 8.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 471 LNTATLRLKRGHRYGLCGKNGTGKSTLMRAITNgqvegFPSPDEVRTFYVEHDIDGSEADTSVLQFILTDKRVL------ 544
Cdd:TIGR02203 348 LDSISLVIEPGETVALVGRSGSGKSTLVNLIPR-----FYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVlfndti 422
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1933195014 545 -----------SSEAEIKEALASVGFND------ERQKQAIGS----LSGGWKMKLALARAMLFKADILLLDEPTNHLD 602
Cdd:TIGR02203 423 anniaygrteqADRAEIERALAAAYAQDfvdklpLGLDTPIGEngvlLSGGQRQRLAIARALLKDAPILILDEATSALD 501
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
476-626 |
8.50e-08 |
|
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: 54.04 E-value: 8.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 476 LRLKRGHRYGLCGKNGTGKSTLMRAITngqveGFPSPDEVRTFYVEHDIDGSEADTSVLQFILTDKRVLS---------- 545
Cdd:cd03298 19 LTFAQGEITAIVGPSGSGKSTLLNLIA-----GFETPQSGRVLINGVDVTAAPPADRPVSMLFQENNLFAhltveqnvgl 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 546 -----------SEAEIKEALASVGFnDERQKQAIGSLSGGWKMKLALARAMLFKADILLLDEPTNHLDVVnvawLENYLT 614
Cdd:cd03298 94 glspglkltaeDRQAIEVALARVGL-AGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPA----LRAEML 168
|
170
....*....|....*....
gi 1933195014 615 SL--KTC-----TSIIVSH 626
Cdd:cd03298 169 DLvlDLHaetkmTVLMVTH 187
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
488-602 |
8.51e-08 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 54.19 E-value: 8.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 488 GKNGTGKSTLMRAITnGQVEGFPSPDEVRtfyVEHDIDGSEAdtSVLQFILTDKRVLsseaEIKEALASVGFNDE---RQ 564
Cdd:COG2401 63 GASGSGKSTLLRLLA-GALKGTPVAGCVD---VPDNQFGREA--SLIDAIGRKGDFK----DAVELLNAVGLSDAvlwLR 132
|
90 100 110
....*....|....*....|....*....|....*...
gi 1933195014 565 KQAigSLSGGWKMKLALARAMLFKADILLLDEPTNHLD 602
Cdd:COG2401 133 RFK--ELSTGQKFRFRLALLLAERPKLLVIDEFCSHLD 168
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
715-984 |
8.57e-08 |
|
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: 53.64 E-value: 8.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 715 DITLQVSLSSRVAILGPNGSGKSTLVKLLIGDMEPNkGGEIWkhpnlvigyvaqhafhhidhhldktpleymlWRyqtGE 794
Cdd:COG4133 20 GLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPS-AGEVL-------------------------------WN---GE 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 795 DLEEMSKANRQiteaeaqkmkegALIVVEGQKRLIEEiitrkklkqsyeyevsfkgLSSSENI--Wlprdelvkrgfekk 872
Cdd:COG4133 65 PIRDAREDYRR------------RLAYLGHADGLKPE-------------------LTVRENLrfW-------------- 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 873 vievdtreAQRLGLLRPlvRREIEKHFADFGLEPefVSHNTMRGLSGGQKVKIVLGAATWRRPHVICLDEPTNYLDRESL 952
Cdd:COG4133 100 --------AALYGLRAD--REAIDEALEAVGLAG--LADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGV 167
|
250 260 270
....*....|....*....|....*....|....
gi 1933195014 953 AALIAALKVF--EGGVLIITHNRDFSESLCHEVW 984
Cdd:COG4133 168 ALLAELIAAHlaRGGAVLLTTHQPLELAAARVLD 201
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
713-752 |
8.70e-08 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 54.74 E-value: 8.70e-08
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1933195014 713 LYDITLQVSLSSRVAILGPNGSGKSTLVKLLIGDMEPNKG 752
Cdd:COG4559 17 LDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSG 56
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
468-602 |
1.06e-07 |
|
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: 53.81 E-value: 1.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 468 KILLNTATLRLKRGHRYGLCGKNGTGKSTLMRAI---------TNGQV--EGFP-SPDEV--RTFYVEHD---IDG---S 527
Cdd:cd03234 20 ARILNDVSLHVESGQVMAILGSSGSGKTTLLDAIsgrvegggtTSGQIlfNGQPrKPDQFqkCVAYVRQDdilLPGltvR 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1933195014 528 EADTSVLQFILtdkRVLSSEAEIKEALASVGFNDERQKQA----IGSLSGGWKMKLALARAMLFKADILLLDEPTNHLD 602
Cdd:cd03234 100 ETLTYTAILRL---PRKSSDAIRKKRVEDVLLRDLALTRIggnlVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLD 175
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
713-995 |
1.29e-07 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 53.80 E-value: 1.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 713 LYDITLQVSLSSRVAILGPNGSGKSTLVKLLIGDmePN---KGGEIWkhpnlvigyvaqhafhhidhhldktpleymlwr 789
Cdd:TIGR01978 16 LKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAGH--PSyevTSGTIL--------------------------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 790 YQtGEDLEEMSkanrqiteaeaqkmkegalivvegqkrlIEEiITRKKLKQSYEYEVSFKGLSSSEniwlprdelvkrgF 869
Cdd:TIGR01978 61 FK-GQDLLELE----------------------------PDE-RARAGLFLAFQYPEEIPGVSNLE-------------F 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 870 EKKVIEVDTREAQRLGLLRPLVRREIEKHFADFGLEPEFVSHNTMRGLSGGQKVK--IVLGAATwrRPHVICLDEPTNYL 947
Cdd:TIGR01978 98 LRSALNARRSARGEEPLDLLDFEKLLKEKLALLDMDEEFLNRSVNEGFSGGEKKRneILQMALL--EPKLAILDEIDSGL 175
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1933195014 948 DRESL---AALIAALKVFEGGVLIITHNRDFSESLCHE-VWAMRDGRLEASG 995
Cdd:TIGR01978 176 DIDALkivAEGINRLREPDRSFLIITHYQRLLNYIKPDyVHVLLDGRIVKSG 227
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
713-752 |
1.33e-07 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 53.93 E-value: 1.33e-07
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1933195014 713 LYDITLQVSLSSRVAILGPNGSGKSTLVKLLIGDMEPNKG 752
Cdd:COG1134 42 LKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSG 81
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
694-789 |
1.59e-07 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 53.58 E-value: 1.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 694 SLLKMRKVGFQYPTQAVqqLYDITLQVSLSSRVAILGPNGSGKSTLVKLLIGDMEPNKgGEIWKHPNLVIGYVAQHAfhH 773
Cdd:PRK09544 3 SLVSLENVSVSFGQRRV--LSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDE-GVIKRNGKLRIGYVPQKL--Y 77
|
90
....*....|....*.
gi 1933195014 774 IDHHLDKTPLEYMLWR 789
Cdd:PRK09544 78 LDTTLPLTVNRFLRLR 93
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
696-991 |
1.71e-07 |
|
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: 52.92 E-value: 1.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 696 LKMRKVGFQYPTQAVqqLYDITLQVSLSSRVAILGPNGSGKSTLVKLLIGdMEPNKGGEIWkhpnlvigyvaqhafhhID 775
Cdd:cd03262 1 IEIKNLHKSFGDFHV--LKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINL-LEEPDSGTII-----------------ID 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 776 HhldktpleymlwryqtgedleemskanrqiteaeaqkmkegalIVVEGQKRLIEEIitRKKLK---QSYEYevsFKGLS 852
Cdd:cd03262 61 G-------------------------------------------LKLTDDKKNINEL--RQKVGmvfQQFNL---FPHLT 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 853 SSENIWLPrdelvkrgfEKKVIEVDTREAQRLGllrplvrreiEKHFADFGLEPEfvSHNTMRGLSGGQKVKIVLGAATW 932
Cdd:cd03262 93 VLENITLA---------PIKVKGMSKAEAEERA----------LELLEKVGLADK--ADAYPAQLSGGQQQRVAIARALA 151
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1933195014 933 RRPHVICLDEPTNYLD----RESLAALIAALKvfEG-GVLIITHNRDFSESLCHEVWAMRDGRL 991
Cdd:cd03262 152 MNPKVMLFDEPTSALDpelvGEVLDVMKDLAE--EGmTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
465-627 |
1.81e-07 |
|
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: 53.03 E-value: 1.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 465 YGAKILLNTATLRLKRGHRYGLCGKNGTGKSTLMRAITngqveGFPSPDEVRTFYVEHDIDG---SEADTS-VLQ----- 535
Cdd:cd03301 10 FGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIA-----GLEEPTSGRIYIGGRDVTDlppKDRDIAmVFQnyaly 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 536 ----------FILTDKRVlsSEAEIKEALASV-------GFNDERQKQaigsLSGGWKMKLALARAMLFKADILLLDEPT 598
Cdd:cd03301 85 phmtvydniaFGLKLRKV--PKDEIDERVREVaellqieHLLDRKPKQ----LSGGQRQRVALGRAIVREPKVFLMDEPL 158
|
170 180 190
....*....|....*....|....*....|...
gi 1933195014 599 NHLD----VVNVAWLENYLTSLKTcTSIIVSHD 627
Cdd:cd03301 159 SNLDaklrVQMRAELKRLQQRLGT-TTIYVTHD 190
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
465-602 |
1.89e-07 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 53.86 E-value: 1.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 465 YGAKILLNTATLRLKRGHRYGLCGKNGTGKSTLMRAIT------NGQV--EG--------------------FPSPDEvR 516
Cdd:PRK13638 11 YQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSgllrpqKGAVlwQGkpldyskrgllalrqqvatvFQDPEQ-Q 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 517 TFYVehDIDgseadtSVLQFILTDKRVlsSEAEIK----EALASVGFNDERQkQAIGSLSGGWKMKLALARAMLFKADIL 592
Cdd:PRK13638 90 IFYT--DID------SDIAFSLRNLGV--PEAEITrrvdEALTLVDAQHFRH-QPIQCLSHGQKKRVAIAGALVLQARYL 158
|
170
....*....|
gi 1933195014 593 LLDEPTNHLD 602
Cdd:PRK13638 159 LLDEPTAGLD 168
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
695-995 |
1.91e-07 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 53.86 E-value: 1.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 695 LLKMRKVGFQYptQAVQQLYDITLQVSLSSRVAILGPNGSGKSTLVKLLIGDMEPNKGGEIWKhpnlvigyvaqhafhhi 774
Cdd:PRK13638 1 MLATSDLWFRY--QDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQ----------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 775 dhhldKTPLEYMlwryqtgedleemskanrqiteaeaqkmKEGaLIVVEGQKRLIEEIITRKKLKQSYEYEVSFkglsSS 854
Cdd:PRK13638 62 -----GKPLDYS----------------------------KRG-LLALRQQVATVFQDPEQQIFYTDIDSDIAF----SL 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 855 ENIWLPRDELVKRgFEKKVIEVDTreaqrlgllrplvrreieKHFadfglepefvSHNTMRGLSGGQKVKIVLGAATWRR 934
Cdd:PRK13638 104 RNLGVPEAEITRR-VDEALTLVDA------------------QHF----------RHQPIQCLSHGQKKRVAIAGALVLQ 154
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1933195014 935 PHVICLDEPTNYLDRESLAALIAALK--VFEGG-VLIITHNRDFSESLCHEVWAMRDGRLEASG 995
Cdd:PRK13638 155 ARYLLLDEPTAGLDPAGRTQMIAIIRriVAQGNhVIISSHDIDLIYEISDAVYVLRQGQILTHG 218
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
466-651 |
2.13e-07 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 52.79 E-value: 2.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 466 GAKILLNTATLRLKRGHRYGLCGKNGTGKSTLMRAITNgqvegFPSPDEVRTFYVEHDIDGSEADT-------------- 531
Cdd:PRK10247 18 GDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVAS-----LISPTSGTLLFEGEDISTLKPEIyrqqvsycaqtptl 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 532 ---SV---LQFILTDKRVLSSEAEIKEALASVGFNDERQKQAIGSLSGGWKMKLALARAMLFKADILLLDEPTNHLD--- 602
Cdd:PRK10247 93 fgdTVydnLIFPWQIRNQQPDPAIFLDDLERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDesn 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1933195014 603 VVNVAWLENYLTSLKTCTSIIVSHDSGFLN---NTITDVLHLNRFKLRRYRG 651
Cdd:PRK10247 173 KHNVNEIIHRYVREQNIAVLWVTHDKDEINhadKVITLQPHAGEMQEARYEL 224
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
693-994 |
2.33e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 53.58 E-value: 2.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 693 KSLLKMRKVGFQY-PTQAVQQLYDITLQVSLSSRVAILGPNGSGKSTLVKLLIGDMEPNKGGeiwkhpnlvigyvaqhaf 771
Cdd:PRK13650 2 SNIIEVKNLTFKYkEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQ------------------ 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 772 hhidhhldktpleymlwryqtgedleemskanrqiteaeaqkmkegalIVVEGQKrLIEEIITRKKLK------------ 839
Cdd:PRK13650 64 ------------------------------------------------IIIDGDL-LTEENVWDIRHKigmvfqnpdnqf 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 840 --QSYEYEVSFkGLsssENIWLPRDELVKRgfekkvieVDtrEAQRLGLLRPLVRREIEKhfadfglepefvshntmrgL 917
Cdd:PRK13650 95 vgATVEDDVAF-GL---ENKGIPHEEMKER--------VN--EALELVGMQDFKEREPAR-------------------L 141
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 918 SGGQKVKIVLGAATWRRPHVICLDEPTNYLDRESLAALIAALKV----FEGGVLIITHNRDfSESLCHEVWAMRDGRLEA 993
Cdd:PRK13650 142 SGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGirddYQMTVISITHDLD-EVALSDRVLVMKNGQVES 220
|
.
gi 1933195014 994 S 994
Cdd:PRK13650 221 T 221
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
715-995 |
2.37e-07 |
|
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: 52.76 E-value: 2.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 715 DITLQVSLSSRVAILGPNGSGKSTLVKLLIGDMEPNkGGEIW-------KHPNLV---IGYVAQhafhhidhhldktple 784
Cdd:cd03265 18 GVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPT-SGRATvaghdvvREPREVrrrIGIVFQ---------------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 785 ymlwryqtgedleeMSKANRQITEAEAQKMkEGALIVVEGQKRlieeiitrkklKQSYEYEVSFKGLssseniWLPRDEL 864
Cdd:cd03265 81 --------------DLSVDDELTGWENLYI-HARLYGVPGAER-----------RERIDELLDFVGL------LEAADRL 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 865 VKRgfekkvievdtreaqrlgllrplvrreiekhfadfglepefvshntmrgLSGGQKVKIVLGAATWRRPHVICLDEPT 944
Cdd:cd03265 129 VKT-------------------------------------------------YSGGMRRRLEIARSLVHRPEVLFLDEPT 159
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1933195014 945 NYLD---RESLAALIAALKVFEG-GVLIITHNRDFSESLCHEVWAMRDGRLEASG 995
Cdd:cd03265 160 IGLDpqtRAHVWEYIEKLKEEFGmTILLTTHYMEEAEQLCDRVAIIDHGRIIAEG 214
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
471-644 |
2.76e-07 |
|
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: 52.82 E-value: 2.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 471 LNTATLRLKRGHRYGLCGKNGTGKSTLMRAI------TNGQVegfpspdevrtfYVEHD---IDGSEADTS--------- 532
Cdd:COG4778 27 LDGVSFSVAAGECVALTGPSGAGKSTLLKCIygnylpDSGSI------------LVRHDggwVDLAQASPReilalrrrt 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 533 ---VLQFILTDKRVlSSEAEIKEALASVGFNDERQKQAIGSL------------------SGGWKMKLALARAMLFKADI 591
Cdd:COG4778 95 igyVSQFLRVIPRV-SALDVVAEPLLERGVDREEARARARELlarlnlperlwdlppatfSGGEQQRVNIARGFIADPPL 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1933195014 592 LLLDEPTNHLDVVNVAWLENYLTSLKTC-TSII-VSHDSGFLNNTITDVLHLNRF 644
Cdd:COG4778 174 LLLDEPTASLDAANRAVVVELIEEAKARgTAIIgIFHDEEVREAVADRVVDVTPF 228
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
696-994 |
2.78e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 54.53 E-value: 2.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 696 LKMRKVGFQYPtqAVQQLYDITLQVSLSSRVAILGPNGSGKSTLVKLLIGDMEPNkGGEIwkhpnlvigyvaqhafhhid 775
Cdd:PRK11288 5 LSFDGIGKTFP--GVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPD-AGSI-------------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 776 hHLDKTPLEYmlwryqtgedleemskanRQITEAEAQKMkegALIVVEGQkrLIEEiitrkklkqsyeyevsfkgLSSSE 855
Cdd:PRK11288 62 -LIDGQEMRF------------------ASTTAALAAGV---AIIYQELH--LVPE-------------------MTVAE 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 856 NIWL---PRdelvKRGFekkvieVDTReaqrlgLLRPLVRREIEKhfadFGLEpefVSHNT-MRGLSGGQKVKIVLGAAT 931
Cdd:PRK11288 99 NLYLgqlPH----KGGI------VNRR------LLNYEAREQLEH----LGVD---IDPDTpLKYLSIGQRQMVEIAKAL 155
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1933195014 932 WRRPHVICLDEPTNYLD-RES--LAALIAALKVfEGGVLI-ITHNRDFSESLCHEVWAMRDGRLEAS 994
Cdd:PRK11288 156 ARNARVIAFDEPTSSLSaREIeqLFRVIRELRA-EGRVILyVSHRMEEIFALCDAITVFKDGRYVAT 221
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
460-602 |
2.84e-07 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 54.33 E-value: 2.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 460 QFSLAYGAKILLNTATLRLKRGHRYGLCGKNGTGKSTLMRAI------TNGQV--EGFPSP----DEVRtfyvehdidGS 527
Cdd:PRK10789 320 QFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIqrhfdvSEGDIrfHDIPLTklqlDSWR---------SR 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 528 EADTSVLQFILTDK--------RVLSSEAEIKEA--LASV---------GFNDERQKQAIgSLSGGWKMKLALARAMLFK 588
Cdd:PRK10789 391 LAVVSQTPFLFSDTvannialgRPDATQQEIEHVarLASVhddilrlpqGYDTEVGERGV-MLSGGQKQRISIARALLLN 469
|
170
....*....|....
gi 1933195014 589 ADILLLDEPTNHLD 602
Cdd:PRK10789 470 AEILILDDALSAVD 483
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
669-752 |
2.91e-07 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 54.40 E-value: 2.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 669 LEALEDYKFKLPDPPLLEGVKTKEKSLlKMRKVGFQYPTQAvQQLYDITLQVSLSSRVAILGPNGSGKSTLVKLLIGDME 748
Cdd:COG1132 314 IFELLDEPPEIPDPPGAVPLPPVRGEI-EFENVSFSYPGDR-PVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYD 391
|
....
gi 1933195014 749 PNKG 752
Cdd:COG1132 392 PTSG 395
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
713-995 |
2.93e-07 |
|
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: 52.26 E-value: 2.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 713 LYDITLQVSLSSRVAILGPNGSGKSTLVKLLIGDMEPNKGgeiwkhpNLVIGyvaqhafhhidhhldktpleymlwryqt 792
Cdd:cd03301 16 LDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSG-------RIYIG---------------------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 793 GEDLEEMSKANRQIteaeaqkmkegALIVvegqkrlieeiitrkklkQSYEYevsFKGLSSSENIWLPrdeLVKRGFEKK 872
Cdd:cd03301 61 GRDVTDLPPKDRDI-----------AMVF------------------QNYAL---YPHMTVYDNIAFG---LKLRKVPKD 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 873 VIEVDTREAQRLgllrplvrreiekhfadfgLEPEFVSHNTMRGLSGGQKVKIVLGAATWRRPHVICLDEPTNYLD---- 948
Cdd:cd03301 106 EIDERVREVAEL-------------------LQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDaklr 166
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1933195014 949 ---RESLAALIAALKVfegGVLIITHNRDFSESLCHEVWAMRDGRLEASG 995
Cdd:cd03301 167 vqmRAELKRLQQRLGT---TTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
713-993 |
3.13e-07 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 52.51 E-value: 3.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 713 LYDITLQVSLSSRVAILGPNGSGKSTLVKLLIGDMEPNKGGEIWKhpnlvigyvaqhafhhidhhldktpleymlwryqt 792
Cdd:PRK11629 25 LHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFN----------------------------------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 793 GEDLEEMSKANRqiteAEAQKMKEGALivvegqkrlieeiitrkklkqsYEYEVSFKGLSSSENIWLPrdeLVKRGfekk 872
Cdd:PRK11629 70 GQPMSKLSSAAK----AELRNQKLGFI----------------------YQFHHLLPDFTALENVAMP---LLIGK---- 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 873 vieVDTREAQRLGLlrplvrreieKHFADFGLEPEfvSHNTMRGLSGGQKVKIVLGAATWRRPHVICLDEPTNYLDR--- 949
Cdd:PRK11629 117 ---KKPAEINSRAL----------EMLAAVGLEHR--ANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDArna 181
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1933195014 950 ESLAALIAALKVFEG-GVLIITHNRDFSESLCHEVwAMRDGRLEA 993
Cdd:PRK11629 182 DSIFQLLGELNRLQGtAFLVVTHDLQLAKRMSRQL-EMRDGRLTA 225
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
461-626 |
3.15e-07 |
|
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: 52.03 E-value: 3.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 461 FSLAYGAKI--LLNTATLRLKRGHRYGLCGKNGTGKSTLMRAI------TNGQVEgfpspdevrtfyvehdIDGSEADT- 531
Cdd:cd03369 12 LSVRYAPDLppVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALfrfleaEEGKIE----------------IDGIDISTi 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 532 ------SVLQFILTDKRVLS-------------SEAEIKEALasvgfndeRQKQAIGSLSGGWKMKLALARAMLFKADIL 592
Cdd:cd03369 76 pledlrSSLTIIPQDPTLFSgtirsnldpfdeySDEEIYGAL--------RVSEGGLNLSQGQRQLLCLARALLKRPRVL 147
|
170 180 190
....*....|....*....|....*....|....*
gi 1933195014 593 LLDEPTNHLDVVNVAWLENYL-TSLKTCTSIIVSH 626
Cdd:cd03369 148 VLDEATASIDYATDALIQKTIrEEFTNSTILTIAH 182
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
463-602 |
3.25e-07 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 54.47 E-value: 3.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 463 LAYGAKILLNTATLRLKRGHRYGLCGKNGTGKSTLMRAITngqveGF-PSPDEVRTFYVE-HDIDGSE---------ADT 531
Cdd:PRK11174 358 LSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALL-----GFlPYQGSLKINGIElRELDPESwrkhlswvgQNP 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 532 SVLQFILTDKRVLS----SEAEIKEALA-----------SVGFNDERQKQAIGsLSGGWKMKLALARAMLFKADILLLDE 596
Cdd:PRK11174 433 QLPHGTLRDNVLLGnpdaSDEQLQQALEnawvseflpllPQGLDTPIGDQAAG-LSVGQAQRLALARALLQPCQLLLLDE 511
|
....*.
gi 1933195014 597 PTNHLD 602
Cdd:PRK11174 512 PTASLD 517
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
696-991 |
3.44e-07 |
|
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: 52.02 E-value: 3.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 696 LKMRKVGFQYPtQAVQQLYDITLQVSLSSRVAILGPNGSGKSTLVKLLIGDMEPNKGgeiwkhpnLVIgyVAQHAFHHId 775
Cdd:cd03292 1 IEFINVTKTYP-NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSG--------TIR--VNGQDVSDL- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 776 hHLDKTPLeymlWRYQTGedleemskanrqiteaeaqkmkegaliVVEGQKRLIEEiitrkklkqsyeyevsfkgLSSSE 855
Cdd:cd03292 69 -RGRAIPY----LRRKIG---------------------------VVFQDFRLLPD-------------------RNVYE 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 856 NIwlprdelvkrGFEKKVIEVDTREAQ-RLGLLRPLVrreiekhfadfGLEPEfvsHNTM-RGLSGGQKVKIVLGAATWR 933
Cdd:cd03292 98 NV----------AFALEVTGVPPREIRkRVPAALELV-----------GLSHK---HRALpAELSGGEQQRVAIARAIVN 153
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1933195014 934 RPHVICLDEPTNYLDRESLAALIAALKVFEGG---VLIITHNRDFSESLCHEVWAMRDGRL 991
Cdd:cd03292 154 SPTILIADEPTGNLDPDTTWEIMNLLKKINKAgttVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
916-995 |
3.53e-07 |
|
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: 54.37 E-value: 3.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 916 GLSGGQKVKIVLGAATWRRPHVICLDEPTNYLDRESLAALIAALKVF--EGG-VLIITHNRDFsESLCHEVWAMRDGRLE 992
Cdd:COG4618 467 RLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALkaRGAtVVVITHRPSL-LAAVDKLLVLRDGRVQ 545
|
...
gi 1933195014 993 ASG 995
Cdd:COG4618 546 AFG 548
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
696-990 |
3.94e-07 |
|
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: 52.19 E-value: 3.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 696 LKMRKVGFQYPtQAVQQLYDITLQVSLSSRVAILGPNGSGKSTLVKLLIGDMEPNKGGEIWKhpnlvigyvaqhafhhid 775
Cdd:cd03256 1 IEVENLSKTYP-NGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLID------------------ 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 776 hhldktpleymlwryqtGEDLEEMS-KANRQITeaeaqkmKEGALIVVEGqkRLIEEiitrkklkqsyeyevsfkgLSSS 854
Cdd:cd03256 62 -----------------GTDINKLKgKALRQLR-------RQIGMIFQQF--NLIER-------------------LSVL 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 855 ENIWLPRdelvkrgfekkvieVDTREAQRlGLLRPLVRREIEKHFA---DFGLEPefvSHNTMRG-LSGGQKVKIVLGAA 930
Cdd:cd03256 97 ENVLSGR--------------LGRRSTWR-SLFGLFPKEEKQRALAaleRVGLLD---KAYQRADqLSGGQQQRVAIARA 158
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1933195014 931 TWRRPHVICLDEPTNYLD----RESLAALIAALKVFEGGVLIITHNRDFSESLCHEVWAMRDGR 990
Cdd:cd03256 159 LMQQPKLILADEPVASLDpassRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGR 222
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
726-972 |
4.30e-07 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 52.37 E-value: 4.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 726 VAILGPNGSGKSTLVKLLIGDMEPNKGgeiwKHpnlvigyvaqhafhhidhhlDKTPLEYMLWRYQTGEDLEEMSKanrq 805
Cdd:cd03236 29 LGLVGPNGIGKSTALKILAGKLKPNLG----KF--------------------DDPPDWDEILDEFRGSELQNYFT---- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 806 iteaeaqKMKEGALIVVegQKRLIEEIITRkklkqsyeyevSFKGlsSSENIWLPRDElvkRGFEKKVIEvdtreaqRLG 885
Cdd:cd03236 81 -------KLLEGDVKVI--VKPQYVDLIPK-----------AVKG--KVGELLKKKDE---RGKLDELVD-------QLE 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 886 lLRPLVRREIEKhfadfglepefvshntmrgLSGGQKVKIVLGAATWRRPHVICLDEPTNYLD---RESLAALIAALKVF 962
Cdd:cd03236 129 -LRHVLDRNIDQ-------------------LSGGELQRVAIAAALARDADFYFFDEPSSYLDikqRLNAARLIRELAED 188
|
250
....*....|
gi 1933195014 963 EGGVLIITHN 972
Cdd:cd03236 189 DNYVLVVEHD 198
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
474-603 |
4.34e-07 |
|
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: 53.92 E-value: 4.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 474 ATLRLKRGHRYGLCGKNGTGKSTLMRAI-----TNGQVegfpspdevrtFYVEHDIDG-SEADT---------------- 531
Cdd:COG4172 305 VSLTLRRGETLGLVGESGSGKSTLGLALlrlipSEGEI-----------RFDGQDLDGlSRRALrplrrrmqvvfqdpfg 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 532 ------SVLQFI---LTDKRVLSSEAE----IKEALASVGFNDERQKQAIGSLSGGWKMKLALARAMLFKADILLLDEPT 598
Cdd:COG4172 374 slsprmTVGQIIaegLRVHGPGLSAAErrarVAEALEEVGLDPAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPT 453
|
....*
gi 1933195014 599 NHLDV 603
Cdd:COG4172 454 SALDV 458
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
711-991 |
5.77e-07 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 52.32 E-value: 5.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 711 QQLYDITLQVSLSSRVAILGPNGSGKSTLVK----LLIGDMEPNKGGEIwkhpnlvIGYVAQHAfHHIDHHLDKTpleym 786
Cdd:PRK09984 18 QALHAVDLNIHHGEMVALLGPSGSGKSTLLRhlsgLITGDKSAGSHIEL-------LGRTVQRE-GRLARDIRKS----- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 787 lwRYQTGEDLEEMSKANRqiteaeaqkmkegaLIVVEgqkrlieeiitrkklkqsyeyEVSFKGLSSSEniwlprdelvk 866
Cdd:PRK09984 85 --RANTGYIFQQFNLVNR--------------LSVLE---------------------NVLIGALGSTP----------- 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 867 rgFEKKVIEVDTREaQRLGLLRPLVRREIeKHFAdfglepefvsHNTMRGLSGGQKVKIVLGAATWRRPHVICLDEPTNY 946
Cdd:PRK09984 117 --FWRTCFSWFTRE-QKQRALQALTRVGM-VHFA----------HQRVSTLSGGQQQRVAIARALMQQAKVILADEPIAS 182
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1933195014 947 LDRESLAALIAALKVF---EGGVLIIT-HNRDFSESLCHEVWAMRDGRL 991
Cdd:PRK09984 183 LDPESARIVMDTLRDInqnDGITVVVTlHQVDYALRYCERIVALRQGHV 231
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
479-640 |
5.81e-07 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 51.98 E-value: 5.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 479 KRGHRYGLCGKNGTGKSTLMRAITN------GQVEGFPSPDEVRTFYvehdiDGSEadtsvLQFILTD------------ 540
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAGklkpnlGKFDDPPDWDEILDEF-----RGSE-----LQNYFTKllegdvkvivkp 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 541 -------KRVLSSEAEIKEALASVGFNDERQKQ---------AIGSLSGGWKMKLALARAMLFKADILLLDEPTNHLDV- 603
Cdd:cd03236 94 qyvdlipKAVKGKVGELLKKKDERGKLDELVDQlelrhvldrNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIk 173
|
170 180 190
....*....|....*....|....*....|....*....
gi 1933195014 604 --VNVAWLENYLTSLKTCTsIIVSHDSGFLnNTITDVLH 640
Cdd:cd03236 174 qrLNAARLIRELAEDDNYV-LVVEHDLAVL-DYLSDYIH 210
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
476-631 |
5.82e-07 |
|
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: 51.32 E-value: 5.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 476 LRLKRGHRYGLCGKNGTGKSTLMRAI------TNGQVEGFPSpdevrTFYVehdidgseADTSVLQFiltdkrvlsseAE 549
Cdd:cd03250 26 LEVPKGELVAIVGPVGSGKSSLLSALlgelekLSGSVSVPGS-----IAYV--------SQEPWIQN-----------GT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 550 IKE-ALASVGFNDERQKQA--------------------IG----SLSGGWKMKLALARAMLFKADILLLDEPTNHLDVV 604
Cdd:cd03250 82 IREnILFGKPFDEERYEKVikacalepdleilpdgdlteIGekgiNLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAH 161
|
170 180 190
....*....|....*....|....*....|..
gi 1933195014 605 NVAWL-ENYLTSL----KTCtsIIVSHDSGFL 631
Cdd:cd03250 162 VGRHIfENCILGLllnnKTR--ILVTHQLQLL 191
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
471-627 |
5.90e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 52.39 E-value: 5.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 471 LNTATLRLKRGHRYGLCGKNGTGKSTLMRAItNGQVEgfPSPDEVRtfyvehdIDGSEADTSVLQFILTDKRV------- 543
Cdd:PRK13639 18 LKGINFKAEKGEMVALLGPNGAGKSTLFLHF-NGILK--PTSGEVL-------IKGEPIKYDKKSLLEVRKTVgivfqnp 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 544 ---------------------LSS---EAEIKEALASVGFNDERQKqAIGSLSGGWKMKLALARAMLFKADILLLDEPTN 599
Cdd:PRK13639 88 ddqlfaptveedvafgplnlgLSKeevEKRVKEALKAVGMEGFENK-PPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTS 166
|
170 180 190
....*....|....*....|....*....|
gi 1933195014 600 HLDVVNVAWLENYLTSL--KTCTSIIVSHD 627
Cdd:PRK13639 167 GLDPMGASQIMKLLYDLnkEGITIIISTHD 196
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
689-752 |
6.01e-07 |
|
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: 51.38 E-value: 6.01e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1933195014 689 KTKEKSLLKMRKVGFQYPTQAVQQLYDITLQVSLSSRVAILGPNGSGKSTLVKLLIGDMEPNKG 752
Cdd:cd03220 14 KGGSSSLKKLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSG 77
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
461-627 |
6.75e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 52.02 E-value: 6.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 461 FSLAYGAKILLNTATLRLKRGHRYGLCGKNGTGKSTLMRAIT--NGQVEGFPSPDEV----RTFYVEHDI---------- 524
Cdd:PRK14271 27 LTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNrmNDKVSGYRYSGDVllggRSIFNYRDVlefrrrvgml 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 525 --DGSEADTSVLQFILTDKRV--LSSEAEIK----EALASVGFND---ERQKQAIGSLSGGWKMKLALARAMLFKADILL 593
Cdd:PRK14271 107 fqRPNPFPMSIMDNVLAGVRAhkLVPRKEFRgvaqARLTEVGLWDavkDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLL 186
|
170 180 190
....*....|....*....|....*....|....*
gi 1933195014 594 LDEPTNHLDVVNVAWLENYLTSLKT-CTSIIVSHD 627
Cdd:PRK14271 187 LDEPTSALDPTTTEKIEEFIRSLADrLTVIIVTHN 221
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
478-627 |
7.40e-07 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 51.64 E-value: 7.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 478 LKRGHRYGLCGKNGTGKSTLMRAI------TNGQVEGFPSPDEVRTFYVEHDIDGSeadtsVLQFILT-DKRVLSS---E 547
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLagvlkpDEGDIEIELDTVSYKPQYIKADYEGT-----VRDLLSSiTKDFYTHpyfK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 548 AEIKEALASVGFNDerqkQAIGSLSGGWKMKLALARAMLFKADILLLDEPTNHLDV---VNVAWLENYLTSLKTCTSIIV 624
Cdd:cd03237 97 TEIAKPLQIEQILD----REVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVeqrLMASKVIRRFAENNEKTAFVV 172
|
...
gi 1933195014 625 SHD 627
Cdd:cd03237 173 EHD 175
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
695-995 |
8.00e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 52.04 E-value: 8.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 695 LLKMRKVGFQYPTQ---AVQQLYDITLQVSLSSRVAILGPNGSGKSTLVKLLIGDMEPNKGgeiwkhpnlvigyvaqhaf 771
Cdd:PRK13643 1 MIKFEKVNYTYQPNspfASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEG------------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 772 hhidhhldktpleymlwryqtgedleemskanrqiteaeaqKMKEGALIVVEGQKRliEEII-TRKKLKQSYEYevsfkg 850
Cdd:PRK13643 62 -----------------------------------------KVTVGDIVVSSTSKQ--KEIKpVRKKVGVVFQF------ 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 851 lssseniwlPRDELvkrgFEKKVIEVDTREAQRLGLLRPLVRREIEKHFADFGLEPEFVSHNTMRgLSGGQKVKIVLGAA 930
Cdd:PRK13643 93 ---------PESQL----FEETVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADEFWEKSPFE-LSGGQMRRVAIAGI 158
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1933195014 931 TWRRPHVICLDEPTNYLDREslaALIAALKVFEG------GVLIITHNRDFSESLCHEVWAMRDGRLEASG 995
Cdd:PRK13643 159 LAMEPEVLVLDEPTAGLDPK---ARIEMMQLFESihqsgqTVVLVTHLMDDVADYADYVYLLEKGHIISCG 226
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
903-995 |
9.05e-07 |
|
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: 51.03 E-value: 9.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 903 GLEPEFVSHNTMRGLSGGQKVKIVLGAATWRRPHVICLDEPTNYLDRESLAA---LIAALKVfEGGVLIITHNRDFSESL 979
Cdd:cd03260 128 ALWDEVKDRLHALGLSGGQQQRLCLARALANEPEVLLLDEPTSALDPISTAKieeLIAELKK-EYTIVIVTHNMQQAARV 206
|
90
....*....|....*.
gi 1933195014 980 CHEVWAMRDGRLEASG 995
Cdd:cd03260 207 ADRTAFLLNGRLVEFG 222
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
571-667 |
9.24e-07 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 51.17 E-value: 9.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 571 LSGGWKMKLALARAMLFKADILLLDEPTNHLDVVNVAWLENYLTSLKTC--TSIIVSHDSGFLNNTITDVLHLNRFKLRR 648
Cdd:COG4161 142 LSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQTgiTQVIVTHEVEFARKVASQVVYMEKGRIIE 221
|
90
....*....|....*....
gi 1933195014 649 YrGNLESFVKAVPEAKSYY 667
Cdd:COG4161 222 Q-GDASHFTQPQTEAFAHY 239
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
696-994 |
1.10e-06 |
|
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: 49.73 E-value: 1.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 696 LKMRKVGFQYPtqAVQQLYDITLQVSLSSRVAILGPNGSGKSTLVKLLIGDMEPNkGGEIWkhpnlvigyvaqhafhhid 775
Cdd:cd03216 1 LELRGITKRFG--GVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPD-SGEIL------------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 776 hhldktpleymlwryqtgedleemskanrqiteaeaqkmkegalivVEGQkrlieeiitrkklkqsyeyEVSFKglssse 855
Cdd:cd03216 59 ----------------------------------------------VDGK-------------------EVSFA------ 67
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 856 niwlprdelvkrgfekkvievDTREAQRLGLlrplvrreiekhfadfglepEFVSHntmrgLSGGQKVKIVLGAATWRRP 935
Cdd:cd03216 68 ---------------------SPRDARRAGI--------------------AMVYQ-----LSVGERQMVEIARALARNA 101
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1933195014 936 HVICLDEPTNYLDRESLAALIAALKVF--EG-GVLIITHNRDFSESLCHEVWAMRDGRLEAS 994
Cdd:cd03216 102 RLLILDEPTAALTPAEVERLFKVIRRLraQGvAVIFISHRLDEVFEIADRVTVLRDGRVVGT 163
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
726-972 |
1.44e-06 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 51.24 E-value: 1.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 726 VAILGPNGSGKSTLVKLL--IGDMEPN---------KGGEIWKHPNLVIGYVAQH--AFHHIDHHLDKTPLEYML----- 787
Cdd:pfam13304 2 NVLIGPNGSGKSNLLEALrfLADFDALvigltdersRNGGIGGIPSLLNGIDPKEpiEFEISEFLEDGVRYRYGLdlere 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 788 ----WRYQTGEDLEEM------SKANRQITEAEAQKMKEGALIVVEGQKRLIEEIITRKKLKQSYEYEVSFKGLSSSENI 857
Cdd:pfam13304 82 dveeKLSSKPTLLEKRlllredSEEREPKFPPEAEELRLGLDVEERIELSLSELSDLISGLLLLSIISPLSFLLLLDEGL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 858 WLPR-------DELVKRGFEKKVIEVDTREAQRLGLLRPLVRREIEKHFADFGLEPE-FVSHN--------TMRGLSGGQ 921
Cdd:pfam13304 162 LLEDwavldlaADLALFPDLKELLQRLVRGLKLADLNLSDLGEGIEKSLLVDDRLRErGLILLenggggelPAFELSDGT 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1933195014 922 KVKIVLGAATWRRPH---VICLDEPTNYLD---RESLAALIAALKVFEGGVLIITHN 972
Cdd:pfam13304 242 KRLLALLAALLSALPkggLLLIDEPESGLHpklLRRLLELLKELSRNGAQLILTTHS 298
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
460-641 |
1.56e-06 |
|
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: 51.65 E-value: 1.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 460 QFSLAYGAKILlnTATLRLKRGHRYGLCGKNGTGKSTLMRAITngqveGFPSPDEVRTFyvehdIDGSE-ADTSVLQFIL 538
Cdd:TIGR02142 4 RFSKRLGDFSL--DADFTLPGQGVTAIFGRSGSGKTTLIRLIA-----GLTRPDEGEIV-----LNGRTlFDSRKGIFLP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 539 TDKRVLS---SEAE------IKEAL---------ASVGFNDERQKQAIG----------SLSGGWKMKLALARAMLFKAD 590
Cdd:TIGR02142 72 PEKRRIGyvfQEARlfphlsVRGNLrygmkrarpSERRISFERVIELLGighllgrlpgRLSGGEKQRVAIGRALLSSPR 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1933195014 591 ILLLDEPTNHLDVVNVAWLENYLTSLKTCTSI---IVSHDsgflnntITDVLHL 641
Cdd:TIGR02142 152 LLLMDEPLAALDDPRKYEILPYLERLHAEFGIpilYVSHS-------LQEVLRL 198
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
471-603 |
1.71e-06 |
|
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: 49.35 E-value: 1.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 471 LNTATLRLKRGHRYGLCGKNGTGKSTLMRAITngqveGFPSPD--EVRtfyvehdIDGSEAdtsvlqfiltdkRVLSSEA 548
Cdd:cd03215 16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALF-----GLRPPAsgEIT-------LDGKPV------------TRRSPRD 71
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1933195014 549 EIKEALASVGfnDERQKQ------------AIGS-LSGGWKMKLALARAMLFKADILLLDEPTNHLDV 603
Cdd:cd03215 72 AIRAGIAYVP--EDRKREglvldlsvaeniALSSlLSGGNQQKVVLARWLARDPRVLILDEPTRGVDV 137
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
488-613 |
1.85e-06 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 49.80 E-value: 1.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 488 GKNGTGKSTLMRAITngqveGFPSPD--EVR----------------TFYVEHdIDGSEADTSV---LQFILTDKRVLSS 546
Cdd:PRK13538 34 GPNGAGKTSLLRILA-----GLARPDagEVLwqgepirrqrdeyhqdLLYLGH-QPGIKTELTAlenLRFYQRLHGPGDD 107
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1933195014 547 EAeIKEALASVGFnDERQKQAIGSLSGGWKMKLALARAMLFKADILLLDEPTNHLDVVNVAWLENYL 613
Cdd:PRK13538 108 EA-LWEALAQVGL-AGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARLEALL 172
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
695-995 |
1.90e-06 |
|
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: 50.36 E-value: 1.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 695 LLKMRKVGFQYPTQAVQQlyDITLQVSLSSRVAILGPNGSGKSTLVKLLIGDMEPNKgGEIWkhpnlvigyvaqhafhhI 774
Cdd:COG1127 5 MIEVRNLTKSFGDRVVLD--GVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDS-GEIL-----------------V 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 775 DhhldktpleymlwryqtGEDLEEMSKANRQiteAEAQKM----KEGALivvegqkrlieeiitrkklkqsyeyevsFKG 850
Cdd:COG1127 65 D-----------------GQDITGLSEKELY---ELRRRIgmlfQGGAL----------------------------FDS 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 851 LSSSENI--------WLPRDELvkrgfEKKVIEVdtreAQRLGLlrplvrREIEKHF-ADfglepefvshntmrgLSGGQ 921
Cdd:COG1127 97 LTVFENVafplrehtDLSEAEI-----RELVLEK----LELVGL------PGAADKMpSE---------------LSGGM 146
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 922 KvK-------IVLgaatwrRPHVICLDEPTNYLDRESLAA---LIAAL-KVFEGGVLIITHNRDFSESLCHEVWAMRDGR 990
Cdd:COG1127 147 R-KrvalaraLAL------DPEILLYDEPTAGLDPITSAVideLIRELrDELGLTSVVVTHDLDSAFAIADRVAVLADGK 219
|
....*
gi 1933195014 991 LEASG 995
Cdd:COG1127 220 IIAEG 224
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
696-995 |
1.90e-06 |
|
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: 49.88 E-value: 1.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 696 LKMRKVGFQYPTQavQQLYDITLQVSlSSRVAILGPNGSGKSTLVKLLIGDMEPNKG------GEIWKHPNL---VIGYV 766
Cdd:cd03264 1 LQLENLTKRYGKK--RALDGVSLTLG-PGMYGLLGPNGAGKTTLMRILATLTPPSSGtiridgQDVLKQPQKlrrRIGYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 767 AQHaFHHIDHHLDKTPLEYMLWryqtgedleemskanrqiteaeaqkmkegalivvegqkrlieeiitrkklkqsyeyev 846
Cdd:cd03264 78 PQE-FGVYPNFTVREFLDYIAW---------------------------------------------------------- 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 847 sFKGLSSSEniwlprdelvkrgfekkvievdtreaqrlgllrplVRREIEKHFADFGLEPefVSHNTMRGLSGGQKVKIV 926
Cdd:cd03264 99 -LKGIPSKE-----------------------------------VKARVDEVLELVNLGD--RAKKKIGSLSGGMRRRVG 140
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1933195014 927 LGAATWRRPHVICLDEPTNYLDRE------SLAALIAALKVfeggVLIITHNRDFSESLCHEVWAMRDGRLEASG 995
Cdd:cd03264 141 IAQALVGDPSILIVDEPTAGLDPEerirfrNLLSELGEDRI----VILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
715-995 |
1.92e-06 |
|
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: 50.23 E-value: 1.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 715 DITLQVSLSSRVAILGPNGSGKSTLVKLLIGDMEPNKgGEIWkhpnlvigyvaqhafhhIDhHLDKTPLeymlwryqtge 794
Cdd:cd03218 18 GVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDS-GKIL-----------------LD-GQDITKL----------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 795 dleEMSKanrqiteaeaqkmkegalivvegqkrlieeiitRKKLKQSY-EYEVS-FKGLSSSENIWLprdelvkrgfekk 872
Cdd:cd03218 68 ---PMHK---------------------------------RARLGIGYlPQEASiFRKLTVEENILA------------- 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 873 VIEVdtreaqrLGLLRPLVRREIEKHFADFGLEPefVSHNTMRGLSGGQKVKIVLGAATWRRPHVICLDEPTNYLDRESL 952
Cdd:cd03218 99 VLEI-------RGLSKKEREEKLEELLEEFHITH--LRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDPIAV 169
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1933195014 953 A---ALIAALKVFEGGVLIITHNRDFSESLCHEVWAMRDGRLEASG 995
Cdd:cd03218 170 QdiqKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEG 215
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
571-626 |
2.05e-06 |
|
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: 50.31 E-value: 2.05e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1933195014 571 LSGGWKMKLALARAMLFKADILLLDEPTNHLDVVN-VAWLENYLTSLKTCTSIIVSH 626
Cdd:cd03253 138 LSGGEKQRVAIARAILKNPPILLLDEATSALDTHTeREIQAALRDVSKGRTTIVIAH 194
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
571-627 |
2.34e-06 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 50.85 E-value: 2.34e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1933195014 571 LSGGWKMKLALARAMLFKADILLLDEPTNHLDvVNV-----AWLENYLTSLKTcTSIIVSHD 627
Cdd:PRK10851 137 LSGGQKQRVALARALAVEPQILLLDEPFGALD-AQVrkelrRWLRQLHEELKF-TSVFVTHD 196
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
699-996 |
2.49e-06 |
|
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: 49.79 E-value: 2.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 699 RKVGFQYPTQAVQQLYDITLQVSLSSRVAILGPNGSGKSTLVKLLIGdMEPNKGGEIwkhpnLVIGyvaqhafhhidHHL 778
Cdd:cd03252 4 EHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQR-FYVPENGRV-----LVDG-----------HDL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 779 DKTPLEYMlwRYQTGEDLEEMSKANRQITEAEAqkmkegalIVVEGQKRliEEIITRKKLKQSYEYEVSfkglssseniw 858
Cdd:cd03252 67 ALADPAWL--RRQVGVVLQENVLFNRSIRDNIA--------LADPGMSM--ERVIEAAKLAGAHDFISE----------- 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 859 LPRdelvkrGFEKKVIEVDTreaqrlgllrplvrreiekhfadfglepefvshntmrGLSGGQKVKIVLGAATWRRPHVI 938
Cdd:cd03252 124 LPE------GYDTIVGEQGA-------------------------------------GLSGGQRQRIAIARALIHNPRIL 160
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1933195014 939 CLDEPTNYLDRESLAALIAALKVFEGG--VLIITHNrdFSESLC-HEVWAMRDGRL-EASGH 996
Cdd:cd03252 161 IFDEATSALDYESEHAIMRNMHDICAGrtVIIIAHR--LSTVKNaDRIIVMEKGRIvEQGSH 220
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
471-602 |
2.60e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 50.50 E-value: 2.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 471 LNTATLRLKRGHRYGLCGKNGTGKSTLMRAI------TNGQ--VEG------------------FPSPDEvrTFY---VE 521
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIdglleaESGQiiIDGdllteenvwdirhkigmvFQNPDN--QFVgatVE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 522 HDIdgseadtsvlQFILTDKRVLSSE--AEIKEALASVGFNDERQKQAiGSLSGGWKMKLALARAMLFKADILLLDEPTN 599
Cdd:PRK13650 101 DDV----------AFGLENKGIPHEEmkERVNEALELVGMQDFKEREP-ARLSGGQKQRVAIAGAVAMRPKIIILDEATS 169
|
...
gi 1933195014 600 HLD 602
Cdd:PRK13650 170 MLD 172
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
475-627 |
2.69e-06 |
|
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: 49.64 E-value: 2.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 475 TLRLKRGHRYGLCGKNGTGKSTLMRAITnGQVegFPSPDEVR-----------------------------------TFY 519
Cdd:cd03267 41 SFTIEKGEIVGFIGPNGAGKTTTLKILS-GLL--QPTSGEVRvaglvpwkrrkkflrrigvvfgqktqlwwdlpvidSFY 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 520 VEHDIDGSEADtsvlQFILTDKRvLSSEAEIKEALasvgfnderqKQAIGSLSGGWKMKLALARAMLFKADILLLDEPTN 599
Cdd:cd03267 118 LLAAIYDLPPA----RFKKRLDE-LSELLDLEELL----------DTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTI 182
|
170 180 190
....*....|....*....|....*....|.
gi 1933195014 600 HLDVVNVAWLENYLTSL---KTCTSIIVSHD 627
Cdd:cd03267 183 GLDVVAQENIRNFLKEYnreRGTTVLLTSHY 213
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
916-996 |
2.74e-06 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 51.38 E-value: 2.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 916 GLSGGQKVKIVLGAATWRRPHVICLDEPTNYLDRESLAALIAALKVFEGG--VLIITHNRDFSESlCHEVWAMRDGRLEA 993
Cdd:PRK11174 485 GLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRqtTLMVTHQLEDLAQ-WDQIWVMQDGQIVQ 563
|
...
gi 1933195014 994 SGH 996
Cdd:PRK11174 564 QGD 566
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
696-995 |
3.02e-06 |
|
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: 49.41 E-value: 3.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 696 LKMRKVGFQYPTQAVqqlyDITLQVSLSSRVAILGPNGSGKSTLVKLLIGDMEPNKGGeiwkhpnLVIGyvaqhafhhid 775
Cdd:cd03298 1 VRLDKIRFSYGEQPM----HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGR-------VLIN----------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 776 hhldktpleymlwryqtGEDLEEMSKANRQITEAeaqkMKEGALivvegqkrlieeiitrkklkqsyeyevsFKGLSSSE 855
Cdd:cd03298 59 -----------------GVDVTAAPPADRPVSML----FQENNL----------------------------FAHLTVEQ 89
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 856 NIWLPRDELVKrgfekkvievdtreaqrlglLRPLVRREIEKHFADFGLEpEFVSHNTmRGLSGGQKVKIVLGAATWRRP 935
Cdd:cd03298 90 NVGLGLSPGLK--------------------LTAEDRQAIEVALARVGLA-GLEKRLP-GELSGGERQRVALARVLVRDK 147
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1933195014 936 HVICLDEPTNYLD---RESLAALIAALKVFEG-GVLIITHNRDFSESLCHEVWAMRDGRLEASG 995
Cdd:cd03298 148 PVLLLDEPFAALDpalRAEMLDLVLDLHAETKmTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
713-773 |
3.24e-06 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 50.53 E-value: 3.24e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1933195014 713 LYDITLQVSLSSRVAILGPNGSGKSTLVKLLIGDMEPNKG-----GE---IWKHP---NlvIGYVAQHA--FHH 773
Cdd:COG1118 18 LDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGrivlnGRdlfTNLPPrerR--VGFVFQHYalFPH 89
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
471-603 |
3.31e-06 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 50.35 E-value: 3.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 471 LNTATLRLKRGHRYGLCGKNGTGKSTLMRAITngQVEgfpSPDEVRTFYVEHDIDGSEADTS---------VLQ------ 535
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLT--MIE---TPTGGELYYQGQDLLKADPEAQkllrqkiqiVFQnpygsl 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 536 -------FILTDKRVLS---SEAE----IKEALASVGFNDERQKQAIGSLSGGWKMKLALARAMLFKADILLLDEPTNHL 601
Cdd:PRK11308 106 nprkkvgQILEEPLLINtslSAAErrekALAMMAKVGLRPEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSAL 185
|
..
gi 1933195014 602 DV 603
Cdd:PRK11308 186 DV 187
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
709-995 |
3.51e-06 |
|
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: 49.35 E-value: 3.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 709 AVQQLYDITLQVSLSSRVAILGPNGSGKSTLVKLLIGdMEPNKGGEIwkhpnlvigyvaqhafhhidhhldktpleymlw 788
Cdd:cd03224 12 KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMG-LLPPRSGSI--------------------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 789 RYQtGEDleemskanrqITEAEAQKM-KEGALIVVEGqkRLIeeiitrkklkqsyeyevsFKGLSSSENI----WLPRDE 863
Cdd:cd03224 58 RFD-GRD----------ITGLPPHERaRAGIGYVPEG--RRI------------------FPELTVEENLllgaYARRRA 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 864 LVKRGFEkKVIEV----DTREAQRLGLlrplvrreiekhfadfglepefvshntmrgLSGGQKVKIVLGAATWRRPHVIC 939
Cdd:cd03224 107 KRKARLE-RVYELfprlKERRKQLAGT------------------------------LSGGEQQMLAIARALMSRPKLLL 155
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1933195014 940 LDEPTNYLD---RESLAALIAALKVFEGGVLIITHNRDFSESLCHEVWAMRDGRLEASG 995
Cdd:cd03224 156 LDEPSEGLApkiVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEG 214
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
870-990 |
3.55e-06 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 50.86 E-value: 3.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 870 EKKVIEVDT------REAQRLGLLRPLVR---REIEKHFADFglepefvSHNtmrgLSGGQKVKIVLGAATWRRPHVICL 940
Cdd:PRK15134 112 EKQLYEVLSlhrgmrREAARGEILNCLDRvgiRQAAKRLTDY-------PHQ----LSGGERQRVMIAMALLTRPELLIA 180
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1933195014 941 DEPTNYLDRESLAALIAALKVFEG----GVLIITHNRDFSESLCHEVWAMRDGR 990
Cdd:PRK15134 181 DEPTTALDVSVQAQILQLLRELQQelnmGLLFITHNLSIVRKLADRVAVMQNGR 234
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
465-641 |
3.58e-06 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 49.63 E-value: 3.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 465 YGAKILLNTATLRLKRGHRYGLCGKNGTGKSTLMRAI------TNGQVE---------GFPSPDEVRTF----------Y 519
Cdd:PRK11124 12 YGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLnllempRSGTLNiagnhfdfsKTPSDKAIRELrrnvgmvfqqY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 520 --------VEHDIdgsEADTSVLQfiLTDKRVLSSEAEIKEALASVGFNDERQKQaigsLSGGWKMKLALARAMLFKADI 591
Cdd:PRK11124 92 nlwphltvQQNLI---EAPCRVLG--LSKDQALARAEKLLERLRLKPYADRFPLH----LSGGQQQRVAIARALMMEPQV 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1933195014 592 LLLDEPTNHLD------VVNVAwLENYLTSLktcTSIIVSHDSGFLNNTITDVLHL 641
Cdd:PRK11124 163 LLFDEPTAALDpeitaqIVSII-RELAETGI---TQVIVTHEVEVARKTASRVVYM 214
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
465-994 |
3.94e-06 |
|
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: 50.59 E-value: 3.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 465 YGAKILLNTATLRLKRGHRYGLCGKNGTGKSTLMRAIT--------NGQV--EGFP------SPDEVRTFYVEHDIDGSE 528
Cdd:TIGR02633 11 FGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSgvyphgtwDGEIywSGSPlkasniRDTERAGIVIIHQELTLV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 529 ADTSVLQFI-----LTDKRVLSSEAEI----KEALASVGFNDERQKQAIGSLSGGWKMKLALARAMLFKADILLLDEPTN 599
Cdd:TIGR02633 91 PELSVAENIflgneITLPGGRMAYNAMylraKNLLRELQLDADNVTRPVGDYGGGQQQLVEIAKALNKQARLLILDEPSS 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 600 HLDVVNVAWLENYLTSLKT--CTSIIVSH---DSGFLNNTITDVLHLNRFKLRRYRGNLESFVKAVPEAKSYYSLEALED 674
Cdd:TIGR02633 171 SLTEKETEILLDIIRDLKAhgVACVYISHklnEVKAVCDTICVIRDGQHVATKDMSTMSEDDIITMMVGREITSLYPHEP 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 675 YKFKlpdppllegvktkeKSLLKMRKVGFQYPTQA-VQQLYDITLQVSLSSRVAILGPNGSGKSTLVKLLIGDMEPNKGG 753
Cdd:TIGR02633 251 HEIG--------------DVILEARNLTCWDVINPhRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKFEG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 754 EIWkhpnlvigyvaqhafhhidhhLDKTPLEymlwryqtgedleemskanrqiTEAEAQKMKEGALIVVEGQKRliEEII 833
Cdd:TIGR02633 317 NVF---------------------INGKPVD----------------------IRNPAQAIRAGIAMVPEDRKR--HGIV 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 834 TRkklkqsyeyevsfkgLSSSENIWLprdELVKRGFEKKVIEvdtrEAQRLGLLRPLVRREIEKHFADFglepefvshNT 913
Cdd:TIGR02633 352 PI---------------LGVGKNITL---SVLKSFCFKMRID----AAAELQIIGSAIQRLKVKTASPF---------LP 400
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 914 MRGLSGGQKVKIVLGAATWRRPHVICLDEPTNYLD---RESLAALIAALKvfEGGVLIITHNRDFSE--SLCHEVWAMRD 988
Cdd:TIGR02633 401 IGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDvgaKYEIYKLINQLA--QEGVAIIVVSSELAEvlGLSDRVLVIGE 478
|
....*.
gi 1933195014 989 GRLEAS 994
Cdd:TIGR02633 479 GKLKGD 484
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
696-752 |
4.18e-06 |
|
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: 50.82 E-value: 4.18e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1933195014 696 LKMRKVGFQYPTQAVQqLYDITLQVSLSSRVAILGPNGSGKSTLVKLLIGDMEPNKG 752
Cdd:TIGR02868 335 LELRDLSAGYPGAPPV-LDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQG 390
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
460-602 |
4.20e-06 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 49.02 E-value: 4.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 460 QFSLAYGAKILLNTATLRLKRGHRYGLCGKNGTGKSTLMRAITngqveGFPSPD---EVRTFYVEHDIDGSEADT----- 531
Cdd:COG4136 6 NLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIA-----GTLSPAfsaSGEVLLNGRRLTALPAEQrrigi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 532 -----------SVLQFIL--TDKRVLSSE--AEIKEALASVGFNDeRQKQAIGSLSGGWKMKLALARAMLFKADILLLDE 596
Cdd:COG4136 81 lfqddllfphlSVGENLAfaLPPTIGRAQrrARVEQALEEAGLAG-FADRDPATLSGGQRARVALLRALLAEPRALLLDE 159
|
....*.
gi 1933195014 597 PTNHLD 602
Cdd:COG4136 160 PFSKLD 165
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
462-598 |
4.40e-06 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 50.89 E-value: 4.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 462 SLAYGAKILLNTATLRLKRGHRYGLCGKNGTGKSTLM------RAITNGQVEGFpspdevrtfyvehdiDGSEADT---- 531
Cdd:NF033858 8 SHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLsliagaRKIQQGRVEVL---------------GGDMADArhrr 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 532 ---------------------SV---LQFILT----DKRvlSSEAEIKEALASVGFNDERQKQAiGSLSGGWKMKLALAR 583
Cdd:NF033858 73 avcpriaympqglgknlyptlSVfenLDFFGRlfgqDAA--ERRRRIDELLRATGLAPFADRPA-GKLSGGMKQKLGLCC 149
|
170
....*....|....*
gi 1933195014 584 AMLFKADILLLDEPT 598
Cdd:NF033858 150 ALIHDPDLLILDEPT 164
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
483-637 |
4.77e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 51.13 E-value: 4.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 483 RYGLCGKNGTGKSTLMRAItngqvegfpspdeVRTFYVEHD---IDGSEadtsVLQFILTD-KRVLS------------- 545
Cdd:PLN03232 1264 KVGVVGRTGAGKSSMLNAL-------------FRIVELEKGrimIDDCD----VAKFGLTDlRRVLSiipqspvlfsgtv 1326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 546 ----------SEAEIKEALASVGFNDERQKQAIG----------SLSGGWKMKLALARAMLFKADILLLDEPTNHLDVVN 605
Cdd:PLN03232 1327 rfnidpfsehNDADLWEALERAHIKDVIDRNPFGldaevseggeNFSVGQRQLLSLARALLRRSKILVLDEATASVDVRT 1406
|
170 180 190
....*....|....*....|....*....|...
gi 1933195014 606 VAWLENYL-TSLKTCTSIIVSHDSgflnNTITD 637
Cdd:PLN03232 1407 DSLIQRTIrEEFKSCTMLVIAHRL----NTIID 1435
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
476-603 |
4.78e-06 |
|
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: 48.87 E-value: 4.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 476 LRLKRGHRYGLCGKNGTGKSTLMRAITngqveGFPSPDEVRTFYVEHDIDGSEADTSVLQFILTD--------------- 540
Cdd:cd03299 20 LEVERGDYFVILGPTGSGKSVLLETIA-----GFIKPDSGKILLNGKDITNLPPEKRDISYVPQNyalfphmtvykniay 94
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1933195014 541 --KRVLSSEAEIKEA---LASVGFNDERQKQAIGSLSGGWKMKLALARAMLFKADILLLDEPTNHLDV 603
Cdd:cd03299 95 glKKRKVDKKEIERKvleIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDV 162
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
696-769 |
5.06e-06 |
|
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: 48.62 E-value: 5.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 696 LKMRKVGFQYPT--QAVQQLYDITLQVSLSSRVAILGPNGSGKSTLVKLLIGDMEPNKG-----GEIWKHPNLVIGYVAQ 768
Cdd:cd03293 1 LEVRNVSKTYGGggGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGevlvdGEPVTGPGPDRGYVFQ 80
|
.
gi 1933195014 769 H 769
Cdd:cd03293 81 Q 81
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
469-626 |
5.23e-06 |
|
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: 49.08 E-value: 5.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 469 ILLNTATLRLKRGHRYGLCGKNGTGKSTLMRAItngqvEGFPSPDEVRTFyvehdIDGSEADTSVLQFILTDKRVLSSE- 547
Cdd:cd03249 17 PILKGLSLTIPPGKTVALVGSSGCGKSTVVSLL-----ERFYDPTSGEIL-----LDGVDIRDLNLRWLRSQIGLVSQEp 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 548 ----AEIKEALAsVGFNDERQKQAI---------------------------GSLSGGWKMKLALARAMLFKADILLLDE 596
Cdd:cd03249 87 vlfdGTIAENIR-YGKPDATDEEVEeaakkanihdfimslpdgydtlvgergSQLSGGQKQRIAIARALLRNPKILLLDE 165
|
170 180 190
....*....|....*....|....*....|.
gi 1933195014 597 PTNHLDVVNVAWLENYLTSL-KTCTSIIVSH 626
Cdd:cd03249 166 ATSALDAESEKLVQEALDRAmKGRTTIVIAH 196
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
461-604 |
5.48e-06 |
|
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: 50.68 E-value: 5.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 461 FSLaYGAKILLNTaTLRLKRGHRYGLCGKNGTGKSTLMRAITnGQVEgfPSPDEVR-----TFYVEHD--IDGSEADTSV 533
Cdd:TIGR01271 434 FSL-YVTPVLKNI-SFKLEKGQLLAVAGSTGSGKSSLLMMIM-GELE--PSEGKIKhsgriSFSPQTSwiMPGTIKDNII 508
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1933195014 534 LQFILTDKRVLS--SEAEIKEALASVGfndERQKQAIG----SLSGGWKMKLALARAMLFKADILLLDEPTNHLDVV 604
Cdd:TIGR01271 509 FGLSYDEYRYTSviKACQLEEDIALFP---EKDKTVLGeggiTLSGGQRARISLARAVYKDADLYLLDSPFTHLDVV 582
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
475-627 |
6.07e-06 |
|
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: 49.67 E-value: 6.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 475 TLRLKRGHRYGLCGKNGTGKSTLMRAIT-----NGQVEGfpspdEVRtfYVEHDIDG-SEAD-----------------T 531
Cdd:COG0444 25 SFDVRRGETLGLVGESGSGKSTLARAILgllppPGITSG-----EIL--FDGEDLLKlSEKElrkirgreiqmifqdpmT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 532 S------VLQFI---LTDKRVLSSE---AEIKEALASVGFNDERQkqAIGS----LSGGwkMK--LALARAMLFKADILL 593
Cdd:COG0444 98 SlnpvmtVGDQIaepLRIHGGLSKAearERAIELLERVGLPDPER--RLDRypheLSGG--MRqrVMIARALALEPKLLI 173
|
170 180 190
....*....|....*....|....*....|....*..
gi 1933195014 594 LDEPTNHLDVVNVAWLENYLTSLK--TCTSII-VSHD 627
Cdd:COG0444 174 ADEPTTALDVTIQAQILNLLKDLQreLGLAILfITHD 210
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
696-756 |
6.14e-06 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 48.60 E-value: 6.14e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1933195014 696 LKMRKVGFQYPTQAVQqlydITLQVSLSSRVAILGPNGSGKSTLVKLLIGdMEPNKGGEIW 756
Cdd:COG3840 2 LRLDDLTYRYGDFPLR----FDLTIAAGERVAILGPSGAGKSTLLNLIAG-FLPPDSGRIL 57
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
914-995 |
6.26e-06 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 49.42 E-value: 6.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 914 MRGLSGGQKVKIVLGAATWRRPHVICLDEPTNYLDR-------ESLAALIAALKVfeggVLIITHNRDFSESLCHEVWAM 986
Cdd:PRK13537 136 VGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPqarhlmwERLRSLLARGKT----ILLTTHFMEEAERLCDRLCVI 211
|
....*....
gi 1933195014 987 RDGRLEASG 995
Cdd:PRK13537 212 EEGRKIAEG 220
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
456-627 |
7.03e-06 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 49.02 E-value: 7.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 456 LCNCQFSLAygAKILLNTATLRLKRGHRYGLCGKNGTGKSTLMR------------AITNGQ-VEGFPSPDEVRTF-YVE 521
Cdd:PRK10575 14 LRNVSFRVP--GRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKmlgrhqppsegeILLDAQpLESWSSKAFARKVaYLP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 522 HDIDGSEADT--------------SVLQFILTDKRvlsseaEIKEALASVGFNDERQKqAIGSLSGGWKMKLALAraMLF 587
Cdd:PRK10575 92 QQLPAAEGMTvrelvaigrypwhgALGRFGAADRE------KVEEAISLVGLKPLAHR-LVDSLSGGERQRAWIA--MLV 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1933195014 588 KAD--ILLLDEPTNHLDV---VNVAWLENYLTSLKTCTSIIVSHD 627
Cdd:PRK10575 163 AQDsrCLLLDEPTSALDIahqVDVLALVHRLSQERGLTVIAVLHD 207
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
713-773 |
7.08e-06 |
|
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: 47.93 E-value: 7.08e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 713 LYDITLQVSLSSRVAILGPNGSGKSTLVKLLIGD-MEPNKGGEIW--------KHPNLVIGYVAQHAFHH 773
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRrTGLGVSGEVLingrpldkRSFRKIIGYVPQDDILH 94
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
466-627 |
7.61e-06 |
|
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: 48.45 E-value: 7.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 466 GAKILLNTATLRLKRGHRYGLCGKNGTGKSTLMRAItNGQVEgfpsPDEVRTFYVEHDI---DGSEADTS---VLQFI-- 537
Cdd:cd03295 12 GGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMI-NRLIE----PTSGEIFIDGEDIreqDPVELRRKigyVIQQIgl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 538 ---LTDKR----VLS----SEAEIK----EALASVGFNDERQKQAI-GSLSGGWKMKLALARAMLFKADILLLDEPTNHL 601
Cdd:cd03295 87 fphMTVEEnialVPKllkwPKEKIReradELLALVGLDPAEFADRYpHELSGGQQQRVGVARALAADPPLLLMDEPFGAL 166
|
170 180
....*....|....*....|....*....
gi 1933195014 602 DVVNVAWLENYLTSLKTC---TSIIVSHD 627
Cdd:cd03295 167 DPITRDQLQEEFKRLQQElgkTIVFVTHD 195
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
695-995 |
7.71e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 49.03 E-value: 7.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 695 LLKMRKVGFQYpTQAVQQLYDITLQVSLSSRVAILGPNGSGKSTLVKLLIGDMEPnKGGEIwkhpnLVIGyvaqhafhhi 774
Cdd:PRK13652 3 LIETRDLCYSY-SGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKP-TSGSV-----LIRG---------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 775 dhhldktpleymlwryqtgedlEEMSKANrqiteaeaqkmkegalivvegqkrlIEEIitRKklkqsyeyevsFKGLSSS 854
Cdd:PRK13652 66 ----------------------EPITKEN-------------------------IREV--RK-----------FVGLVFQ 85
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 855 EniwlPRDELVKRGFEKKVIEVDTReaqrLGLLRPLVRREIEKHFADFGLEP--EFVSHNtmrgLSGGQKVKIVLGAATW 932
Cdd:PRK13652 86 N----PDDQIFSPTVEQDIAFGPIN----LGLDEETVAHRVSSALHMLGLEElrDRVPHH----LSGGEKKRVAIAGVIA 153
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1933195014 933 RRPHVICLDEPTNYLDRESLAALIAALKVF--EGGVLII--THNRDFSESLCHEVWAMRDGRLEASG 995
Cdd:PRK13652 154 MEPQVLVLDEPTAGLDPQGVKELIDFLNDLpeTYGMTVIfsTHQLDLVPEMADYIYVMDKGRIVAYG 220
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
726-971 |
8.72e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 49.81 E-value: 8.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 726 VAILGPNGSGKSTLVKLLIGDMEPNKGgeiwkhpnlvigyvaqhafhhidhhldktpleymlwRYQTGEDLEEMSKANRQ 805
Cdd:PRK13409 102 TGILGPNGIGKTTAVKILSGELIPNLG------------------------------------DYEEEPSWDEVLKRFRG 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 806 iTEAEA--QKMKEGALIVVegQK-RLIEEIitRKklkqsyeyevSFKGLSSseniwlprdELVKRGFEKKVI-EVdtreA 881
Cdd:PRK13409 146 -TELQNyfKKLYNGEIKVV--HKpQYVDLI--PK----------VFKGKVR---------ELLKKVDERGKLdEV----V 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 882 QRLGlLRPLVRREIEKhfadfglepefvshntmrgLSGG--QKVKIVlgAATWRRPHVICLDEPTNYLD---RESLAALI 956
Cdd:PRK13409 198 ERLG-LENILDRDISE-------------------LSGGelQRVAIA--AALLRDADFYFFDEPTSYLDirqRLNVARLI 255
|
250
....*....|....*.
gi 1933195014 957 AALKvfEG-GVLIITH 971
Cdd:PRK13409 256 RELA--EGkYVLVVEH 269
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
693-752 |
9.58e-06 |
|
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: 47.85 E-value: 9.58e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1933195014 693 KSLLKMRKVGFQYPTQ-AVQQLYDITLQVSLSSRVAILGPNGSGKSTLVKLLIGDMEPNKG 752
Cdd:cd03248 9 KGIVKFQNVTFAYPTRpDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGG 69
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
470-627 |
9.74e-06 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 48.27 E-value: 9.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 470 LLNTATLRLKRGHRYGLCGKNGTGKSTLMRAI------TNGQV--EGFP-------SPDEVRT-----FYVEHDI--DGS 527
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLggldtpTSGDVifNGQPmsklssaAKAELRNqklgfIYQFHHLlpDFT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 528 EADTSVLQFILTDKRVLSSEAEIKEALASVGFnDERQKQAIGSLSGGWKMKLALARAMLFKADILLLDEPTNHLDVVNVA 607
Cdd:PRK11629 104 ALENVAMPLLIGKKKPAEINSRALEMLAAVGL-EHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNAD 182
|
170 180
....*....|....*....|...
gi 1933195014 608 WLENYLTSL---KTCTSIIVSHD 627
Cdd:PRK11629 183 SIFQLLGELnrlQGTAFLVVTHD 205
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
713-995 |
1.01e-05 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 48.30 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 713 LYDITLQVSLSSRVAILGPNGSGKSTLVKLLIGdMEPNKgGEI---------WKHPNL--VIGYVAQH--------AFHH 773
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAG-LLPGQ-GEIllngrplsdWSAAELarHRAYLSQQqsppfampVFQY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 774 IDHHLDktpleymlwryqtgedleemskanrqiteaeaqkmkegALIVVEGQKRLIEEIitrkklkqsyeyevsfkglss 853
Cdd:COG4138 90 LALHQP--------------------------------------AGASSEAVEQLLAQL--------------------- 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 854 seniwlprdelvkrgfekkvievdtreAQRLGLLRPLVRReiekhfadfglepefVSHntmrgLSGG--QKVKIvlgAAT 931
Cdd:COG4138 111 ---------------------------AEALGLEDKLSRP---------------LTQ-----LSGGewQRVRL---AAV 140
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1933195014 932 ----WRR--PH--VICLDEPTNYLDRESLAALIAALKVF-EGGVLIITHNRDFSESL--CHEVWAMRDGRLEASG 995
Cdd:COG4138 141 llqvWPTinPEgqLLLLDEPMNSLDVAQQAALDRLLRELcQQGITVVMSSHDLNHTLrhADRVWLLKQGKLVASG 215
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
478-603 |
1.05e-05 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 49.23 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 478 LKRGHRYGLCGKNGTGKSTLMRAI------TNGQVEGFPSPDEVRT---------FYVEHDI--DGSEADTSVLQFI-LT 539
Cdd:PRK10762 275 LRKGEILGVSGLMGAGRTELMKVLygalprTSGYVTLDGHEVVTRSpqdglangiVYISEDRkrDGLVLGMSVKENMsLT 354
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1933195014 540 DKRVLSSEA-EIKEA--LASVG-----FN--DERQKQAIGSLSGGWKMKLALARAMLFKADILLLDEPTNHLDV 603
Cdd:PRK10762 355 ALRYFSRAGgSLKHAdeQQAVSdfirlFNikTPSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDV 428
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
882-1010 |
1.06e-05 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 48.43 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 882 QRLGLLRPLVRREIEKHFADFGLEP----EFVSHntmrgLSGGQKVKIVLGAATWRRPHVICLDEPTNYLDRESLAALIA 957
Cdd:PRK10619 119 QVLGLSKQEARERAVKYLAKVGIDEraqgKYPVH-----LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLR 193
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1933195014 958 AL-KVFEGG--VLIITHNRDFSESLCHEVWAMRDGRLEASGH-NWVEGQGSGPRIDK 1010
Cdd:PRK10619 194 IMqQLAEEGktMVVVTHEMGFARHVSSHVIFLHQGKIEEEGApEQLFGNPQSPRLQQ 250
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
695-991 |
1.10e-05 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 49.25 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 695 LLKMRKVGFQYPtqAVQQLYDITLQVSLSSRVAILGPNGSGKSTLVKLLIGDMEPNKgGEIW--------KHPN----LV 762
Cdd:COG3845 5 ALELRGITKRFG--GVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDS-GEILidgkpvriRSPRdaiaLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 763 IGYVAQHafhhidhhldktpleYMLwryqtgedleemskanrqiteaeaqkmkegalivvegqkrlieeiitrkklkqsy 842
Cdd:COG3845 82 IGMVHQH---------------FML------------------------------------------------------- 91
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 843 eyevsFKGLSSSENIWLPRDELvKRGFekkvieVDTREAqrlgllrplvRREIEKHFADFGLE--PEFVSHNtmrgLSGG 920
Cdd:COG3845 92 -----VPNLTVAENIVLGLEPT-KGGR------LDRKAA----------RARIRELSERYGLDvdPDAKVED----LSVG 145
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1933195014 921 --QKVKIVLgaATWRRPHVICLDEPTNYLDRESLAALIAALKVF--EG-GVLIITHnrDFSE--SLCHEVWAMRDGRL 991
Cdd:COG3845 146 eqQRVEILK--ALYRGARILILDEPTAVLTPQEADELFEILRRLaaEGkSIIFITH--KLREvmAIADRVTVLRRGKV 219
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
696-991 |
1.23e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 48.29 E-value: 1.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 696 LKMRKVGFQY----PTQAvQQLYDITLQVSLSSRVAILGPNGSGKSTLVKLLIGDMEPNKGgeiwkhpnlvigyvaqhaf 771
Cdd:PRK13641 3 IKFENVDYIYspgtPMEK-KGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSG------------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 772 hhidhhldktpleymlwryqtgedleEMSKANRQITEAEAQKmkegalivveGQKRLieeiitRKKLKQSYEYevsfkgl 851
Cdd:PRK13641 63 --------------------------TITIAGYHITPETGNK----------NLKKL------RKKVSLVFQF------- 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 852 ssseniwlPRDELvkrgFEKKVIEVDTREAQRLGLLRPLVRREIEKHFADFGLEPEFVSHNTMRgLSGGQKVKIVLGAAT 931
Cdd:PRK13641 94 --------PEAQL----FENTVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSEDLISKSPFE-LSGGQMRRVAIAGVM 160
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1933195014 932 WRRPHVICLDEPTNYLDRESLAALIAALKVFEGG---VLIITHNRDFSESLCHEVWAMRDGRL 991
Cdd:PRK13641 161 AYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAghtVILVTHNMDDVAEYADDVLVLEHGKL 223
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
488-615 |
1.28e-05 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 47.54 E-value: 1.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 488 GKNGTGKSTLMRAIT------NGQVE--GFPSPDEVRTFYVEH--DIDGSEADTSVLQFI-----LTDKRVLSSEAEike 552
Cdd:PRK13543 44 GDNGAGKTTLLRVLAgllhveSGQIQidGKTATRGDRSRFMAYlgHLPGLKADLSTLENLhflcgLHGRRAKQMPGS--- 120
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1933195014 553 ALASVGFNDERQKqAIGSLSGGWKMKLALARAMLFKADILLLDEPTNHLDVVNVAWLENYLTS 615
Cdd:PRK13543 121 ALAIVGLAGYEDT-LVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITLVNRMISA 182
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
914-981 |
1.28e-05 |
|
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: 47.22 E-value: 1.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 914 MRG-LSGGQKVKI----------VLGAatwrRPHVICLDEPTNYLDRE----SLAALIAALKVFEGG-VLIITHNRDFSE 977
Cdd:cd03240 112 MRGrCSGGEKVLAsliirlalaeTFGS----NCGILALDEPTTNLDEEnieeSLAEIIEERKSQKNFqLIVITHDEELVD 187
|
....
gi 1933195014 978 SLCH 981
Cdd:cd03240 188 AADH 191
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
694-995 |
1.32e-05 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 47.82 E-value: 1.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 694 SLLKMRKVGFQYPTQAVqqLYDITLQVSLSSRVAILGPNGSGKSTLVKLL------------IGDMEPNKGGEIWKHPNL 761
Cdd:PRK11264 2 SAIEVKNLVKKFHGQTV--LHGIDLEVKPGEVVAIIGPSGSGKTTLLRCInlleqpeagtirVGDITIDTARSLSQQKGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 762 V------IGYVAQHaFHHIDHhldKTPLEYMLwryqtgedleemskanrqiteaeaqkmkEGALIVvegqkrlieeiitr 835
Cdd:PRK11264 80 IrqlrqhVGFVFQN-FNLFPH---RTVLENII----------------------------EGPVIV-------------- 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 836 kklkqsyeyevsfKGLssseniwlPRDELVKRGfekkvievdtreaqrlgllrplvrREIekhFADFGLEPEFVSHNtmR 915
Cdd:PRK11264 114 -------------KGE--------PKEEATARA------------------------REL---LAKVGLAGKETSYP--R 143
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 916 GLSGGQKVKIVLGAATWRRPHVICLDEPTNYLDRE---SLAALIAALKVFEGGVLIITHNRDFSESLCHEVWAMRDGRLE 992
Cdd:PRK11264 144 RLSGGQQQRVAIARALAMRPEVILFDEPTSALDPElvgEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIV 223
|
...
gi 1933195014 993 ASG 995
Cdd:PRK11264 224 EQG 226
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
546-626 |
1.33e-05 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 49.19 E-value: 1.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 546 SEAEIKEALASVGFND--ERQKQ----AIG----SLSGGWKMKLALARAMLFKADILLLDEPTNHLDVVNVAWLENYLTS 615
Cdd:PRK13657 437 TDEEMRAAAERAQAHDfiERKPDgydtVVGergrQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDE 516
|
90
....*....|..
gi 1933195014 616 L-KTCTSIIVSH 626
Cdd:PRK13657 517 LmKGRTTFIIAH 528
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
470-630 |
1.39e-05 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 47.82 E-value: 1.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 470 LLNTATLRLKRGHRYGLCGKNGTGKSTLMRAITNgqvegFPSPDEVRTFYVEHDIDGSEA-------------------- 529
Cdd:PRK11264 18 VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINL-----LEQPEAGTIRVGDITIDTARSlsqqkglirqlrqhvgfvfq 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 530 ------DTSVLQFILTDKRVL------SSEAEIKEALASVGFNDeRQKQAIGSLSGGWKMKLALARAMLFKADILLLDEP 597
Cdd:PRK11264 93 nfnlfpHRTVLENIIEGPVIVkgepkeEATARARELLAKVGLAG-KETSYPRRLSGGQQQRVAIARALAMRPEVILFDEP 171
|
170 180 190
....*....|....*....|....*....|....*
gi 1933195014 598 TNHLDVVNVAWLENYLTSL--KTCTSIIVSHDSGF 630
Cdd:PRK11264 172 TSALDPELVGEVLNTIRQLaqEKRTMVIVTHEMSF 206
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
703-995 |
1.50e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 47.81 E-value: 1.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 703 FQYP--TQAvqqLYDITLQVSLSSRVAILGPNGSGKSTLVKLLIGDMEPNKGgeiwkhpnlvigyvaqhafhhidhhldk 780
Cdd:PRK13647 12 FRYKdgTKA---LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRG---------------------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 781 tpleymlwryqtgedleEMSKANRQITEAEAQKmkegalivVEGQKRLIEEIITRKKLKQSYEYEVSFKGLssseNIWLP 860
Cdd:PRK13647 61 -----------------RVKVMGREVNAENEKW--------VRSKVGLVFQDPDDQVFSSTVWDDVAFGPV----NMGLD 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 861 RDELVKRgfekkvievdTREAQRLgllrplVRREIEKHFADFglepefvsHntmrgLSGGQKVKIVLGAATWRRPHVICL 940
Cdd:PRK13647 112 KDEVERR----------VEEALKA------VRMWDFRDKPPY--------H-----LSYGQKKRVAIAGVLAMDPDVIVL 162
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1933195014 941 DEPTNYLD---RESLAALIAALKVFEGGVLIITHNRDFSESLCHEVWAMRDGRLEASG 995
Cdd:PRK13647 163 DEPMAYLDprgQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEG 220
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
464-626 |
1.62e-05 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 48.77 E-value: 1.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 464 AYGAKILLNTATLRLKRGHRYGLCGKNGTGKSTLMRAIT----NGQVEG--FPSPDEVRTfyveHDIDGSEA-------- 529
Cdd:PRK13549 14 TFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSgvypHGTYEGeiIFEGEELQA----SNIRDTERagiaiihq 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 530 ------DTSVLQFI----------LTDKRVLSSEAEikEALASVGFN-DERQKqaIGSLSGGWKMKLALARAMLFKADIL 592
Cdd:PRK13549 90 elalvkELSVLENIflgneitpggIMDYDAMYLRAQ--KLLAQLKLDiNPATP--VGNLGLGQQQLVEIAKALNKQARLL 165
|
170 180 190
....*....|....*....|....*....|....*...
gi 1933195014 593 LLDEPTNHLDVVNVAWLENYLTSLK----TCtsIIVSH 626
Cdd:PRK13549 166 ILDEPTASLTESETAVLLDIIRDLKahgiAC--IYISH 201
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
697-752 |
2.05e-05 |
|
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: 47.22 E-value: 2.05e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1933195014 697 KMRKVGFQYPTQaVQQLYDITLQVSLSSRVAILGPNGSGKSTLVKLLIGDMEPNKG 752
Cdd:cd03254 4 EFENVNFSYDEK-KPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKG 58
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
701-743 |
2.10e-05 |
|
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: 47.23 E-value: 2.10e-05
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1933195014 701 VGFQYPTQAVQQLYDITLQVSLSSRVAILGPNGSGKSTLVKLL 743
Cdd:cd03251 6 VTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLI 48
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
709-756 |
2.22e-05 |
|
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: 46.90 E-value: 2.22e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1933195014 709 AVQQLYDITLQVSLSSRVAILGPNGSGKSTLVKLLIGdMEPNKGGEIW 756
Cdd:COG0410 15 GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISG-LLPPRSGSIR 61
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
703-768 |
2.26e-05 |
|
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: 47.02 E-value: 2.26e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1933195014 703 FQYPTQaVQQLYDITLQV-----SLSSRVAILGPNGSGKSTLVKLLIGDMEPNKGGEIWkhPNLVIGYVAQ 768
Cdd:cd03237 1 YTYPTM-KKTLGEFTLEVeggsiSESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEI--ELDTVSYKPQ 68
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
695-756 |
2.68e-05 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 46.88 E-value: 2.68e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1933195014 695 LLKMRKVGFQYPTQAVQqlydITLQVSLSSRVAILGPNGSGKSTLVKLLIGDMEPnKGGEIW 756
Cdd:PRK10771 1 MLKLTDITWLYHHLPMR----FDLTVERGERVAILGPSGAGKSTLLNLIAGFLTP-ASGSLT 57
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
715-995 |
2.73e-05 |
|
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: 47.80 E-value: 2.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 715 DITLQVSLSSRVAILGPNGSGKSTLVKLLIGDMEPNKG-----GEIW----KHPNL-----VIGYVAQHA--FHHIDHhl 778
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGeivlnGRTLfdsrKGIFLppekrRIGYVFQEArlFPHLSV-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 779 dKTPLEYMLWRyQTGEDleemskanRQITEAeaqkmkegalivvegqkrlieeiitrkklkqsyeyevsfkglssseniw 858
Cdd:TIGR02142 93 -RGNLRYGMKR-ARPSE--------RRISFE------------------------------------------------- 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 859 lprdelvkrgfekKVIEVdtreaqrLGLlRPLVRREIEKhfadfglepefvshntmrgLSGGQKVKIVLGAATWRRPHVI 938
Cdd:TIGR02142 114 -------------RVIEL-------LGI-GHLLGRLPGR-------------------LSGGEKQRVAIGRALLSSPRLL 153
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1933195014 939 CLDEPTNYLDRESLAALIAALKV----FEGGVLIITHNRDFSESLCHEVWAMRDGRLEASG 995
Cdd:TIGR02142 154 LMDEPLAALDDPRKYEILPYLERlhaeFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAG 214
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
695-995 |
2.73e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 46.99 E-value: 2.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 695 LLKMRKVGFQYP--TQAvqqLYDITLQVSLSSRVAILGPNGSGKSTLVKLLIGDMEPNKGGEIwkhpnlvigyvaqhafh 772
Cdd:PRK13639 1 ILETRDLKYSYPdgTEA---LKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVL----------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 773 hidhhLDKTPLEYmlwryqtgeDLEEMSKANRQITeaeaqkmkegalIVVEGQKRLIeeiitrkkLKQSYEYEVSFKGLs 852
Cdd:PRK13639 61 -----IKGEPIKY---------DKKSLLEVRKTVG------------IVFQNPDDQL--------FAPTVEEDVAFGPL- 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 853 sseNIWLPRDELVKRgfekkvievdTREA-QRLGLLrplvrreiekhfadfGLEPEFVSHntmrgLSGGQKVKIVLGAAT 931
Cdd:PRK13639 106 ---NLGLSKEEVEKR----------VKEAlKAVGME---------------GFENKPPHH-----LSGGQKKRVAIAGIL 152
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1933195014 932 WRRPHVICLDEPTNYLDRESLAALIAALKVF--EGGVLII-THNRDFSESLCHEVWAMRDGRLEASG 995
Cdd:PRK13639 153 AMKPEIIVLDEPTSGLDPMGASQIMKLLYDLnkEGITIIIsTHDVDLVPVYADKVYVMSDGKIIKEG 219
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
696-995 |
2.81e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 47.32 E-value: 2.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 696 LKMRKVGFQYPTQ---AVQQLYDITLQVSLSSRVAILGPNGSGKSTLVKLLIGDMEPNKGgeiwkhpnlvigyvaqhafh 772
Cdd:PRK13634 3 ITFQKVEHRYQYKtpfERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSG-------------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 773 hidhhldktpleymlwRYQTGEDLEEMSKANRQIteaEAQKMKEGalIVV---EGQkrLIEEIItrkklkqsyEYEVSFk 849
Cdd:PRK13634 63 ----------------TVTIGERVITAGKKNKKL---KPLRKKVG--IVFqfpEHQ--LFEETV---------EKDICF- 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 850 glsSSENIWLPRDELVKRGfeKKVIEvdtreaqrlgllrpLVrreiekhfadfGLEPEFVSHNTMRgLSGGQKVKIVLGA 929
Cdd:PRK13634 110 ---GPMNFGVSEEDAKQKA--REMIE--------------LV-----------GLPEELLARSPFE-LSGGQMRRVAIAG 158
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1933195014 930 ATWRRPHVICLDEPTNYLD---RESLAALIAALKVfEGGVLII--THNRDFSESLCHEVWAMRDGRLEASG 995
Cdd:PRK13634 159 VLAMEPEVLVLDEPTAGLDpkgRKEMMEMFYKLHK-EKGLTTVlvTHSMEDAARYADQIVVMHKGTVFLQG 228
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
465-602 |
2.84e-05 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 47.00 E-value: 2.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 465 YGAKILLNTATLRLKRGHRYGLCGKNGTGKSTLMRAITngqveGFPSPDEVRTFYVEHDIDGSEADTSVL---QFILTDK 541
Cdd:PRK11248 11 YGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIA-----GFVPYQHGSITLDGKPVEGPGAERGVVfqnEGLLPWR 85
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1933195014 542 RVLSS---------------EAEIKEALASVGFnDERQKQAIGSLSGGWKMKLALARAMLFKADILLLDEPTNHLD 602
Cdd:PRK11248 86 NVQDNvafglqlagvekmqrLEIAHQMLKKVGL-EGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALD 160
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
917-995 |
3.08e-05 |
|
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: 46.42 E-value: 3.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 917 LSGGQKVKIVLGAATWRRPHVICLDEPTNYLDRESLAALIAALKVF--EGG--VLIITHNRDFSESLCHEVWAMRDGRLE 992
Cdd:cd03258 141 LSGGQKQRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDInrELGltIVLITHEMEVVKRICDRVAVMEKGEVV 220
|
...
gi 1933195014 993 ASG 995
Cdd:cd03258 221 EEG 223
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
914-971 |
3.10e-05 |
|
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: 46.00 E-value: 3.10e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1933195014 914 MRGLSGGQKVKIVLGAATWRRPHVICLDEPTNYLDRESLAALIAALK--VFEG-GVLIITH 971
Cdd:cd03213 109 LRGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRrlADTGrTIICSIH 169
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
694-756 |
3.14e-05 |
|
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: 46.66 E-value: 3.14e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1933195014 694 SLLKMRKVGFQYPTQA--VQQLYDITLQVSLSSRVAILGPNGSGKSTLVKLLIGdMEPNKGGEIW 756
Cdd:COG4181 7 PIIELRGLTKTVGTGAgeLTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAG-LDRPTSGTVR 70
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
569-632 |
3.21e-05 |
|
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: 47.82 E-value: 3.21e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1933195014 569 GSLSGGWKMKLALARAMLFKADILLLDEPTNHLDVVNVAWLENYLTSLKT--CTSIIVSHDSGFLN 632
Cdd:COG4618 466 ARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKArgATVVVITHRPSLLA 531
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
903-991 |
3.26e-05 |
|
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: 45.50 E-value: 3.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 903 GLEPEF-VSHNTM--RGLSGG--QKVkiVLGAATWRRPHVICLDEPTNYLD---RESLAALIAALKvfEGGVLIITHNRD 974
Cdd:cd03215 88 GLVLDLsVAENIAlsSLLSGGnqQKV--VLARWLARDPRVLILDEPTRGVDvgaKAEIYRLIRELA--DAGKAVLLISSE 163
|
90
....*....|....*....
gi 1933195014 975 FSE--SLCHEVWAMRDGRL 991
Cdd:cd03215 164 LDEllGLCDRILVMYEGRI 182
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
470-628 |
3.31e-05 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 46.31 E-value: 3.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 470 LLNTATLRLKRGHRYGLCGKNGTGKSTLMRAI------TNGQVEGFPSP-----DEVR-------------TFYVEHDID 525
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILaglddgSSGEVSLVGQPlhqmdEEARaklrakhvgfvfqSFMLIPTLN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 526 GSEadTSVLQFILTDKRVLSSEAEIKEALASVGFNdERQKQAIGSLSGGWKMKLALARAMLFKADILLLDEPTNHLDVVN 605
Cdd:PRK10584 105 ALE--NVELPALLRGESSRQSRNGAKALLEQLGLG-KRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQT 181
|
170 180
....*....|....*....|....*.
gi 1933195014 606 VAWLENYLTSLK---TCTSIIVSHDS 628
Cdd:PRK10584 182 GDKIADLLFSLNrehGTTLILVTHDL 207
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
695-995 |
3.31e-05 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 46.53 E-value: 3.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 695 LLKMRKVGFQYPTQAVqqLYDITLQVSLSSRVAILGPNGSGKSTLVKLLIGdMEPNKGGEIW----------KHPNLV-- 762
Cdd:COG1126 1 MIEIENLHKSFGDLEV--LKGISLDVEKGEVVVIIGPSGSGKSTLLRCINL-LEEPDSGTITvdgedltdskKDINKLrr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 763 -IGYVAQHA--FHHidhhldKTPLEymlwryqtgedleemskaNrqITEAeaqkmkegaLIVVEGqkrlieeiitrkklk 839
Cdd:COG1126 78 kVGMVFQQFnlFPH------LTVLE------------------N--VTLA---------PIKVKK--------------- 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 840 qsyeyevsfkglssseniwLPRDELVKRGfekkvievdtREA-QRLGLLrplvrreiekHFADfglepEFVSHntmrgLS 918
Cdd:COG1126 108 -------------------MSKAEAEERA----------MELlERVGLA----------DKAD-----AYPAQ-----LS 138
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 919 GGQK--VKIVlgaatwR----RPHVICLDEPTNYLDRE----------SLAAliaalkvfEG-GVLIITHNRDFSESLCH 981
Cdd:COG1126 139 GGQQqrVAIA------RalamEPKVMLFDEPTSALDPElvgevldvmrDLAK--------EGmTMVVVTHEMGFAREVAD 204
|
330
....*....|....
gi 1933195014 982 EVWAMRDGRLEASG 995
Cdd:COG1126 205 RVVFMDGGRIVEEG 218
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
912-971 |
3.83e-05 |
|
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: 46.38 E-value: 3.83e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1933195014 912 NTMRG-----LSGGQKVKIVLGAATWRRPHVICLDEPTNYLDRESLAALIAALKVFEGG--VLIITH 971
Cdd:cd03249 130 DTLVGergsqLSGGQKQRIAIARALLRNPKILLLDEATSALDAESEKLVQEALDRAMKGrtTIVIAH 196
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
696-995 |
4.23e-05 |
|
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: 45.67 E-value: 4.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 696 LKMRKVGFQYPTQAVqqLYDITLQVSLSSRVAILGPNGSGKSTLVKLLIGDMEPNkGGEIwkhpnlvigyvaqhafhhid 775
Cdd:cd03268 1 LKTNDLTKTYGKKRV--LDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPD-SGEI-------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 776 hhldktpleymlwrYQTGEDLEEMSKANRQIteaeaqkmkeGALIvvegqkrlieeiitrkklkqsyEYEVSFKGLSSSE 855
Cdd:cd03268 58 --------------TFDGKSYQKNIEALRRI----------GALI----------------------EAPGFYPNLTARE 91
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 856 NIwlprdelvkrgfekkvievdtreaQRLGLLRPLVRREIEKHFADFGLEPEfvSHNTMRGLSGGQKVKIVLGAATWRRP 935
Cdd:cd03268 92 NL------------------------RLLARLLGIRKKRIDEVLDVVGLKDS--AKKKVKGFSLGMKQRLGIALALLGNP 145
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1933195014 936 HVICLDEPTNYLDRESLA---ALIAALKVFEGGVLIITHNRDFSESLCHEVWAMRDGRLEASG 995
Cdd:cd03268 146 DLLILDEPTNGLDPDGIKelrELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
674-980 |
4.35e-05 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 47.00 E-value: 4.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 674 DYKFKLPDPPLLEGVKtkekSLLKMRKVgfqyPTQAVQqlyDITLQVSLSSRVAILGPNGSGKSTLVKLLIGDMEPNkGG 753
Cdd:COG4586 10 TYRVYEKEPGLKGALK----GLFRREYR----EVEAVD---DISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPT-SG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 754 EIwkhpnLVIGYVaqhafhhidhhldktPleymlWRYQtgedleemsKAN-RQITeaeaqkmkegaliVVEGQKrlieei 832
Cdd:COG4586 78 EV-----RVLGYV---------------P-----FKRR---------KEFaRRIG-------------VVFGQR------ 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 833 itrkklkqsyeyevsfkglssSENIW-LPrdelVKRGFE--KKVIEVDTRE-AQRLGLLRPLvrreiekhfadFGLEpEF 908
Cdd:COG4586 105 ---------------------SQLWWdLP----AIDSFRllKAIYRIPDAEyKKRLDELVEL-----------LDLG-EL 147
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1933195014 909 VshNTM-RGLSGGQKVKIVLGAATWRRPHVICLDEPTNYLDRESLAALIAALKVF--EGGVLII--THNRDFSESLC 980
Cdd:COG4586 148 L--DTPvRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYnrERGTTILltSHDMDDIEALC 222
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
728-995 |
4.37e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 46.77 E-value: 4.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 728 ILGPNGSGKSTLVKLLIGDMEPNKGgEIWKHpNLVIGyvaqhafHHIDhhldktpleymlwryqtgedleemskANRQIT 807
Cdd:PRK13631 57 IIGNSGSGKSTLVTHFNGLIKSKYG-TIQVG-DIYIG-------DKKN--------------------------NHELIT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 808 EAEAQKMKEGalivvegqKRLieeiitRKKLKQSYEYevsfkglssseniwlPRDELVKRGFEKKVIevdtREAQRLGLL 887
Cdd:PRK13631 102 NPYSKKIKNF--------KEL------RRRVSMVFQF---------------PEYQLFKDTIEKDIM----FGPVALGVK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 888 RPLVRREIEKHFADFGLEPEFVSHNTMrGLSGGQKVKIVLGAATWRRPHVICLDEPTNYLDRES---LAALIAALKVFEG 964
Cdd:PRK13631 149 KSEAKKLAKFYLNKMGLDDSYLERSPF-GLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGeheMMQLILDAKANNK 227
|
250 260 270
....*....|....*....|....*....|.
gi 1933195014 965 GVLIITHNRDFSESLCHEVWAMRDGRLEASG 995
Cdd:PRK13631 228 TVFVITHTMEHVLEVADEVIVMDKGKILKTG 258
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
695-972 |
4.74e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 46.52 E-value: 4.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 695 LLKMRKVGFQYPtQAVQQLYDITLQVSLSSRVAILGPNGSGKSTLVKLLIGDMEPNKGGEIWKhpnlvigyvaqhafhhi 774
Cdd:PRK13644 1 MIRLENVSYSYP-DGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVS----------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 775 dhhldktpleymlwryqtGEDLEEMSKanrqiteaeAQKMKEGALIVVEGQKrliEEIITRkklkqSYEYEVSFkglsSS 854
Cdd:PRK13644 63 ------------------GIDTGDFSK---------LQGIRKLVGIVFQNPE---TQFVGR-----TVEEDLAF----GP 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 855 ENIWLPRDElvkrgfekkvievdtreaqrlgllrplVRREIEKHFADFGLEPefVSHNTMRGLSGGQKVKIVLGAATWRR 934
Cdd:PRK13644 104 ENLCLPPIE---------------------------IRKRVDRALAEIGLEK--YRHRSPKTLSGGQGQCVALAGILTME 154
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1933195014 935 PHVICLDEPTNYLDRESLAALIAALK-VFEGG--VLIITHN 972
Cdd:PRK13644 155 PECLIFDEVTSMLDPDSGIAVLERIKkLHEKGktIVYITHN 195
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
543-603 |
4.79e-05 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 47.23 E-value: 4.79e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1933195014 543 VLSSEAEIKEALASVgfndERQK-------QAIGSLSGGWKMKLALARAMLFKADILLLDEPTNHLDV 603
Cdd:PRK13549 375 RIDDAAELKTILESI----QRLKvktaspeLAIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDV 438
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
713-774 |
5.07e-05 |
|
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: 45.79 E-value: 5.07e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1933195014 713 LYDITLQVSLSSRVAILGPNGSGKSTLVKLLIGdMEPNKGGEIWKHPNLV---------IGYVAQH--AFHHI 774
Cdd:cd03296 18 LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAG-LERPDSGTILFGGEDAtdvpvqernVGFVFQHyaLFRHM 89
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
551-627 |
5.48e-05 |
|
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: 45.89 E-value: 5.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 551 KEALASVGFnDERQKQAIGSLSGGWKMKLALARAMLFKADILLLDEPTNHLDVVNVAWLENYLTSLKT---CTSIIVSHD 627
Cdd:COG4181 128 RALLERVGL-GHRLDHYPAQLSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRergTTLVLVTHD 206
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
693-778 |
5.60e-05 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 47.09 E-value: 5.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 693 KSLLKMRKVGFQYPtqAVQQLYDITLQVSLSSRVAILGPNGSGKSTLVKLLIGDMEPNKGGEIwkhpnlvigyVAQHAFH 772
Cdd:PRK09700 3 TPYISMAGIGKSFG--PVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTIT----------INNINYN 70
|
....*.
gi 1933195014 773 HIDHHL 778
Cdd:PRK09700 71 KLDHKL 76
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
467-602 |
5.89e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 46.19 E-value: 5.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 467 AKILLNTATLRLKRGHRYGLCGKNGTGKSTLMRaitngQVEGFPSPDEVRTFYVEHDIDGSEADTS--------VLQF-- 536
Cdd:PRK13637 19 EKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQ-----HLNGLLKPTSGKIIIDGVDITDKKVKLSdirkkvglVFQYpe 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 537 -------ILTD-----KRVLSSEAEI----KEALASVGFNDERQK-QAIGSLSGGWKMKLALARAMLFKADILLLDEPTN 599
Cdd:PRK13637 94 yqlfeetIEKDiafgpINLGLSEEEIenrvKRAMNIVGLDYEDYKdKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTA 173
|
...
gi 1933195014 600 HLD 602
Cdd:PRK13637 174 GLD 176
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
713-756 |
6.16e-05 |
|
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: 45.21 E-value: 6.16e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1933195014 713 LYDITLQVSLSSRVAILGPNGSGKSTLVKLLIGDMEPN-KGGEIW 756
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKYEvTEGEIL 60
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
488-633 |
6.30e-05 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 44.66 E-value: 6.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 488 GKNGTGKSTLMRAItnGQVEGFPSPDEVRTFYVEhdiDGSEADTSVLQFILTDKRVLSSEAEIKeALAsvgfnderqkqa 567
Cdd:cd03227 28 GPNGSGKSTILDAI--GLALGGAQSATRRRSGVK---AGCIVAAVSAELIFTRLQLSGGEKELS-ALA------------ 89
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1933195014 568 igslsggwkmkLALARAMLFKADILLLDEPTNHLDVVNVAWLENYL--TSLKTCTSIIVSHDSGFLNN 633
Cdd:cd03227 90 -----------LILALASLKPRPLYILDEIDRGLDPRDGQALAEAIleHLVKGAQVIVITHLPELAEL 146
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
671-753 |
6.32e-05 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 46.89 E-value: 6.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 671 ALEDYKFKLPDPPLLEGVKTkekslLKMRKVGFQYPTQAVQqLYDITLQVSLSSRVAILGPNGSGKSTLVKLLIGDMEPN 750
Cdd:PRK10522 303 ALAPYKAEFPRPQAFPDWQT-----LELRNVTFAYQDNGFS-VGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQ 376
|
...
gi 1933195014 751 KGG 753
Cdd:PRK10522 377 SGE 379
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
547-627 |
6.38e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 45.80 E-value: 6.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 547 EAEIKEALASVGFNDERQKQAIgSLSGGWKMKLALARAMLFKADILLLDEPTNHLDVVNVAWLENYLTSLK---TCTSII 623
Cdd:PRK14258 128 ESALKDADLWDEIKHKIHKSAL-DLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRlrsELTMVI 206
|
....
gi 1933195014 624 VSHD 627
Cdd:PRK14258 207 VSHN 210
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
468-693 |
6.74e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 45.98 E-value: 6.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 468 KILLNTATLRLKRGHRYGLCGKNGTGKSTLMRAItNGQVEgfPSPDEVrtfyvehDIDGSE--ADTS------------- 532
Cdd:PRK13641 20 KKGLDNISFELEEGSFVALVGHTGSGKSTLMQHF-NALLK--PSSGTI-------TIAGYHitPETGnknlkklrkkvsl 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 533 VLQF---------ILTD-----KRVLSSEAEIKEA----LASVGFNDERQKQAIGSLSGGWKMKLALARAMLFKADILLL 594
Cdd:PRK13641 90 VFQFpeaqlfentVLKDvefgpKNFGFSEDEAKEKalkwLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 595 DEPTNHLDVVN----VAWLENYLTSLKTCtsIIVSHDSGFLNNTITDVLHLNRFKLRRYRGNLESFVKAVPEAKSYYSLE 670
Cdd:PRK13641 170 DEPAAGLDPEGrkemMQLFKDYQKAGHTV--ILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDKEWLKKHYLDEP 247
|
250 260 270
....*....|....*....|....*....|....*
gi 1933195014 671 A-------LEDYKFKLPDPP-----LLEGVKTKEK 693
Cdd:PRK13641 248 AtsrfaskLEKGGFKFSEMPltideLVDGIKNNLK 282
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
466-616 |
6.80e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 45.95 E-value: 6.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 466 GAKILLNTATLRLKRGHRYGLCGKNGTGKSTLMRAI------TNGQV--EGFP----SPDEVRTF--YVEHDIDGSEADT 531
Cdd:PRK13652 15 GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFngilkpTSGSVliRGEPitkeNIREVRKFvgLVFQNPDDQIFSP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 532 SVLQFILTDKRVLSSEAE-----IKEALASVGFNDERQKqAIGSLSGGWKMKLALARAMLFKADILLLDEPTNHLDVVNV 606
Cdd:PRK13652 95 TVEQDIAFGPINLGLDEEtvahrVSSALHMLGLEELRDR-VPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGV 173
|
170
....*....|
gi 1933195014 607 AWLENYLTSL 616
Cdd:PRK13652 174 KELIDFLNDL 183
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
460-602 |
7.25e-05 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 46.33 E-value: 7.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 460 QFSLAYGAKILLNTATLRLKRGHRYGLCGKNGTGKSTLMRAI------TNGQVEgfpspdevrtfyvehdIDGSEADT-S 532
Cdd:PRK11153 10 VFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCInllerpTSGRVL----------------VDGQDLTAlS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 533 VLQFILTDKRV---------LSS-----------------EAEIK----EALASVGFNDERQK---QaigsLSGGWKMKL 579
Cdd:PRK11153 74 EKELRKARRQIgmifqhfnlLSSrtvfdnvalplelagtpKAEIKarvtELLELVGLSDKADRypaQ----LSGGQKQRV 149
|
170 180
....*....|....*....|...
gi 1933195014 580 ALARAMLFKADILLLDEPTNHLD 602
Cdd:PRK11153 150 AIARALASNPKVLLCDEATSALD 172
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
691-756 |
7.54e-05 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 45.91 E-value: 7.54e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1933195014 691 KEKSLLKMRKVGFQYPTQAVqqLYDITLQVSLSSRVAILGPNGSGKSTLVKLLIGDMEPNKgGEIW 756
Cdd:PRK11831 3 SVANLVDMRGVSFTRGNRCI--FDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDH-GEIL 65
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
551-701 |
7.61e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 45.85 E-value: 7.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 551 KEALASVGFNDERQKQAIGSLSGGWKMKLALARAMLFKADILLLDEPTNHLDVVNVAWLENYLTSL--KTCTSIIVSHDs 628
Cdd:PRK13651 146 AKYIELVGLDESYLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLnkQGKTIILVTHD- 224
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1933195014 629 gfLNNtitdVLHLNRFKLRRYRGnlesfvKAVPEAKSYyslEALEDYKF----KLPDPPLLEGVKTKEKSLLKMRKV 701
Cdd:PRK13651 225 --LDN----VLEWTKRTIFFKDG------KIIKDGDTY---DILSDNKFlienNMEPPKLLNFVNKLEKKGIDVPKV 286
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
475-602 |
8.01e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 45.89 E-value: 8.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 475 TLRLKRGHRYGLCGKNGTGKSTLMRaITNGQVegFPSPDEVRTFYVEHDIDGSEADTS--------VLQFI---LTDKRV 543
Cdd:PRK13649 27 NLTIEDGSYTAFIGHTGSGKSTIMQ-LLNGLH--VPTQGSVRVDDTLITSTSKNKDIKqirkkvglVFQFPesqLFEETV 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1933195014 544 L---------------SSEAEIKEALASVGFNDERQKQAIGSLSGGWKMKLALARAMLFKADILLLDEPTNHLD 602
Cdd:PRK13649 104 LkdvafgpqnfgvsqeEAEALAREKLALVGISESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLD 177
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
488-602 |
8.97e-05 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 45.24 E-value: 8.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 488 GKNGTGKSTLMRAITngqveGFPSPDEVRTFYVEHDIDGSEADTSV----------------LQFILTDKRVLSSE--AE 549
Cdd:COG4525 40 GASGCGKTTLLNLIA-----GFLAPSSGEITLDGVPVTGPGADRGVvfqkdallpwlnvldnVAFGLRLRGVPKAErrAR 114
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1933195014 550 IKEALASVGFNDERQKqAIGSLSGGWKMKLALARAMLFKADILLLDEPTNHLD 602
Cdd:COG4525 115 AEELLALVGLADFARR-RIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALD 166
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
471-627 |
1.01e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 45.51 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 471 LNTATLRLKRGHRYGLCGKNGTGKSTLMRAITngqveGFPSPDEVRTFYVEHDID-----------------------GS 527
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMI-----GIEKVKSGEIFYNNQAITddnfeklrkhigivfqnpdnqfvGS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 528 EADTSVlQFILTDKRVLSSE--AEIKEALASVGFNDERQKQAiGSLSGGWKMKLALARAMLFKADILLLDEPTNHLDV-- 603
Cdd:PRK13648 100 IVKYDV-AFGLENHAVPYDEmhRRVSEALKQVDMLERADYEP-NALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPda 177
|
170 180
....*....|....*....|....*
gi 1933195014 604 -VNVAWLENYLTSLKTCTSIIVSHD 627
Cdd:PRK13648 178 rQNLLDLVRKVKSEHNITIISITHD 202
|
|
| CD_DDE_transposase_like |
cd18978 |
chromodomain of Rhizopus microsporus putative DDE transposases, and similar proteins; This ... |
829-862 |
1.28e-04 |
|
chromodomain of Rhizopus microsporus putative DDE transposases, and similar proteins; This subgroup includes the CHROMO (CHRromatin Organization Modifier) domain found in Rhizopus microsporus putative DDE transposases, and similar proteins. The chromodomain, is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain.
Pssm-ID: 349334 Cd Length: 52 Bit Score: 40.76 E-value: 1.28e-04
10 20 30
....*....|....*....|....*....|....
gi 1933195014 829 IEEIITRKKLKQSYEYEVSFKGLSSSENIWLPRD 862
Cdd:cd18978 6 VEKIINHRGEKNRRKYLVKWKGYDDTDNSWVTQE 39
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
465-627 |
1.30e-04 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 45.45 E-value: 1.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 465 YGAKILLNTATLRLKRGHRYGLCGKNGTGKSTLMRAI------TNGQVEgfpspdevrtfyvehdIDGSEADT------- 531
Cdd:COG3839 13 YGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIagledpTSGEIL----------------IGGRDVTDlppkdrn 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 532 --------------SV---LQFILTDKRVlsSEAEIK----EALASVG---FNDERQKQaigsLSGGWKMKLALARAMLF 587
Cdd:COG3839 77 iamvfqsyalyphmTVyenIAFPLKLRKV--PKAEIDrrvrEAAELLGledLLDRKPKQ----LSGGQRQRVALGRALVR 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1933195014 588 KADILLLDEPTNHLDvvnvAWLENYL--------TSLKTcTSIIVSHD 627
Cdd:COG3839 151 EPKVFLLDEPLSNLD----AKLRVEMraeikrlhRRLGT-TTIYVTHD 193
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
461-603 |
1.33e-04 |
|
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: 45.23 E-value: 1.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 461 FSLaYGAKILLNTaTLRLKRGHRYGLCGKNGTGKSTLMRAITnGQVEgfPSPDEVR-------TFYVEHDIDGSEADTSV 533
Cdd:cd03291 45 LCL-VGAPVLKNI-NLKIEKGEMLAITGSTGSGKTSLLMLIL-GELE--PSEGKIKhsgrisfSSQFSWIMPGTIKENII 119
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1933195014 534 LQFILTDKRVLS--SEAEIKEALASVGfndERQKQAIG----SLSGGWKMKLALARAMLFKADILLLDEPTNHLDV 603
Cdd:cd03291 120 FGVSYDEYRYKSvvKACQLEEDITKFP---EKDNTVLGeggiTLSGGQRARISLARAVYKDADLYLLDSPFGYLDV 192
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
699-752 |
1.33e-04 |
|
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: 44.53 E-value: 1.33e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1933195014 699 RKVGFQYPTqAVQQLYDITLQVSLSSRVAILGPNGSGKSTLVKLLIGDMEPNKG 752
Cdd:cd03253 4 ENVTFAYDP-GRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSG 56
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
688-971 |
1.64e-04 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 45.78 E-value: 1.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 688 VKTKEKSLLKMRKVGFQYPTQAVQQLYDITLQVSLSSRVAILGPNGSGKSTLVKLLIGDMEPNKgGEIWkhpnlvigyva 767
Cdd:PRK11176 334 VIERAKGDIEFRNVTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDE-GEIL----------- 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 768 qhafhhidhhLDktpleymlwryqtGEDLEEMSKAN--RQITeaeaqkmkegaliVVEGQKRLIEEIItrkklkqsyeye 845
Cdd:PRK11176 402 ----------LD-------------GHDLRDYTLASlrNQVA-------------LVSQNVHLFNDTI------------ 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 846 vsfkglssSENIWLPRDELvkrgFEKKVIEVDTREAQRLGLlrplvrreIEKhfADFGLepefvshNTMRG-----LSGG 920
Cdd:PRK11176 434 --------ANNIAYARTEQ----YSREQIEEAARMAYAMDF--------INK--MDNGL-------DTVIGengvlLSGG 484
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1933195014 921 QKVKIVLGAATWRRPHVICLDEPTNYLDRESLAALIAALKVFEGG--VLIITH 971
Cdd:PRK11176 485 QRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNrtSLVIAH 537
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
650-756 |
1.69e-04 |
|
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: 45.56 E-value: 1.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 650 RGNLESFVKAVPE-AKSYYSLEALEDYKFKL--PDPPLLEGVKTKEKSL---LKMRKVGFQYPTQAVQQLY-----DITL 718
Cdd:COG4615 276 RGPLSQLVGALPTlSRANVALRKIEELELALaaAEPAAADAAAPPAPADfqtLELRGVTYRYPGEDGDEGFtlgpiDLTI 355
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1933195014 719 QvslssR---VAILGPNGSGKSTLVKLLIGDMEPNkGGEIW 756
Cdd:COG4615 356 R-----RgelVFIVGGNGSGKSTLAKLLTGLYRPE-SGEIL 390
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
488-624 |
1.83e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 43.71 E-value: 1.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 488 GKNGTGKSTLMRAIT-------------NGQVEGFPSPdevRTFYVEHDIdGSEADTSVLQFILTDKRVLSSEAEIKEAL 554
Cdd:PRK13541 33 GANGCGKSSLLRMIAgimqpssgniyykNCNINNIAKP---YCTYIGHNL-GLKLEMTVFENLKFWSEIYNSAETLYAAI 108
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 555 ASVGFNDERQKQAIgSLSGGWKMKLALARAMLFKADILLLDEPTNHLDVVNVAWLENyLTSLKTCTSIIV 624
Cdd:PRK13541 109 HYFKLHDLLDEKCY-SLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNN-LIVMKANSGGIV 176
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
726-971 |
1.88e-04 |
|
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: 45.55 E-value: 1.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 726 VAILGPNGSGKSTLVKLLIGDMEPNKGgeiwkhpnlvigyvaqhafhhidhhldktpleymlwRYQTGEDLEEMSKANRQ 805
Cdd:COG1245 102 TGILGPNGIGKSTALKILSGELKPNLG------------------------------------DYDEEPSWDEVLKRFRG 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 806 iTEAEA--QKMKEGALIVVegqkrlieeiitrkkLKQSYEYEVS--FKGLSSseniwlprdELVKRGFEKKVI-EVdtre 880
Cdd:COG1245 146 -TELQDyfKKLANGEIKVA---------------HKPQYVDLIPkvFKGTVR---------ELLEKVDERGKLdEL---- 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 881 AQRLGlLRPLVRREIEKhfadfglepefvshntmrgLSGG--QKVKIVlgAATWRRPHVICLDEPTNYLD---RESLAAL 955
Cdd:COG1245 197 AEKLG-LENILDRDISE-------------------LSGGelQRVAIA--AALLRDADFYFFDEPSSYLDiyqRLNVARL 254
|
250
....*....|....*.
gi 1933195014 956 IAALKVFEGGVLIITH 971
Cdd:COG1245 255 IRELAEEGKYVLVVEH 270
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
713-972 |
1.88e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 44.27 E-value: 1.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 713 LYDITLQVSLSSRVAILGPNGSGKSTLVKLLigdmepnkggeiwkhpnlvigyvaqhafhhidhhldktpleymlwryqt 792
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVL------------------------------------------------- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 793 gedleemskaNRQITEAEAQKMKEGALIVVEGQKRLIEEIITRKKLKQSYEYEVSFKGLSSSENIWLPrdeLVKRGFEKK 872
Cdd:PRK14246 57 ----------NRLIEIYDSKIKVDGKVLYFGKDIFQIDAIKLRKEVGMVFQQPNPFPHLSIYDNIAYP---LKSHGIKEK 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 873 vievdtREAQRLgllrplvrreIEKHFADFGLEPEFVS--HNTMRGLSGGQKVKIVLGAATWRRPHVICLDEPTNYLD-- 948
Cdd:PRK14246 124 ------REIKKI----------VEECLRKVGLWKEVYDrlNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDiv 187
|
250 260
....*....|....*....|....*
gi 1933195014 949 -RESLAALIAALKVfEGGVLIITHN 972
Cdd:PRK14246 188 nSQAIEKLITELKN-EIAIVIVSHN 211
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
470-603 |
1.99e-04 |
|
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: 44.00 E-value: 1.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 470 LLNTATLRLKRGHRYGLCGKNGTGKSTLMRAITN------GQV--EGFPSPDEVRTFYveHDIDGSEADTSVL------- 534
Cdd:cd03248 29 VLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENfyqpqgGQVllDGKPISQYEHKYL--HSKVSLVGQEPVLfarslqd 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 535 --QFILTDKrvlsSEAEIKEALASVGFNDERQKQAIG----------SLSGGWKMKLALARAMLFKADILLLDEPTNHLD 602
Cdd:cd03248 107 niAYGLQSC----SFECVKEAAQKAHAHSFISELASGydtevgekgsQLSGGQKQRVAIARALIRNPQVLILDEATSALD 182
|
.
gi 1933195014 603 V 603
Cdd:cd03248 183 A 183
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
564-603 |
2.00e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 45.11 E-value: 2.00e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1933195014 564 QKQAIGSLSGGWKMKLALARAMLFKADILLLDEPTNHLDV 603
Cdd:PRK10982 385 HRTQIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDV 424
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
475-602 |
2.17e-04 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 43.80 E-value: 2.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 475 TLRLKRGHRYGLCGKNGTGKSTLMRAITngqveGFPSPDEVRTFyvehdIDGSE-ADTSVLQ---FILTDKRVLSSEAEI 550
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIA-----GFLTPASGSLT-----LNGQDhTTTPPSRrpvSMLFQENNLFSHLTV 88
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1933195014 551 KEALAsVGFN-------DERQK-QAI--------------GSLSGGWKMKLALARAMLFKADILLLDEPTNHLD 602
Cdd:PRK10771 89 AQNIG-LGLNpglklnaAQREKlHAIarqmgiedllarlpGQLSGGQRQRVALARCLVREQPILLLDEPFSALD 161
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
471-626 |
2.26e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 45.17 E-value: 2.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 471 LNTATLRLKRGHRYGLCGKNGTGKSTLMRAIT----NGQVEG---FpsPDEVRTFyveHDIDGSEADTSV-----LQFI- 537
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSgvypHGSYEGeilF--DGEVCRF---KDIRDSEALGIViihqeLALIp 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 538 ---LTDKRVLSSE-------------AEIKEALASVGFnDERQKQAIGSLSGGwKMKLA-LARAMLFKADILLLDEPTNH 600
Cdd:NF040905 92 ylsIAENIFLGNErakrgvidwnetnRRARELLAKVGL-DESPDTLVTDIGVG-KQQLVeIAKALSKDVKLLILDEPTAA 169
|
170 180
....*....|....*....|....*...
gi 1933195014 601 LDVVNVAWLENYLTSLKT--CTSIIVSH 626
Cdd:NF040905 170 LNEEDSAALLDLLLELKAqgITSIIISH 197
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
711-774 |
2.28e-04 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 44.69 E-value: 2.28e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1933195014 711 QQLYDITLQVSLSSRVAILGPNGSGKSTLVKLLIGdMEPNKGGEIWKHPNLV---------IGYVAQH--AFHHI 774
Cdd:PRK10851 16 QVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAG-LEHQTSGHIRFHGTDVsrlhardrkVGFVFQHyaLFRHM 89
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
694-995 |
2.29e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 44.41 E-value: 2.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 694 SLLKMRKVGFQYPTQAVQQLYDITLQVSLSSRVAILGPNGSGKSTLVKLLIGDMEPNkggeiwKHPNLVIgyvaqhafhh 773
Cdd:PRK13640 4 NIVEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPD------DNPNSKI---------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 774 idhHLDKTPLeymlwryqtgedleemskanrqiTEAEAQKMKEGALIVVEGQKrlieeiitRKKLKQSYEYEVSFkGLss 853
Cdd:PRK13640 68 ---TVDGITL-----------------------TAKTVWDIREKVGIVFQNPD--------NQFVGATVGDDVAF-GL-- 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 854 sENIWLPRDELVKrgFEKKVIEvdtreaqRLGLLrplvrreiekHFADfgLEPEFvshntmrgLSGGQKVKIVLGAATWR 933
Cdd:PRK13640 111 -ENRAVPRPEMIK--IVRDVLA-------DVGML----------DYID--SEPAN--------LSGGQKQRVAIAGILAV 160
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1933195014 934 RPHVICLDEPTNYLD---RESLAALIAALKVFEGGVLI-ITHNRDfSESLCHEVWAMRDGRLEASG 995
Cdd:PRK13640 161 EPKIIILDESTSMLDpagKEQILKLIRKLKKKNNLTVIsITHDID-EANMADQVLVLDDGKLLAQG 225
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
693-755 |
2.41e-04 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 44.01 E-value: 2.41e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 693 KSLLKMRKVG--FQYPT-----QAVQQLYDITLQVSLSSRVAILGPNGSGKSTLVKLLIGDMEPNkGGEI 755
Cdd:PRK15112 2 ETLLEVRNLSktFRYRTgwfrrQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPT-SGEL 70
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
569-603 |
2.49e-04 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 44.48 E-value: 2.49e-04
10 20 30
....*....|....*....|....*....|....*
gi 1933195014 569 GSLSGGWKMKLALARAMLFKADILLLDEPTNHLDV 603
Cdd:PRK11144 127 GSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDL 161
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
570-626 |
2.68e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 45.41 E-value: 2.68e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 570 SLSGGWKMKLALARAMLFKADILLLDEPTNHLDVVNVAWLENYLTSLKTC---TSIIVSH 626
Cdd:PTZ00265 1358 SLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKadkTIITIAH 1417
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
918-990 |
2.81e-04 |
|
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: 43.58 E-value: 2.81e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1933195014 918 SGGQKVKIVLGAATWRRPHVICLDEPTNYLD---RESLAALIAALKVfEGGVLI-ITHNRDFSESLCHEVWAMRDGR 990
Cdd:COG4778 154 SGGEQQRVNIARGFIADPPLLLLDEPTASLDaanRAVVVELIEEAKA-RGTAIIgIFHDEEVREAVADRVVDVTPFS 229
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
917-995 |
2.94e-04 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 44.44 E-value: 2.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 917 LSGGQKVKIVLGAATWRRPHVICLDEPTNYLDR-------ESLAALIAALKVfeggVLIITHNRDFSESLCHEVWAMRDG 989
Cdd:PRK13536 173 LSGGMKRRLTLARALINDPQLLILDEPTTGLDPharhliwERLRSLLARGKT----ILLTTHFMEEAERLCDRLCVLEAG 248
|
....*.
gi 1933195014 990 RLEASG 995
Cdd:PRK13536 249 RKIAEG 254
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
465-629 |
2.97e-04 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 43.92 E-value: 2.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 465 YGAKILLNTATLRLKRGHRYGLCGKNGTGKSTLMRAI----------TNGQV--EGFP-SPDEVRTFYVEHDIDGSEADT 531
Cdd:PRK10418 13 QAAQPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAAlgilpagvrqTAGRVllDGKPvAPCALRGRKIATIMQNPRSAF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 532 SVLQFILTDKR-------VLSSEAEIKEALASVGF-NDERQKQAIG-SLSGGWKMKLALARAMLFKADILLLDEPTNHLD 602
Cdd:PRK10418 93 NPLHTMHTHARetclalgKPADDATLTAALEAVGLeNAARVLKLYPfEMSGGMLQRMMIALALLCEAPFIIADEPTTDLD 172
|
170 180 190
....*....|....*....|....*....|
gi 1933195014 603 VVNVAWLENYLTSL---KTCTSIIVSHDSG 629
Cdd:PRK10418 173 VVAQARILDLLESIvqkRALGMLLVTHDMG 202
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
672-743 |
3.05e-04 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 44.57 E-value: 3.05e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1933195014 672 LEDYKFKLPDPPLLEGVKtKEKSLLKMRKVGFQYPTQAvQQLYDITLQVSLSSRVAILGPNGSGKSTLVKLL 743
Cdd:PRK13657 312 VEDAVPDVRDPPGAIDLG-RVKGAVEFDDVSFSYDNSR-QGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLL 381
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
693-752 |
3.10e-04 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 43.55 E-value: 3.10e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 693 KSLLKMRKVGFQYPTQAVqqLYDITLQVSLSSRVAILGPNGSGKSTLVKLLIGDMEPNKG 752
Cdd:PRK10247 5 SPLLQLQNVGYLAGDAKI--LNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSG 62
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
458-634 |
3.19e-04 |
|
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: 44.94 E-value: 3.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 458 NCQFSLAYGAKILLNTATLRLKRGHRYGLCGKNGTGKSTLMRAI------------TNGQVEGFPSPDEVRTFYVEHDID 525
Cdd:TIGR00957 641 NATFTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALlaemdkveghvhMKGSVAYVPQQAWIQNDSLRENIL 720
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 526 GSEA-----DTSVLQF--ILTDKRVLSS--EAEIKEAlasvGFNderqkqaigsLSGGWKMKLALARAMLFKADILLLDE 596
Cdd:TIGR00957 721 FGKAlnekyYQQVLEAcaLLPDLEILPSgdRTEIGEK----GVN----------LSGGQKQRVSLARAVYSNADIYLFDD 786
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1933195014 597 PTNHLDV-VNVAWLENYLTS---LKTCTSIIVSHDSGFLNNT 634
Cdd:TIGR00957 787 PLSAVDAhVGKHIFEHVIGPegvLKNKTRILVTHGISYLPQV 828
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
570-626 |
3.23e-04 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 44.62 E-value: 3.23e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1933195014 570 SLSGGWKMKLALARAMLFKADILLLDEPTNHLDVVNVAWLENYLTSL-KTCTSIIVSH 626
Cdd:PRK11176 480 LLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELqKNRTSLVIAH 537
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
713-1000 |
3.89e-04 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 43.48 E-value: 3.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 713 LYDITLQVSLSSRVAILGPNGSGKSTLVKLLIGdmepnkggeiwkHPnlviGYvaqhafhhidhhldktpleymlwryqt 792
Cdd:CHL00131 23 LKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG------------HP----AY--------------------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 793 gedleemskanrQITEAEaqkmkegalIVVEGQKRLIEEIITRKKLK--QSYEYEVSFKGLSSSENIWLPRDElvKRGFE 870
Cdd:CHL00131 60 ------------KILEGD---------ILFKGESILDLEPEERAHLGifLAFQYPIEIPGVSNADFLRLAYNS--KRKFQ 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 871 KKViEVDTREAqrLGLLRP---LVrreiekhfadfGLEPEFVSHNTMRGLSGGQKVK------IVLgaatwrRPHVICLD 941
Cdd:CHL00131 117 GLP-ELDPLEF--LEIINEklkLV-----------GMDPSFLSRNVNEGFSGGEKKRneilqmALL------DSELAILD 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 942 EPTNYLDRESL---AALIAALKVFEGGVLIITH--------NRDFseslcheVWAMRDGR------------LEASGHNW 998
Cdd:CHL00131 177 ETDSGLDIDALkiiAEGINKLMTSENSIILITHyqrlldyiKPDY-------VHVMQNGKiiktgdaelakeLEKKGYDW 249
|
..
gi 1933195014 999 VE 1000
Cdd:CHL00131 250 LK 251
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
720-769 |
4.37e-04 |
|
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: 42.17 E-value: 4.37e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1933195014 720 VSLSSRVAILGPNGSGKSTLVKLLIGDMEPNKGGEIWkhPNLVIGYVAQH 769
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEW--DGITPVYKPQY 69
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
727-948 |
4.48e-04 |
|
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: 43.03 E-value: 4.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 727 AILGPNGSGKSTLVKLLIGDME--PNKGGEIWkhpnlvigyvaqhafhhidhhLDKTPLEYMLWRYQTGedleemskanr 804
Cdd:cd03234 37 AILGSSGSGKTTLLDAISGRVEggGTTSGQIL---------------------FNGQPRKPDQFQKCVA----------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 805 qiteaeaqkmkegaliVVEGQKRLIEEIITRkklkQSYEYEVSFKglssseniwLPRdelVKRGFEKKVIEVDTREAQrL 884
Cdd:cd03234 85 ----------------YVRQDDILLPGLTVR----ETLTYTAILR---------LPR---KSSDAIRKKRVEDVLLRD-L 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1933195014 885 GLLRplvrreiekhfadfglepefVSHNTMRGLSGGQKVKIVLGAATWRRPHVICLDEPTNYLD 948
Cdd:cd03234 132 ALTR--------------------IGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLD 175
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
695-991 |
4.72e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 43.16 E-value: 4.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 695 LLKMRKVGFQYPTQA-VQQLYDITLQVSLSSRVAILGPNGSGKSTLVKLLIGDMEPNKGgeiwkhpnlvigyvaqhafhh 773
Cdd:PRK13642 4 ILEVENLVFKYEKESdVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEG--------------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 774 idhhldktpleymlwryqtgedleemskanrqITEAEAQKMKEGALIVVEGQKRLIEEIITRKKLKQSYEYEVSFkglsS 853
Cdd:PRK13642 63 --------------------------------KVKIDGELLTAENVWNLRRKIGMVFQNPDNQFVGATVEDDVAF----G 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 854 SENIWLPRDELVKRGFEK----KVIEVDTREAQRLgllrplvrreiekhfadfglepefvshntmrglSGGQKVKIVLGA 929
Cdd:PRK13642 107 MENQGIPREEMIKRVDEAllavNMLDFKTREPARL---------------------------------SGGQKQRVAVAG 153
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1933195014 930 ATWRRPHVICLDEPTNYLD---RESLAALIAALK-VFEGGVLIITHNRDFSESlCHEVWAMRDGRL 991
Cdd:PRK13642 154 IIALRPEIIILDESTSMLDptgRQEIMRVIHEIKeKYQLTVLSITHDLDEAAS-SDRILVMKAGEI 218
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
917-996 |
4.75e-04 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 43.00 E-value: 4.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 917 LSGG--QKVKIvlgAAT----WRR--PH--VICLDEPTNYLDRESLAALIAALKVF-EGGVLIITHNRDFSESL--CHEV 983
Cdd:PRK03695 127 LSGGewQRVRL---AAVvlqvWPDinPAgqLLLLDEPMNSLDVAQQAALDRLLSELcQQGIAVVMSSHDLNHTLrhADRV 203
|
90
....*....|...
gi 1933195014 984 WAMRDGRLEASGH 996
Cdd:PRK03695 204 WLLKQGKLLASGR 216
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
711-991 |
6.13e-04 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 42.69 E-value: 6.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 711 QQLYDITLQVSLSSRVAILGPNGSGKSTLVKLLigdmepnkggeiwkhpNLVigyvaqhafhhidhhldKTPleymlwry 790
Cdd:PRK11124 16 QALFDITLDCPQGETLVLLGPSGAGKSSLLRVL----------------NLL-----------------EMP-------- 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 791 QTGedleEMSKANRQITEAEAQKMKEGALIvvegqkrlieeiitRKKLK---QSYeyevsfkglssseNIWlPRDELVkr 867
Cdd:PRK11124 55 RSG----TLNIAGNHFDFSKTPSDKAIREL--------------RRNVGmvfQQY-------------NLW-PHLTVQ-- 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 868 gfeKKVIEVDTREaqrLGLLRPLVRREIEKHFADFGLEP---EFVSHntmrgLSGGQKVKIVLGAATWRRPHVICLDEPT 944
Cdd:PRK11124 101 ---QNLIEAPCRV---LGLSKDQALARAEKLLERLRLKPyadRFPLH-----LSGGQQQRVAIARALMMEPQVLLFDEPT 169
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1933195014 945 NYLDRESLAALIAALK-VFEGGV--LIITHNRDFSESLCHEVWAMRDGRL 991
Cdd:PRK11124 170 AALDPEITAQIVSIIReLAETGItqVIVTHEVEVARKTASRVVYMENGHI 219
|
|
| CD_CSD |
cd00024 |
CHROMO (CHRromatin Organization Modifier) domains and chromo shadow domains; Members of this ... |
829-864 |
6.88e-04 |
|
CHROMO (CHRromatin Organization Modifier) domains and chromo shadow domains; Members of this group are chromodomains or chromo shadow domains; these are SH3-fold-beta-barrel domains of the chromo-like superfamily. Chromodomains lack the first strand of the SH3-fold-beta-barrel, this first strand is altered by insertion in the chromo shadow domains. The chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and which appears to play a role in the functional organization of the eukaryotic nucleus. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. Chromodomain-containing proteins include: i) those having an N-terminal chromodomain followed by a related chromo shadow domain, such as Drosophila and human heterochromatin protein Su(var)205 (HP1), and mammalian modifier 1 and 2; ii) those having a single chromodomain, such as Drosophila protein Polycomb (Pc), mammalian modifier 3, human Mi-2 autoantigen, and several yeast and Caenorhabditis elegans proteins of unknown function; iii) those having paired tandem chromodomains, such as mammalian DNA-binding/helicase proteins CHD-1 to CHD-4 and yeast protein CHD1; (iv) and elongation factor eEF3, a member of the ATP-binding cassette (ABC) family of proteins, that serves an essential function in the translation cycle of fungi. eEF3 is a soluble factor lacking a transmembrane domain and having two ABC domains arranged in tandem, with a unique chromodomain inserted within the ABC2 domain.
Pssm-ID: 349274 [Multi-domain] Cd Length: 50 Bit Score: 38.61 E-value: 6.88e-04
10 20 30
....*....|....*....|....*....|....*.
gi 1933195014 829 IEEIITRKKLKQSYEYEVSFKGLSSSENIWLPRDEL 864
Cdd:cd00024 3 VEKILDHRVRKGKLEYLVKWKGYPPEENTWEPEENL 38
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
917-988 |
7.14e-04 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 42.74 E-value: 7.14e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1933195014 917 LSGGQKVKIVLGAATWRRPHVICLDEPTNYLD---RESLAALIAALKVFEG-GVLIITHnrDFSESLchevwAMRD 988
Cdd:PRK11247 134 LSGGQKQRVALARALIHRPGLLLLDEPLGALDaltRIEMQDLIESLWQQHGfTVLLVTH--DVSEAV-----AMAD 202
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
485-637 |
7.29e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 43.96 E-value: 7.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 485 GLCGKNGTGKSTLMRAItngqvegfpspdeVRTFYVEHD---IDGSEadtsVLQFILTDKR----------VLSS----- 546
Cdd:PLN03130 1269 GIVGRTGAGKSSMLNAL-------------FRIVELERGrilIDGCD----ISKFGLMDLRkvlgiipqapVLFSgtvrf 1331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 547 ---------EAEIKEALASVGFNDERQKQAIG----------SLSGGWKMKLALARAMLFKADILLLDEPTNHLDVVNVA 607
Cdd:PLN03130 1332 nldpfnehnDADLWESLERAHLKDVIRRNSLGldaevseageNFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDA 1411
|
170 180 190
....*....|....*....|....*....|.
gi 1933195014 608 WLENYL-TSLKTCTSIIVSHDSgflnNTITD 637
Cdd:PLN03130 1412 LIQKTIrEEFKSCTMLIIAHRL----NTIID 1438
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
711-995 |
8.25e-04 |
|
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: 42.78 E-value: 8.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 711 QQLYDITLQVSLSS----RVAILGPNGSGKSTLVKLLIGDMEPNKG-----GEIW------------KHPnlvIGYVAQH 769
Cdd:COG4148 9 LRRGGFTLDVDFTLpgrgVTALFGPSGSGKTTLLRAIAGLERPDSGrirlgGEVLqdsargiflpphRRR---IGYVFQE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 770 A--FHHidhhLD-KTPLEYMLWRyqtgedleeMSKANRQITEAEaqkmkegalivvegqkrlieeiitrkklkqsyeyev 846
Cdd:COG4148 86 ArlFPH----LSvRGNLLYGRKR---------APRAERRISFDE------------------------------------ 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 847 sfkglssseniwlprdelvkrgfekkVIEVdtreaqrLGLlRPLVRReiekhfadfglepefvshnTMRGLSGGQKVKIV 926
Cdd:COG4148 117 --------------------------VVEL-------LGI-GHLLDR-------------------RPATLSGGERQRVA 143
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1933195014 927 LGAATWRRPHVICLDEPTNYLDRES-------LAALIAALKVfegGVLIITHNRDFSESLCHEVWAMRDGRLEASG 995
Cdd:COG4148 144 IGRALLSSPRLLLMDEPLAALDLARkaeilpyLERLRDELDI---PILYVSHSLDEVARLADHVVLLEQGRVVASG 216
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
694-743 |
8.36e-04 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 43.17 E-value: 8.36e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1933195014 694 SLLKMRKVGFQYPT--QAVQQLYDITLQVSLSSRVAILGPNGSGKSTLVKLL 743
Cdd:PRK10535 3 ALLELKDIRRSYPSgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNIL 54
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
695-745 |
8.57e-04 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 42.99 E-value: 8.57e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1933195014 695 LLKMRKVGFQYPtqAVQQLYDITLQVSLSSRVAILGPNGSGKSTLVKLLIG 745
Cdd:PRK13549 5 LLEMKNITKTFG--GVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSG 53
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
713-995 |
1.02e-03 |
|
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: 41.84 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 713 LYDITLQVSLSSRVAILGPNGSGKSTLVKLLIGDMEPNKGgeiwkhpNLVIGyvaqhafhhidhhldktpleymlwryqt 792
Cdd:cd03300 16 LDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSG-------EILLD---------------------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 793 GEDLEEMSKANRQITeaeaqkmkegalIVVegqkrlieeiitrkklkQSYEYevsFKGLSSSENIWLPrdeLVKRGFEKK 872
Cdd:cd03300 61 GKDITNLPPHKRPVN------------TVF-----------------QNYAL---FPHLTVFENIAFG---LRLKKLPKA 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 873 VIEVDTREAQRLGLLRPLVRREIEKhfadfglepefvshntmrgLSGGQKVKIVLGAATWRRPHVICLDEPTNYLD---R 949
Cdd:cd03300 106 EIKERVAEALDLVQLEGYANRKPSQ-------------------LSGGQQQRVAIARALVNEPKVLLLDEPLGALDlklR 166
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1933195014 950 ESLAALIAAL-KVFEGGVLIITHNRDFSESLCHEVWAMRDGRLEASG 995
Cdd:cd03300 167 KDMQLELKRLqKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIG 213
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
695-752 |
1.14e-03 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 41.99 E-value: 1.14e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1933195014 695 LLKMRKVGFQYPTQAVqqLYDITLQVSLSSRVAILGPNGSGKSTLVKLLIGDMEPNKG 752
Cdd:PRK11248 1 MLQISHLYADYGGKPA--LEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHG 56
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
693-995 |
1.15e-03 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 42.73 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 693 KSLLKMRKVGFQYPTQAVQQLYDITLQvslSSRV-AILGPNGSGKSTLVKLLIGdMEPNKGGEIwkhpnlvigYVAQHAF 771
Cdd:PRK15439 9 PPLLCARSISKQYSGVEVLKGIDFTLH---AGEVhALLGGNGAGKSTLMKIIAG-IVPPDSGTL---------EIGGNPC 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 772 HHidhhldktpleymlwryqtgedleemskanrqITEAEAQKMkeGALIVveGQKRLIeeiitrkklkqsyeyevsFKGL 851
Cdd:PRK15439 76 AR--------------------------------LTPAKAHQL--GIYLV--PQEPLL------------------FPNL 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 852 SSSENIW--LPRDELVKRGFEKKVIEVDTR---EAQRlGLL----RPLVrrEIekhfadfglepefvshntMRGLsggqk 922
Cdd:PRK15439 102 SVKENILfgLPKRQASMQKMKQLLAALGCQldlDSSA-GSLevadRQIV--EI------------------LRGL----- 155
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1933195014 923 vkivlgaatWRRPHVICLDEPTNYL---DRESLAALIAALKVFEGGVLIITHNRDFSESLCHEVWAMRDGRLEASG 995
Cdd:PRK15439 156 ---------MRDSRILILDEPTASLtpaETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSG 222
|
|
| CD_POL_like |
cd18972 |
chromodomain of a Moniliophthora perniciosa FA553 putative retrotransposon polyprotein, and ... |
829-864 |
1.23e-03 |
|
chromodomain of a Moniliophthora perniciosa FA553 putative retrotransposon polyprotein, and similar proteins; This subgroup includes the CHROMO (CHRromatin Organization Modifier) domain found in a Moniliophthora perniciosa FA553 putative retrotelement polyprotein, which includes domains in the following order: a reverse transcriptase, RNase H, and an integrase, here the chromodomain is found at the C-terminus of the integrase domain. The chromodomain, is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related "chromo shadow" domain
Pssm-ID: 349328 Cd Length: 50 Bit Score: 37.88 E-value: 1.23e-03
10 20 30
....*....|....*....|....*....|....*.
gi 1933195014 829 IEEIITRKKLKQSYEYEVSFKGLSSSENIWLPRDEL 864
Cdd:cd18972 3 VEAIVGHKPKKKPRQFLVSWLGYDSSHNEWKQKEEL 38
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
471-627 |
1.32e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 42.03 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 471 LNTATLRLKRGHRYGLCGKNGTGKSTLMRAItNGQveGFPSPDEVRTFYVE-HDIDGSEADTSV-LQFILTDKRVLSSEA 548
Cdd:PRK13647 21 LKGLSLSIPEGSKTALLGPNGAGKSTLLLHL-NGI--YLPQRGRVKVMGREvNAENEKWVRSKVgLVFQDPDDQVFSSTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 549 E--------------------IKEALASVGFNDERQKqAIGSLSGGWKMKLALARAMLFKADILLLDEPTNHLDVVNVAW 608
Cdd:PRK13647 98 WddvafgpvnmgldkdeverrVEEALKAVRMWDFRDK-PPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQET 176
|
170 180
....*....|....*....|.
gi 1933195014 609 LENYLTSL--KTCTSIIVSHD 627
Cdd:PRK13647 177 LMEILDRLhnQGKTVIVATHD 197
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
726-755 |
1.46e-03 |
|
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: 40.43 E-value: 1.46e-03
10 20 30
....*....|....*....|....*....|
gi 1933195014 726 VAILGPNGSGKSTLVKLLIGDMEPNKGGEI 755
Cdd:smart00382 5 ILIVGPPGSGKTTLARALARELGPPGGGVI 34
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
917-990 |
1.53e-03 |
|
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: 42.36 E-value: 1.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 917 LSGGQKVKIVLGAATWRRPHVICLDEPTNYLDR-------ESLAALIAALKVfegGVLIITHnrDFS--ESLCHEVWAMR 987
Cdd:COG4172 426 FSGGQRQRIAIARALILEPKLLVLDEPTSALDVsvqaqilDLLRDLQREHGL---AYLFISH--DLAvvRALAHRVMVMK 500
|
...
gi 1933195014 988 DGR 990
Cdd:COG4172 501 DGK 503
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
713-755 |
1.57e-03 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 42.40 E-value: 1.57e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1933195014 713 LYDITLQVSLSSRVAILGPNGSGKSTLVKLLIGDMEPNKgGEI 755
Cdd:PRK10790 357 LQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTE-GEI 398
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
901-991 |
1.61e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 41.69 E-value: 1.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 901 DFGLEPEFVSHNTMRgLSGGQKVKIVLGAATWRRPHVICLDEPTNYLD---RESLAALIAALKVFEGGVLI-ITHNRDFS 976
Cdd:PRK13646 131 DLGFSRDVMSQSPFQ-MSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDpqsKRQVMRLLKSLQTDENKTIIlVSHDMNEV 209
|
90
....*....|....*
gi 1933195014 977 ESLCHEVWAMRDGRL 991
Cdd:PRK13646 210 ARYADEVIVMKEGSI 224
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
475-634 |
1.63e-03 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 41.36 E-value: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 475 TLRLKRGHRYGLCGKNGTGKSTLMRAIT-----NGQVE--GFP----SPDE---VRTFYVEHDIdgSEADTSVLQFILTD 540
Cdd:COG4138 16 SAQVNAGELIHLIGPNGAGKSTLLARMAgllpgQGEILlnGRPlsdwSAAElarHRAYLSQQQS--PPFAMPVFQYLALH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 541 KRVLSSEAEIKEALASV----GFNDERQKQaIGSLSGG-WKmKLALARAML-------FKADILLLDEPTNHLDVVNVAW 608
Cdd:COG4138 94 QPAGASSEAVEQLLAQLaealGLEDKLSRP-LTQLSGGeWQ-RVRLAAVLLqvwptinPEGQLLLLDEPMNSLDVAQQAA 171
|
170 180
....*....|....*....|....*...
gi 1933195014 609 LENYLTSLKTC-TSIIVS-HDsgfLNNT 634
Cdd:COG4138 172 LDRLLRELCQQgITVVMSsHD---LNHT 196
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
571-626 |
1.65e-03 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 42.40 E-value: 1.65e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1933195014 571 LSGGWKMKLALARAMLFKADILLLDEPTNHLDVVNVAWLENyLTSLKTCTSIIVSH 626
Cdd:TIGR00958 618 LSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQE-SRSRASRTVLLIAH 672
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
882-995 |
1.75e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 41.57 E-value: 1.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 882 QRLGLLRPLVRREIEKHFADFGLEPEFVSHNTMRGLSGGQKVKIVLGAATWRRPHVICLDEPTNYLD---RESLAALIAA 958
Cdd:PRK13637 110 INLGLSEEEIENRVKRAMNIVGLDYEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDpkgRDEILNKIKE 189
|
90 100 110
....*....|....*....|....*....|....*...
gi 1933195014 959 L-KVFEGGVLIITHNRDFSESLCHEVWAMRDGRLEASG 995
Cdd:PRK13637 190 LhKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQG 227
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
570-641 |
1.76e-03 |
|
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: 40.63 E-value: 1.76e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1933195014 570 SLSGGWKMKLALARAMLFKADILLLDEPTNHLDV---VNVAWLENYLTSLKTCTSIIVSHDSGFLnNTITDVLHL 641
Cdd:cd03222 71 DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIeqrLNAARAIRRLSEEGKKTALVVEHDLAVL-DYLSDRIHV 144
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
916-983 |
1.89e-03 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 40.04 E-value: 1.89e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1933195014 916 GLSGGQKVKIVL-----GAATWRRPhVICLDEPTNYLD---RESLAALIAALKVFEGGVLIITHNRDFSESLCHEV 983
Cdd:cd03227 77 QLSGGEKELSALalilaLASLKPRP-LYILDEIDRGLDprdGQALAEAILEHLVKGAQVIVITHLPELAELADKLI 151
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
715-771 |
1.89e-03 |
|
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: 40.21 E-value: 1.89e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1933195014 715 DITLQVSLSSRVAILGPNGSGKSTLVKlLIGDMEPNKGGEIWKHPNLVIGYVAQHAF 771
Cdd:cd03223 19 DLSFEIKPGDRLLITGPSGTGKSSLFR-ALAGLWPWGSGRIGMPEGEDLLFLPQRPY 74
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
486-646 |
1.90e-03 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 41.07 E-value: 1.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 486 LCGKNGTGKSTLMRAIT-----------NGQ-VEGFPSPD--EVRTFYVEHDidGSEADTSVLQFI---LTDKRVLS-SE 547
Cdd:PRK03695 27 LVGPNGAGKSTLLARMAgllpgsgsiqfAGQpLEAWSAAElaRHRAYLSQQQ--TPPFAMPVFQYLtlhQPDKTRTEaVA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 548 AEIKEALASVGFND--ERqkqAIGSLSGG-WKmKLALARAML-------FKADILLLDEPTNHLDVVNVAWLENYLTSLk 617
Cdd:PRK03695 105 SALNEVAEALGLDDklGR---SVNQLSGGeWQ-RVRLAAVVLqvwpdinPAGQLLLLDEPMNSLDVAQQAALDRLLSEL- 179
|
170 180 190
....*....|....*....|....*....|....*.
gi 1933195014 618 tCT---SIIVS-HDsgfLNNTI---TDVLHLNRFKL 646
Cdd:PRK03695 180 -CQqgiAVVMSsHD---LNHTLrhaDRVWLLKQGKL 211
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
572-629 |
2.07e-03 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 41.63 E-value: 2.07e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1933195014 572 SGGWKMKLALARAMLFKADILLLDEPTNHLDVVNVAWLENYLTSLKT--CTSII-VSHDSG 629
Cdd:PRK09473 163 SGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKRefNTAIImITHDLG 223
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
709-755 |
2.19e-03 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 40.85 E-value: 2.19e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1933195014 709 AVQQLYDITLQVSLSSRVAILGPNGSGKSTLVKlLIGDMEPNKGGEI 755
Cdd:PRK09493 13 PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLR-CINKLEEITSGDL 58
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
713-752 |
2.38e-03 |
|
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: 41.73 E-value: 2.38e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1933195014 713 LYDITLQVSLSSRVAILGPNGSGKSTLVKLLIGDMEPNKG 752
Cdd:COG5265 374 LKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSG 413
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
538-603 |
2.47e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 41.70 E-value: 2.47e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1933195014 538 LTDKRVLSSEAEIKEAlasvgfNDERQK---------QAIGSLSGGWKMKLALARAMLFKADILLLDEPTNHLDV 603
Cdd:NF040905 369 VSRRGVIDENEEIKVA------EEYRKKmniktpsvfQKVGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDV 437
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
918-995 |
2.89e-03 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 41.26 E-value: 2.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 918 SGGQKVKIVLGAATWRRPHVICLDEPTNYLDRESLAALIAALK--VFEGG-VLIITHNRDFSESLCHEVWAMRDGRLEAS 994
Cdd:NF000106 146 SGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRsmVRDGAtVLLTTQYMEEAEQLAHELTVIDRGRVIAD 225
|
.
gi 1933195014 995 G 995
Cdd:NF000106 226 G 226
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
666-771 |
2.92e-03 |
|
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: 41.85 E-value: 2.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 666 YYSLEALEdykfklPDPPLLEGVKTKEKSLLKMRKVGFQYPTQAVQQLYDITLQVSLSSRVAILGPNGSGKSTLVKLLIG 745
Cdd:TIGR00957 613 FLSHEELE------PDSIERRTIKPGEGNSITVHNATFTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLA 686
|
90 100
....*....|....*....|....*.
gi 1933195014 746 DMEPNKGGEIWKHPnlvIGYVAQHAF 771
Cdd:TIGR00957 687 EMDKVEGHVHMKGS---VAYVPQQAW 709
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
466-627 |
2.93e-03 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 41.17 E-value: 2.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 466 GAKILLNTATLRLKRGHRYGLCGKNGTGKSTLMRAI------TNGQV--EGFP----SPDEVRtfyvehDIDGSEADTSV 533
Cdd:PRK10070 39 GLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLnrliepTRGQVliDGVDiakiSDAELR------EVRRKKIAMVF 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 534 LQFILTDKRVLSSEAEIKEALASVGfNDERQKQAIGSL----------------SGGWKMKLALARAMLFKADILLLDEP 597
Cdd:PRK10070 113 QSFALMPHMTVLDNTAFGMELAGIN-AEERREKALDALrqvglenyahsypdelSGGMRQRVGLARALAINPDILLMDEA 191
|
170 180 190
....*....|....*....|....*....|...
gi 1933195014 598 TNHLDVVNVAWLENYLTSLKTC---TSIIVSHD 627
Cdd:PRK10070 192 FSALDPLIRTEMQDELVKLQAKhqrTIVFISHD 224
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
562-627 |
3.14e-03 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 41.17 E-value: 3.14e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1933195014 562 ERQKQAigsLSGGWKMKLALARAMLFKADILLLDEPTNHLDV-------VNVAWLENYLtslkTCTSIIVSHD 627
Cdd:PRK11000 128 DRKPKA---LSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAalrvqmrIEISRLHKRL----GRTMIYVTHD 193
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
466-602 |
3.15e-03 |
|
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: 39.92 E-value: 3.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 466 GAKILLNTATLRLKRGHRYGLCGKNGTGKSTLMRAI----TNGQVEG------FPSPDEVR--TFYVEHdidgseADtsv 533
Cdd:cd03232 18 GKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLagrkTAGVITGeilingRPLDKNFQrsTGYVEQ------QD--- 88
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1933195014 534 lqfiltdkrVLSSEAEIKEALasvgfndeRQKQAIGSLSGGWKMKLALARAMLFKADILLLDEPTNHLD 602
Cdd:cd03232 89 ---------VHSPNLTVREAL--------RFSALLRGLSVEQRKRLTIGVELAAKPSILFLDEPTSGLD 140
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
911-995 |
3.21e-03 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 40.64 E-value: 3.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 911 HNTMRGLSGGQKVKIVLGAATWRRPHVICLDEPTNYLDRESLAALIAALKVF--EG-GVLIITHNRDFSESLChEVWAMR 987
Cdd:PRK15056 137 HRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELrdEGkTMLVSTHNLGSVTEFC-DYTVMV 215
|
....*...
gi 1933195014 988 DGRLEASG 995
Cdd:PRK15056 216 KGTVLASG 223
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
461-649 |
3.45e-03 |
|
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: 41.47 E-value: 3.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 461 FSLAY--GAKILLNTATLRLKRGHRYGLCGKNGTGKSTLMRAI--TNGQVEGfpspdEVRtfyvehdIDG-SEADTSV-- 533
Cdd:TIGR00957 1290 YCLRYreDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLfrINESAEG-----EII-------IDGlNIAKIGLhd 1357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 534 LQFILT----DKRVLS-------------SEAEIKEALASVGFNDERQKQAIG----------SLSGGWKMKLALARAML 586
Cdd:TIGR00957 1358 LRFKITiipqDPVLFSgslrmnldpfsqySDEEVWWALELAHLKTFVSALPDKldhecaeggeNLSVGQRQLVCLARALL 1437
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1933195014 587 FKADILLLDEPTNHLDVVNVAWLENYL-TSLKTCTSIIVSHDSgflnNTITD---VLHLNRFKLRRY 649
Cdd:TIGR00957 1438 RKTKILVLDEATAAVDLETDNLIQSTIrTQFEDCTVLTIAHRL----NTIMDytrVIVLDKGEVAEF 1500
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
692-756 |
3.46e-03 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 40.85 E-value: 3.46e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1933195014 692 EKSLLKMRKVGFQYPTQAVqqLYDITLQVSLSSRVAILGPNGSGKSTLVKLLIGdMEPNKGGEIW 756
Cdd:COG3842 2 AMPALELENVSKRYGDVTA--LDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAG-FETPDSGRIL 63
|
|
| CHROMO |
smart00298 |
Chromatin organization modifier domain; |
829-875 |
3.61e-03 |
|
Chromatin organization modifier domain;
Pssm-ID: 214605 [Multi-domain] Cd Length: 55 Bit Score: 36.42 E-value: 3.61e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1933195014 829 IEEII-TRKKLKQSYEYEVSFKGLSSSENIWLPRDELVkrGFEKKVIE 875
Cdd:smart00298 4 VEKILdHRWKKKGELEYLVKWKGYSYSEDTWEPEENLL--NCSKKLDN 49
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
552-740 |
3.75e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 41.35 E-value: 3.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 552 EALASVGFNDERQKQAIGSLSGGWKMKLALARAMLF---KADILLLDEPTNHLDVVNVAWLENYLTSL--KTCTSIIVSH 626
Cdd:PRK00635 791 HALCSLGLDYLPLGRPLSSLSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLHTHDIKALIYVLQSLthQGHTVVIIEH 870
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 627 DSGFLNntITDVLhlnrFKLRRYRGNLESFVKA--VPE---AKSYYSLEALEDYKFKLPDPPLLegvKTKEKSLLKMRKV 701
Cdd:PRK00635 871 NMHVVK--VADYV----LELGPEGGNLGGYLLAscSPEeliHLHTPTAKALRPYLSSPQELPYL---PDPSPKPPVPADI 941
|
170 180 190
....*....|....*....|....*....|....*....
gi 1933195014 702 GFQYPTQavQQLYDITLQVSLSSRVAILGPNGSGKSTLV 740
Cdd:PRK00635 942 TIKNAYQ--HNLKHIDLSLPRNALTAVTGPSASGKHSLV 978
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
711-778 |
4.56e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 39.47 E-value: 4.56e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1933195014 711 QQLYDITLQVSLSSRVAILGPNGSGKSTLVKLLIGDMEPNkGGEIWKHpNLVIGYVAQHAFHHIDHHL 778
Cdd:PRK13541 14 KNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPS-SGNIYYK-NCNINNIAKPYCTYIGHNL 79
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
917-991 |
4.88e-03 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 39.76 E-value: 4.88e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1933195014 917 LSGGQKVKIVLGAATWRRPHVICLDEPTNYLDR---ESLAALIAALKVFEGGVLI-ITHNRDFSeSLCHEVWAMRDGRL 991
Cdd:PRK10584 147 LSGGEQQRVALARAFNGRPDVLFADEPTGNLDRqtgDKIADLLFSLNREHGTTLIlVTHDLQLA-ARCDRRLRLVNGQL 224
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
917-995 |
5.05e-03 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 40.99 E-value: 5.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 917 LSGGQKVKIVLGAATWRRPHVICLDEPTNYLDRESLAALIAALKVFEG----GVLIITHNRDFSESLCHEVWAMRDGRLE 992
Cdd:PRK10261 169 LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKemsmGVIFITHDMGVVAEIADRVLVMYQGEAV 248
|
...
gi 1933195014 993 ASG 995
Cdd:PRK10261 249 ETG 251
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
917-996 |
5.33e-03 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 40.17 E-value: 5.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 917 LSGGQK--VKIVLGAATwrRPHVICLDEPTNYLDRESLAALIAALKVF--EGG--VLIITHNRDFSESLCHEVWAMRDGR 990
Cdd:PRK11153 141 LSGGQKqrVAIARALAS--NPKVLLCDEATSALDPATTRSILELLKDInrELGltIVLITHEMDVVKRICDRVAVIDAGR 218
|
....*.
gi 1933195014 991 LEASGH 996
Cdd:PRK11153 219 LVEQGT 224
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
546-625 |
6.17e-03 |
|
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: 40.77 E-value: 6.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 546 SEAEIKEALASVGFNDERQKQAiGSLSGGWKMKLALARAMLFKADILLLDEPTNHLDVVNVAWLENYLTSLKTCTSIIVS 625
Cdd:TIGR01257 1038 AQLEMEAMLEDTGLHHKRNEEA-QDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMS 1116
|
|
| SbcC_Walker_B |
pfam13558 |
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from ... |
894-960 |
6.26e-03 |
|
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from eukaryotes and the prokaryotic homolog SbcCD complex subunit C. RAD50-ATPase forms a complex with Mre11-nuclease that detects and processes diverse and obstructed DNA ends. This domain is separated of the Walker A domain by a long coiled-coil domain and forms the nucleotide-binding domain (NBD) when the coiled coils fold back on themselves and bring together Walker A and B domains. Two RAD50-NBDs forms heterotetramers with a Mre11 nuclease dimer that assemble as catalytic head module that binds and cleaves DNA in an ATP-dependent reaction. Through secondary structural analysis, it has been suggested that there is a wide structural conservation in the Rad50/SMC protein family as seen in structural similarities between RAD50's hook and ABC-ATPase MukB's elbow region.
Pssm-ID: 463921 [Multi-domain] Cd Length: 90 Bit Score: 36.83 E-value: 6.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 894 EIEKHFADfglEPEFVSHNTMRGLSGGQKVK---IVLGAA-------TWRRPHVIC---LDEPTNYLDRESLAALIAALK 960
Cdd:pfam13558 13 EVEVRDED---GSEVETYRRSGGLSGGEKQLlayLPLAAAlaaqygsAEGRPPAPRlvfLDEAFAKLDEENIRTALELLR 89
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
697-756 |
6.40e-03 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 39.68 E-value: 6.40e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 697 KMRKVGFQYPTQAVqqLYDITLQVSLSSRVAILGPNGSGKSTLVKlLIGDMEPNKGGEIW 756
Cdd:COG4604 3 EIKNVSKRYGGKVV--LDDVSLTIPKGGITALIGPNGAGKSTLLS-MISRLLPPDSGEVL 59
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
726-756 |
6.99e-03 |
|
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: 38.88 E-value: 6.99e-03
10 20 30
....*....|....*....|....*....|.
gi 1933195014 726 VAILGPNGSGKSTLVKLLIGDMEPNKGGEIW 756
Cdd:TIGR01189 29 LQVTGPNGIGKTTLLRILAGLLRPDSGEVRW 59
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
917-997 |
7.02e-03 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 39.09 E-value: 7.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 917 LSGGQKVKIVLGAATWRRPHVICLDEPTNYLDrESLAALIaaLKVFEG------GVLIITHNRDFSESLCHEVWAMRDGR 990
Cdd:PRK10908 138 LSGGEQQRVGIARAVVNKPAVLLADEPTGNLD-DALSEGI--LRLFEEfnrvgvTVLMATHDIGLISRRSYRMLTLSDGH 214
|
....*..
gi 1933195014 991 LEASGHN 997
Cdd:PRK10908 215 LHGGVGG 221
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
698-752 |
7.16e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 40.10 E-value: 7.16e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1933195014 698 MRKVGFQYPtqAVQQLYDITLQVSLSSRVAILGPNGSGKSTLVKLLIGDMEPNKG 752
Cdd:PRK10982 1 MSNISKSFP--GVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSG 53
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
887-995 |
7.60e-03 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 39.49 E-value: 7.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 887 LRPLVRREIEKHFADFGLEPEFVSH---NTMRGLSGGQKVKIVLGAATWRRPHVICLDEPTNYLDRES---LAALIAALK 960
Cdd:PRK10895 105 IRDDLSAEQREDRANELMEEFHIEHlrdSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPISvidIKRIIEHLR 184
|
90 100 110
....*....|....*....|....*....|....*
gi 1933195014 961 VFEGGVLIITHNRDFSESLCHEVWAMRDGRLEASG 995
Cdd:PRK10895 185 DSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHG 219
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
571-602 |
8.72e-03 |
|
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: 40.19 E-value: 8.72e-03
10 20 30
....*....|....*....|....*....|..
gi 1933195014 571 LSGGWKMKLALARAMLFKADILLLDEPTNHLD 602
Cdd:COG5265 495 LSGGEKQRVAIARTLLKNPPILIFDEATSALD 526
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
912-960 |
9.12e-03 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 40.03 E-value: 9.12e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1933195014 912 NTMRGLSGGQKVKIVLGAATWRRPHVICLDEPTNYLDRESLAALIAALK 960
Cdd:TIGR00955 162 GRVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLK 210
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
917-995 |
9.44e-03 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 38.84 E-value: 9.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933195014 917 LSGGQKVKIVLGAATWRRPHVICLDEPTNYLDRE---SLAALIAALKvfEGGV--LIITHNRDFSESLCHEVWAMRDGRL 991
Cdd:COG4161 142 LSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEitaQVVEIIRELS--QTGItqVIVTHEVEFARKVASQVVYMEKGRI 219
|
....
gi 1933195014 992 EASG 995
Cdd:COG4161 220 IEQG 223
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
676-752 |
9.59e-03 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 39.87 E-value: 9.59e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1933195014 676 KFKLPDPPLlegvkTKEKSLLKMRKVG-FQYPtqavqqLYDITLQVSLSSRVAILGPNGSGKSTLVKLLIGDMEPNKG 752
Cdd:PRK13545 13 KYKMYNKPF-----DKLKDLFFRSKDGeYHYA------LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKG 79
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
571-604 |
9.66e-03 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 39.30 E-value: 9.66e-03
10 20 30
....*....|....*....|....*....|....
gi 1933195014 571 LSGGWKMKLALARAMLFKADILLLDEPTNHLDVV 604
Cdd:COG4586 155 LSLGQRMRCELAAALLHRPKILFLDEPTIGLDVV 188
|
|
| |
