|
Name |
Accession |
Description |
Interval |
E-value |
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
437-973 |
4.11e-89 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 295.44 E-value: 4.11e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 437 SLAYGAKILLNKTQLRLKRARRYGICGPNGCGKSTLMRAIA------NGQVDgfpTQEECRTVYVEHDIDgTHSDTSVLD 510
Cdd:COG0488 5 SKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAgelepdSGEVS---IPKGLRIGYLPQEPP-LDDDLTVLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 511 FVFESGVGTKEAIKDK---------------------------------------LIEFGFTDEMIAMPISALSGGWKMK 551
Cdd:COG0488 81 TVLDGDAELRALEAELeeleaklaepdedlerlaelqeefealggweaearaeeiLSGLGFPEEDLDRPVSELSGGWRRR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 552 LALARAVLRNADILLLDEPTNHLDTVNVAWLVNYLNTCGITSITISHDSVFLDNVCEYIINYEGLKLRKYKGNFTEFVK- 630
Cdd:COG0488 161 VALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVATRILELDRGKLTLYPGNYSAYLEq 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 631 -----------------------------KCPAAKA---------YEEL-------SNTDLEFKFPEPGYLeGvktkqKA 665
Cdd:COG0488 241 raerleqeaaayakqqkkiakeeefirrfRAKARKAkqaqsrikaLEKLereepprRDKTVEIRFPPPERL-G-----KK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 666 IVKVTNMEFQYPGtsKPQITDINFQCSLSSRIAVIGPNGAGKSTLINVLTGELLPTSGEVYTHENCRIAYIKQHafaHIE 745
Cdd:COG0488 315 VLELEGLSKSYGD--KTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETVKIGYFDQH---QEE 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 746 SHLDKTPSEYIqwrfqtgedretmdranRQINENDAEamnkifkiegtprriagIHSRrkfkntyeyecSFLlgenigmk 825
Cdd:COG0488 390 LDPDKTVLDEL-----------------RDGAPGGTE-----------------QEVR-----------GYL-------- 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 826 serwvpmmsvdnawiprgelveshskmvaevdmkealasGQFrpltrkeieehcsmlGLDPEIVsHSRIRGLSGGQKVKL 905
Cdd:COG0488 417 ---------------------------------------GRF---------------LFSGDDA-FKPVGVLSGGEKARL 441
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6323278 906 VLAAGTWQRPHLIVLDEPTNYLDRDSLGALSKALKEFEGGVIIITHSAEFTKNLTEEVWAVKDGRMTP 973
Cdd:COG0488 442 ALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDFPGTVLLVSHDRYFLDRVATRILEFEDGGVRE 509
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
436-973 |
6.51e-57 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 210.10 E-value: 6.51e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 436 FSLAYGAKILLNKTQLRLKRARRYGICGPNGCGKSTLMRAIANGQVDGFPTQeeCRTVYVEHDIDGthSDTSVLDFVFES 515
Cdd:PLN03073 183 FSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMAMHAIDGIPKN--CQILHVEQEVVG--DDTTALQCVLNT 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 516 GVG-----------------------------------TKEAIKDKLIE-----------------------FGFTDEMI 537
Cdd:PLN03073 259 DIErtqlleeeaqlvaqqrelefetetgkgkgankdgvDKDAVSQRLEEiykrlelidaytaearaasilagLSFTPEMQ 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 538 AMPISALSGGWKMKLALARAVLRNADILLLDEPTNHLDTVNVAWLVNYLNTCGITSITISHDSVFLDNVCEYIINYEGLK 617
Cdd:PLN03073 339 VKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPKTFIVVSHAREFLNTVVTDILHLHGQK 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 618 LRKYKGNFTEF-------VKKCPAA--------------------------------KAYEEL-------SNTDLEFKFP 651
Cdd:PLN03073 419 LVTYKGDYDTFertreeqLKNQQKAfesnersrshmqafidkfrynakraslvqsriKALDRLghvdavvNDPDYKFEFP 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 652 EPGylegvKTKQKAIVKVTNMEFQYPGtsKPQI-TDINFQCSLSSRIAVIGPNGAGKSTLINVLTGELLPTSGEVYTHEN 730
Cdd:PLN03073 499 TPD-----DRPGPPIISFSDASFGYPG--GPLLfKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAK 571
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 731 CRIAYIKQHafaHIES-HLDKTPSEYiqwrfqtgedretmdranrqinendaeaMNKIFKieGTPRRIAGIHSRrkfknt 809
Cdd:PLN03073 572 VRMAVFSQH---HVDGlDLSSNPLLY----------------------------MMRCFP--GVPEQKLRAHLG------ 612
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 810 yeyecSFLLGENIGMKserwvPMMSvdnawiprgelveshskmvaevdmkealasgqfrpltrkeieehcsmlgldpeiv 889
Cdd:PLN03073 613 -----SFGVTGNLALQ-----PMYT------------------------------------------------------- 627
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 890 shsrirgLSGGQKVKLVLAAGTWQRPHLIVLDEPTNYLDRDSLGALSKALKEFEGGVIIITHSAEFTKNLTEEVWAVKDG 969
Cdd:PLN03073 628 -------LSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGLVLFQGGVLMVSHDEHLISGSVDELWVVSEG 700
|
....
gi 6323278 970 RMTP 973
Cdd:PLN03073 701 KVTP 704
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
441-973 |
6.03e-46 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 176.13 E-value: 6.03e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 441 GAKILLNKTQLRLKRARRYGICGPNGCGKSTLMRAIANG-QVDG----FP--------TQE-----------------EC 490
Cdd:PRK10636 12 GVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEiSADGgsytFPgnwqlawvNQEtpalpqpaleyvidgdrEY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 491 RTVYVEHDIDGTHSDTSVLDFVFesgvGTKEAIKDKLIE---------FGFTDEMIAMPISALSGGWKMKLALARAVLRN 561
Cdd:PRK10636 92 RQLEAQLHDANERNDGHAIATIH----GKLDAIDAWTIRsraasllhgLGFSNEQLERPVSDFSGGWRMRLNLAQALICR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 562 ADILLLDEPTNHLDTVNVAWLVNYLNTCGITSITISHDSVFLDNVCEYIINYEGLKLRKYKGNFTEFVK----------- 630
Cdd:PRK10636 168 SDLLLLDEPTNHLDLDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQQSLFEYTGNYSSFEVqratrlaqqqa 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 631 -------------------KCPAAKAYEELSNTDL----------------EFKFPEPGYLEGvktkqkaivKVTNMEFQ 675
Cdd:PRK10636 248 myesqqervahlqsyidrfRAKATKAKQAQSRIKMlermeliapahvdnpfHFSFRAPESLPN---------PLLKMEKV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 676 YPGTSKPQITD-INFQCSLSSRIAVIGPNGAGKSTLINVLTGELLPTSGEVYTHENCRIAYIKQHAFAHIEShlDKTPSE 754
Cdd:PRK10636 319 SAGYGDRIILDsIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLGYFAQHQLEFLRA--DESPLQ 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 755 YIQwrfqtgedretmdranrqinendaeamnkifkiegtprRIAGIHSRRKFKNtyeyecsFLLGenIGMKSERwvpmms 834
Cdd:PRK10636 397 HLA--------------------------------------RLAPQELEQKLRD-------YLGG--FGFQGDK------ 423
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 835 vdnawiprgelveshskmVAEvdmkealASGQFrpltrkeieehcsmlgldpeivshsrirglSGGQKVKLVLAAGTWQR 914
Cdd:PRK10636 424 ------------------VTE-------ETRRF------------------------------SGGEKARLVLALIVWQR 448
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 6323278 915 PHLIVLDEPTNYLDRDSLGALSKALKEFEGGVIIITHSAEFTKNLTEEVWAVKDGRMTP 973
Cdd:PRK10636 449 PNLLLLDEPTNHLDLDMRQALTEALIDFEGALVVVSHDRHLLRSTTDDLYLVHDGKVEP 507
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
437-964 |
1.10e-42 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 166.28 E-value: 1.10e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 437 SLAYGAKILLNKTQLRLKRARRYGICGPNGCGKSTLMRAIANGQV--DG-FPTQEECRTVYVEHD----IDGThsdtsVL 509
Cdd:PRK11147 10 WLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLldDGrIIYEQDLIVARLQQDpprnVEGT-----VY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 510 DFVFEsGVGTK-EAIKD-----KLIEFGFTDEMIA---------------------------------MPISALSGGWKM 550
Cdd:PRK11147 85 DFVAE-GIEEQaEYLKRyhdisHLVETDPSEKNLNelaklqeqldhhnlwqlenrinevlaqlgldpdAALSSLSGGWLR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 551 KLALARAVLRNADILLLDEPTNHLDTVNVAWLVNYLNTCGITSITISHDSVFLDNVCEYIINYEGLKLRKYKGNFTEFVK 630
Cdd:PRK11147 164 KAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLDRGKLVSYPGNYDQYLL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 631 KCPAAKAYEELSNTDLEFKFP--EPGYLEGVKTKQ----------KA---------------------------IV-KVT 670
Cdd:PRK11147 244 EKEEALRVEELQNAEFDRKLAqeEVWIRQGIKARRtrnegrvralKAlrrerserrevmgtakmqveeasrsgkIVfEME 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 671 NMEFQYPGtsKPQITDINFQCSLSSRIAVIGPNGAGKSTLINVLTGELLPTSGEVYTHENCRIAYIKQHafahieshldk 750
Cdd:PRK11147 324 NVNYQIDG--KQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKLEVAYFDQH----------- 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 751 tpseyiqwrfqtgedRETMDrANRQINENDAEAMNKIfKIEGTPRRIAGihsrrkfkntyeYECSFLLgenigmkserwv 830
Cdd:PRK11147 391 ---------------RAELD-PEKTVMDNLAEGKQEV-MVNGRPRHVLG------------YLQDFLF------------ 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 831 pmmsvdnawiprgelvesHSKmvaevdmkealasgqfRPLTrkeieehcsmlgldPeivshsrIRGLSGGQKVKLVLAAG 910
Cdd:PRK11147 430 ------------------HPK----------------RAMT--------------P-------VKALSGGERNRLLLARL 454
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 6323278 911 TWQRPHLIVLDEPTNYLDRDSLGALSKALKEFEGGVIIITHSAEFTKNLTEEVW 964
Cdd:PRK11147 455 FLKPSNLLILDEPTNDLDVETLELLEELLDSYQGTVLLVSHDRQFVDNTVTECW 508
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
431-617 |
1.42e-42 |
|
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: 151.83 E-value: 1.42e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 431 LCNCEFSLAYGAKILLNKTQLRLKRARRYGICGPNGCGKSTLMRAIANgqvdgfptqeecrtvyvehdidgthsdtsvlD 510
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAG-------------------------------E 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 511 FVFESGvgtkEAIKDKLIEFGFtdemiampISALSGGWKMKLALARAVLRNADILLLDEPTNHLDTVNVAWLVNYLNTCG 590
Cdd:cd03221 50 LEPDEG----IVTWGSTVKIGY--------FEQLSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEALKEYP 117
|
170 180
....*....|....*....|....*..
gi 6323278 591 ITSITISHDSVFLDNVCEYIINYEGLK 617
Cdd:cd03221 118 GTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
440-972 |
1.81e-39 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 154.66 E-value: 1.81e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 440 YGAKILLNKTQLRLKRARRYGICGPNGCGKSTLMRAIA------NGQVD-------GFPTQ-----EECR---TVYVEH- 497
Cdd:PRK15064 11 FGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGgdlepsAGNVSldpnerlGKLRQdqfafEEFTvldTVIMGHt 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 498 -------------------DIDGTHsdTSVLDFVF-ESGVGTKEA-IKDKLIEFGFTDEMIAMPISALSGGWKMKLALAR 556
Cdd:PRK15064 91 elwevkqerdriyalpemsEEDGMK--VADLEVKFaEMDGYTAEArAGELLLGVGIPEEQHYGLMSEVAPGWKLRVLLAQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 557 AVLRNADILLLDEPTNHLDTVNVAWLVNYLNTCGITSITISHDSVFLDNVCEYIINYEGLKLRKYKGNFTEFVKKcpAAK 636
Cdd:PRK15064 169 ALFSNPDILLLDEPTNNLDINTIRWLEDVLNERNSTMIIISHDRHFLNSVCTHMADLDYGELRVYPGNYDEYMTA--ATQ 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 637 AYEEL--SNTDLEFKFPEpgyLEGV---------KTKQ-----KAIVKVTNMEF-----QYP------------------ 677
Cdd:PRK15064 247 ARERLlaDNAKKKAQIAE---LQSFvsrfsanasKAKQatsraKQIDKIKLEEVkpssrQNPfirfeqdkklhrnaleve 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 678 GTSK-----PQITDINFQCSLSSRIAVIGPNGAGKSTLINVLTGELLPTSGEVYTHENCRIAYIKQ---HAFAHieshlD 749
Cdd:PRK15064 324 NLTKgfdngPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENANIGYYAQdhaYDFEN-----D 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 750 KTPSEYI-QWRfqTGEDRETMDRanrqinendaeamnkifkiegtprriaGIHSRrkfkntyeyecsFLLGENIGMKSer 828
Cdd:PRK15064 399 LTLFDWMsQWR--QEGDDEQAVR---------------------------GTLGR------------LLFSQDDIKKS-- 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 829 wvpmmsvdnawiprgelveshskmvaevdmkealasgqfrpltrkeieehcsmlgldpeivshsrIRGLSGGQKVKLVLA 908
Cdd:PRK15064 436 -----------------------------------------------------------------VKVLSGGEKGRMLFG 450
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6323278 909 AGTWQRPHLIVLDEPTNYLDRDSLGALSKALKEFEGGVIIITHSAEFTKNLTEEVWAVKDGRMT 972
Cdd:PRK15064 451 KLMMQKPNVLVMDEPTNHMDMESIESLNMALEKYEGTLIFVSHDREFVSSLATRIIEITPDGVV 514
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
437-951 |
8.76e-39 |
|
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: 152.78 E-value: 8.76e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 437 SLAYGAKIllnktqlrlkrarryGICGPNGCGKSTLMRAIA--NGQVDGFPTQEECRTV-YVEHD--IDGTHSdtsVLDF 511
Cdd:TIGR03719 27 SFFPGAKI---------------GVLGLNGAGKSTLLRIMAgvDKDFNGEARPQPGIKVgYLPQEpqLDPTKT---VREN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 512 VFEsGVGTKEAIKDKL--IEFGFTD----------EM--------------------IAM----------PISALSGGWK 549
Cdd:TIGR03719 89 VEE-GVAEIKDALDRFneISAKYAEpdadfdklaaEQaelqeiidaadawdldsqleIAMdalrcppwdaDVTKLSGGER 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 550 MKLALARAVLRNADILLLDEPTNHLDTVNVAWLVNYLNTCGITSITISHDSVFLDNVCEYIINYEGLKLRKYKGNFT--- 626
Cdd:TIGR03719 168 RRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPWEGNYSswl 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 627 -------------------------EFVKKCPAAK---------AYEELSNTDLEFK------FPEPGYLEGVKtkqkaI 666
Cdd:TIGR03719 248 eqkqkrleqeekeesarqktlkrelEWVRQSPKGRqakskarlaRYEELLSQEFQKRnetaeiYIPPGPRLGDK-----V 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 667 VKVTNMEFQYpgTSKPQITDINFQCSLSSRIAVIGPNGAGKSTLINVLTGELLPTSGEVYTHENCRIAYIKQhafahIES 746
Cdd:TIGR03719 323 IEAENLTKAF--GDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVKLAYVDQ-----SRD 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 747 HLD--KTPSEYIqwrfQTGEDreTMDRANRQINendaeamnkifkiegtprriagihSRrkfkntyeyecsfllgenigm 824
Cdd:TIGR03719 396 ALDpnKTVWEEI----SGGLD--IIKLGKREIP------------------------SR--------------------- 424
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 825 kserwvpmmsvdnAWIprgelveshskmvaevdmkealasGQFrpltrkeieehcSMLGLDPEivshSRIRGLSGGQKVK 904
Cdd:TIGR03719 425 -------------AYV------------------------GRF------------NFKGSDQQ----KKVGQLSGGERNR 451
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 6323278 905 LVLAAGTWQRPHLIVLDEPTNYLDRDSLGALSKALKEFEGGVIIITH 951
Cdd:TIGR03719 452 VHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEALLNFAGCAVVISH 498
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
437-631 |
8.50e-36 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 143.28 E-value: 8.50e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 437 SLAYGAKILLNKTQLRLKRARRYGICGPNGCGKSTLMRAIAnGQVDgfPTQEECR---TV---YVEHDIDGTHSDTSVLD 510
Cdd:COG0488 322 SKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLA-GELE--PDSGTVKlgeTVkigYFDQHQEELDPDKTVLD 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 511 FVFESGVGTKEA-IKDKLIEFGFTDEMIAMPISALSGGWKMKLALARAVLRNADILLLDEPTNHLDTVNVAWLVNYLNTC 589
Cdd:COG0488 399 ELRDGAPGGTEQeVRGYLGRFLFSGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDF 478
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 6323278 590 GITSITISHDSVFLDNVCEYIINYEGLKLRKYKGNFTEFVKK 631
Cdd:COG0488 479 PGTVLLVSHDRYFLDRVATRILEFEDGGVREYPGGYDDYLEK 520
|
|
| 4HB |
pfam17947 |
Four helical bundle domain; This domain is found in elongation factor 3A where it packs ... |
336-411 |
2.39e-34 |
|
Four helical bundle domain; This domain is found in elongation factor 3A where it packs against the bottom of the concave face of the HEAT domain.
Pssm-ID: 407796 Cd Length: 78 Bit Score: 126.10 E-value: 2.39e-34
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6323278 336 GDVSTTLQVVNELLKD--ETVAPRFKIVVEYIAAIGADLIDERIIDQQAWFTHITPYMTIFLHEKKAKDILDEFRKRA 411
Cdd:pfam17947 1 GDISTVLAILKEILSSkhKKVAEKFEPVLEYIAAIAGQLIDEKEIDQATWTENLKPYVTVIVGEADAKSIVDTLRKRA 78
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
440-951 |
8.20e-33 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 134.86 E-value: 8.20e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 440 YGAKIllnktqlrlkrarryGICGPNGCGKSTLMRAIA------NGQV---DGFptqeecrTV-YVEHD--IDGTHSdts 507
Cdd:PRK11819 32 PGAKI---------------GVLGLNGAGKSTLLRIMAgvdkefEGEArpaPGI-------KVgYLPQEpqLDPEKT--- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 508 VLDFVfESGVGTKEAIKDKLIEFG--FTDEM------------------------------IAM----------PISALS 545
Cdd:PRK11819 87 VRENV-EEGVAEVKAALDRFNEIYaaYAEPDadfdalaaeqgelqeiidaadawdldsqleIAMdalrcppwdaKVTKLS 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 546 GGWKMKLALARAVLRNADILLLDEPTNHLDTVNVAWLVNYLNTCGITSITISHDSVFLDNVCEYIINYEGLKLRKYKGNF 625
Cdd:PRK11819 166 GGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPWEGNY 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 626 T----------------------------EFVKKCPAA---------KAYEELS-------NTDLEFKFPEPGYLEGVkt 661
Cdd:PRK11819 246 SswleqkakrlaqeekqeaarqkalkrelEWVRQSPKArqakskarlARYEELLseeyqkrNETNEIFIPPGPRLGDK-- 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 662 kqkaIVKVTNMEFQYPGtsKPQITDINFQCSLSSRIAVIGPNGAGKSTLINVLTGELLPTSGEVYTHENCRIAYIKQHaf 741
Cdd:PRK11819 324 ----VIEAENLSKSFGD--RLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGETVKLAYVDQS-- 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 742 ahiESHLD--KTPSEYIqwrfqtGEDRETMDRANRQINendaeamnkifkiegtprriagihSRrkfkntyEYECSFllg 819
Cdd:PRK11819 396 ---RDALDpnKTVWEEI------SGGLDIIKVGNREIP------------------------SR-------AYVGRF--- 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 820 enigmkserwvpmmsvdnawiprgelveshskmvaevdmkealasgQFRpltrkeieehcsmlGLDPEivshSRIRGLSG 899
Cdd:PRK11819 433 ----------------------------------------------NFK--------------GGDQQ----KKVGVLSG 448
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 6323278 900 GQKVKLVLAAGTWQRPHLIVLDEPTNYLDRDSLGALSKALKEFEGGVIIITH 951
Cdd:PRK11819 449 GERNRLHLAKTLKQGGNVLLLDEPTNDLDVETLRALEEALLEFPGCAVVISH 500
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
669-973 |
7.05e-32 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 131.34 E-value: 7.05e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 669 VTNMEFQYPGtsKPQITDINFQCSLSSRIAVIGPNGAGKSTLINVLTGELLPTSGEVYTHENCRIAYIKQHAFAhiesHL 748
Cdd:COG0488 1 LENLSKSFGG--RPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRIGYLPQEPPL----DD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 749 DKTPSEYIQWRFQ-TGEDRETMDRANRQINENDAEAMnkifkiegtprRIAGIHSRRKFKNTYEYEcsfllgenigmkse 827
Cdd:COG0488 75 DLTVLDTVLDGDAeLRALEAELEELEAKLAEPDEDLE-----------RLAELQEEFEALGGWEAE-------------- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 828 rwvpmmsvdnawiprgelveshskmvAEVdmkEALASGqfrpltrkeieehcsmLGLDPEIvSHSRIRGLSGGQKVKLVL 907
Cdd:COG0488 130 --------------------------ARA---EEILSG----------------LGFPEED-LDRPVSELSGGWRRRVAL 163
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6323278 908 AAGTWQRPHLIVLDEPTNYLDRDSLGALSKALKEFEGGVIIITHSAEFTKNLTEEVWAVKDGRMTP 973
Cdd:COG0488 164 ARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVATRILELDRGKLTL 229
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
436-611 |
1.31e-28 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 114.14 E-value: 1.31e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 436 FSLAYGAKILLNKTQLRLKRARRYGICGPNGCGKSTLMRAIAN------GQV--DGFPTQE----ECRT--VYVEHD--- 498
Cdd:COG4619 6 LSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADldpptsGEIylDGKPLSAmpppEWRRqvAYVPQEpal 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 499 IDGTHSDTSVLDFVFESGVGTKEAIKDKLIEFGFTDEMIAMPISALSGGWKMKLALARAVLRNADILLLDEPTNHLDTVN 578
Cdd:COG4619 86 WGGTVRDNLPFPFQLRERKFDRERALELLERLGLPPDILDKPVERLSGGERQRLALIRALLLQPDVLLLDEPTSALDPEN 165
|
170 180 190
....*....|....*....|....*....|....*..
gi 6323278 579 ----VAWLVNYLNTCGITSITISHDSVFLDNVCEYII 611
Cdd:COG4619 166 trrvEELLREYLAEEGRAVLWVSHDPEQIERVADRVL 202
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
434-611 |
8.01e-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: 110.41 E-value: 8.01e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 434 CEFSLAYGAKILLNKTQLRLKRARRYGICGPNGCGKSTLMRAIANGQvdgFPTQEECRtvyvehdIDGTHSDTSVLdfvf 513
Cdd:cd00267 3 ENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLL---KPTSGEIL-------IDGKDIAKLPL---- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 514 esgvgtkEAIKDKliefgftdemIAMpISALSGGWKMKLALARAVLRNADILLLDEPTNHLDTVNVAWLVNYLNT---CG 590
Cdd:cd00267 69 -------EELRRR----------IGY-VPQLSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLRElaeEG 130
|
170 180
....*....|....*....|.
gi 6323278 591 ITSITISHDSVFLDNVCEYII 611
Cdd:cd00267 131 RTVIIVTHDPELAELAADRVI 151
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
667-970 |
1.41e-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: 106.38 E-value: 1.41e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 667 VKVTNMEFQYPGtsKPQITDINFQCSLSSRIAVIGPNGAGKSTLINVLTGELLPTSGEVYTHENCRIAYIKQhafahies 746
Cdd:cd03221 1 IELENLSKTYGG--KLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFEQ-------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 747 hldktpseyiqwrfqtgedretmdranrqinendaeamnkifkiegtprriagihsrrkfkntyeyecsfllgenigmks 826
Cdd:cd03221 --------------------------------------------------------------------------------
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 827 erwvpmmsvdnawiprgelveshskmvaevdmkealasgqfrpltrkeieehcsmlgldpeivshsrirgLSGGQKVKLV 906
Cdd:cd03221 71 ----------------------------------------------------------------------LSGGEKMRLA 80
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6323278 907 LAAGTWQRPHLIVLDEPTNYLDRDSLGALSKALKEFEGGVIIITHSAEFTKNLTEEVWAVKDGR 970
Cdd:cd03221 81 LAKLLLENPNLLLLDEPTNHLDLESIEALEEALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
433-970 |
9.87e-26 |
|
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: 112.69 E-value: 9.87e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 433 NCEFSLAYGAKILLNKTQLRLKRARRYGICGPNGCGKSTLMRAIA-----NGQVDG-----------FPTQEECRTV-YV 495
Cdd:COG1123 9 DLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMgllphGGRISGevlldgrdlleLSEALRGRRIgMV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 496 EHDIDGTHSDTSVLD---FVFESGVGTKEAIKDKLIE----FGFtDEMIAMPISALSGGWKMKLALARAVLRNADILLLD 568
Cdd:COG1123 89 FQDPMTQLNPVTVGDqiaEALENLGLSRAEARARVLElleaVGL-ERRLDRYPHQLSGGQRQRVAIAMALALDPDLLIAD 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 569 EPTNHLDTV---NVAWLVNYLN-TCGITSITISHD-SVFLDNVCEYIINYEGlklrkykgnftEFVKKCPAAkayEELSN 643
Cdd:COG1123 168 EPTTALDVTtqaEILDLLRELQrERGTTVLLITHDlGVVAEIADRVVVMDDG-----------RIVEDGPPE---EILAA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 644 TDLEFKFPEPGYLEGVKTKQKA----IVKVTNMEFQYPGTSKPQIT---DINFQCSLSSRIAVIGPNGAGKSTLINVLTG 716
Cdd:COG1123 234 PQALAAVPRLGAARGRAAPAAAaaepLLEVRNLSKRYPVRGKGGVRavdDVSLTLRRGETLGLVGESGSGKSTLARLLLG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 717 ELLPTSGEVythencriayikqhafahieshldktpseyiqwRFQtGEDRETMDRANRqinendaeamnkifkiegtpRR 796
Cdd:COG1123 314 LLRPTSGSI---------------------------------LFD-GKDLTKLSRRSL--------------------RE 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 797 IagihsRRK----FKNTYEyecSFllgenigmkserwVPMMSVdnawiprGELVEshskmvaevdmkEALAsgQFRPLTR 872
Cdd:COG1123 340 L-----RRRvqmvFQDPYS---SL-------------NPRMTV-------GDIIA------------EPLR--LHGLLSR 377
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 873 KEIEEHC----SMLGLDPEIVsHSRIRGLSGGQKVKLVLAAGTWQRPHLIVLDEPTNYLD---RDSLGALSKAL-KEFEG 944
Cdd:COG1123 378 AERRERVaellERVGLPPDLA-DRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALDvsvQAQILNLLRDLqRELGL 456
|
570 580
....*....|....*....|....*.
gi 6323278 945 GVIIITHSAEFTKNLTEEVWAVKDGR 970
Cdd:COG1123 457 TYLFISHDLAVVRYIADRVAVMYDGR 482
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
437-606 |
3.11e-25 |
|
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: 104.48 E-value: 3.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 437 SLAYGAKILLNKTQLRLKRARRYGICGPNGCGKSTLMRAIA------NGQV--DGFPTQEECRTV-----YVEHDiDGTH 503
Cdd:COG4133 9 SCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAgllppsAGEVlwNGEPIRDAREDYrrrlaYLGHA-DGLK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 504 SDTSV---LDFVFE-SGV-GTKEAIKDKLIEFGFTDeMIAMPISALSGGWKMKLALARAVLRNADILLLDEPTNHLDTVN 578
Cdd:COG4133 88 PELTVrenLRFWAAlYGLrADREAIDEALEAVGLAG-LADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAG 166
|
170 180 190
....*....|....*....|....*....|..
gi 6323278 579 VAWLVNYLNT----CGITSITiSHDSVFLDNV 606
Cdd:COG4133 167 VALLAELIAAhlarGGAVLLT-THQPLELAAA 197
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
440-611 |
1.31e-24 |
|
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: 101.71 E-value: 1.31e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 440 YGAKILLNKTQLRLKRARRYGICGPNGCGKSTLMRAIAN------GQ--VDGFPTQEECRTVYvehdidgthsdtSVLDF 511
Cdd:cd03230 10 YGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGllkpdsGEikVLGKDIKKEPEEVK------------RRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 512 VFEsgvgtkeaikdkliEFGFTDEMIAMPISALSGGWKMKLALARAVLRNADILLLDEPTNHLDTVNVAWLVNYLNTC-- 589
Cdd:cd03230 78 LPE--------------EPSLYENLTVRENLKLSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWELLRELkk 143
|
170 180
....*....|....*....|...
gi 6323278 590 -GITSITISHDSVFLDNVCEYII 611
Cdd:cd03230 144 eGKTILLSSHILEEAERLCDRVA 166
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
437-599 |
8.78e-24 |
|
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: 101.66 E-value: 8.78e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 437 SLAYGAKILLNKTQLRLKRARRYGICGPNGCGKSTLMRAIAN------GQV--DG-----FPTQEECRTV-YV--EHDID 500
Cdd:COG1120 8 SVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGllkpssGEVllDGrdlasLSRRELARRIaYVpqEPPAP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 501 GthsDTSVLDFV------FESGVGT-----KEAIKDKLIEFGfTDEMIAMPISALSGGWKMKLALARAVLRNADILLLDE 569
Cdd:COG1120 88 F---GLTVRELValgrypHLGLFGRpsaedREAVEEALERTG-LEHLADRPVDELSGGERQRVLIARALAQEPPLLLLDE 163
|
170 180 190
....*....|....*....|....*....|....
gi 6323278 570 PTNHLD---TVNVAWLVNYLN-TCGITSITISHD 599
Cdd:COG1120 164 PTSHLDlahQLEVLELLRRLArERGRTVVMVLHD 197
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
439-611 |
1.03e-22 |
|
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: 98.39 E-value: 1.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 439 AYGAKILLNKTQLRLKRARRYGICGPNGCGKSTLMRAIAN------G--QVDGFPTQEECRTV-----YVeHDIDGTHSD 505
Cdd:COG4555 10 KYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGllkpdsGsiLIDGEDVRKEPREArrqigVL-PDERGLYDR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 506 TSVLDFV------FESGVGTKEAIKDKLIE-FGFtDEMIAMPISALSGGWKMKLALARAVLRNADILLLDEPTNHLDTVN 578
Cdd:COG4555 89 LTVRENIryfaelYGLFDEELKKRIEELIElLGL-EEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNGLDVMA 167
|
170 180 190
....*....|....*....|....*....|....*.
gi 6323278 579 VAWLVNYLNTCGITSITI---SHDSVFLDNVCEYII 611
Cdd:COG4555 168 RRLLREILRALKKEGKTVlfsSHIMQEVEALCDRVV 203
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
437-599 |
1.53e-22 |
|
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: 96.83 E-value: 1.53e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 437 SLAYGAKILLNKTQLRLKRARRYGICGPNGCGKSTLMRAI------ANGQ--VDGFPTQEECRTV-YVE--HDIDGThSD 505
Cdd:cd03235 6 TVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAIlgllkpTSGSirVFGKPLEKERKRIgYVPqrRSIDRD-FP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 506 TSVLDFVFESGVGTKEAIK----------DKLIEFGFTDEMIAMPISALSGGWKMKLALARAVLRNADILLLDEPTNHLD 575
Cdd:cd03235 85 ISVRDVVLMGLYGHKGLFRrlskadkakvDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVD 164
|
170 180
....*....|....*....|....*..
gi 6323278 576 TVNVAW---LVNYLNTCGITSITISHD 599
Cdd:cd03235 165 PKTQEDiyeLLRELRREGMTILVVTHD 191
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
436-611 |
1.77e-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: 96.77 E-value: 1.77e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 436 FSLAY--GAKILLNKTQLRLKRARRYGICGPNGCGKSTLMRAIA------NGQV--DGFPTQEECRTVYVEHdIdGT--- 502
Cdd:cd03225 5 LSFSYpdGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNgllgptSGEVlvDGKDLTKLSLKELRRK-V-GLvfq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 503 HSD-----TSVLD---FVFES-GVGTKEAIK--DKLIEFGFTDEMIAMPISALSGGWKMKLALARAVLRNADILLLDEPT 571
Cdd:cd03225 83 NPDdqffgPTVEEevaFGLENlGLPEEEIEErvEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPT 162
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 6323278 572 NHLDTVNVAWLVNY---LNTCGITSITISHDSVFLDNVCEYII 611
Cdd:cd03225 163 AGLDPAGRRELLELlkkLKAEGKTIIIVTHDLDLLLELADRVI 205
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
451-572 |
3.23e-22 |
|
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: 93.87 E-value: 3.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 451 LRLKRARRYGICGPNGCGKSTLMRAIA------NGQV--DGFPTQEECRT------VYVEHDiDGTHSDTSVLDFVFESG 516
Cdd:pfam00005 6 LTLNPGEILALVGPNGAGKSTLLKLIAgllsptEGTIllDGQDLTDDERKslrkeiGYVFQD-PQLFPRLTVRENLRLGL 84
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6323278 517 VG---TKEAIKDKLIEF-------GFTDEMIAMPISALSGGWKMKLALARAVLRNADILLLDEPTN 572
Cdd:pfam00005 85 LLkglSKREKDARAEEAleklglgDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
437-599 |
3.60e-21 |
|
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: 91.73 E-value: 3.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 437 SLAYGAKILLNKTQLRLKRARRYGICGPNGCGKSTLMRAIA------NGQV--DG-----FPTQEECRTV-YVEHDIDgt 502
Cdd:cd03214 6 SVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAgllkpsSGEIllDGkdlasLSPKELARKIaYVPQALE-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 503 hsDTSVLDFvfesgvgtkeaiKDKliefgftdemiamPISALSGGWKMKLALARAVLRNADILLLDEPTNHLDTVNVAWL 582
Cdd:cd03214 84 --LLGLAHL------------ADR-------------PFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIEL 136
|
170 180
....*....|....*....|.
gi 6323278 583 VNYL----NTCGITSITISHD 599
Cdd:cd03214 137 LELLrrlaRERGKTVVMVLHD 157
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
437-610 |
1.85e-20 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 91.69 E-value: 1.85e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 437 SLAYGAKILLNKTQLRLKRARRYGICGPNGCGKSTLMRAIAN------GQV--DGFPTQEECRTV-YV--EHDIDGTHSd 505
Cdd:COG1121 13 TVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGllpptsGTVrlFGKPPRRARRRIgYVpqRAEVDWDFP- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 506 TSVLDFVfESGV------------GTKEAIKDKLIEFGFTDeMIAMPISALSGGWKMKLALARAVLRNADILLLDEPTNH 573
Cdd:COG1121 92 ITVRDVV-LMGRygrrglfrrpsrADREAVDEALERVGLED-LADRPIGELSGGQQQRVLLARALAQDPDLLLLDEPFAG 169
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 6323278 574 LDTVNVAW---LVNYLNTCGITSITISHDsvfLDNVCEYI 610
Cdd:COG1121 170 VDAATEEAlyeLLRELRREGKTILVVTHD---LGAVREYF 206
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
668-970 |
1.69e-19 |
|
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: 87.91 E-value: 1.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 668 KVTNMEFQYPGTSKPQITDINFQCSLSSRIAVIGPNGAGKSTLINVLTGELLPTSGEVYTHENCRIAYIKQHAFAHIesh 747
Cdd:cd03225 1 ELKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKV--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 748 ldktpsEYIqwrFQtgedretmdRANRQInendaeamnkifkiegtprriagihsrrkFKNTYEYECSFLLgENIGMkse 827
Cdd:cd03225 78 ------GLV---FQ---------NPDDQF-----------------------------FGPTVEEEVAFGL-ENLGL--- 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 828 rwvpmmsvdnawiprgelveSHSKMVAEVDmkEALASGQFRPLTRKEIEEhcsmlgldpeivshsrirgLSGGQKVKLVL 907
Cdd:cd03225 107 --------------------PEEEIEERVE--EALELVGLEGLRDRSPFT-------------------LSGGQKQRVAI 145
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6323278 908 AAGTWQRPHLIVLDEPTNYLDRDSLGALSKALKEF--EG-GVIIITHSAEFTKNLTEEVWAVKDGR 970
Cdd:cd03225 146 AGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLkaEGkTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
440-586 |
2.29e-19 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 88.20 E-value: 2.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 440 YGAKILLNKTQLRLKRARRYGICGPNGCGKSTLMRAIAN------GQ--VDGFPTQEECRTV-----YV-EHDidGTHSD 505
Cdd:COG1131 10 YGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGllrptsGEvrVLGEDVARDPAEVrrrigYVpQEP--ALYPD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 506 TSVLDFV--FES--GVGTKEAIK--DKLIE-FGFTDEMiAMPISALSGGWKMKLALARAVLRNADILLLDEPTNHLDTVN 578
Cdd:COG1131 88 LTVRENLrfFARlyGLPRKEAREriDELLElFGLTDAA-DRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDPEA 166
|
....*...
gi 6323278 579 VAWLVNYL 586
Cdd:COG1131 167 RRELWELL 174
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
433-618 |
2.91e-19 |
|
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: 87.31 E-value: 2.91e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 433 NCEFSLAYGAKILLNKTqLRLKRARRYGICGPNGCGKSTLMRAIA------NGQV--DG--FPTQEECRTV-YVEHDIDG 501
Cdd:cd03226 4 NISFSYKKGTEILDDLS-LDLYAGEIIALTGKNGAGKTTLAKILAglikesSGSIllNGkpIKAKERRKSIgYVMQDVDY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 502 THSDTSVLDfvfESGVGTKEAIKDK------LIEFGFTDEMIAMPISaLSGGWKMKLALARAVLRNADILLLDEPTNHLD 575
Cdd:cd03226 83 QLFTDSVRE---ELLLGLKELDAGNeqaetvLKDLDLYALKERHPLS-LSGGQKQRLAIAAALLSGKDLLIFDEPTSGLD 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 6323278 576 ---TVNVAWLVNYLNTCGITSITISHDSVFLDNVCEYIINYEGLKL 618
Cdd:cd03226 159 yknMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| CD_eEF3 |
cd18626 |
chromodomain-like insertion in an ATPase domain of elongation factor eEF3; Eukaryotic ... |
794-861 |
3.20e-19 |
|
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: 82.26 E-value: 3.20e-19
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6323278 794 PRRIAGIHSRRKFKNTYEYECSfllgenigmkserWVPMMSVDNAWIPRGELVE-SHSKMVAEVDMKEA 861
Cdd:cd18626 1 KRVIEKIVGRRKLKKSYEYEVK-------------WKGMSSKDNSWIPREELEEmGFEKLVQEVDDKEA 56
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
437-598 |
4.53e-19 |
|
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: 85.51 E-value: 4.53e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 437 SLAYGAKI--LLNKTQLRLKRARRYGICGPNGCGKSTLMRAIA------------NGQ-VDGFPTQEECRTV-YVEHDId 500
Cdd:cd03228 7 SFSYPGRPkpVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLrlydptsgeiliDGVdLRDLDLESLRKNIaYVPQDP- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 501 gthsdtsvldFVFEsgvGTkeaIKDKLiefgftdemiampisaLSGGWKMKLALARAVLRNADILLLDEPTNHLDTVNVA 580
Cdd:cd03228 86 ----------FLFS---GT---IRENI----------------LSGGQRQRIAIARALLRDPPILILDEATSALDPETEA 133
|
170 180
....*....|....*....|
gi 6323278 581 WLVNYLN--TCGITSITISH 598
Cdd:cd03228 134 LILEALRalAKGKTVIVIAH 153
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
406-628 |
5.77e-19 |
|
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: 91.92 E-value: 5.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 406 EFRKRAVDN---IPVGPNFDDEEDEGEDLCNcefslAYGAKILLNKTQLRLKRARRYGICGPNGCGKSTLMRAIAnGQVD 482
Cdd:TIGR03719 300 EFQKRNETAeiyIPPGPRLGDKVIEAENLTK-----AFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMIT-GQEQ 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 483 gfPTQEECR---TV---YVEH---DIDGTHSdtsvldfVFE--SG------VGTKEaIKDK--LIEFGFTDEMIAMPISA 543
Cdd:TIGR03719 374 --PDSGTIEigeTVklaYVDQsrdALDPNKT-------VWEeiSGgldiikLGKRE-IPSRayVGRFNFKGSDQQKKVGQ 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 544 LSGGWKMKLALARAVLRNADILLLDEPTNHLDTVNVAWLVNYLNTCGITSITISHDSVFLDNVCEYIINYEG-LKLRKYK 622
Cdd:TIGR03719 444 LSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEALLNFAGCAVVISHDRWFLDRIATHILAFEGdSHVEWFE 523
|
....*.
gi 6323278 623 GNFTEF 628
Cdd:TIGR03719 524 GNFSEY 529
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
633-975 |
7.00e-19 |
|
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: 92.20 E-value: 7.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 633 PAAKAYEELSNTDLEfkfPEPGYLEGVKTKQKAIVKVTNMEFQYPGTSKPQITDINFQCSLSSRIAVIGPNGAGKSTLIN 712
Cdd:COG2274 443 IALERLDDILDLPPE---REEGRSKLSLPRLKGDIELENVSFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLK 519
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 713 VLTGELLPTSGEVYthencriayikqhafahieshLDktpseyiqwrfqtGEDRETMDRAN--RQINENDAEamNKIFki 790
Cdd:COG2274 520 LLLGLYEPTSGRIL---------------------ID-------------GIDLRQIDPASlrRQIGVVLQD--VFLF-- 561
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 791 EGTprrIAgihsrrkfkntyeyecsfllgENIGMkserwvpmmsvdnawiprgelveshskmvaevdmkealasgqFRP- 869
Cdd:COG2274 562 SGT---IR---------------------ENITL------------------------------------------GDPd 575
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 870 LTRKEIEEHCSMLGLDPEIVSH-----SRI----RGLSGGQKVKLVLAAGTWQRPHLIVLDEPTNYLDRDSLGALSKALK 940
Cdd:COG2274 576 ATDEEIIEAARLAGLHDFIEALpmgydTVVgeggSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLR 655
|
330 340 350
....*....|....*....|....*....|....*..
gi 6323278 941 EFEGG--VIIITHSAEfTKNLTEEVWAVKDGRMTPSG 975
Cdd:COG2274 656 RLLKGrtVIIIAHRLS-TIRLADRIIVLDKGRIVEDG 691
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
460-735 |
1.39e-18 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 91.02 E-value: 1.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 460 GICGPNGCGKSTLMRAIA-----N-GQVDGFPTQEEC---------------------RTV----YVE---HDIDGTHSD 505
Cdd:PRK13409 103 GILGPNGIGKTTAVKILSgelipNlGDYEEEPSWDEVlkrfrgtelqnyfkklyngeiKVVhkpqYVDlipKVFKGKVRE 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 506 tsVLDFVFESGVgtkeaiKDKLIEFGFTDEMIAMPISALSGGWKMKLALARAVLRNADILLLDEPTNHLDT---VNVAWL 582
Cdd:PRK13409 183 --LLKKVDERGK------LDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIrqrLNVARL 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 583 VNYLnTCGITSITISHDSVFLDNVCEYI----------------------INY--------EGLKLRKYKgnfTEFVKKC 632
Cdd:PRK13409 255 IREL-AEGKYVLVVEHDLAVLDYLADNVhiaygepgaygvvskpkgvrvgINEylkgylpeENMRIRPEP---IEFEERP 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 633 PAAKAYEE--LSNTDLEFKFP------EPGYLegvktkqkaivkvtnmefqYPGtskpQItdinfqcslssrIAVIGPNG 704
Cdd:PRK13409 331 PRDESEREtlVEYPDLTKKLGdfslevEGGEI-------------------YEG----EV------------IGIVGPNG 375
|
330 340 350
....*....|....*....|....*....|.
gi 6323278 705 AGKSTLINVLTGELLPTSGEVYTheNCRIAY 735
Cdd:PRK13409 376 IGKTTFAKLLAGVLKPDEGEVDP--ELKISY 404
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
668-975 |
3.07e-18 |
|
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: 85.29 E-value: 3.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 668 KVTNMEFQYPgtSKPQITDINFQCSLSSRIAVIGPNGAGKSTLINVLTGELLPTSGEVYthencriayikqhafahIEsh 747
Cdd:COG4555 3 EVENLSKKYG--KVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSIL-----------------ID-- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 748 ldktpseyiqwrfqtGEDretmdranrqINENDAEAMNKIFKIEGTPrriaGIHSRRKFKntyeyecsfllgENIGMkse 827
Cdd:COG4555 62 ---------------GED----------VRKEPREARRQIGVLPDER----GLYDRLTVR------------ENIRY--- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 828 rwvpmmsvdnawiprgelveshskmvaevdmkEALASGQFRPLTRKEIEEHCSMLGLDPEIvsHSRIRGLSGGQKVKLVL 907
Cdd:COG4555 98 --------------------------------FAELYGLFDEELKKRIEELIELLGLEEFL--DRRVGELSTGMKKKVAL 143
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6323278 908 AAGTWQRPHLIVLDEPTNYLDRDSLGALSKALKEF--EGGVIII-THSAEFTKNLTEEVWAVKDGRMTPSG 975
Cdd:COG4555 144 ARALVHDPKVLLLDEPTNGLDVMARRLLREILRALkkEGKTVLFsSHIMQEVEALCDRVVILHKGKVVAQG 214
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
437-611 |
8.63e-18 |
|
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: 83.54 E-value: 8.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 437 SLAY-GAKILLNKTQLRLKRARRYGICGPNGCGKSTLMRAIaNG---------QVDGFPTQEE-----CRTV-YVEHDID 500
Cdd:COG1122 7 SFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLL-NGllkptsgevLVDGKDITKKnlrelRRKVgLVFQNPD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 501 gthsD----TSVLD---FVFE-SGVGTKEA---IKDKLIEFGFTDeMIAMPISALSGGWKMKLALARAVLRNADILLLDE 569
Cdd:COG1122 86 ----DqlfaPTVEEdvaFGPEnLGLPREEIrerVEEALELVGLEH-LADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDE 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 6323278 570 PTNHLDTVNVAWLVNY---LNTCGITSITISHDSVFLDNVCEYII 611
Cdd:COG1122 161 PTAGLDPRGRRELLELlkrLNKEGKTVIIVTHDLDLVAELADRVI 205
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
667-975 |
8.71e-18 |
|
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: 83.54 E-value: 8.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 667 VKVTNMEFQYPGtSKPQITDINFQCSLSSRIAVIGPNGAGKSTLINVLTGELLPTSGEVYthencriayikqhafahies 746
Cdd:COG1122 1 IELENLSFSYPG-GTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVL-------------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 747 hldktpseyiqwrfqtgedretmdranrqinendaeamnkifkIEGTPRRIAGIHSRRK-------------FKNTYEYE 813
Cdd:COG1122 60 -------------------------------------------VDGKDITKKNLRELRRkvglvfqnpddqlFAPTVEED 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 814 CSFLLgENIGMkserwvpmmsvdnawiprgelveSHSKMVAEVDmkEALAsgqfrpltrkeieehcsMLGLDPeiVSHSR 893
Cdd:COG1122 97 VAFGP-ENLGL-----------------------PREEIRERVE--EALE-----------------LVGLEH--LADRP 131
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 894 IRGLSGGQKvKLVLAAGTW-QRPHLIVLDEPTNYLD---RDSLGALSKALKEFEGGVIIITHSAEFTKNLTEEVWAVKDG 969
Cdd:COG1122 132 PHELSGGQK-QRVAIAGVLaMEPEVLVLDEPTAGLDprgRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDG 210
|
....*.
gi 6323278 970 RMTPSG 975
Cdd:COG1122 211 RIVADG 216
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
460-756 |
9.19e-18 |
|
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: 88.30 E-value: 9.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 460 GICGPNGCGKSTLMRAIA-----N-GQVDGFPTQEEC---------------------RTV----YVE---HDIDGTHSD 505
Cdd:COG1245 103 GILGPNGIGKSTALKILSgelkpNlGDYDEEPSWDEVlkrfrgtelqdyfkklangeiKVAhkpqYVDlipKVFKGTVRE 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 506 tsVLDFVFESGVgtkeaiKDKLIEFGFTDEMIAMPISALSGGWKMKLALARAVLRNADILLLDEPTNHLDT---VNVAWL 582
Cdd:COG1245 183 --LLEKVDERGK------LDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIyqrLNVARL 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 583 VNYLNTCGITSITISHDSVFLDNVCEYI----------------------INY--------EGLKLRKYKGNFTefVKKC 632
Cdd:COG1245 255 IRELAEEGKYVLVVEHDLAILDYLADYVhilygepgvygvvskpksvrvgINQyldgylpeENVRIRDEPIEFE--VHAP 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 633 PAAKAYEELSN-TDLEFKFP------EPGYLegvktkqkaivkvtnmefqYPGTSkpqitdinfqcslssrIAVIGPNGA 705
Cdd:COG1245 333 RREKEEETLVEyPDLTKSYGgfslevEGGEI-------------------REGEV----------------LGIVGPNGI 377
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 6323278 706 GKSTLINVLTGELLPTSGEVytHENCRIAYIKQhafaHIESHLDKTPSEYI 756
Cdd:COG1245 378 GKTTFAKILAGVLKPDEGEV--DEDLKISYKPQ----YISPDYDGTVEEFL 422
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
440-611 |
1.43e-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: 81.46 E-value: 1.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 440 YGAKILLNKTQLRLKRARRYGICGPNGCGKSTLMRAIA------NGQV--DGfptqeecRTVYVEHDIDGTHSDTsvLDF 511
Cdd:cd03229 10 YGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAgleepdSGSIliDG-------EDLTDLEDELPPLRRR--IGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 512 VFESG--VGTKEAIkdkliefgftdEMIAMPisaLSGGWKMKLALARAVLRNADILLLDEPTNHLDTVNVAWLVNYLNT- 588
Cdd:cd03229 81 VFQDFalFPHLTVL-----------ENIALG---LSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRREVRALLKSl 146
|
170 180
....*....|....*....|....*.
gi 6323278 589 ---CGITSITISHDSVFLDNVCEYII 611
Cdd:cd03229 147 qaqLGITVVLVTHDLDEAARLADRVV 172
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
436-599 |
2.67e-17 |
|
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: 81.80 E-value: 2.67e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 436 FSLAYGAKILLNKTQLRLKRARRYGICGPNGCGKSTLMRAIA------------NGQ-VDGFPTQEecRTV-YV-EHDID 500
Cdd:cd03259 6 LSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAglerpdsgeiliDGRdVTGVPPER--RNIgMVfQDYAL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 501 GTHsdTSVLD---FVFESGVGTKEAIKDKLIE----FGFTDEMIAMPiSALSGGWKMKLALARAVLRNADILLLDEPTNH 573
Cdd:cd03259 84 FPH--LTVAEniaFGLKLRGVPKAEIRARVREllelVGLEGLLNRYP-HELSGGQQQRVALARALAREPSLLLLDEPLSA 160
|
170 180 190
....*....|....*....|....*....|.
gi 6323278 574 LDTvNVAW-----LVNYLNTCGITSITISHD 599
Cdd:cd03259 161 LDA-KLREelreeLKELQRELGITTIYVTHD 190
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
437-611 |
6.80e-17 |
|
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: 81.01 E-value: 6.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 437 SLAYGAKILLNKTQLRLKRARRYGICGPNGCGKSTLMRAIAnGQVDgfPTQEEcrtVYVE-HDIDGTH------------ 503
Cdd:cd03261 7 TKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIV-GLLR--PDSGE---VLIDgEDISGLSeaelyrlrrrmg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 504 ---------SDTSVLDFV----FESGVGTKEAIKD----KLIEFGFTDEMIAMPiSALSGGWKMKLALARAVLRNADILL 566
Cdd:cd03261 81 mlfqsgalfDSLTVFENVafplREHTRLSEEEIREivleKLEAVGLRGAEDLYP-AELSGGMKKRVALARALALDPELLL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 6323278 567 LDEPTNHLDTVNVAWLVNYLNTC----GITSITISHDSVFLDNVCEYII 611
Cdd:cd03261 160 YDEPTAGLDPIASGVIDDLIRSLkkelGLTSIMVTHDLDTAFAIADRIA 208
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
437-611 |
7.49e-17 |
|
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: 85.66 E-value: 7.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 437 SLAYG--AKILLNKTQLRLKRARRYGICGPNGCGKSTLMRAIA------NGQV--DGFPTQEECRTV------YVEHDID 500
Cdd:COG2274 480 SFRYPgdSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLglyeptSGRIliDGIDLRQIDPASlrrqigVVLQDVF 559
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 501 ---GThsdtsVLD-FVFESGVGTKEAIKDKLIEFGFTDEMIAMP------I----SALSGGWKMKLALARAVLRNADILL 566
Cdd:COG2274 560 lfsGT-----IREnITLGDPDATDEEIIEAARLAGLHDFIEALPmgydtvVgeggSNLSGGQRQRLAIARALLRNPRILI 634
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 6323278 567 LDEPTNHLDTVNVAWLVNYLNT--CGITSITISHDSVFLDNvCEYII 611
Cdd:COG2274 635 LDEATSALDAETEAIILENLRRllKGRTVIIIAHRLSTIRL-ADRII 680
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
698-954 |
2.22e-16 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 78.43 E-value: 2.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 698 AVIGPNGAGKSTLINVLTGELLPTSGEVYTHENCRIAYIKQHafahieSHLDKT-PSeyiqwrfqTGEDRETMDRanrqi 776
Cdd:NF040873 22 AVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQR------SEVPDSlPL--------TVRDLVAMGR----- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 777 nendaeamnkifkiegtprriagihsrrkfkntyeyecsfllgenigmkserwvpmmsvdnaWIPRGELveshskmvaev 856
Cdd:NF040873 83 --------------------------------------------------------------WARRGLW----------- 89
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 857 dmkealasgqfRPLT---RKEIEEHCSMLGLDPeiVSHSRIRGLSGGQKVKLVLAAGTWQRPHLIVLDEPTNYLDRDSLG 933
Cdd:NF040873 90 -----------RRLTrddRAAVDDALERVGLAD--LAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRE 156
|
250 260
....*....|....*....|....
gi 6323278 934 ALSKALKEFEG---GVIIITHSAE 954
Cdd:NF040873 157 RIIALLAEEHArgaTVVVVTHDLE 180
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
684-925 |
4.00e-16 |
|
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: 76.53 E-value: 4.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 684 ITDINFQCSLSSRIAVIGPNGAGKSTLINVLTGELLPTSGEVythencriayikqhafahieshldktpseyiqwrfqtg 763
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTI-------------------------------------- 42
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 764 edretmdranrqinendaeamnkifKIEGTPRRIAGIHSRRKfkntyeyecsfllgeNIGMKSE--RWVPMMSV-DNAWI 840
Cdd:pfam00005 43 -------------------------LLDGQDLTDDERKSLRK---------------EIGYVFQdpQLFPRLTVrENLRL 82
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 841 PRgeLVESHSKMVAEVDMKEALasgqfrpltrkeieEHCSMLGLDPEIVsHSRIRGLSGGQKVKLVLAAGTWQRPHLIVL 920
Cdd:pfam00005 83 GL--LLKGLSKREKDARAEEAL--------------EKLGLGDLADRPV-GERPGTLSGGQRQRVAIARALLTKPKLLLL 145
|
....*
gi 6323278 921 DEPTN 925
Cdd:pfam00005 146 DEPTA 150
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
665-951 |
6.22e-16 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 78.59 E-value: 6.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 665 AIVKVTNMEFQYPGtsKPQITDINFQCSLSSRIAVIGPNGAGKSTLINVLTGELLPTSGEV------YTHENCRIAYIKQ 738
Cdd:COG1121 5 PAIELENLTVSYGG--RPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVrlfgkpPRRARRRIGYVPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 739 HAfahieshldktpseYIQWRFqtgedretmdranrqinendaeamnkifkiegtPrriagihsrrkfkntyeyecsfll 818
Cdd:COG1121 83 RA--------------EVDWDF---------------------------------P------------------------ 91
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 819 genigmkserwvpmMSVdnawiprGELVES--HSKMvaevdmkealasGQFRPLTRKE---IEEHCSMLGLDPeiVSHSR 893
Cdd:COG1121 92 --------------ITV-------RDVVLMgrYGRR------------GLFRRPSRADreaVDEALERVGLED--LADRP 136
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6323278 894 IRGLSGGQKVKLVLA---AgtwQRPHLIVLDEPTNYLDRDSLGALSKALKEF--EG-GVIIITH 951
Cdd:COG1121 137 IGELSGGQQQRVLLAralA---QDPDLLLLDEPFAGVDAATEEALYELLRELrrEGkTILVVTH 197
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
686-951 |
6.27e-16 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 78.18 E-value: 6.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 686 DINFQCSLSSRIAVIGPNGAGKSTLINVLTGELLPTSGEVythencRIAyikqhafahieshldktpseyiqwrfqtGED 765
Cdd:COG1131 18 GVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEV------RVL----------------------------GED 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 766 retmdranrqINENDAEAMnkifkiegtpRRIAgihsrrkfkntyeyecsfLLGENIGMkserwVPMMSVdnawiprGEL 845
Cdd:COG1131 64 ----------VARDPAEVR----------RRIG------------------YVPQEPAL-----YPDLTV-------REN 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 846 VESHSKMvAEVDMKEAlasgqfrpltRKEIEEHCSMLGLDPeiVSHSRIRGLSGGQKVKLVLAAGTWQRPHLIVLDEPTN 925
Cdd:COG1131 94 LRFFARL-YGLPRKEA----------RERIDELLELFGLTD--AADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTS 160
|
250 260
....*....|....*....|....*....
gi 6323278 926 YLD---RDSLGALSKALKEFEGGVIIITH 951
Cdd:COG1131 161 GLDpeaRRELWELLRELAAEGKTVLLSTH 189
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
651-966 |
6.47e-16 |
|
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: 81.95 E-value: 6.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 651 PEPGYLEGVKTKQKAIVkVTNMEFQYPGTSkPQITDINFQCSLSSRIAVIGPNGAGKSTLINVLTGELLPTSGEVythen 730
Cdd:TIGR02857 307 PLAGKAPVTAAPASSLE-FSGVSVAYPGRR-PALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSI----- 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 731 cRIAYIKqhaFAHIESHldktpseyiQWRfqtgedretmdranrqinendaeamnkifkiegtpRRIAgihsrrkfknty 810
Cdd:TIGR02857 380 -AVNGVP---LADADAD---------SWR-----------------------------------DQIA------------ 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 811 eyecsfllgenigmkserWVPmmsvDNAWIPRGELVES--HSKMVA-EVDMKEALASGQFRPLTrKEIEEhcsmlGLDPE 887
Cdd:TIGR02857 400 ------------------WVP----QHPFLFAGTIAENirLARPDAsDAEIREALERAGLDEFV-AALPQ-----GLDTP 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 888 IVSHSriRGLSGGQKVKLVLAAGTWQRPHLIVLDEPTNYLDRDSLGALSKALKEFEGG--VIIITHSAEFTKNLtEEVWA 965
Cdd:TIGR02857 452 IGEGG--AGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGrtVLLVTHRLALAALA-DRIVV 528
|
.
gi 6323278 966 V 966
Cdd:TIGR02857 529 L 529
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
667-976 |
1.09e-15 |
|
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: 81.34 E-value: 1.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 667 VKVTNMEFQYPGtSKPQITDINFQCSLSSRIAVIGPNGAGKSTLINVLTGELLPTSGEVythencriayikqhafahies 746
Cdd:COG4988 337 IELEDVSFSYPG-GRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSI--------------------- 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 747 hldktpseyiqwrfqtgedretmdranrqinendaeamnkifKIEGTPRRIAGIHSRRKfkntyeyecsfllgeNIGmks 826
Cdd:COG4988 395 ------------------------------------------LINGVDLSDLDPASWRR---------------QIA--- 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 827 erWVPmmsvDNAWIPRGELveshskmvaevdmKEALASGqfRP-LTRKEIEEHCSMLGLDPEIVS-----HSRI----RG 896
Cdd:COG4988 415 --WVP----QNPYLFAGTI-------------RENLRLG--RPdASDEELEAALEAAGLDEFVAAlpdglDTPLgeggRG 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 897 LSGGQKVKLVLAAGTWQRPHLIVLDEPTNYLDRDSLGALSKALKEFEGG--VIIITHSAEFTKNLtEEVWAVKDGRMTPS 974
Cdd:COG4988 474 LSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGrtVILITHRLALLAQA-DRILVLDDGRIVEQ 552
|
..
gi 6323278 975 GH 976
Cdd:COG4988 553 GT 554
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
451-611 |
1.85e-15 |
|
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: 77.15 E-value: 1.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 451 LRLKRARRYGICGPNGCGKSTLMRAIA------NGQV--DGFP-----TQEECRTV-YVEHDIDGT-HSDTSVLDFVFE- 514
Cdd:COG1124 26 LEVAPGESFGLVGESGSGKSTLLRALAglerpwSGEVtfDGRPvtrrrRKAFRRRVqMVFQDPYASlHPRHTVDRILAEp 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 515 ---SGVG-TKEAIKDKLIEFGFTDEMIAMPISALSGGWKMKLALARAVLRNADILLLDEPTNHLDTVNVAWLVNYLNTC- 589
Cdd:COG1124 106 lriHGLPdREERIAELLEQVGLPPSFLDRYPHQLSGGQRQRVAIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLr 185
|
170 180
....*....|....*....|....*
gi 6323278 590 ---GITSITISHDSVFLDNVCEYII 611
Cdd:COG1124 186 eerGLTYLFVSHDLAVVAHLCDRVA 210
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
435-609 |
2.02e-15 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 77.36 E-value: 2.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 435 EFSLAYGAKILLNKTQLRLKRARRYGICGPNGCGKSTLMRAIA------NGQV-------DGFPTQEECRTVYVEHDIDG 501
Cdd:PRK11231 7 NLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFArlltpqSGTVflgdkpiSMLSSRQLARRLALLPQHHL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 502 THSDTSVLDFVfESG-----------VGTKEAIKDKLIEFGFTDEMIAMPISALSGGWKMKLALARAVLRNADILLLDEP 570
Cdd:PRK11231 87 TPEGITVRELV-AYGrspwlslwgrlSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEP 165
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 6323278 571 TNHLD---TVNVAWLVNYLNTCGITSITISHDsvfLDNVCEY 609
Cdd:PRK11231 166 TTYLDinhQVELMRLMRELNTQGKTVVTVLHD---LNQASRY 204
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
460-611 |
3.33e-15 |
|
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: 76.78 E-value: 3.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 460 GICGPNGCGKSTLMRAIAN------GQVD-------GFPTQEE-CRTVYVEHDIDgTHSDTSVLDFV------FESGVGT 519
Cdd:TIGR03873 31 GLLGPNGSGKSTLLRLLAGalrpdaGTVDlagvdlhGLSRRARaRRVALVEQDSD-TAVPLTVRDVValgripHRSLWAG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 520 KEAIKDKLiefgfTDEMIAM---------PISALSGGWKMKLALARAVLRNADILLLDEPTNHLDT---VNVAWLVNYLN 587
Cdd:TIGR03873 110 DSPHDAAV-----VDRALARtelshladrDMSTLSGGERQRVHVARALAQEPKLLLLDEPTNHLDVraqLETLALVRELA 184
|
170 180
....*....|....*....|....
gi 6323278 588 TCGITSITISHDSVFLDNVCEYII 611
Cdd:TIGR03873 185 ATGVTVVAALHDLNLAASYCDHVV 208
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
431-598 |
3.86e-15 |
|
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: 74.17 E-value: 3.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 431 LCNCEFSLAYGAKILLNKTQLRLKRARRYGICGPNGCGKSTLMRAIANGQVdgfPTQEECRtvyvehdIDGTHSDTSVLD 510
Cdd:cd03246 3 VENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLR---PTSGRVR-------LDGADISQWDPN 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 511 fVFESGVGTKeAIKDKLieFGFTdemIAMPIsaLSGGWKMKLALARAVLRNADILLLDEPTNHLDTVNVAWL---VNYLN 587
Cdd:cd03246 73 -ELGDHVGYL-PQDDEL--FSGS---IAENI--LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALnqaIAALK 143
|
170
....*....|.
gi 6323278 588 TCGITSITISH 598
Cdd:cd03246 144 AAGATRIVIAH 154
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
667-741 |
1.01e-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: 73.19 E-value: 1.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 667 VKVTNMEFQYPGTSKPQITDINFQCSLSSRIAVIGPNGAGKSTLINVLTGELLPTSGEV---------YTHENCR--IAY 735
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEIlidgvdlrdLDLESLRknIAY 80
|
....*.
gi 6323278 736 IKQHAF 741
Cdd:cd03228 81 VPQDPF 86
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
436-603 |
1.85e-14 |
|
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: 73.66 E-value: 1.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 436 FSLAYGAKILLNKTQLRLKRARRYGICGPNGCGKSTLMRAIAN------GQV--DGFPtqeecrtvyvehdIDGTHSDTS 507
Cdd:cd03293 10 YGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGlerptsGEVlvDGEP-------------VTGPGPDRG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 508 vldFVFES--------------------GVGTKEAIK--DKLIEF----GFTDemiAMPiSALSGGWKMKLALARAVLRN 561
Cdd:cd03293 77 ---YVFQQdallpwltvldnvalglelqGVPKAEAREraEELLELvglsGFEN---AYP-HQLSGGMRQRVALARALAVD 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 6323278 562 ADILLLDEPTNHLD--TVNV--AWLVNYLNTCGITSITISHD---SVFL 603
Cdd:cd03293 150 PDVLLLDEPFSALDalTREQlqEELLDIWRETGKTVLLVTHDideAVFL 198
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
684-951 |
1.98e-14 |
|
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: 74.01 E-value: 1.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 684 ITDINFQCSLSSRIAVIGPNGAGKSTLINVLTGELLPTSGEVythencriayikqhafahieshldktpseyiqwRFQtG 763
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSV---------------------------------LFD-G 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 764 EDretmdranrqinendaeamnkifkIEGT-PRRIA--GIhsRRKFKNTyeyecsfllgenigmkseRWVPMMSV-DNAW 839
Cdd:cd03219 62 ED------------------------ITGLpPHEIArlGI--GRTFQIP------------------RLFPELTVlENVM 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 840 IPRGELVESHSKMVAEVDMKEALasgqfrpltRKEIEEHCSMLGLDPeiVSHSRIRGLSGGQKVKLVLAAGTWQRPHLIV 919
Cdd:cd03219 98 VAAQARTGSGLLLARARREEREA---------RERAEELLERVGLAD--LADRPAGELSYGQQRRLEIARALATDPKLLL 166
|
250 260 270
....*....|....*....|....*....|....*
gi 6323278 920 LDEPT---NYLDRDSLGALSKALKEFEGGVIIITH 951
Cdd:cd03219 167 LDEPAaglNPEETEELAELIRELRERGITVLLVEH 201
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
440-598 |
2.69e-14 |
|
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: 73.02 E-value: 2.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 440 YGAKILLNKTQLRLKRARRYGICGPNGCGKSTLMRAIAngqvdGF--PTQEECRT--VYVEHDIDGTHSDTSVLDF---- 511
Cdd:cd03268 10 YGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIIL-----GLikPDSGEITFdgKSYQKNIEALRRIGALIEApgfy 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 512 ----------VFESGVGTKEAIKDKLIEFGFTDEMIAMPISALSGGWKMKLALARAVLRNADILLLDEPTNHLDTVNVAW 581
Cdd:cd03268 85 pnltarenlrLLARLLGIRKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGIKE 164
|
170 180
....*....|....*....|
gi 6323278 582 LVNY---LNTCGITSITISH 598
Cdd:cd03268 165 LRELilsLRDQGITVLISSH 184
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
663-951 |
3.12e-14 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 74.28 E-value: 3.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 663 QKAIVKVTNMEFQYPGTSKPQITDINFQCSLSSRIAVIGPNGAGKSTLINVLTGELLPTSGEVythencriayikqhafa 742
Cdd:PRK13635 2 KEEIIRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTI----------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 743 hieshldktpseyiqwrfqtgedretmdranrqinendaeamnKIFKIEGTPRRIAGIhsRRK----FKN--------TY 810
Cdd:PRK13635 65 -------------------------------------------TVGGMVLSEETVWDV--RRQvgmvFQNpdnqfvgaTV 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 811 EYECSFLLgENIGmkserwvpmmsvdnawIPRGELVESHSKMVAEVDMKEalasgqFrpltrkeieehcsmlgLDPEivS 890
Cdd:PRK13635 100 QDDVAFGL-ENIG----------------VPREEMVERVDQALRQVGMED------F----------------LNRE--P 138
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6323278 891 HSrirgLSGGQKVKLVLAAGTWQRPHLIVLDEPTNYLD---RDSLGALSKALKEfEGG--VIIITH 951
Cdd:PRK13635 139 HR----LSGGQKQRVAIAGVLALQPDIIILDEATSMLDprgRREVLETVRQLKE-QKGitVLSITH 199
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
441-599 |
3.25e-14 |
|
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: 76.63 E-value: 3.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 441 GAKILLNKTQLRLKRARRYGICGPNGCGKSTLMRAIA------NGQV--DGFPTQE------ECRTVYVEHDidgTHS-D 505
Cdd:TIGR02868 346 GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAglldplQGEVtlDGVPVSSldqdevRRRVSVCAQD---AHLfD 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 506 TSVLDFV-FESGVGTKEAIKDKLIEFGFTDEMIAMPI----------SALSGGWKMKLALARAVLRNADILLLDEPTNHL 574
Cdd:TIGR02868 423 TTVRENLrLARPDATDEELWAALERVGLADWLRALPDgldtvlgeggARLSGGERQRLALARALLADAPILLLDEPTEHL 502
|
170 180
....*....|....*....|....*..
gi 6323278 575 DTVNVAWLVNYLN--TCGITSITISHD 599
Cdd:TIGR02868 503 DAETADELLEDLLaaLSGRTVVLITHH 529
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
451-611 |
3.34e-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: 73.01 E-value: 3.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 451 LRLKRARRYGICGPNGCGKSTLMRAIA------NGQV--DGFPTQE----ECRTV--YVEHDI--------------DGT 502
Cdd:cd03245 25 LTIRAGEKVAIIGRVGSGKSTLLKLLAglykptSGSVllDGTDIRQldpaDLRRNigYVPQDVtlfygtlrdnitlgAPL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 503 HSDTSVLDFVFESGVgTKEAIKDKLiefGFtDEMIAMPISALSGGWKMKLALARAVLRNADILLLDEPTNHLDTVNVAWL 582
Cdd:cd03245 105 ADDERILRAAELAGV-TDFVNKHPN---GL-DLQIGERGRGLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERL 179
|
170 180 190
....*....|....*....|....*....|.
gi 6323278 583 VNYLN--TCGITSITISHDSVFLDNVCEYII 611
Cdd:cd03245 180 KERLRqlLGDKTLIIITHRPSLLDLVDRIIV 210
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
437-599 |
3.41e-14 |
|
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: 76.72 E-value: 3.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 437 SLAY-GAKILLNKTQLRLKRARRYGICGPNGCGKSTLMRAIA------NGQ--VDGFPTQEECRT------VYVEHD--- 498
Cdd:COG4988 343 SFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLgflppySGSilINGVDLSDLDPAswrrqiAWVPQNpyl 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 499 IDGThsdtsVLDFV-FESGVGTKEAIKDKLIEFGFTDEMIAMP------I----SALSGGWKMKLALARAVLRNADILLL 567
Cdd:COG4988 423 FAGT-----IRENLrLGRPDASDEELEAALEAAGLDEFVAALPdgldtpLgeggRGLSGGQAQRLALARALLRDAPLLLL 497
|
170 180 190
....*....|....*....|....*....|....
gi 6323278 568 DEPTNHLDTVNVAWLVNYLNTC--GITSITISHD 599
Cdd:COG4988 498 DEPTAHLDAETEAEILQALRRLakGRTVILITHR 531
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
440-598 |
3.80e-14 |
|
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: 71.31 E-value: 3.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 440 YGAKILLNKTQLRLKRARRYGICGPNGCGKSTLMRAIANGQVdgfPTQEECRtvyvehdIDGThsdtsvlDFVFESgvgT 519
Cdd:cd03216 10 FGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYK---PDSGEIL-------VDGK-------EVSFAS---P 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 520 KEAIKDKliefgftdemIAMpISALSGGWKMKLALARAVLRNADILLLDEPTNHLDTVNVAWLVNYLNTC---GITSITI 596
Cdd:cd03216 70 RDARRAG----------IAM-VYQLSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIRRLraqGVAVIFI 138
|
..
gi 6323278 597 SH 598
Cdd:cd03216 139 SH 140
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
463-599 |
4.93e-14 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 74.80 E-value: 4.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 463 GPNGCGKSTLMRAIAngqvdGFPTQEECRTVYVEHDIDgthSDTSVLD----FVF-------------------ESGVGT 519
Cdd:COG1118 35 GPSGSGKTTLLRIIA-----GLETPDSGRIVLNGRDLF---TNLPPRErrvgFVFqhyalfphmtvaeniafglRVRPPS 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 520 KEAIKDKliefgfTDEMIAM----------PiSALSGGWKMKLALARAVLRNADILLLDEPTNHLDTvNVA-----WLVN 584
Cdd:COG1118 107 KAEIRAR------VEELLELvqlegladryP-SQLSGGQRQRVALARALAVEPEVLLLDEPFGALDA-KVRkelrrWLRR 178
|
170
....*....|....*
gi 6323278 585 YLNTCGITSITISHD 599
Cdd:COG1118 179 LHDELGGTTVFVTHD 193
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
676-995 |
5.07e-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: 76.13 E-value: 5.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 676 YPGTsKPQITDINFQCSLSSRIAVIGPNGAGKSTLINVLTGELLPTSGEVYTHENCRIAYIKQhafahiESHLD--KTPS 753
Cdd:TIGR03719 14 VPPK-KEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQPGIKVGYLPQ------EPQLDptKTVR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 754 EYIQwrFQTGEDRETMDRANR---QINENDAEaMNKIFKIEGTprriagihsrrkfkntyeyecsflLGENIGMKserwv 830
Cdd:TIGR03719 87 ENVE--EGVAEIKDALDRFNEisaKYAEPDAD-FDKLAAEQAE------------------------LQEIIDAA----- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 831 pmmsvdNAWiprgelvESHSKMvaEVDMkEALasgqfrpltrkeieeHCsmlgldPE---IVSHsrirgLSGGQKVKLVL 907
Cdd:TIGR03719 135 ------DAW-------DLDSQL--EIAM-DAL---------------RC------PPwdaDVTK-----LSGGERRRVAL 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 908 AAGTWQRPHLIVLDEPTNYLDRDSLGALSKALKEFEGGVIIITHSAEFTKNLTEEVWAVKDGRMTPSGHN---WVSGQGA 984
Cdd:TIGR03719 173 CRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPWEGNyssWLEQKQK 252
|
330
....*....|.
gi 6323278 985 GPRIEKKEDEE 995
Cdd:TIGR03719 253 RLEQEEKEESA 263
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
406-628 |
6.26e-14 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 75.93 E-value: 6.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 406 EFRKRAVDN---IPVGPNFDDEEDEGEDLcncefSLAYGAKILLNKTQLRLKRARRYGICGPNGCGKSTLMRAIAnGQVD 482
Cdd:PRK11819 302 EYQKRNETNeifIPPGPRLGDKVIEAENL-----SKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMIT-GQEQ 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 483 gfPTQEECR---TV---YVEH---DIDGTHSdtsvldfVFE--SG------VGTKEaIKDK--LIEFGF--TDEmiAMPI 541
Cdd:PRK11819 376 --PDSGTIKigeTVklaYVDQsrdALDPNKT-------VWEeiSGgldiikVGNRE-IPSRayVGRFNFkgGDQ--QKKV 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 542 SALSGGWKMKLALARAVLRNADILLLDEPTNHLDTVNVAWLVNYLNTCGITSITISHDSVFLDNVCEYIINYEG-LKLRK 620
Cdd:PRK11819 444 GVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVETLRALEEALLEFPGCAVVISHDRWFLDRIATHILAFEGdSQVEW 523
|
....*...
gi 6323278 621 YKGNFTEF 628
Cdd:PRK11819 524 FEGNFQEY 531
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
671-971 |
7.27e-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: 71.85 E-value: 7.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 671 NMEFQYPGTSKPQITDINFQCSLSSRIAVIGPNGAGKSTLINVLTGELLPTSGEVYthencriayikqhafahieshLDK 750
Cdd:cd03245 7 NVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVL---------------------LDG 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 751 TPSeyiqwrfqtgedretmdranRQINENDaeamnkifkiegtprriagihsrrkfkntyeyecsflLGENIGmkserWV 830
Cdd:cd03245 66 TDI--------------------RQLDPAD-------------------------------------LRRNIG-----YV 83
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 831 PmmsvDNAWIPRGELveshskmvaevdmKEALASGqfRPL-TRKEIEEHCSMLGLDPEIVSH---------SRIRGLSGG 900
Cdd:cd03245 84 P----QDVTLFYGTL-------------RDNITLG--APLaDDERILRAAELAGVTDFVNKHpngldlqigERGRGLSGG 144
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6323278 901 QKVKLVLAAGTWQRPHLIVLDEPTNYLDRDSLGALSKALKEFEGG--VIIITHSAEFTkNLTEEVWAVKDGRM 971
Cdd:cd03245 145 QRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGDktLIIITHRPSLL-DLVDRIIVMDSGRI 216
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
436-603 |
9.32e-14 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 72.43 E-value: 9.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 436 FSLAYGAKILLNKTQLRLKRARRYGICGPNGCGKSTLMRAIAngqvdGF--PTQEEcrtVYVE-HDIDGTHSDT------ 506
Cdd:COG1116 17 FPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIA-----GLekPTSGE---VLVDgKPVTGPGPDRgvvfqe 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 507 -------SVLD---FVFE-SGVGTKEAIK--DKLIE-FGFTDEMIAMPiSALSGGWKMKLALARAVLRNADILLLDEPTN 572
Cdd:COG1116 89 pallpwlTVLDnvaLGLElRGVPKAERREraRELLElVGLAGFEDAYP-HQLSGGMRQRVAIARALANDPEVLLMDEPFG 167
|
170 180 190
....*....|....*....|....*....|....*...
gi 6323278 573 HLD--TVNV--AWLVNYLNTCGITSITISHD---SVFL 603
Cdd:COG1116 168 ALDalTRERlqDELLRLWQETGKTVLFVTHDvdeAVFL 205
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
669-726 |
9.63e-14 |
|
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: 70.32 E-value: 9.63e-14
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 6323278 669 VTNMEFQYPGTSKPQITDINFQCSLSSRIAVIGPNGAGKSTLINVLTGELLPTSGEVY 726
Cdd:cd03246 3 VENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVR 60
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
437-611 |
1.28e-13 |
|
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: 71.55 E-value: 1.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 437 SLAYGAKILLNKTQLRLKRARRYGICGPNGCGKSTLMRAIAnGQV---DGfptqeecrTVYVE-HDIdgTHSDTSVLD-- 510
Cdd:COG1127 12 TKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLII-GLLrpdSG--------EILVDgQDI--TGLSEKELYel 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 511 -----FVFESG-------VG-------------TKEAIKD----KLIEFGFTDEMIAMPiSALSGGwkMK--LALARAVL 559
Cdd:COG1127 81 rrrigMLFQGGalfdsltVFenvafplrehtdlSEAEIRElvleKLELVGLPGAADKMP-SELSGG--MRkrVALARALA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 6323278 560 RNADILLLDEPTNHLDTVNVAWLVNYLNTC----GITSITISHD--SVFldNVCEYII 611
Cdd:COG1127 158 LDPEILLYDEPTAGLDPITSAVIDELIRELrdelGLTSVVVTHDldSAF--AIADRVA 213
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
460-615 |
1.73e-13 |
|
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: 74.44 E-value: 1.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 460 GICGPNGCGKSTLMRAIA------NGQVDG-----FPTQeecrtvYVEHDIDGTHSDtsVLDFVFESGVGTK----EAIK 524
Cdd:COG1245 370 GIVGPNGIGKTTFAKILAgvlkpdEGEVDEdlkisYKPQ------YISPDYDGTVEE--FLRSANTDDFGSSyyktEIIK 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 525 ----DKLIEfgftdemiaMPISALSGGWKMKLALARAVLRNADILLLDEPTNHLDT---VNVAWLV-NYLNTCGITSITI 596
Cdd:COG1245 442 plglEKLLD---------KNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVeqrLAVAKAIrRFAENRGKTAMVV 512
|
170
....*....|....*....
gi 6323278 597 SHDSVFLDNVCEYIINYEG 615
Cdd:COG1245 513 DHDIYLIDYISDRLMVFEG 531
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
697-950 |
2.22e-13 |
|
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: 70.20 E-value: 2.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 697 IAVIGPNGAGKSTLINVLTGELLPTSGEVYthencriayikqhafahieshldktpseyiqwrfqtgedretmdranrqi 776
Cdd:COG4133 31 LALTGPNGSGKTTLLRILAGLLPPSAGEVL-------------------------------------------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 777 nendaeamnkifkIEGTPRRIAGIHSRRKFkntyeyecsFLLGENIGMKSErwvpmMSVdnawiprGELVESHSKMvaev 856
Cdd:COG4133 61 -------------WNGEPIRDAREDYRRRL---------AYLGHADGLKPE-----LTV-------RENLRFWAAL---- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 857 dmkealaSGqfRPLTRKEIEEHCSMLGLDPeiVSHSRIRGLSGGQKVKLVLAAGTWQRPHLIVLDEPTNYLDRDSLGALS 936
Cdd:COG4133 103 -------YG--LRADREAIDEALEAVGLAG--LADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLA 171
|
250
....*....|....*.
gi 6323278 937 KALKEF--EGGVIIIT 950
Cdd:COG4133 172 ELIAAHlaRGGAVLLT 187
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
437-575 |
2.68e-13 |
|
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: 73.86 E-value: 2.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 437 SLAY-GAKILLNKTQLRLKRARRYGICGPNGCGKSTLMRAIAnGQVDgfPTQEECRTVyvehDIDGTHSDTSVLD----- 510
Cdd:TIGR02857 328 SVAYpGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLL-GFVD--PTEGSIAVN----GVPLADADADSWRdqiaw 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 511 -----FVFESGV----------GTKEAIKDKLIEFGFTD------EMIAMPI----SALSGGWKMKLALARAVLRNADIL 565
Cdd:TIGR02857 401 vpqhpFLFAGTIaenirlarpdASDAEIREALERAGLDEfvaalpQGLDTPIgeggAGLSGGQAQRLALARAFLRDAPLL 480
|
170
....*....|
gi 6323278 566 LLDEPTNHLD 575
Cdd:TIGR02857 481 LLDEPTAHLD 490
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
437-575 |
4.03e-13 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 73.67 E-value: 4.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 437 SLAYGAKILLNKTQLRLKRARRYGICGPNGCGKSTLMRAIANGQVdgfPTQEECRTV-------YVEHDIDGTHSDTSVL 509
Cdd:PRK10636 319 SAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELA---PVSGEIGLAkgiklgyFAQHQLEFLRADESPL 395
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6323278 510 DFVFE-SGVGTKEAIKDKLIEFGFTDEMIAMPISALSGGWKMKLALARAVLRNADILLLDEPTNHLD 575
Cdd:PRK10636 396 QHLARlAPQELEQKLRDYLGGFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLD 462
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
439-631 |
4.40e-13 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 73.00 E-value: 4.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 439 AYGAKILLNKTQLRLKRARRYGICGPNGCGKSTLMRAIAN------GQVD-------GFPTQEEcrtvyvEHDIDgthSD 505
Cdd:PRK15064 328 GFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGelepdsGTVKwsenaniGYYAQDH------AYDFE---ND 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 506 TSVLDFV--FESGVGTKEAIKDKLIEFGFTDEMIAMPISALSGGWKMKLALARAVLRNADILLLDEPTNHLD-----TVN 578
Cdd:PRK15064 399 LTLFDWMsqWRQEGDDEQAVRGTLGRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDmesieSLN 478
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 6323278 579 VAwLVNYLNTCgitsITISHDSVFLDNVCEYIINYEGLKLRKYKGNFTEFVKK 631
Cdd:PRK15064 479 MA-LEKYEGTL----IFVSHDREFVSSLATRIIEITPDGVVDFSGTYEEYLRS 526
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
666-971 |
5.53e-13 |
|
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: 70.07 E-value: 5.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 666 IVKVTNMEFQYPGtsKPQITDINFQCSLSSRIAVIGPNGAGKSTLINVLTGELLPTSGEVYthencriayikqhafahie 745
Cdd:COG1120 1 MLEAENLSVGYGG--RPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVL------------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 746 shLDktpseyiqwrfqtGEDRETMDRANRqinendAeamnkifkiegtpRRIAgihsrrkfkntyeyecsfllgenigmk 825
Cdd:COG1120 60 --LD-------------GRDLASLSRREL------A-------------RRIA--------------------------- 78
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 826 serWVPMMSVDNAWIPRGELVE----SHSKMvaevdmkealasgqFRPLTRKEIE------EHCSMLGLdpeivSHSRIR 895
Cdd:COG1120 79 ---YVPQEPPAPFGLTVRELVAlgryPHLGL--------------FGRPSAEDREaveealERTGLEHL-----ADRPVD 136
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 896 GLSGG--QKVKL--VLAagtwQRPHLIVLDEPTNYLD---RDSLGALSKALKEFEG-GVIIITH----SAEFtknlTEEV 963
Cdd:COG1120 137 ELSGGerQRVLIarALA----QEPPLLLLDEPTSHLDlahQLEVLELLRRLARERGrTVVMVLHdlnlAARY----ADRL 208
|
....*...
gi 6323278 964 WAVKDGRM 971
Cdd:COG1120 209 VLLKDGRI 216
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
437-630 |
6.36e-13 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 72.97 E-value: 6.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 437 SLAY-GAKILLNKTQLRLKRARRYGICGPNGCGKSTLMRAIA------NGQVdgFPTQEECRTVYVEHDIDGTHSDTSVL 509
Cdd:PLN03073 515 SFGYpGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISgelqpsSGTV--FRSAKVRMAVFSQHHVDGLDLSSNPL 592
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 510 DFVFESGVGTKEA-IKDKLIEFGFTDEMIAMPISALSGGWKMKLALARAVLRNADILLLDEPTNHLDTVNVAWLVNYLNT 588
Cdd:PLN03073 593 LYMMRCFPGVPEQkLRAHLGSFGVTGNLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGLVL 672
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 6323278 589 CGITSITISHDSVFLD-NVCEYIINYEGlKLRKYKGNFTEFVK 630
Cdd:PLN03073 673 FQGGVLMVSHDEHLISgSVDELWVVSEG-KVTPFHGTFHDYKK 714
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
440-575 |
6.54e-13 |
|
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: 68.76 E-value: 6.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 440 YGAKILLNKTQLRLKRARrYGICGPNGCGKSTLMRAIA------NGQV--DGFPTQEECRTV-----YVEHDIdGTHSDT 506
Cdd:cd03264 10 YGKKRALDGVSLTLGPGM-YGLLGPNGAGKTTLMRILAtltppsSGTIriDGQDVLKQPQKLrrrigYLPQEF-GVYPNF 87
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6323278 507 SVLDFV----FESGVGTKEAIK--DKLIE----FGFTDEmiamPISALSGGWKMKLALARAVLRNADILLLDEPTNHLD 575
Cdd:cd03264 88 TVREFLdyiaWLKGIPSKEVKArvDEVLElvnlGDRAKK----KIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLD 162
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
695-951 |
7.48e-13 |
|
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: 69.68 E-value: 7.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 695 SRIAVIGPNGAGKSTLINVLTGELLPTSGEVythencriayikqhafahieshldktpseyiqwRFQtGEDretmdranr 774
Cdd:COG0411 31 EIVGLIGPNGAGKTTLFNLITGFYRPTSGRI---------------------------------LFD-GRD--------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 775 qinendaeamnkifkIEG-TPRRIA--GIhsRRKFKNTyeyecsfllgenigmkseRWVPMMSV-DNAWIPRgelvesHS 850
Cdd:COG0411 68 ---------------ITGlPPHRIArlGI--ARTFQNP------------------RLFPELTVlENVLVAA------HA 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 851 KmvaevdMKEALASGQFRPL--------TRKEIEEHCSMLGLDPeiVSHSRIRGLSGGQKvKLV-----LAAgtwqRPHL 917
Cdd:COG0411 107 R------LGRGLLAALLRLPrarreereARERAEELLERVGLAD--RADEPAGNLSYGQQ-RRLeiaraLAT----EPKL 173
|
250 260 270
....*....|....*....|....*....|....*...
gi 6323278 918 IVLDEPT---NYLDRDSLGALSKALKEFEG-GVIIITH 951
Cdd:COG0411 174 LLLDEPAaglNPEETEELAELIRRLRDERGiTILLIEH 211
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
668-951 |
9.22e-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: 68.33 E-value: 9.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 668 KVTNMEFQYPGtsKPQITDINFQCSLSSRIAVIGPNGAGKSTLINVLTGELLPTSGEV------YTHENCRIAYIKQHaf 741
Cdd:cd03235 1 EVEDLTVSYGG--HPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIrvfgkpLEKERKRIGYVPQR-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 742 ahieshldktpsEYIQWRFQ-TGEDRETMDRANRqinendaeamnkifkiegtpRRIAGIHSRRKFKntyeyecsfllge 820
Cdd:cd03235 77 ------------RSIDRDFPiSVRDVVLMGLYGH--------------------KGLFRRLSKADKA------------- 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 821 nigmkserwvpmmSVDNAwiprgelveshskmVAEVDMKEalasgqfrpltrkeieehcsmlgldpeiVSHSRIRGLSGG 900
Cdd:cd03235 112 -------------KVDEA--------------LERVGLSE----------------------------LADRQIGELSGG 136
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 6323278 901 QKVKLVLAAGTWQRPHLIVLDEPTNYLDRDSLGALSKALKEF--EG-GVIIITH 951
Cdd:cd03235 137 QQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELrrEGmTILVVTH 190
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
440-575 |
1.81e-12 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 69.45 E-value: 1.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 440 YGAKILLNKTQLRLKRARRYGICGPNGCGKSTLMRAI------ANGQVD--GFPTQEECR----TVYVEHDIDGTHSDTS 507
Cdd:PRK13537 17 YGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLlglthpDAGSISlcGEPVPSRARharqRVGVVPQFDNLDPDFT 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6323278 508 VLD--FVFESGVG----TKEAIKDKLIEFGFTDEMIAMPISALSGGWKMKLALARAVLRNADILLLDEPTNHLD 575
Cdd:PRK13537 97 VREnlLVFGRYFGlsaaAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLD 170
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
441-598 |
1.84e-12 |
|
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: 67.19 E-value: 1.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 441 GAKILLNKTQLRLKRARRYGICGPNGCGKSTLMRAIAN--------GQV--DGFPTQEE---CRTVYVEHDiDGTHSDTS 507
Cdd:cd03213 20 SGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrrtglgvsGEVliNGRPLDKRsfrKIIGYVPQD-DILHPTLT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 508 VldfvfesgvgtKEAIkdkliefgftdeMIAMPISALSGGWKMKLALARAVLRNADILLLDEPTNHLDTVNVAWLVNYL- 586
Cdd:cd03213 99 V-----------RETL------------MFAAKLRGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLr 155
|
170
....*....|....*
gi 6323278 587 ---NTcGITSITISH 598
Cdd:cd03213 156 rlaDT-GRTIICSIH 169
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
667-970 |
2.07e-12 |
|
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: 68.63 E-value: 2.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 667 VKVTNMEFQY-PGTS--KPQITDINFQCSLSSRIAVIGPNGAGKSTLINVLTGELLPTSGEVYThencriayikqhafah 743
Cdd:TIGR04521 1 IKLKNVSYIYqPGTPfeKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTI---------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 744 ieshldktpseyiqwrfqtgedretmdrANRQINENDAEAMNKIfkiegtprriagihsRRK------------FKNTYE 811
Cdd:TIGR04521 65 ----------------------------DGRDITAKKKKKLKDL---------------RKKvglvfqfpehqlFEETVY 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 812 YECSFllG-ENIGMKSERwvpmmsvdnawiprgelveshskmvAEVDMKEALAsgqfrpltrkeieehcsMLGLDPEIVS 890
Cdd:TIGR04521 102 KDIAF--GpKNLGLSEEE-------------------------AEERVKEALE-----------------LVGLDEEYLE 137
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 891 HSRIRgLSGGQKVKL----VLAagtwQRPHLIVLDEPTNYLD---RDSLGALSKALKEFEG-GVIIITHSAEFTKNLTEE 962
Cdd:TIGR04521 138 RSPFE-LSGGQMRRVaiagVLA----MEPEVLILDEPTAGLDpkgRKEILDLFKRLHKEKGlTVILVTHSMEDVAEYADR 212
|
....*...
gi 6323278 963 VWAVKDGR 970
Cdd:TIGR04521 213 VIVMHKGK 220
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
439-575 |
2.09e-12 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 69.86 E-value: 2.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 439 AYGAKILLNKTQLRLKRARRYGICGPNGCGKSTLMRAI--------ANGQVDGFPTQEECRT----VYVEHDIDGTHSDT 506
Cdd:PRK13536 50 SYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMIlgmtspdaGKITVLGVPVPARARLararIGVVPQFDNLDLEF 129
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6323278 507 SVLD--FVFESGVGTK----EAIKDKLIEFGFTDEMIAMPISALSGGWKMKLALARAVLRNADILLLDEPTNHLD 575
Cdd:PRK13536 130 TVREnlLVFGRYFGMStreiEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLD 204
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
668-975 |
2.21e-12 |
|
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: 66.69 E-value: 2.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 668 KVTNMEFQYPGtsKPQITDINFQCSLSSRIAVIGPNGAGKSTLINVLTGELLPTSGEVYthencriayikqhafahiesh 747
Cdd:cd03214 1 EVENLSVGYGG--RTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEIL--------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 748 LDktpseyiqwrfqtGEDRETMDRANRqinendAeamnkifkiegtpRRIAgihsrrkfkntyeyecsfllgenigmkse 827
Cdd:cd03214 58 LD-------------GKDLASLSPKEL------A-------------RKIA----------------------------- 76
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 828 rWVPmmsvdnawiprgelveshsKMVAEVDMKEalasgqfrpLTRKEIEEhcsmlgldpeivshsrirgLSGGQKVKLVL 907
Cdd:cd03214 77 -YVP-------------------QALELLGLAH---------LADRPFNE-------------------LSGGERQRVLL 108
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6323278 908 AAGTWQRPHLIVLDEPTNYLD---RDSLGALSKALKEFEG-GVIIITHSAEFTKNLTEEVWAVKDGRMTPSG 975
Cdd:cd03214 109 ARALAQEPPILLLDEPTSHLDiahQIELLELLRRLARERGkTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
437-599 |
2.95e-12 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 69.87 E-value: 2.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 437 SLAYGAKILLNKTQLRLKRARRYGICGPNGCGKSTLMRAIaNG---------QVDGFPTqEECRTVYVEHDIDGTHSDTS 507
Cdd:PRK09536 10 SVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAI-NGtltptagtvLVAGDDV-EALSARAASRRVASVPQDTS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 508 V-LDF----VFESG-----------VGTKEAIKDKLIEFGFTDEMIAMPISALSGGWKMKLALARAVLRNADILLLDEPT 571
Cdd:PRK09536 88 LsFEFdvrqVVEMGrtphrsrfdtwTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPT 167
|
170 180 190
....*....|....*....|....*....|.
gi 6323278 572 NHLD---TVNVAWLVNYLNTCGITSITISHD 599
Cdd:PRK09536 168 ASLDinhQVRTLELVRRLVDDGKTAVAAIHD 198
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
437-606 |
4.17e-12 |
|
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: 70.18 E-value: 4.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 437 SLAY--GAKILLNKTQLRLKRARRYGICGPNGCGKSTL----MRAIA--NGQV--DGFPTQEecrtvYVEHDIdgtHSDT 506
Cdd:COG4987 340 SFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLlallLRFLDpqSGSItlGGVDLRD-----LDEDDL---RRRI 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 507 SVLD---FVFESGVG----------TKEAIKDKLIEFGFTDEMIAMPI----------SALSGGWKMKLALARAVLRNAD 563
Cdd:COG4987 412 AVVPqrpHLFDTTLRenlrlarpdaTDEELWAALERVGLGDWLAALPDgldtwlgeggRRLSGGERRRLALARALLRDAP 491
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 6323278 564 ILLLDEPTNHLDTVNVAWLVNYLNTC--GITSITISHDSVFLDNV 606
Cdd:COG4987 492 ILLLDEPTEGLDAATEQALLADLLEAlaGRTVLLITHRLAGLERM 536
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
437-629 |
4.51e-12 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 69.98 E-value: 4.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 437 SLAYGAKILLNKTQLRLKRARRYGICGPNGCGKSTLMRAIAnGQVdgfptQEECRTVYVehdidGTH------------- 503
Cdd:PRK11147 326 NYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLML-GQL-----QADSGRIHC-----GTKlevayfdqhrael 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 504 -SDTSVLDFVFEsgvGTKEAI---KDK-----LIEFGFTdEMIAM-PISALSGGWKMKLALARAVLRNADILLLDEPTNH 573
Cdd:PRK11147 395 dPEKTVMDNLAE---GKQEVMvngRPRhvlgyLQDFLFH-PKRAMtPVKALSGGERNRLLLARLFLKPSNLLILDEPTND 470
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 6323278 574 LDTVNVAWLVNYLNTCGITSITISHDSVFLDN-VCEYIInYEGlklrkyKGNFTEFV 629
Cdd:PRK11147 471 LDVETLELLEELLDSYQGTVLLVSHDRQFVDNtVTECWI-FEG------NGKIGRYV 520
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
460-622 |
5.03e-12 |
|
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: 66.55 E-value: 5.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 460 GICGPNGCGKSTLMRAIA------NGQ--VDGFPTQEECRTVyvehdidgthsDTSVLD----FVFES------------ 515
Cdd:cd03297 27 GIFGASGAGKSTLLRCIAglekpdGGTivLNGTVLFDSRKKI-----------NLPPQQrkigLVFQQyalfphlnvren 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 516 ---GVGTKEAIKDKLiefgFTDEMIAM---------PISALSGGWKMKLALARAVLRNADILLLDEPTNHLDTVNVAWLV 583
Cdd:cd03297 96 lafGLKRKRNREDRI----SVDELLDLlgldhllnrYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 6323278 584 NYLNTC----GITSITISHDSVFLDNVCEYIINYEGLKLRKYK 622
Cdd:cd03297 172 PELKQIkknlNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
443-598 |
6.70e-12 |
|
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: 64.87 E-value: 6.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 443 KILLNKTQLRLKRARRYGICGPNGCGKSTLMRAIA------NGQVdGFPTQEEC----RTVYVehdidgthsdtsvldfv 512
Cdd:cd03223 14 RVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAglwpwgSGRI-GMPEGEDLlflpQRPYL----------------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 513 fesGVGT-KEAIkdkliefgftdemiAMPIS-ALSGGWKMKLALARAVLRNADILLLDEPTNHLDTVNVAWLVNYLNTCG 590
Cdd:cd03223 76 ---PLGTlREQL--------------IYPWDdVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKELG 138
|
....*...
gi 6323278 591 ITSITISH 598
Cdd:cd03223 139 ITVISVGH 146
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
436-586 |
8.54e-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: 65.85 E-value: 8.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 436 FSLAYGAKILLNKTQLRLKRARRYGICGPNGCGKSTLMRAIA--------NGQVDGFPT----QEECRTVYVEHDIDGTH 503
Cdd:cd03266 11 FRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAgllepdagFATVDGFDVvkepAEARRRLGFVSDSTGLY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 504 SDTSVLDFV--FESGVGTK----EAIKDKLIEFGFTDEMIAMPISALSGGWKMKLALARAVLRNADILLLDEPTNHLDTV 577
Cdd:cd03266 91 DRLTARENLeyFAGLYGLKgdelTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVM 170
|
....*....
gi 6323278 578 NVAWLVNYL 586
Cdd:cd03266 171 ATRALREFI 179
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
676-961 |
9.13e-12 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 68.99 E-value: 9.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 676 YPGTsKPQITDInfqcSLS----SRIAVIGPNGAGKSTLINVLTGELLPTSGEVYTHENCRIAYIKQhafahiESHLD-- 749
Cdd:PRK11819 16 VPPK-KQILKDI----SLSffpgAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPAPGIKVGYLPQ------EPQLDpe 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 750 KTPSEYIQWRFqtGEDRETMDRANrQINENDAEamnkifkiegtprriagihsrrkfkntyeyecsfllgenigmkserw 829
Cdd:PRK11819 85 KTVRENVEEGV--AEVKAALDRFN-EIYAAYAE----------------------------------------------- 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 830 vPMMSVDnawiprgELVESHSKMVAEVDMKEA--LASgqfrpltrkEIEEHCSMLGLDP--EIVSHsrirgLSGGQK--- 902
Cdd:PRK11819 115 -PDADFD-------ALAAEQGELQEIIDAADAwdLDS---------QLEIAMDALRCPPwdAKVTK-----LSGGERrrv 172
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6323278 903 --VKLVLaagtwQRPHLIVLDEPTNYLDRDSLGALSKALKEFEGGVIIITHSAEFTKNLTE 961
Cdd:PRK11819 173 alCRLLL-----EKPDMLLLDEPTNHLDAESVAWLEQFLHDYPGTVVAVTHDRYFLDNVAG 228
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
460-610 |
9.68e-12 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 66.24 E-value: 9.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 460 GICGPNGCGKSTLMRAIAN------GQVDGFPTQEECRTVY------------VEHDIDGTHSDTSVlDFVFESGVGTKE 521
Cdd:cd03236 30 GLVGPNGIGKSTALKILAGklkpnlGKFDDPPDWDEILDEFrgselqnyftklLEGDVKVIVKPQYV-DLIPKAVKGKVG 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 522 AIKDKLIEFGFTDEMIAM---------PISALSGGWKMKLALARAVLRNADILLLDEPTNHLDT---VNVAWLVNYLNTC 589
Cdd:cd03236 109 ELLKKKDERGKLDELVDQlelrhvldrNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIkqrLNAARLIRELAED 188
|
170 180
....*....|....*....|.
gi 6323278 590 GITSITISHDSVFLDNVCEYI 610
Cdd:cd03236 189 DNYVLVVEHDLAVLDYLSDYI 209
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
440-605 |
1.31e-11 |
|
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: 65.12 E-value: 1.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 440 YGAKIL-LNKTQLRLKRARRYGICGPNGCGKSTLMRAIA------NGQ--VDGFPTQE--ECRTVYVEHDIDGTHSDTSV 508
Cdd:cd03292 10 YPNGTAaLDGINISISAGEFVFLVGPSGAGKSTLLKLIYkeelptSGTirVNGQDVSDlrGRAIPYLRRKIGVVFQDFRL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 509 LDF--VFE--------SGVGTKEA---IKDKLIEFGFTDEMIAMPiSALSGGWKMKLALARAVLRNADILLLDEPTNHLD 575
Cdd:cd03292 90 LPDrnVYEnvafalevTGVPPREIrkrVPAALELVGLSHKHRALP-AELSGGEQQRVAIARAIVNSPTILIADEPTGNLD 168
|
170 180 190
....*....|....*....|....*....|...
gi 6323278 576 TVN---VAWLVNYLNTCGITSITISHDSVFLDN 605
Cdd:cd03292 169 PDTtweIMNLLKKINKAGTTVVVATHAKELVDT 201
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
680-726 |
1.43e-11 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 65.91 E-value: 1.43e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 6323278 680 SKPQITDINFQCSLSSRIAVIGPNGAGKSTLINVLTGELLPTSGEVY 726
Cdd:COG4559 13 GRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVR 59
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
644-975 |
1.46e-11 |
|
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: 65.43 E-value: 1.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 644 TDLEFKFPEPGYLEGVKTKQKAIVKvtnMEFQypgtSKPQITDINFQCSLSSRIAVIGPNGAGKSTLINVLTGELLPTSG 723
Cdd:cd03267 4 SNLSKSYRVYSKEPGLIGSLKSLFK---RKYR----EVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 724 EVythencRIAyikqhafahieshldktpsEYIQWRfqtgedretmdranrqinendaeamnkifkiegtpRRIAgiHSR 803
Cdd:cd03267 77 EV------RVA-------------------GLVPWK-----------------------------------RRKK--FLR 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 804 RkfkntyeyeCSFLLGEnigmKSERWvpmmsvdnaW-IPrgeLVESHSKMVAEVDMKEALAsgqfrpltRKEIEEHCSML 882
Cdd:cd03267 95 R---------IGVVFGQ----KTQLW---------WdLP---VIDSFYLLAAIYDLPPARF--------KKRLDELSELL 141
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 883 GLDPEIvsHSRIRGLSGGQKVKLVLAAGTWQRPHLIVLDEPTNYLDRDSLGALSKALKEF----EGGVIIITHSAEFTKN 958
Cdd:cd03267 142 DLEELL--DTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYnrerGTTVLLTSHYMKDIEA 219
|
330
....*....|....*..
gi 6323278 959 LTEEVWAVKDGRMTPSG 975
Cdd:cd03267 220 LARRVLVIDKGRLLYDG 236
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
435-611 |
1.53e-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: 64.99 E-value: 1.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 435 EFSLAYGAKILLNKTQLRLKRARRYGICGPNGCGKSTLMRAIAN------G--QVDGFPTQEECRTV--YVEHDiDGTHS 504
Cdd:cd03269 5 NVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGiilpdsGevLFDGKPLDIAARNRigYLPEE-RGLYP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 505 DTSVLD----FVFESGVGTKEAIK--DKLIE-FGFTDEMiAMPISALSGGWKMKLALARAVLRNADILLLDEPTNHLDTV 577
Cdd:cd03269 84 KMKVIDqlvyLAQLKGLKKEEARRriDEWLErLELSEYA-NKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPV 162
|
170 180 190
....*....|....*....|....*....|....*..
gi 6323278 578 NVAWL---VNYLNTCGITSITISHDSVFLDNVCEYII 611
Cdd:cd03269 163 NVELLkdvIRELARAGKTVILSTHQMELVEELCDRVL 199
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
671-951 |
1.59e-11 |
|
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: 68.35 E-value: 1.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 671 NMEFQYPGTSKPQITDINFQCSLSSRIAVIGPNGAGKSTLINVLTGELLPTSGEVY--THEncriayIKQHAFAHIESHL 748
Cdd:TIGR03375 468 NVSFAYPGQETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLldGVD------IRQIDPADLRRNI 541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 749 DKTPSEyiQWRFQtGEDRETMDRANRQINenDAEAMNKIfkiegtprRIAGIHsrrkfkntyeyecsfllgenigmkser 828
Cdd:TIGR03375 542 GYVPQD--PRLFY-GTLRDNIALGAPYAD--DEEILRAA--------ELAGVT--------------------------- 581
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 829 wvpmmsvdnawiprgELVESHSKmvaevdmkealasgqfrpltrkeieehcsmlGLDPEIvsHSRIRGLSGGQKVKLVLA 908
Cdd:TIGR03375 582 ---------------EFVRRHPD-------------------------------GLDMQI--GERGRSLSGGQRQAVALA 613
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 6323278 909 AGTWQRPHLIVLDEPTNYLDRDSLGALSKALKEFEGG--VIIITH 951
Cdd:TIGR03375 614 RALLRDPPILLLDEPTSAMDNRSEERFKDRLKRWLAGktLVLVTH 658
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
460-615 |
2.54e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 67.53 E-value: 2.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 460 GICGPNGCGKSTLMRAIA------NGQVDGFPT-----QeecrtvYVEHDIDGThsdtsVLDFVfesgvgtkEAIKDKL- 527
Cdd:PRK13409 369 GIVGPNGIGKTTFAKLLAgvlkpdEGEVDPELKisykpQ------YIKPDYDGT-----VEDLL--------RSITDDLg 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 528 -------IEFGFT-DEMIAMPISALSGGWKMKLALARAVLRNADILLLDEPTNHLDT---VNVAWLV-NYLNTCGITSIT 595
Cdd:PRK13409 430 ssyykseIIKPLQlERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVeqrLAVAKAIrRIAEEREATALV 509
|
170 180
....*....|....*....|
gi 6323278 596 ISHDSVFLDNVCEYIINYEG 615
Cdd:PRK13409 510 VDHDIYMIDYISDRLMVFEG 529
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
666-971 |
2.62e-11 |
|
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: 64.45 E-value: 2.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 666 IVKVTNMEFQYPGTSKPQ--ITDINFQCSLSSRIAVIGPNGAGKSTLINVLTGELLPTSGEVYTHencriayikqhafah 743
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVkaLDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFD--------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 744 ieshldktpseyiqwrfqtGEDRETMDRanrqinendaeamnKIFKIEGtpRRIAGIhsrrkFKNtyeyecsfllgenig 823
Cdd:cd03257 66 -------------------GKDLLKLSR--------------RLRKIRR--KEIQMV-----FQD--------------- 90
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 824 mkserwvPMMSVDnawiPR-------GELVESHSKMVAEVDMKEALAsgqfrpltrkEIEEHcsmLGLDPEiVSHSRIRG 896
Cdd:cd03257 91 -------PMSSLN----PRmtigeqiAEPLRIHGKLSKKEARKEAVL----------LLLVG---VGLPEE-VLNRYPHE 145
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 897 LSGGQKVKLVLAAGTWQRPHLIVLDEPTNYLDRDS----LGALSKALKEFEGGVIIITHSAEFTKNLTEEVwAV-KDGRM 971
Cdd:cd03257 146 LSGGQRQRVAIARALALNPKLLIADEPTSALDVSVqaqiLDLLKKLQEELGLTLLFITHDLGVVAKIADRV-AVmYAGKI 224
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
460-615 |
3.22e-11 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 64.74 E-value: 3.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 460 GICGPNGCGKSTLMRAIANG-QVDGFPTQEECRTV-----YVEHDIDGThsdtsVLDFVFE--SGVGTKEAIKDKLIEFG 531
Cdd:cd03237 29 GILGPNGIGKTTFIKMLAGVlKPDEGDIEIELDTVsykpqYIKADYEGT-----VRDLLSSitKDFYTHPYFKTEIAKPL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 532 FTDEMIAMPISALSGGWKMKLALARAVLRNADILLLDEPTNHLDT---VNVAWLVN-YLNTCGITSITISHDSVFLDNVC 607
Cdd:cd03237 104 QIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVeqrLMASKVIRrFAENNEKTAFVVEHDIIMIDYLA 183
|
....*...
gi 6323278 608 EYIINYEG 615
Cdd:cd03237 184 DRLIVFEG 191
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
897-970 |
3.42e-11 |
|
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: 62.65 E-value: 3.42e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6323278 897 LSGGQKVKLVLAAGTWQRPHLIVLDEPTNYLDRDSLGALSKALKEF-EGG--VIIITHSAEFTKNLTEEVWAVKDGR 970
Cdd:cd00267 81 LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLRELaEEGrtVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
664-975 |
3.68e-11 |
|
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: 66.85 E-value: 3.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 664 KAIVKVTNMEFQYPGTSKPQITDINFQCSLSSRIAVIGPNGAGKSTLINVLTGeLLPTSGEVythencriayikqhafah 743
Cdd:COG1123 2 TPLLEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMG-LLPHGGRI------------------ 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 744 ieshldktpseyiqwrfqTGEdretmdranrqinendaeamnkiFKIEGTPRRIAGIHsrrkfkntyeyecsfLLGENIG 823
Cdd:COG1123 63 ------------------SGE-----------------------VLLDGRDLLELSEA---------------LRGRRIG 86
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 824 MKSERwvPMMSVDNAWIprgelveshskmvaEVDMKEAL-ASGQFRPLTRKEIEEHCSMLGLdpEIVSHSRIRGLSGGQK 902
Cdd:COG1123 87 MVFQD--PMTQLNPVTV--------------GDQIAEALeNLGLSRAEARARVLELLEAVGL--ERRLDRYPHQLSGGQR 148
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6323278 903 VKLVLAAGTWQRPHLIVLDEPTNYLD----RDSLGALSKALKEFEGGVIIITHSAEFTKNLTEEVWAVKDGRMTPSG 975
Cdd:COG1123 149 QRVAIAMALALDPDLLIADEPTTALDvttqAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDG 225
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
667-954 |
3.93e-11 |
|
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: 64.06 E-value: 3.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 667 VKVTNMEFQYPGTSKPQITDINF-----QCslssrIAVIGPNGAGKSTLINVLTGELLPTSGEVYTHENcriaYIKQHAf 741
Cdd:cd03263 1 LQIRNLTKTYKKGTKPAVDDLSLnvykgEI-----FGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGY----SIRTDR- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 742 AHIESHLDKTPSEYIQWRFQTGedRETMdranrqinendaeamnKIF-KIEGTPRRIAgihsrrkfkntyeyecsfllge 820
Cdd:cd03263 71 KAARQSLGYCPQFDALFDELTV--REHL----------------RFYaRLKGLPKSEI---------------------- 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 821 nigmkserwvpmmsvdnawiprgelveshskmvaevdmkealasgqfrpltRKEIEEHCSMLGLDPeiVSHSRIRGLSGG 900
Cdd:cd03263 111 ---------------------------------------------------KEEVELLLRVLGLTD--KANKRARTLSGG 137
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 6323278 901 QKVKLVLAAGTWQRPHLIVLDEPTNYLD---RDSLGALSKALKEfEGGVIIITHSAE 954
Cdd:cd03263 138 MKRKLSLAIALIGGPSVLLLDEPTSGLDpasRRAIWDLILEVRK-GRSIILTTHSMD 193
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
439-599 |
4.46e-11 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 63.02 E-value: 4.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 439 AYGAKILLNKTQLRLKRARRYGICGPNGCGKSTLMRAIA------NGQVDGFPTqeeCRTVYVEHDIDGthSDT---SVL 509
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAgvlrptSGTVRRAGG---ARVAYVPQRSEV--PDSlplTVR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 510 DFVfesGVGT--------------KEAIKDKLIEFGFTDeMIAMPISALSGGWKMKLALARAVLRNADILLLDEPTNHLD 575
Cdd:NF040873 76 DLV---AMGRwarrglwrrltrddRAAVDDALERVGLAD-LAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLD 151
|
170 180
....*....|....*....|....*..
gi 6323278 576 T---VNVAWLVNYLNTCGITSITISHD 599
Cdd:NF040873 152 AesrERIIALLAEEHARGATVVVVTHD 178
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
668-970 |
4.90e-11 |
|
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: 64.13 E-value: 4.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 668 KVTNMEFQYPGtSKPQITDINFQCSLSSRIAVIGPNGAGKSTLINVLTGELLPTSGEVYthencriayikqhafahiesh 747
Cdd:cd03256 2 EVENLSKTYPN-GKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVL--------------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 748 ldktpseyiqwrfqtgedretmdranrqinendaeamnkifkIEGTPRRIAGIHSRRKFKntyeyecsfllgENIGM--K 825
Cdd:cd03256 60 ------------------------------------------IDGTDINKLKGKALRQLR------------RQIGMifQ 85
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 826 SERWVPMMSV-DNAWIPRgelVESHSkmvaevdmkeaLASGQFRPLTRKEIEEHCSML---GLDPeiVSHSRIRGLSGGQ 901
Cdd:cd03256 86 QFNLIERLSVlENVLSGR---LGRRS-----------TWRSLFGLFPKEEKQRALAALervGLLD--KAYQRADQLSGGQ 149
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6323278 902 KVKLVLAAGTWQRPHLIVLDEPTNYLD----RDSLGALSKALKEFEGGVIIITHSAEFTKNLTEEVWAVKDGR 970
Cdd:cd03256 150 QQRVAIARALMQQPKLILADEPVASLDpassRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGR 222
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
686-734 |
5.11e-11 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 63.95 E-value: 5.11e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 6323278 686 DINFQCSLSSRIAVIGPNGAGKSTLINVLTGELLPTSGEVYTheNCRIA 734
Cdd:COG1134 44 DVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEV--NGRVS 90
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
667-726 |
6.31e-11 |
|
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: 62.03 E-value: 6.31e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 667 VKVTNMEFQYPgtSKPQITDINFQCSLSSRIAVIGPNGAGKSTLINVLTGELLPTSGEVY 726
Cdd:cd03230 1 IEVRNLSKRYG--KKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIK 58
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
461-584 |
6.34e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 62.97 E-value: 6.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 461 ICGPNGCGKSTLMRAIAngqvdGFPTQEECRTVYVEHDIDGTHsdtsvldfVFESG--VGTKEAIKDKL-----IEF--- 530
Cdd:PRK13539 33 LTGPNGSGKTTLLRLIA-----GLLPPAAGTIKLDGGDIDDPD--------VAEAChyLGHRNAMKPALtvaenLEFwaa 99
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6323278 531 --GFTDEMIAMPISA-------------LSGGWKMKLALARAVLRNADILLLDEPTNHLDTVNVAWLVN 584
Cdd:PRK13539 100 flGGEELDIAAALEAvglaplahlpfgyLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFAE 168
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
872-975 |
6.81e-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: 63.08 E-value: 6.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 872 RKEIEEHCSMLGLDPeiVSHSRIRGLSGGQKVKLVLAAGTWQRPHLIVLDEPTNYLDRDS----LGALSKALKEFEGGVI 947
Cdd:cd03297 109 RISVDELLDLLGLDH--LLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALrlqlLPELKQIKKNLNIPVI 186
|
90 100
....*....|....*....|....*...
gi 6323278 948 IITHSAEFTKNLTEEVWAVKDGRMTPSG 975
Cdd:cd03297 187 FVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
451-599 |
6.88e-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: 63.28 E-value: 6.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 451 LRLKRARRYGICGPNGCGKSTLMRAIanGQVDgFPTQEECRtvyvehdIDGThsDTSVLD-------------FVFES-- 515
Cdd:cd03255 25 LSIEKGEFVAIVGPSGSGKSTLLNIL--GGLD-RPTSGEVR-------VDGT--DISKLSekelaafrrrhigFVFQSfn 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 516 ------------------GVGTKEAIKD--KLIE-FGFTDEMIAMPiSALSGGWKMKLALARAVLRNADILLLDEPTNHL 574
Cdd:cd03255 93 llpdltalenvelplllaGVPKKERRERaeELLErVGLGDRLNHYP-SELSGGQQQRVAIARALANDPKIILADEPTGNL 171
|
170 180
....*....|....*....|....*....
gi 6323278 575 DTVN----VAWLVNYLNTCGITSITISHD 599
Cdd:cd03255 172 DSETgkevMELLRELNKEAGTTIVVVTHD 200
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
451-605 |
7.99e-11 |
|
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: 62.90 E-value: 7.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 451 LRLKRARRYGICGPNGCGKSTLMRAIAngqvdGFPTQEECRTVYveHDIDGTHSDTSV--LDFVF-----------ESGV 517
Cdd:cd03298 19 LTFAQGEITAIVGPSGSGKSTLLNLIA-----GFETPQSGRVLI--NGVDVTAAPPADrpVSMLFqennlfahltvEQNV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 518 G------------TKEAIKDKLIEFGFTDEMIAMPiSALSGGWKMKLALARAVLRNADILLLDEPTNHLDTVNVAWLVNY 585
Cdd:cd03298 92 GlglspglkltaeDRQAIEVALARVGLAGLEKRLP-GELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDL 170
|
170 180 190
....*....|....*....|....*....|....
gi 6323278 586 LNTC----GITSITISHD----------SVFLDN 605
Cdd:cd03298 171 VLDLhaetKMTVLMVTHQpedakrlaqrVVFLDN 204
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
649-736 |
8.17e-11 |
|
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: 62.94 E-value: 8.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 649 KFPEPGYLEGVKTKQKAIVKVTNMEfqypgtSKPQITDINFQCSLSSRIAVIGPNGAGKSTLINVLTGELLPTSGEVYTH 728
Cdd:cd03220 9 SYPTYKGGSSSLKKLGILGRKGEVG------EFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVR 82
|
....*...
gi 6323278 729 enCRIAYI 736
Cdd:cd03220 83 --GRVSSL 88
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
443-575 |
9.17e-11 |
|
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: 63.06 E-value: 9.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 443 KILLNKTQLRLKRARRYGICGPNGCGKSTLMRAIA---------NGQV--DGFP-----TQEECrtVYVEHDiDGTHSDT 506
Cdd:cd03234 20 ARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISgrvegggttSGQIlfNGQPrkpdqFQKCV--AYVRQD-DILLPGL 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6323278 507 SVLDFV-----FESGVGTKEAIKDKLIEFGF----TDEMIA-MPISALSGGWKMKLALARAVLRNADILLLDEPTNHLD 575
Cdd:cd03234 97 TVRETLtytaiLRLPRKSSDAIRKKRVEDVLlrdlALTRIGgNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLD 175
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
634-971 |
9.78e-11 |
|
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: 65.45 E-value: 9.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 634 AAKAYEELSNTDLEFKF-------PEPgylEGVktkqkaiVKVTNMEFQYPGTSKPQITDINFQCSLSSRIAVIGPNGAG 706
Cdd:TIGR01842 287 ARQAYKRLNELLANYPSrdpamplPEP---EGH-------LSVENVTIVPPGGKKPTLRGISFSLQAGEALAIIGPSGSG 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 707 KSTLINVLTGELLPTSGEVythencriayikqhafahiesHLDKtpSEYIQWrfqtgeDRETMDRanrqinendaeamnk 786
Cdd:TIGR01842 357 KSTLARLIVGIWPPTSGSV---------------------RLDG--ADLKQW------DRETFGK--------------- 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 787 ifKIEGTPRRIagihsrRKFKNTyeyecsflLGENIGmkseRWvpmmsvdnawiprGELVESHSKMVAevdmkeALASGQ 866
Cdd:TIGR01842 393 --HIGYLPQDV------ELFPGT--------VAENIA----RF-------------GENADPEKIIEA------AKLAGV 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 867 FRPLTRKEieehcsmLGLDPEIvsHSRIRGLSGGQKVKLVLAAGTWQRPHLIVLDEPTNYLDRDSLGALSKALKEFE--- 943
Cdd:TIGR01842 434 HELILRLP-------DGYDTVI--GPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALKarg 504
|
330 340
....*....|....*....|....*...
gi 6323278 944 GGVIIITHSAEFTkNLTEEVWAVKDGRM 971
Cdd:TIGR01842 505 ITVVVITHRPSLL-GCVDKILVLQDGRI 531
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
451-598 |
1.00e-10 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 65.57 E-value: 1.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 451 LRLKRARRYGICGPNGCGKSTLMRAIA------NGQV--DGFP----TQEECRT--VYVEHDIdgthsdtsvldFVFEsg 516
Cdd:COG1132 361 LTIPPGETVALVGPSGSGKSTLVNLLLrfydptSGRIliDGVDirdlTLESLRRqiGVVPQDT-----------FLFS-- 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 517 vGT-KEAIKdklieFG---FTDEMI--------------AMP------I----SALSGGWKMKLALARAVLRNADILLLD 568
Cdd:COG1132 428 -GTiRENIR-----YGrpdATDEEVeeaakaaqahefieALPdgydtvVgergVNLSGGQRQRIAIARALLKDPPILILD 501
|
170 180 190
....*....|....*....|....*....|..
gi 6323278 569 EPTNHLDTVNVAWLVNYLN--TCGITSITISH 598
Cdd:COG1132 502 EATSALDTETEALIQEALErlMKGRTTIVIAH 533
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
437-598 |
1.01e-10 |
|
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: 63.18 E-value: 1.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 437 SLAYGAKILLNKTQLRLKRARRYGICGPNGCGKSTLMRaIANGQVdgFPTQEECRTV------------------YVEHD 498
Cdd:COG1119 10 TVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLS-LITGDL--PPTYGNDVRLfgerrggedvwelrkrigLVSPA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 499 IDGTH-SDTSVLDFV---FESGVGT--------KEAIKDKLIEFGFtDEMIAMPISALSGGWKMKLALARAVLRNADILL 566
Cdd:COG1119 87 LQLRFpRDETVLDVVlsgFFDSIGLyreptdeqRERARELLELLGL-AHLADRPFGTLSQGEQRRVLIARALVKDPELLI 165
|
170 180 190
....*....|....*....|....*....|....*.
gi 6323278 567 LDEPTNHLDTVNVAWLVNYLNTC----GITSITISH 598
Cdd:COG1119 166 LDEPTAGLDLGARELLLALLDKLaaegAPTLVLVTH 201
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
451-611 |
1.21e-10 |
|
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: 62.84 E-value: 1.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 451 LRLKRARRYGICGPNGCGKSTLMRAIA------------NGQ-VDGFPTQEECR----------------TVYvEHDIDG 501
Cdd:cd03219 21 FSVRPGEIHGLIGPNGAGKTTLFNLISgflrptsgsvlfDGEdITGLPPHEIARlgigrtfqiprlfpelTVL-ENVMVA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 502 THSDTSVlDFVFESGVGTKEAIKDK---LIEF-GFTDEMiAMPISALSGGWKMKLALARAVLRNADILLLDEPT---NHL 574
Cdd:cd03219 100 AQARTGS-GLLLARARREEREARERaeeLLERvGLADLA-DRPAGELSYGQQRRLEIARALATDPKLLLLDEPAaglNPE 177
|
170 180 190
....*....|....*....|....*....|....*..
gi 6323278 575 DTVNVAWLVNYLNTCGITSITISHDSVFLDNVCEYII 611
Cdd:cd03219 178 ETEELAELIRELRERGITVLLVEHDMDVVMSLADRVT 214
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
439-571 |
1.37e-10 |
|
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: 62.45 E-value: 1.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 439 AYGAKILLNKTQLRLKRARRYGICGPNGCGKSTLMRAIA------------NGQ-VDGFPTQEECRT--VYV--EHDIDG 501
Cdd:cd03224 9 GYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMgllpprsgsirfDGRdITGLPPHERARAgiGYVpeGRRIFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 502 THSdtsvldfVFE-----SGVGTKEAIKDKLiefgftDEMIAM-PI---------SALSGGWKMKLALARAVLRNADILL 566
Cdd:cd03224 89 ELT-------VEEnlllgAYARRRAKRKARL------ERVYELfPRlkerrkqlaGTLSGGEQQMLAIARALMSRPKLLL 155
|
....*
gi 6323278 567 LDEPT 571
Cdd:cd03224 156 LDEPS 160
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
433-575 |
1.75e-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: 61.18 E-value: 1.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 433 NCEFSLAYGAKILLNKTQLRLKRARRYGICGPNGCGKSTLMRAIA------NGQV--DGFPTQ--EECRTVYVehdidgt 502
Cdd:cd03247 5 NVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTgdlkpqQGEItlDGVPVSdlEKALSSLI------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 503 hsdtSVLD---FVFE----SGVGTKeaikdkliefgftdemiampisaLSGGWKMKLALARAVLRNADILLLDEPTNHLD 575
Cdd:cd03247 78 ----SVLNqrpYLFDttlrNNLGRR-----------------------FSGGERQRLALARILLQDAPIVLLDEPTVGLD 130
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
435-609 |
1.91e-10 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 62.70 E-value: 1.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 435 EFSLAYGAKILLNKTQLRLKRARRYGICGPNGCGKSTLMRAI------ANGQV--DG-----FPTQEECRTVYVEHDIDG 501
Cdd:PRK10253 12 QLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLsrlmtpAHGHVwlDGehiqhYASKEVARRIGLLAQNAT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 502 THSDTSVLDFVFESGV-----------GTKEAIKDKLIEFGFTDeMIAMPISALSGGWKMKLALARAVLRNADILLLDEP 570
Cdd:PRK10253 92 TPGDITVQELVARGRYphqplftrwrkEDEEAVTKAMQATGITH-LADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEP 170
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 6323278 571 TNHLD---TVNVAWLVNYLN-TCGITSITISHDsvfLDNVCEY 609
Cdd:PRK10253 171 TTWLDishQIDLLELLSELNrEKGYTLAAVLHD---LNQACRY 210
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
439-611 |
2.06e-10 |
|
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: 61.78 E-value: 2.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 439 AYGAKILLNKTQLRLKRARRYGICGPNGCGKSTLMRAIaNGQVDgfPTQEecrTVYVE-HDIDGTHSDTSVLD----FVF 513
Cdd:cd03262 9 SFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCI-NLLEE--PDSG---TIIIDgLKLTDDKKNINELRqkvgMVF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 514 ES---------------------GVGTKEAIK---DKLIEFGFTDEMIAMPiSALSGGWKMKLALARAVLRNADILLLDE 569
Cdd:cd03262 83 QQfnlfphltvlenitlapikvkGMSKAEAEEralELLEKVGLADKADAYP-AQLSGGQQQRVAIARALAMNPKVMLFDE 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 6323278 570 PTNHLD--TVN-VAWLVNYLNTCGITSITISHDSVFLDNVCEYII 611
Cdd:cd03262 162 PTSALDpeLVGeVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVI 206
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
461-605 |
2.62e-10 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 61.61 E-value: 2.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 461 ICGPNGCGKSTLMRAIANGQVdgfPTQEEcrtVYV-EHDIDG-THSDTSVL---------DF-------VFE-------- 514
Cdd:COG2884 33 LTGPSGAGKSTLLKLLYGEER---PTSGQ---VLVnGQDLSRlKRREIPYLrrrigvvfqDFrllpdrtVYEnvalplrv 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 515 SGVGTKEaIKDKLIE----FGFTDEMIAMPIsALSGGWKMKLALARAVLRNADILLLDEPTNHLDTVNVAWLVNYL---N 587
Cdd:COG2884 107 TGKSRKE-IRRRVREvldlVGLSDKAKALPH-ELSGGEQQRVAIARALVNRPELLLADEPTGNLDPETSWEIMELLeeiN 184
|
170
....*....|....*...
gi 6323278 588 TCGITSITISHDSVFLDN 605
Cdd:COG2884 185 RRGTTVLIATHDLELVDR 202
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
667-741 |
2.76e-10 |
|
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: 60.95 E-value: 2.76e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6323278 667 VKVTNMEFQYPG---TSKPQITDINFQCSLSSRIAVIGPNGAGKSTLINVLTGELLPTSGEVYTheNCRIAYIKQHAF 741
Cdd:cd03250 1 ISVEDASFTWDSgeqETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSV--PGSIAYVSQEPW 76
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
451-611 |
2.84e-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: 61.37 E-value: 2.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 451 LRLKRARRYGICGPNGCGKSTLMRAIANGqvdGFPTQEEcrtVYVEHDIDGTHSDT-----------------SVLDFVF 513
Cdd:cd03257 26 FSIKKGETLGLVGESGSGKSTLARAILGL---LKPTSGS---IIFDGKDLLKLSRRlrkirrkeiqmvfqdpmSSLNPRM 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 514 EsgVGT------------------KEAIKDKLIEFGFTDEMIAMPISALSGGWKMKLALARAVLRNADILLLDEPTNHLD 575
Cdd:cd03257 100 T--IGEqiaeplrihgklskkearKEAVLLLLVGVGLPEEVLNRYPHELSGGQRQRVAIARALALNPKLLIADEPTSALD 177
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 6323278 576 TVNVAWLVNYLNT----CGITSITISHDSVFLDNVCEYII 611
Cdd:cd03257 178 VSVQAQILDLLKKlqeeLGLTLLFITHDLGVVAKIADRVA 217
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
503-975 |
2.95e-10 |
|
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: 64.05 E-value: 2.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 503 HSDTSVLDFVFES----GVGTKEAIKD--KLIEFGFTDEMIAMPISALSGGWKMKLALARAVLRNADILLLDEPTNHLD- 575
Cdd:TIGR03269 122 YGDDTVLDNVLEAleeiGYEGKEAVGRavDLIEMVQLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDp 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 576 -TVNVA--WLVNYLNTCGITSITISHDSVFLDNVCEYIINYEGLKLRKyKGNFTEFVKKcpaakayeelsntdlefkfpe 652
Cdd:TIGR03269 202 qTAKLVhnALEEAVKASGISMVLTSHWPEVIEDLSDKAIWLENGEIKE-EGTPDEVVAV--------------------- 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 653 pgYLEGVKTKQKA--------IVKVTNMEFQYPGTSKPQIT---DINFQCSLSSRIAVIGPNGAGKSTLINVLTGELLPT 721
Cdd:TIGR03269 260 --FMEGVSEVEKEcevevgepIIKVRNVSKRYISVDRGVVKavdNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPT 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 722 SGEVYthencriayikqhafahieshldktpseyiqwrFQTGEDRETMdranrqineNDAEAMNKifkieGTPRRIAGIh 801
Cdd:TIGR03269 338 SGEVN---------------------------------VRVGDEWVDM---------TKPGPDGR-----GRAKRYIGI- 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 802 srrkfkntyeyecsflLGENIGMKSERWVpmmsVDNAWIPRG-ELVESHSKMVAEVDMKEAlasgqfrPLTRKEIEEhcs 880
Cdd:TIGR03269 370 ----------------LHQEYDLYPHRTV----LDNLTEAIGlELPDELARMKAVITLKMV-------GFDEEKAEE--- 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 881 MLGLDPEivshsrirGLSGGQKVKLVLAAGTWQRPHLIVLDEPTNYLD----RDSLGALSKALKEFEGGVIIITHSAEFT 956
Cdd:TIGR03269 420 ILDKYPD--------ELSEGERHRVALAQVLIKEPRIVILDEPTGTMDpitkVDVTHSILKAREEMEQTFIIVSHDMDFV 491
|
490
....*....|....*....
gi 6323278 957 KNLTEEVWAVKDGRMTPSG 975
Cdd:TIGR03269 492 LDVCDRAALMRDGKIVKIG 510
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
463-599 |
3.71e-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: 3.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 463 GPNGCGKSTLMRAIAngqvdGF--PTQEEcrtVYV-EHDIDGT---HSDTSvldFVFES--------------------G 516
Cdd:COG3842 38 GPSGCGKTTLLRMIA-----GFetPDSGR---ILLdGRDVTGLppeKRNVG---MVFQDyalfphltvaenvafglrmrG 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 517 VGtKEAIKDKliefgfTDEMIAM---------PISALSGGWKMKLALARAVLRNADILLLDEPTNHLDtVNV-----AWL 582
Cdd:COG3842 107 VP-KAEIRAR------VAELLELvglegladrYPHQLSGGQQQRVALARALAPEPRVLLLDEPLSALD-AKLreemrEEL 178
|
170
....*....|....*..
gi 6323278 583 VNYLNTCGITSITISHD 599
Cdd:COG3842 179 RRLQRELGITFIYVTHD 195
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
660-726 |
4.59e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 61.55 E-value: 4.59e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6323278 660 KTKQKAIvKVTNMEFQYPGTSKPQITDINFQCSLSSRIAVIGPNGAGKSTLINVLTGELLPTSGEVY 726
Cdd:PRK13632 2 KNKSVMI-KVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIK 67
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
664-951 |
4.87e-10 |
|
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: 63.23 E-value: 4.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 664 KAIVKVTNMEFQYPGTSKPQITDINFQCSLSSRIAVIGPNGAGKSTLINVLTGELLPTSGEVYthencriayikqhafah 743
Cdd:COG4618 328 KGRLSVENLTVVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVR----------------- 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 744 ieshLDktpseyiqwrfqtGEDRETMDRANR--------QinenDAEamnkIFkiEGTprrIAgihsrrkfkntyeyecs 815
Cdd:COG4618 391 ----LD-------------GADLSQWDREELgrhigylpQ----DVE----LF--DGT---IA----------------- 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 816 fllgENIGMkserwvpMMSVDnawiprGELVESHSKMVAEVDMKEALAsgqfrpltrkeieehcsmLGLDPEIVSHSriR 895
Cdd:COG4618 424 ----ENIAR-------FGDAD------PEKVVAAAKLAGVHEMILRLP------------------DGYDTRIGEGG--A 466
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 6323278 896 GLSGGQKVKLVLAAGTWQRPHLIVLDEPTNYLDRDSLGALSKALKEF--EGG-VIIITH 951
Cdd:COG4618 467 RLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALkaRGAtVVVITH 525
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
443-600 |
5.33e-10 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 63.29 E-value: 5.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 443 KILLNKTQLRLKRARRYGICGPNGCGKSTLMRAIA------NGQVDgFPTQEEC----RTVYVehdIDGT--------HS 504
Cdd:COG4178 376 RPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAglwpygSGRIA-RPAGARVlflpQRPYL---PLGTlreallypAT 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 505 DTSVLDfvfesgvgtkEAIKDKLIEFGFTD-----------EMIampisaLSGGWKMKLALARAVLRNADILLLDEPTNH 573
Cdd:COG4178 452 AEAFSD----------AELREALEAVGLGHlaerldeeadwDQV------LSLGEQQRLAFARLLLHKPDWLFLDEATSA 515
|
170 180
....*....|....*....|....*....
gi 6323278 574 LDTVNVAWLVNYLNTC--GITSITISHDS 600
Cdd:COG4178 516 LDEENEAALYQLLREElpGTTVISVGHRS 544
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
674-971 |
6.04e-10 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 60.22 E-value: 6.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 674 FQYPGTSKPQITDINFQCSLSSRIAVIGPNGAGKSTLINVLTGELLPTSGEVYTHENCRIAYikqhafahieshldkTPs 753
Cdd:COG4619 6 LSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAM---------------PP- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 754 eyIQWRfqtgedretmdranrqinendaeamnkifkiegtpRRIAGIHSRrkfkntyeyecSFLLGENIGmkserwvpmm 833
Cdd:COG4619 70 --PEWR-----------------------------------RQVAYVPQE-----------PALWGGTVR---------- 91
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 834 svDNawIPRGELVesHSKMVAEVDMKEALAsgqfrpltrkeieehcsMLGLDPEIVsHSRIRGLSGGQKVKLVLAAGTWQ 913
Cdd:COG4619 92 --DN--LPFPFQL--RERKFDRERALELLE-----------------RLGLPPDIL-DKPVERLSGGERQRLALIRALLL 147
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6323278 914 RPHLIVLDEPTNYLDRDSLGALSKALKEF----EGGVIIITHSAEFTKNLTEEVWAVKDGRM 971
Cdd:COG4619 148 QPDVLLLDEPTSALDPENTRRVEELLREYlaeeGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
897-955 |
6.22e-10 |
|
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: 59.96 E-value: 6.22e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6323278 897 LSGGQKVKLVLAAGTWQRPHLIVLDEPTNYLDRDSLGALSKALKEF--EGG-VIIITHSAEF 955
Cdd:cd03226 127 LSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMERVGELIRELaaQGKaVIVITHDYEF 188
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
669-766 |
6.46e-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: 59.25 E-value: 6.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 669 VTNMEFQYPGTSKPQITDINFQCSLSSRIAVIGPNGAGKSTLINVLTGELLPTSGEVY-------THENCRIAYIkqhAF 741
Cdd:cd03247 3 INNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITldgvpvsDLEKALSSLI---SV 79
|
90 100
....*....|....*....|....*.
gi 6323278 742 AHIESHL-DKTPSEYIQWRFQTGEDR 766
Cdd:cd03247 80 LNQRPYLfDTTLRNNLGRRFSGGERQ 105
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
435-578 |
6.52e-10 |
|
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: 60.27 E-value: 6.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 435 EFSLAYGAKILLNKTQLRLKRARRYGICGPNGCGKSTLMRAIaNGQVDGFPtqeECR---TVYVE-HDIDGthSDTSVLD 510
Cdd:cd03260 5 DLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLL-NRLNDLIP---GAPdegEVLLDgKDIYD--LDVDVLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 511 ------FVFES-------------------GVGTKEAIkDKLIEFGFtdEMIAMP--------ISALSGGWKMKLALARA 557
Cdd:cd03260 79 lrrrvgMVFQKpnpfpgsiydnvayglrlhGIKLKEEL-DERVEEAL--RKAALWdevkdrlhALGLSGGQQQRLCLARA 155
|
170 180
....*....|....*....|.
gi 6323278 558 VLRNADILLLDEPTNHLDTVN 578
Cdd:cd03260 156 LANEPEVLLLDEPTSALDPIS 176
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
440-575 |
7.47e-10 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 60.85 E-value: 7.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 440 YGAKILLNKTQLRLKRARRYGICGPNGCGKSTLMRAIAN-----------GQVDGFPTQEECRTVYvehdidgthSDT-- 506
Cdd:PRK11247 22 YGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGletpsagellaGTAPLAEAREDTRLMF---------QDArl 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6323278 507 ----SVLDFVfesGVGTKEAIKDK----LIEFGFTDEMIAMPiSALSGGWKMKLALARAVLRNADILLLDEPTNHLD 575
Cdd:PRK11247 93 lpwkKVIDNV---GLGLKGQWRDAalqaLAAVGLADRANEWP-AALSGGQKQRVALARALIHRPGLLLLDEPLGALD 165
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
460-612 |
7.78e-10 |
|
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: 60.14 E-value: 7.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 460 GICGPNGCGKSTLMRAI-ANGQVDGfptqeecRTVYVEHD---IDGTHSD------------------------TSVLDF 511
Cdd:COG4778 41 ALTGPSGAGKSTLLKCIyGNYLPDS-------GSILVRHDggwVDLAQASpreilalrrrtigyvsqflrviprVSALDV 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 512 V----FESGVGTKEAI---KDKLIEFGFTDEMIAMPISALSGGWKMKLALARAVLRNADILLLDEPTNHLDTVNVAWLVN 584
Cdd:COG4778 114 VaeplLERGVDREEARaraRELLARLNLPERLWDLPPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVE 193
|
170 180 190
....*....|....*....|....*....|.
gi 6323278 585 YLNTC---GITSITISHDSVFLDNVCEYIIN 612
Cdd:COG4778 194 LIEEAkarGTAIIGIFHDEEVREAVADRVVD 224
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
439-599 |
1.15e-09 |
|
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: 59.94 E-value: 1.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 439 AYGAKILLNKTQLRLKRARRYGICGPNGCGKSTLMRAIAngqvdGFPTQEECRTVYVEHDIDGTHSDTSVLDFVFES--- 515
Cdd:cd03300 9 FYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIA-----GFETPTSGEILLDGKDITNLPPHKRPVNTVFQNyal 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 516 ----------GVGTKEAIKDKLIEFGFTDEMIAM---------PISALSGGWKMKLALARAVLRNADILLLDEPTNHLDT 576
Cdd:cd03300 84 fphltvfeniAFGLRLKKLPKAEIKERVAEALDLvqlegyanrKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDL 163
|
170 180
....*....|....*....|....*..
gi 6323278 577 VNVAW----LVNYLNTCGITSITISHD 599
Cdd:cd03300 164 KLRKDmqleLKRLQKELGITFVFVTHD 190
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
446-599 |
1.19e-09 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 59.67 E-value: 1.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 446 LNKTQLRLKRARRYGICGPNGCGKSTLMRAIAngqvdGF--PTQEECRtvyvehdIDGThsDTSVLD------------- 510
Cdd:COG1136 24 LRGVSLSIEAGEFVAIVGPSGSGKSTLLNILG-----GLdrPTSGEVL-------IDGQ--DISSLSerelarlrrrhig 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 511 FVFES--------------------GVGTKEAIK--DKLIE-FGFTDEMIAMPiSALSGGWKMKLALARAVLRNADILLL 567
Cdd:COG1136 90 FVFQFfnllpeltalenvalplllaGVSRKERREraRELLErVGLGDRLDHRP-SQLSGGQQQRVAIARALVNRPKLILA 168
|
170 180 190
....*....|....*....|....*....|....*.
gi 6323278 568 DEPTNHLDTVNVAWLVNYLNTC----GITSITISHD 599
Cdd:COG1136 169 DEPTGNLDSKTGEEVLELLRELnrelGTTIVMVTHD 204
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
680-725 |
1.52e-09 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 59.79 E-value: 1.52e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 6323278 680 SKPQITDINFQCSLSSRIAVIGPNGAGKSTLINVLTGELLPTSGEV 725
Cdd:PRK13548 14 GRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEV 59
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
441-600 |
1.59e-09 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 59.34 E-value: 1.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 441 GAKILLNKTQLRLKRARRYGICGPNGCGKSTLMRAIAN------GQV--DGFP----TQEECR---------------TV 493
Cdd:PRK10247 18 GDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASlisptsGTLlfEGEDistlKPEIYRqqvsycaqtptlfgdTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 494 YvehdidgthsDTSVLDFVFESGVGTKEAIKDKLIEFGFTDEMIAMPISALSGGWKMKLALARAVLRNADILLLDEPTNH 573
Cdd:PRK10247 98 Y----------DNLIFPWQIRNQQPDPAIFLDDLERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSA 167
|
170 180 190
....*....|....*....|....*....|.
gi 6323278 574 LD---TVNVAWLVN-YLNTCGITSITISHDS 600
Cdd:PRK10247 168 LDesnKHNVNEIIHrYVREQNIAVLWVTHDK 198
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
435-598 |
1.61e-09 |
|
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: 59.52 E-value: 1.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 435 EFSLAYGAKILLNKTQLRLKRARRYGICGPNGCGKSTLMRAIaNG---------QVDGFPTQE----------------- 488
Cdd:cd03258 10 VFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCI-NGlerptsgsvLVDGTDLTLlsgkelrkarrrigmif 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 489 ------ECRTVY--VEHDIDGTHSDtsvldfvfesgvgtKEAIKDK---LIEF-GFTDEMIAMPiSALSGGWKMKLALAR 556
Cdd:cd03258 89 qhfnllSSRTVFenVALPLEIAGVP--------------KAEIEERvleLLELvGLEDKADAYP-AQLSGGQKQRVGIAR 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 6323278 557 AVLRNADILLLDEPTNHLD---TVNVAWLVNYLN-TCGITSITISH 598
Cdd:cd03258 154 ALANNPKVLLCDEATSALDpetTQSILALLRDINrELGLTIVLITH 199
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
440-599 |
1.83e-09 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 60.87 E-value: 1.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 440 YGAKILLNKTQLRLKRARRYGICGPNGCGKSTLMRAIAngqvdGFPTQEECRTVYVEHDIDGTHSDTSVLDFVFES---- 515
Cdd:PRK10851 12 FGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIA-----GLEHQTSGHIRFHGTDVSRLHARDRKVGFVFQHyalf 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 516 -----------GVG--------TKEAIKDKLIEFGftdEMIAMP------ISALSGGWKMKLALARAVLRNADILLLDEP 570
Cdd:PRK10851 87 rhmtvfdniafGLTvlprrerpNAAAIKAKVTQLL---EMVQLAhladryPAQLSGGQKQRVALARALAVEPQILLLDEP 163
|
170 180 190
....*....|....*....|....*....|....
gi 6323278 571 TNHLDTvNV-----AWLVNYLNTCGITSITISHD 599
Cdd:PRK10851 164 FGALDA-QVrkelrRWLRQLHEELKFTSVFVTHD 196
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
435-580 |
1.92e-09 |
|
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: 58.66 E-value: 1.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 435 EFSLAYGAKILLNKTQLRLKRARRYGICGPNGCGKSTLMRAIA------------NGQVDGFPTQEECRTV-YVEHdIDG 501
Cdd:cd03231 5 ELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAglspplagrvllNGGPLDFQRDSIARGLlYLGH-APG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 502 THSDTSVLD-FVFESGVGTKEAIKDKLIEF---GFTDemiaMPISALSGGWKMKLALARAVLRNADILLLDEPTNHLDTV 577
Cdd:cd03231 84 IKTTLSVLEnLRFWHADHSDEQVEEALARVglnGFED----RPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKA 159
|
...
gi 6323278 578 NVA 580
Cdd:cd03231 160 GVA 162
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
440-575 |
1.93e-09 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 60.47 E-value: 1.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 440 YGAKILLNKTQLRLKRARRYGICGPNGCGKSTLMRAIAngqvdGF--PTQEECRtvyvehdIDGTH-SDTSVLD----FV 512
Cdd:COG3839 13 YGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIA-----GLedPTSGEIL-------IGGRDvTDLPPKDrniaMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 513 FES--------------------GVgTKEAIKDKLiefgftDEMIAM----------PiSALSGGWKMKLALARAVLRNA 562
Cdd:COG3839 81 FQSyalyphmtvyeniafplklrKV-PKAEIDRRV------REAAELlgledlldrkP-KQLSGGQRQRVALGRALVREP 152
|
170
....*....|...
gi 6323278 563 DILLLDEPTNHLD 575
Cdd:COG3839 153 KVFLLDEPLSNLD 165
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
871-970 |
2.26e-09 |
|
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: 57.97 E-value: 2.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 871 TRKEIEEHCSMLGLDPEIVSHSRIR-----GLSGGQKVKLVLAAGTWQRPHLIVLDEPTNYLD---RDSLGALSKALKEF 942
Cdd:cd03229 70 ELPPLRRRIGMVFQDFALFPHLTVLenialGLSGGQQQRVALARALAMDPDVLLLDEPTSALDpitRREVRALLKSLQAQ 149
|
90 100
....*....|....*....|....*....
gi 6323278 943 EG-GVIIITHSAEFTKNLTEEVWAVKDGR 970
Cdd:cd03229 150 LGiTVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
440-611 |
2.63e-09 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 59.74 E-value: 2.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 440 YGAKILLNKTQLRLKRARRYGICGPNGCGKSTLMRAIAN------GQV--DGFPTQ-----------EEcRTVYvehdid 500
Cdd:COG4152 11 FGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGilapdsGEVlwDGEPLDpedrrrigylpEE-RGLY------ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 501 gthSDTSVLDFV--FES--GVGTKEAIK--DKLIE-FGFTDeMIAMPISALSGGWKMKLALARAVLRNADILLLDEPTNH 573
Cdd:COG4152 84 ---PKMKVGEQLvyLARlkGLSKAEAKRraDEWLErLGLGD-RANKKVEELSKGNQQKVQLIAALLHDPELLILDEPFSG 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 6323278 574 LDTVNVAWLVN---YLNTCGITSITISHDsvfLDNV---CEYII 611
Cdd:COG4152 160 LDPVNVELLKDvirELAAKGTTVIFSSHQ---MELVeelCDRIV 200
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
440-599 |
2.82e-09 |
|
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: 58.89 E-value: 2.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 440 YGAKILLNKTQLRLKRARRYGICGPNGCGKSTLMRAIAngqvdGFPTQEECRTVYVEHDIDGTHSDTSVLDFVFE----- 514
Cdd:cd03296 12 FGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIA-----GLERPDSGTILFGGEDATDVPVQERNVGFVFQhyalf 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 515 ------------------SGVGTKEAIKDKLIEF-------GFTDEMiamPiSALSGGWKMKLALARAVLRNADILLLDE 569
Cdd:cd03296 87 rhmtvfdnvafglrvkprSERPPEAEIRAKVHELlklvqldWLADRY---P-AQLSGGQRQRVALARALAVEPKVLLLDE 162
|
170 180 190
....*....|....*....|....*....|....*
gi 6323278 570 PTNHLDTvNV-----AWLVNYLNTCGITSITISHD 599
Cdd:cd03296 163 PFGALDA-KVrkelrRWLRRLHDELHVTTVFVTHD 196
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
667-951 |
2.95e-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: 2.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 667 VKVTNMEFQYP--GTSKPQITDINFQCSLSSRIAVIGPNGAGKSTLINVLTGELLPTSGEVYthencriayikqhafahi 744
Cdd:COG1124 2 LEVRNLSVSYGqgGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVT------------------ 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 745 eshldktpseyiqwrfqtgedretmdranrqinendaeamnkifkIEGTPRRIAGIHSRRKfkntyeyecsfllgeNIGM 824
Cdd:COG1124 64 ---------------------------------------------FDGRPVTRRRRKAFRR---------------RVQM 83
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 825 kserwV---PMMSVDnawiPRgelveshsKMVAEVdMKEALASgQFRPLTRKEIEEHCSMLGLDPEIVsHSRIRGLSGGQ 901
Cdd:COG1124 84 -----VfqdPYASLH----PR--------HTVDRI-LAEPLRI-HGLPDREERIAELLEQVGLPPSFL-DRYPHQLSGGQ 143
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 6323278 902 KVKLVLAAGTWQRPHLIVLDEPTNYLD---RDSLGALSKALKEFEG-GVIIITH 951
Cdd:COG1124 144 RQRVAIARALILEPELLLLDEPTSALDvsvQAEILNLLKDLREERGlTYLFVSH 197
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
698-975 |
3.25e-09 |
|
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: 58.35 E-value: 3.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 698 AVIGPNGAGKSTLINVLTG-----ELLPTSGEVYthencriayikqhafahieshLDktpseyiqwrfqtGEDretmdra 772
Cdd:cd03260 30 ALIGPSGCGKSTLLRLLNRlndliPGAPDEGEVL---------------------LD-------------GKD------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 773 nrqinendaeamnkIFKIEGTPrriagIHSRRKfkntyeyecsfllgenIGMKSERWVPM-MSV-DN-AWIPRgeLVESH 849
Cdd:cd03260 69 --------------IYDLDVDV-----LELRRR----------------VGMVFQKPNPFpGSIyDNvAYGLR--LHGIK 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 850 SKMVAEVDMKEALasgqfrpltrkeieehcSMLGLDPEIVSHSRIRGLSGGQKVKLVLAAGTWQRPHLIVLDEPTNYLDR 929
Cdd:cd03260 112 LKEELDERVEEAL-----------------RKAALWDEVKDRLHALGLSGGQQQRLCLARALANEPEVLLLDEPTSALDP 174
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 6323278 930 DSLGALSKALKEF--EGGVIIITHSAEFTKNLTEEVWAVKDGRMTPSG 975
Cdd:cd03260 175 ISTAKIEELIAELkkEYTIVIVTHNMQQAARVADRTAFLLNGRLVEFG 222
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
687-976 |
3.77e-09 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 60.63 E-value: 3.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 687 INFQCSLSSRIAVIGPNGAGKSTLINVLTGeLLPTSGEVythencRIAyikqhafaHIE-SHLDKTpseyiQWRfqtged 765
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLG-FLPYQGSL------KIN--------GIElRELDPE-----SWR------ 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 766 retmdranRQIN---ENdaeamnkifkiegtPRRIAGIhsrrkfkntyeyecsflLGENIGMKSerwvPMMSvdnawipr 842
Cdd:PRK11174 423 --------KHLSwvgQN--------------PQLPHGT-----------------LRDNVLLGN----PDAS-------- 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 843 gelveshskmvaEVDMKEALASGQfrpltrkeIEEHCSML--GLDPEIVSHSRirGLSGGQKVKLVLAAGTWQRPHLIVL 920
Cdd:PRK11174 452 ------------DEQLQQALENAW--------VSEFLPLLpqGLDTPIGDQAA--GLSVGQAQRLALARALLQPCQLLLL 509
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 6323278 921 DEPTNYLDRDSLGALSKALKEFEGG--VIIITHSAEFTKNLtEEVWAVKDGRMTPSGH 976
Cdd:PRK11174 510 DEPTASLDAHSEQLVMQALNAASRRqtTLMVTHQLEDLAQW-DQIWVMQDGQIVQQGD 566
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
437-599 |
3.91e-09 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 58.59 E-value: 3.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 437 SLAYGAKILLNKTQLRLKRARRYGICGPNGCGKSTLMRAIAnGQVDgfPT------QEECRTVYVEHDIdgtHSDT---- 506
Cdd:PRK09544 11 SVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVL-GLVA--PDegvikrNGKLRIGYVPQKL---YLDTtlpl 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 507 SVLDFVFESGvGTKEAIKDKLIEFGFTDEMIAMPISALSGGWKMKLALARAVLRNADILLLDEPTNHLDtVN--VAW--L 582
Cdd:PRK09544 85 TVNRFLRLRP-GTKKEDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVD-VNgqVALydL 162
|
170 180
....*....|....*....|
gi 6323278 583 VNYLNT---CGItsITISHD 599
Cdd:PRK09544 163 IDQLRReldCAV--LMVSHD 180
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
463-614 |
4.12e-09 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 58.49 E-value: 4.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 463 GPNGCGKSTLMR-------------AIANGQVDgFPTQEECRT----------VYVEHDIdGTHsdTSVLDFVFES---- 515
Cdd:COG4161 35 GPSGAGKSSLLRvlnlletpdsgqlNIAGHQFD-FSQKPSEKAirllrqkvgmVFQQYNL-WPH--LTVMENLIEApckv 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 516 -GVGTKEAIK--DKLIE-FGFTDEMIAMPIsALSGGWKMKLALARAVLRNADILLLDEPTNHLD---TVNVAWLVNYLNT 588
Cdd:COG4161 111 lGLSKEQAREkaMKLLArLRLTDKADRFPL-HLSGGQQQRVAIARALMMEPQVLLFDEPTAALDpeiTAQVVEIIRELSQ 189
|
170 180
....*....|....*....|....*.
gi 6323278 589 CGITSITISHDSVFLDNVCEYIINYE 614
Cdd:COG4161 190 TGITQVIVTHEVEFARKVASQVVYME 215
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
461-598 |
4.13e-09 |
|
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: 58.40 E-value: 4.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 461 ICGPNGCGKSTLMRAI------ANGQV--DGFP----TQEECRTV--YVEHDidgthsdtSVL--DFVFES-GVGTKEAI 523
Cdd:cd03253 32 IVGPSGSGKSTILRLLfrfydvSSGSIliDGQDirevTLDSLRRAigVVPQD--------TVLfnDTIGYNiRYGRPDAT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 524 KDKLIEF----GFTDEMIAMPIS----------ALSGGWKMKLALARAVLRNADILLLDEPTNHLDTVNVAWLVNYLNTC 589
Cdd:cd03253 104 DEEVIEAakaaQIHDKIMRFPDGydtivgerglKLSGGEKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDV 183
|
170
....*....|.
gi 6323278 590 --GITSITISH 598
Cdd:cd03253 184 skGRTTIVIAH 194
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
667-970 |
5.79e-09 |
|
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: 57.50 E-value: 5.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 667 VKVTNMEFQYPGTSKPQ--ITDINFQCSLSSRIAVIGPNGAGKSTLINVLTGELLPTSGEVYthencriayikqhafahi 744
Cdd:cd03255 1 IELKNLSKTYGGGGEKVqaLKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVR------------------ 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 745 eshldktpseyiqwrfqtgedretmdranrqinendaeamnkifkIEGTPrrIAGIHSRRKfkntyeyecSFLLGENIGM 824
Cdd:cd03255 63 ---------------------------------------------VDGTD--ISKLSEKEL---------AAFRRRHIGF 86
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 825 --KSERWVPMMSV-DNAWIPrgelveshskmvaevdmkeALASGQFRPLTRKEIEEHCSMLGLDpEIVSHsRIRGLSGGQ 901
Cdd:cd03255 87 vfQSFNLLPDLTAlENVELP-------------------LLLAGVPKKERRERAEELLERVGLG-DRLNH-YPSELSGGQ 145
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6323278 902 KVKLVLAAGTWQRPHLIVLDEPTNYLDRDS----LGALSKALKEFEGGVIIITHSAEFTKnLTEEVWAVKDGR 970
Cdd:cd03255 146 QQRVAIARALANDPKIILADEPTGNLDSETgkevMELLRELNKEAGTTIVVVTHDPELAE-YADRIIELRDGK 217
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
665-727 |
6.14e-09 |
|
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: 57.79 E-value: 6.14e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6323278 665 AIVKVTNMEFQYPGtsKPQITDINFQCSLSSRIAVIGPNGAGKSTLINVLTGELLPTSGEVYT 727
Cdd:COG1119 2 PLLELRNVTVRRGG--KTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDVR 62
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
698-951 |
6.35e-09 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 57.77 E-value: 6.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 698 AVIGPNGAGKSTLINVLTG--ELLPTSGEVythencriayikqhafahiesHLDktpseyiqwrfqtGED---RETMDRA 772
Cdd:COG0396 30 AIMGPNGSGKSTLAKVLMGhpKYEVTSGSI---------------------LLD-------------GEDileLSPDERA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 773 NRqinendaeamnKIFKIEGTPRRIAGIhsrrkfKNTYeyecsFLlgenigmkserwvpmMSVDNAWipRGElveshskm 852
Cdd:COG0396 76 RA-----------GIFLAFQYPVEIPGV------SVSN-----FL---------------RTALNAR--RGE-------- 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 853 vaEVDMKEALasgqfrpltrKEIEEHCSMLGLDPEIVSHSRIRGLSGGQKVK---LVLAAgtwQRPHLIVLDEPTNYLDR 929
Cdd:COG0396 109 --ELSAREFL----------KLLKEKMKELGLDEDFLDRYVNEGFSGGEKKRneiLQMLL---LEPKLAILDETDSGLDI 173
|
250 260
....*....|....*....|....*
gi 6323278 930 DSLGALSKALKEF---EGGVIIITH 951
Cdd:COG0396 174 DALRIVAEGVNKLrspDRGILIITH 198
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
435-577 |
6.54e-09 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 57.86 E-value: 6.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 435 EFSLAYGAKILLNKTQLRLKRARRYGICGPNGCGKSTLMRAIaNGQVDGFPTQEECRTV-YVEHDIDGTHSDTSVL---- 509
Cdd:PRK14239 10 DLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSI-NRMNDLNPEVTITGSIvYNGHNIYSPRTDTVDLrkei 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 510 DFVFE-------------------SGVGTK----EAIKDKLIEFGFTDEM---IAMPISALSGGWKMKLALARAVLRNAD 563
Cdd:PRK14239 89 GMVFQqpnpfpmsiyenvvyglrlKGIKDKqvldEAVEKSLKGASIWDEVkdrLHDSALGLSGGQQQRVCIARVLATSPK 168
|
170
....*....|....
gi 6323278 564 ILLLDEPTNHLDTV 577
Cdd:PRK14239 169 IILLDEPTSALDPI 182
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
461-599 |
6.65e-09 |
|
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: 56.98 E-value: 6.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 461 ICGPNGCGKSTLMRAIA------NGQVD----GFPTQEECRT---VYVEHdIDGTHSDTSV---LDFVFESGVGTKEAIK 524
Cdd:TIGR01189 31 VTGPNGIGKTTLLRILAgllrpdSGEVRwngtPLAEQRDEPHeniLYLGH-LPGLKPELSAlenLHFWAAIHGGAQRTIE 109
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6323278 525 DKLIEFGFTDeMIAMPISALSGGWKMKLALARAVLRNADILLLDEPTNHLDTVNVAWLVN----YLNTCGITSITISHD 599
Cdd:TIGR01189 110 DALAAVGLTG-FEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVALLAGllraHLARGGIVLLTTHQD 187
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
666-725 |
7.92e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 57.89 E-value: 7.92e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 666 IVKVTNMEFQYPGtSKPQITDINFQCSLSSRIAVIGPNGAGKSTLINVLTGELLPTSGEV 725
Cdd:PRK13652 3 LIETRDLCYSYSG-SKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSV 61
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
542-598 |
9.83e-09 |
|
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: 57.16 E-value: 9.83e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 6323278 542 SALSGGWKMKLALARAVLRNADILLLDEPTNHLDTVNVAWLVNYLNTC--GITSITISH 598
Cdd:cd03249 138 SQLSGGQKQRIAIARALLRNPKILLLDEATSALDAESEKLVQEALDRAmkGRTTIVIAH 196
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
446-598 |
1.06e-08 |
|
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: 56.73 E-value: 1.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 446 LNKTQLRLKRARRYGICGPNGCGKSTLMRAI------ANGQ--VDGFPTQ----EECR---------------TVYVEHD 498
Cdd:cd03244 20 LKNISFSIKPGEKVGIVGRTGSGKSSLLLALfrlvelSSGSilIDGVDISkiglHDLRsrisiipqdpvlfsgTIRSNLD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 499 IDGTHSDTSVLDfVFESgVGTKEAIKDKLiefGFTDEMIAMPISALSGGWKMKLALARAVLRNADILLLDEPTNHLDTVN 578
Cdd:cd03244 100 PFGEYSDEELWQ-ALER-VGLKEFVESLP---GGLDTVVEEGGENLSVGQRQLLCLARALLRKSKILVLDEATASVDPET 174
|
170 180
....*....|....*....|..
gi 6323278 579 VAWLVNYLNTC--GITSITISH 598
Cdd:cd03244 175 DALIQKTIREAfkDCTVLTIAH 196
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
667-726 |
1.26e-08 |
|
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: 56.46 E-value: 1.26e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 667 VKVTNMEFQYPGTsKPQITDINFQCSLSSRIAVIGPNGAGKSTLINVLTGELLPTSGEVY 726
Cdd:cd03254 3 IEFENVNFSYDEK-KPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQIL 61
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
674-741 |
1.36e-08 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 58.64 E-value: 1.36e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6323278 674 FQYPGtSKPQITDINFQCSLSSRIAVIGPNGAGKSTLINVLTGELLPTSGEV---------YTHENCR--IAYIKQHAF 741
Cdd:COG1132 347 FSYPG-DRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRIlidgvdirdLTLESLRrqIGVVPQDTF 424
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
433-569 |
1.59e-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: 56.39 E-value: 1.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 433 NCEFSLAYGAKILLNKTQLRLKRARRYGICGPNGCGKSTLMRAIAngQVDgFPTqeecrtvyvEHDIDGTHSDTSVLDFv 512
Cdd:cd03220 25 ILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLA--GIY-PPD---------SGTVTVRGRVSSLLGL- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 513 fesGVG--------------------TKEAIKDKLIEF-GFTD--EMIAMPISALSGGWKMKLALARAVLRNADILLLDE 569
Cdd:cd03220 92 ---GGGfnpeltgreniylngrllglSRKEIDEKIDEIiEFSElgDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDE 168
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
451-569 |
2.00e-08 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 56.24 E-value: 2.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 451 LRLKRARRYGICGPNGCGKSTLMRAIAngqvdG--FPTQEECRtvyvehdIDGTHSdtSVLDFvfesGVG---------- 518
Cdd:COG1134 47 FEVERGESVGIIGRNGAGKSTLLKLIA-----GilEPTSGRVE-------VNGRVS--ALLEL----GAGfhpeltgren 108
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6323278 519 ----------TKEAIKDKL---IEF---GftdEMIAMPISALSGGWKMKLALARAVLRNADILLLDE 569
Cdd:COG1134 109 iylngrllglSRKEIDEKFdeiVEFaelG---DFIDQPVKTYSSGMRARLAFAVATAVDPDILLVDE 172
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
461-610 |
2.16e-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: 2.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 461 ICGPNGCGKSTLMRAIANGQVDGFPTQeeCRTVYVEHDIDGTHSDTSVLDFVFESGVGTKEAIKDKLIEF--------GF 532
Cdd:cd03240 27 IVGQNGAGKTTIIEALKYALTGELPPN--SKGGAHDPKLIREGEVRAQVKLAFENANGKKYTITRSLAILenvifchqGE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 533 TDEMIAMPISALSGGWKMK------LALARAVLRNADILLLDEPTNHLDTVNVAW----LVNYLNTCGITS-ITISHDSV 601
Cdd:cd03240 105 SNWPLLDMRGRCSGGEKVLasliirLALAETFGSNCGILALDEPTTNLDEENIEEslaeIIEERKSQKNFQlIVITHDEE 184
|
....*....
gi 6323278 602 FLDNVCEYI 610
Cdd:cd03240 185 LVDAADHIY 193
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
457-604 |
2.21e-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: 54.30 E-value: 2.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 457 RRYGICGPNGCGKSTLMRAIANGqvdgfpTQEECRTVYVehdIDGTHSDTSVLDFVFESGVGTKEAikdkliefgftdem 536
Cdd:smart00382 3 EVILIVGPPGSGKTTLARALARE------LGPPGGGVIY---IDGEDILEEVLDQLLLIIVGGKKA-------------- 59
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6323278 537 iampisALSGGWKMKLALARAVLRNADILLLDEPTNHLDTVNVAWLV---------NYLNTCGITSITISHDSVFLD 604
Cdd:smart00382 60 ------SGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLlleelrlllLLKSEKNLTVILTTNDEKDLG 130
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
440-601 |
2.29e-08 |
|
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: 55.72 E-value: 2.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 440 YGAKILLNKTQLRLKRARRYGICGPNGCGKSTLMRAIAngqvdGFPTQEECRtVYVE----HDIDGTHSDT--------- 506
Cdd:cd03301 10 FGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIA-----GLEEPTSGR-IYIGgrdvTDLPPKDRDIamvfqnyal 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 507 ----SVLD---FVFESGVGTKEAIKDKLIEFGFT---DEMIAMPISALSGGWKMKLALARAVLRNADILLLDEPTNHLDT 576
Cdd:cd03301 84 yphmTVYDniaFGLKLRKVPKDEIDERVREVAELlqiEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDA 163
|
170 180
....*....|....*....|....*....
gi 6323278 577 -VNVAW---LVNYLNTCGITSITISHDSV 601
Cdd:cd03301 164 kLRVQMraeLKRLQQRLGTTTIYVTHDQV 192
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
444-598 |
2.78e-08 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 57.84 E-value: 2.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 444 ILLNKTQLRLKRARRYGICGPNGCGKSTLMRAIAN-----GQVDGFPtqEECRTVYVEHD---IDGTHSDT-----SVLD 510
Cdd:TIGR00954 466 VLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGElwpvyGGRLTKP--AKGKLFYVPQRpymTLGTLRDQiiypdSSED 543
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 511 FvFESGVGTKEAIK-------DKLIEFGFTDEMIAMPISALSGGWKMKLALARAVLRNADILLLDEPTNHLdTVNV-AWL 582
Cdd:TIGR00954 544 M-KRRGLSDKDLEQildnvqlTHILEREGGWSAVQDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAV-SVDVeGYM 621
|
170
....*....|....*.
gi 6323278 583 VNYLNTCGITSITISH 598
Cdd:TIGR00954 622 YRLCREFGITLFSVSH 637
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
666-970 |
3.01e-08 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 55.77 E-value: 3.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 666 IVKVTNMEFQYPGtSKPQITDINFQCSLSSRIAVIGPNGAGKSTLINVLTGELLPTSGEVYthencriayikqhafahie 745
Cdd:TIGR02315 1 MLEVENLSKVYPN-GKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSIL------------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 746 shldktpseyiqwrfqtgedretmdranrqinendaeamnkifkIEGTPRRIAGIHSRRKFKntyeyecsfllgENIGMK 825
Cdd:TIGR02315 61 --------------------------------------------LEGTDITKLRGKKLRKLR------------RRIGMI 84
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 826 SERW--VPMMSV-DNAWIPRgelveshskmvaeVDMKEALASGqFRPLTRKEIEEHCSML---GLDPEivSHSRIRGLSG 899
Cdd:TIGR02315 85 FQHYnlIERLTVlENVLHGR-------------LGYKPTWRSL-LGRFSEEDKERALSALervGLADK--AYQRADQLSG 148
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6323278 900 GQKVKLVLAAGTWQRPHLIVLDEPTNYLDRDS----LGALSKALKEFEGGVIIITHSAEFTKNLTEEVWAVKDGR 970
Cdd:TIGR02315 149 GQQQRVAIARALAQQPDLILADEPIASLDPKTskqvMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGE 223
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
440-575 |
3.04e-08 |
|
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: 55.45 E-value: 3.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 440 YGAKILLNKTQLRLKRARRYGICGPNGCGKSTLMRAIAN--------GQVDGFPTQEECRTVyvEHDIDGTHSDTSVLDF 511
Cdd:cd03265 10 YGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTllkptsgrATVAGHDVVREPREV--RRRIGIVFQDLSVDDE 87
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6323278 512 V--FES--------GVGTKEAIK--DKLIEFGFTDEMIAMPISALSGGWKMKLALARAVLRNADILLLDEPTNHLD 575
Cdd:cd03265 88 LtgWENlyiharlyGVPGAERREriDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLD 163
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
451-611 |
3.40e-08 |
|
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: 55.82 E-value: 3.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 451 LRLKRARRYGICGPNGCGKSTLMRAIA------------NGQ-VDGFPTQEECR----------------TVyVEHDIDG 501
Cdd:COG0411 25 LEVERGEIVGLIGPNGAGKTTLFNLITgfyrptsgrilfDGRdITGLPPHRIARlgiartfqnprlfpelTV-LENVLVA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 502 THS--DTSVLDFVFESGVGTKE--AIKDK---LIEF-GFTDEMiAMPISALSGGWKMKLALARAVLRNADILLLDEPT-- 571
Cdd:COG0411 104 AHArlGRGLLAALLRLPRARREerEARERaeeLLERvGLADRA-DEPAGNLSYGQQRRLEIARALATEPKLLLLDEPAag 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 6323278 572 -NHLDTVNVAWLVNYLN-TCGITSITISHD--SVFldNVCEYII 611
Cdd:COG0411 183 lNPEETEELAELIRRLRdERGITILLIEHDmdLVM--GLADRIV 224
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
435-598 |
3.53e-08 |
|
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: 57.44 E-value: 3.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 435 EFSLAYGAKILLNKTqLRLKRARRYGICGPNGCGKSTLMRAIAN------GQV--DGFPTQEECRTV------YVEHD-- 498
Cdd:TIGR01193 480 SYSYGYGSNILSDIS-LTIKMNSKTTIVGMSGSGKSTLAKLLVGffqarsGEIllNGFSLKDIDRHTlrqfinYLPQEpy 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 499 -IDGthsdtSVLD-FVFESGVGTKEAIKDKLIEFG-FTDEMIAMPI----------SALSGGWKMKLALARAVLRNADIL 565
Cdd:TIGR01193 559 iFSG-----SILEnLLLGAKENVSQDEIWAACEIAeIKDDIENMPLgyqtelseegSSISGGQKQRIALARALLTDSKVL 633
|
170 180 190
....*....|....*....|....*....|....
gi 6323278 566 LLDEPTNHLDTVNVAWLV-NYLNTCGITSITISH 598
Cdd:TIGR01193 634 ILDESTSNLDTITEKKIVnNLLNLQDKTIIFVAH 667
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
437-575 |
3.92e-08 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 55.51 E-value: 3.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 437 SLAYGAKILLNKTQLRLKRARRYGICGPNGCGKSTLMRAIA------------NGQ-VDGFPTQE--ECRTVYVEHdidg 501
Cdd:COG4559 8 SVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTgeltpssgevrlNGRpLAAWSPWElaRRRAVLPQH---- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 502 thsdtSVLDF---VFE------SGVGTKEAIKDKLIEfgftdEMIAM---------PISALSGGWKMKLALARA---VLR 560
Cdd:COG4559 84 -----SSLAFpftVEEvvalgrAPHGSSAAQDRQIVR-----EALALvglahlagrSYQTLSGGEQQRVQLARVlaqLWE 153
|
170
....*....|....*....
gi 6323278 561 NAD----ILLLDEPTNHLD 575
Cdd:COG4559 154 PVDggprWLFLDEPTSALD 172
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
677-743 |
4.00e-08 |
|
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: 54.48 E-value: 4.00e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6323278 677 PGTSKPQI-TDINFQCSLSSRIAVIGPNGAGKSTLINVLTGEL--LPTSGEVY-----THEN---CRIAYIKQHAFAH 743
Cdd:cd03213 17 PSKSGKQLlKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRtgLGVSGEVLingrpLDKRsfrKIIGYVPQDDILH 94
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
675-971 |
4.26e-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: 54.72 E-value: 4.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 675 QYPGTSkPQITDINFQCSLSSRIAVIGPNGAGKSTLINVLTGELLPTSGEVythencriayikqhafahieshldktpse 754
Cdd:cd03292 9 TYPNGT-AALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTI----------------------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 755 yiqwrfqtgedretmdranrqinendaeamnkifKIEGTPrrIAGIHSRRkfkntyeyecSFLLGENIGM--KSERWVPM 832
Cdd:cd03292 59 ----------------------------------RVNGQD--VSDLRGRA----------IPYLRRKIGVvfQDFRLLPD 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 833 MSV-DNAWIPRgelveshskMVAEVDMKEAlasgqfrpltRKEIEEHCSMLGLDPEivSHSRIRGLSGGQKVKLVLAAGT 911
Cdd:cd03292 93 RNVyENVAFAL---------EVTGVPPREI----------RKRVPAALELVGLSHK--HRALPAELSGGEQQRVAIARAI 151
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6323278 912 WQRPHLIVLDEPTNYLDRDSLGALSKALKEFEGG---VIIITHSAEFTKNLTEEVWAVKDGRM 971
Cdd:cd03292 152 VNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAgttVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
686-975 |
4.84e-08 |
|
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: 54.68 E-value: 4.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 686 DINFQCSLSSRIAVIGPNGAGKSTLINVLTGELLPTSGEvythencriayikqhafAHIESHldktpseyiqwrfqtged 765
Cdd:cd03265 18 GVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGR-----------------ATVAGH------------------ 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 766 retmdranrqinendaeamnKIFKIEGTPRRiagihsrrkfkntyeyecsfllgeNIGmkserWVP-MMSVDNAWIPRgE 844
Cdd:cd03265 63 --------------------DVVREPREVRR------------------------RIG-----IVFqDLSVDDELTGW-E 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 845 LVESHSKMvaevdmkealaSGQFRPLTRKEIEEHCSMLGLDPeiVSHSRIRGLSGGQKVKLVLAAGTWQRPHLIVLDEPT 924
Cdd:cd03265 93 NLYIHARL-----------YGVPGAERRERIDELLDFVGLLE--AADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPT 159
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 6323278 925 NYLD---RDSLGALSKALKEFEGGVIII-THSAEFTKNLTEEVWAVKDGRMTPSG 975
Cdd:cd03265 160 IGLDpqtRAHVWEYIEKLKEEFGMTILLtTHYMEEAEQLCDRVAIIDHGRIIAEG 214
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
666-975 |
5.38e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 55.47 E-value: 5.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 666 IVKVTNMEFQYP-GTSKpqITDINFQCSLSSRIAVIGPNGAGKSTLINVLTGELLPTSGEVYthencriayikqhafahi 744
Cdd:PRK13639 1 ILETRDLKYSYPdGTEA--LKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVL------------------ 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 745 eshLDKTPSEYiqwrfqtgedretmdranrqinenDAEAMNKIfkiegtpRRIAGIhsrrKFKNTyeyecsfllgenigm 824
Cdd:PRK13639 61 ---IKGEPIKY------------------------DKKSLLEV-------RKTVGI----VFQNP--------------- 87
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 825 KSERWVPMMSVDNAWiprGELVESHSKMVAEVDMKEALASgqfrpltrkeieehCSMLGLDPEIVSHsrirgLSGGQKVK 904
Cdd:PRK13639 88 DDQLFAPTVEEDVAF---GPLNLGLSKEEVEKRVKEALKA--------------VGMEGFENKPPHH-----LSGGQKKR 145
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6323278 905 LVLAAGTWQRPHLIVLDEPTNYLDRDSLGALSKALKEF--EGGVIII-THSAEFTKNLTEEVWAVKDGRMTPSG 975
Cdd:PRK13639 146 VAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLnkEGITIIIsTHDVDLVPVYADKVYVMSDGKIIKEG 219
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
463-599 |
5.84e-08 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 55.02 E-value: 5.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 463 GPNGCGKSTLMRA-------------IANGQVD--GFPTQEECRT-------VYVEHDIdGTHsdTSVLDFVFES----- 515
Cdd:PRK11124 35 GPSGAGKSSLLRVlnllemprsgtlnIAGNHFDfsKTPSDKAIRElrrnvgmVFQQYNL-WPH--LTVQQNLIEApcrvl 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 516 GVGTKEAIK--DKLIE-FGFTDEMIAMPISaLSGGWKMKLALARAVLRNADILLLDEPTNHLD---TVNVAWLVNYLNTC 589
Cdd:PRK11124 112 GLSKDQALAraEKLLErLRLKPYADRFPLH-LSGGQQQRVAIARALMMEPQVLLFDEPTAALDpeiTAQIVSIIRELAET 190
|
170
....*....|
gi 6323278 590 GITSITISHD 599
Cdd:PRK11124 191 GITQVIVTHE 200
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
686-725 |
6.52e-08 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 55.48 E-value: 6.52e-08
10 20 30 40
....*....|....*....|....*....|....*....|
gi 6323278 686 DINFQCSLSSRIAVIGPNGAGKSTLINVLTGELLPTSGEV 725
Cdd:COG4586 40 DISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEV 79
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
660-975 |
6.65e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 55.48 E-value: 6.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 660 KTKQKAIVKVTN----MEFQypgtskpQITDINFQCSLSSRIAVIGPNGAGKSTLINVLTGELLPTSGEV---YTHENcr 732
Cdd:PRK13651 2 QIKVKNIVKIFNkklpTELK-------ALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewiFKDEK-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 733 iayikqhafahieshlDKTPSEYIQWRFQTGEDRETMDRanrqinendaeamnKIFKIEGTPRRIAGIHS---RRKFKNT 809
Cdd:PRK13651 73 ----------------NKKKTKEKEKVLEKLVIQKTRFK--------------KIKKIKEIRRRVGVVFQfaeYQLFEQT 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 810 YEYECSFllgeniGMKSerwvpmMSVDNawiprgelveshskmvaevdmKEALAsgqfrpLTRKEIEehcsMLGLDPEIV 889
Cdd:PRK13651 123 IEKDIIF------GPVS------MGVSK---------------------EEAKK------RAAKYIE----LVGLDESYL 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 890 SHSRIrGLSGGQKVKLVLAAGTWQRPHLIVLDEPTNYLDRDSLGALSKALKE-FEGG--VIIITHSAEFTKNLTEEVWAV 966
Cdd:PRK13651 160 QRSPF-ELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNlNKQGktIILVTHDLDNVLEWTKRTIFF 238
|
....*....
gi 6323278 967 KDGRMTPSG 975
Cdd:PRK13651 239 KDGKIIKDG 247
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
665-971 |
1.25e-07 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 53.91 E-value: 1.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 665 AIVKVTNMEFQYPGtSKPQITDINFQCSLSSRIAVIGPNGAGKSTLINVLTGELLPTSGEVythencriayikqhafahi 744
Cdd:COG3638 1 PMLELRNLSKRYPG-GTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEI------------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 745 esHLDktpseyiqwrfqtgedretmdraNRQINENDAEAMNKIfkiegtPRRIAGIHSrrkfkntyeyecSFLLgenigm 824
Cdd:COG3638 61 --LVD-----------------------GQDVTALRGRALRRL------RRRIGMIFQ------------QFNL------ 91
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 825 kserwVPMMSV-DNAWIPR-GE--LVESHSKMVAEVDMKEALASgqfrpLTRKEIEEHCsmlgldpeivsHSRIRGLSGG 900
Cdd:COG3638 92 -----VPRLSVlTNVLAGRlGRtsTWRSLLGLFPPEDRERALEA-----LERVGLADKA-----------YQRADQLSGG 150
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6323278 901 QK--VKL--VLAagtwQRPHLIVLDEPTNYLD----RDSLGALSKALKEFEGGVIIITHSAEFTKNLTEEVWAVKDGRM 971
Cdd:COG3638 151 QQqrVAIarALV----QEPKLILADEPVASLDpktaRQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRV 225
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
438-580 |
1.30e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 54.15 E-value: 1.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 438 LAYGAKILLNKTQLRLKRARRYGICGPNGCGKSTLMR-----------AIANGQV--DG-----FPTQEECRTVYVEHDI 499
Cdd:PRK14247 11 VSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRvfnrlielypeARVSGEVylDGqdifkMDVIELRRRVQMVFQI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 500 DGTHSDTSV---------LDFVFESGVGTKEAIKDKLIEFGFTDEM---IAMPISALSGGWKMKLALARAVLRNADILLL 567
Cdd:PRK14247 91 PNPIPNLSIfenvalglkLNRLVKSKKELQERVRWALEKAQLWDEVkdrLDAPAGKLSGGQQQRLCIARALAFQPEVLLA 170
|
170
....*....|...
gi 6323278 568 DEPTNHLDTVNVA 580
Cdd:PRK14247 171 DEPTANLDPENTA 183
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
461-575 |
1.37e-07 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 53.84 E-value: 1.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 461 ICGPNGCGKSTLMRAIaNG--QVD-GfptqeecrTVYVEhDIDGTHSDTSVLD------FVFES---------------- 515
Cdd:COG1126 32 IIGPSGSGKSTLLRCI-NLleEPDsG--------TITVD-GEDLTDSKKDINKlrrkvgMVFQQfnlfphltvlenvtla 101
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6323278 516 -----GVGTKEAIKD--KLIE-FGFTDEMIAMPiSALSGGWKMKLALARAVLRNADILLLDEPTNHLD 575
Cdd:COG1126 102 pikvkKMSKAEAEERamELLErVGLADKADAYP-AQLSGGQQQRVAIARALAMEPKVMLFDEPTSALD 168
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
663-952 |
1.42e-07 |
|
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: 55.44 E-value: 1.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 663 QKAIVKVTNMEFQYPGtSKPQITDINFQCSLSSRIAVIGPNGAGKSTLINVLTGELLPTSGEVythencriayikqhafa 742
Cdd:TIGR02868 331 GKPTLELRDLSAGYPG-APPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEV----------------- 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 743 hieshldkTPSEYIQWRFQTGEDRetmdranrqinendaeamnkifkiegtpRRIAGIHSRrkfkntyeyecSFLLGENI 822
Cdd:TIGR02868 393 --------TLDGVPVSSLDQDEVR----------------------------RRVSVCAQD-----------AHLFDTTV 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 823 GmkserwvpmmsvDNAWIPRGElveshskmVAEVDMKEALASGQFRPLTRKEIEehcsmlGLDPEIVSHSRIrgLSGGQK 902
Cdd:TIGR02868 426 R------------ENLRLARPD--------ATDEELWAALERVGLADWLRALPD------GLDTVLGEGGAR--LSGGER 477
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 6323278 903 VKLVLAAGTWQRPHLIVLDEPTNYLD----RDSLGALSKALKEFegGVIIITHS 952
Cdd:TIGR02868 478 QRLALARALLADAPILLLDEPTEHLDaetaDELLEDLLAALSGR--TVVLITHH 529
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
451-575 |
1.44e-07 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 53.43 E-value: 1.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 451 LRLKRARRYGICGPNGCGKSTLMRAIAngqvdGF--PTQEECRtvyvehdIDG-THSDTSV----LDFVFES-------- 515
Cdd:PRK10771 20 LTVERGERVAILGPSGAGKSTLLNLIA-----GFltPASGSLT-------LNGqDHTTTPPsrrpVSMLFQEnnlfshlt 87
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6323278 516 -----GVG----------TKEAIKDKLIEFGFTDEMIAMPiSALSGGWKMKLALARAVLRNADILLLDEPTNHLD 575
Cdd:PRK10771 88 vaqniGLGlnpglklnaaQREKLHAIARQMGIEDLLARLP-GQLSGGQRQRVALARCLVREQPILLLDEPFSALD 161
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
647-725 |
1.44e-07 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 55.60 E-value: 1.44e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6323278 647 EFKFPEPgylEGVKTKQKAIvKVTNMEFQYPGTSKPQITDINFQCSLSSRIAVIGPNGAGKSTLINVLTGELLPTSGEV 725
Cdd:PRK11160 323 EVTFPTT---STAAADQVSL-TLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEI 397
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
439-599 |
1.49e-07 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 54.73 E-value: 1.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 439 AYGAKILLNKTQLRLKRARRYGICGPNGCGKSTLMRAIA------NGQVdgFptqeecrtvyvehdIDG---THSDTSVL 509
Cdd:PRK11432 15 RFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAglekptEGQI--F--------------IDGedvTHRSIQQR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 510 D--FVFES-------------GVG------TKEAIKDKLIEF-------GFTDEMiampISALSGGWKMKLALARAVLRN 561
Cdd:PRK11432 79 DicMVFQSyalfphmslgenvGYGlkmlgvPKEERKQRVKEAlelvdlaGFEDRY----VDQISGGQQQRVALARALILK 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 6323278 562 ADILLLDEPTNHLDT-------VNVAWLVNYLNtcgITSITISHD 599
Cdd:PRK11432 155 PKVLLFDEPLSNLDAnlrrsmrEKIRELQQQFN---ITSLYVTHD 196
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
459-599 |
1.54e-07 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 54.84 E-value: 1.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 459 YGICGPNGCGKSTLMRAIAngqvdGFPTQEECRTVYVEHDIDGTHSDTSVLDFVFESGVGTKEAIKDKLIEFGF------ 532
Cdd:PRK11607 48 FALLGASGCGKSTLLRMLA-----GFEQPTAGQIMLDGVDLSHVPPYQRPINMMFQSYALFPHMTVEQNIAFGLkqdklp 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 533 -------TDEMIAM----------PiSALSGGWKMKLALARAVLRNADILLLDEPTNHLDT-------VNVawlVNYLNT 588
Cdd:PRK11607 123 kaeiasrVNEMLGLvhmqefakrkP-HQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKklrdrmqLEV---VDILER 198
|
170
....*....|.
gi 6323278 589 CGITSITISHD 599
Cdd:PRK11607 199 VGVTCVMVTHD 209
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
697-726 |
1.56e-07 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 53.94 E-value: 1.56e-07
10 20 30
....*....|....*....|....*....|
gi 6323278 697 IAVIGPNGAGKSTLINVLTGELLPTSGEVY 726
Cdd:COG1101 35 VTVIGSNGAGKSTLLNAIAGSLPPDSGSIL 64
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
666-975 |
1.62e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 54.04 E-value: 1.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 666 IVKVTNMEFQYPGTSKPQITDINFQCSLSSRIAVIGPNGAGKSTLINVLTGELLPTsgevythencriayikqhafahie 745
Cdd:PRK13640 5 IVEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPD------------------------ 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 746 shldktpseyiqwrfqtgedretmDRANRQINENDAEAMNK-IFKIegtpRRIAGIhsrrKFKNTYEYECSFLLGENIGM 824
Cdd:PRK13640 61 ------------------------DNPNSKITVDGITLTAKtVWDI----REKVGI----VFQNPDNQFVGATVGDDVAF 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 825 KSErwvpmmsvdNAWIPRGELVESHSKMVAEVDMKEALASgqfrpltrkeieehcsmlglDPEivshsrirGLSGGQKVK 904
Cdd:PRK13640 109 GLE---------NRAVPRPEMIKIVRDVLADVGMLDYIDS--------------------EPA--------NLSGGQKQR 151
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6323278 905 LVLAAGTWQRPHLIVLDEPTNYLD---RDSLGALSKALKEFEGGVII-ITHSAEfTKNLTEEVWAVKDGRMTPSG 975
Cdd:PRK13640 152 VAIAGILAVEPKIIILDESTSMLDpagKEQILKLIRKLKKKNNLTVIsITHDID-EANMADQVLVLDDGKLLAQG 225
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
460-615 |
1.64e-07 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 52.19 E-value: 1.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 460 GICGPNGCGKSTLMRAIAnGQVDgfPTQEEcrtvyVEHDidgthsdtsvldfvfesgvGTKEAIKDKLIEfgftdemiam 539
Cdd:cd03222 29 GIVGPNGTGKTTAVKILA-GQLI--PNGDN-----DEWD-------------------GITPVYKPQYID---------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 540 pisaLSGGWKMKLALARAVLRNADILLLDEPTNHLDT---VNVAWLVNYLNTCGI-TSITISHDSVFLDNVCEYIINYEG 615
Cdd:cd03222 72 ----LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIeqrLNAARAIRRLSEEGKkTALVVEHDLAVLDYLSDRIHVFEG 147
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
433-598 |
1.73e-07 |
|
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: 53.38 E-value: 1.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 433 NCEFSLAYGAKILLNKTqLRLKRARRYGICGPNGCGKSTLMRAI------ANGQV--DGFPTQEECRTV------YVEHD 498
Cdd:cd03254 7 NVNFSYDEKKPVLKDIN-FSIKPGETVAIVGPTGAGKTTLINLLmrfydpQKGQIliDGIDIRDISRKSlrsmigVVLQD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 499 iDGTHSDTSVLDFVFESGVGTKEAIKDKLIEFGFTDEMIAMPI----------SALSGGWKMKLALARAVLRNADILLLD 568
Cdd:cd03254 86 -TFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNgydtvlgengGNLSQGERQLLAIARAMLRDPKILILD 164
|
170 180 190
....*....|....*....|....*....|..
gi 6323278 569 EPTNHLDTVNVAWLVNYLNTC--GITSITISH 598
Cdd:cd03254 165 EATSNIDTETEKLIQEALEKLmkGRTSIIIAH 196
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
673-975 |
1.79e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 53.87 E-value: 1.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 673 EFQY-PGT--SKPQITDINFQCSLSSRIAVIGPNGAGKSTLINVLTGELLPTSGEVythencriayikqhafahieshld 749
Cdd:PRK13634 9 EHRYqYKTpfERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTV------------------------ 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 750 ktpseyiqwrfQTGEdretmdranRQINendAEAMNKIFKiegTPRRIAGI------HsrRKFKNTYEYECSFllG-ENI 822
Cdd:PRK13634 65 -----------TIGE---------RVIT---AGKKNKKLK---PLRKKVGIvfqfpeH--QLFEETVEKDICF--GpMNF 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 823 GMKSERwvpmmsvdnawiprgelveshskmvAEVDMKEALAsgqfrpltrkeieehcsMLGLDPEIVSHSRIRgLSGGQK 902
Cdd:PRK13634 115 GVSEED-------------------------AKQKAREMIE-----------------LVGLPEELLARSPFE-LSGGQM 151
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6323278 903 VKLVLAAGTWQRPHLIVLDEPTNYLD----RDSLGALSKALKEFEGGVIIITHSAEFTKNLTEEVWAVKDGRMTPSG 975
Cdd:PRK13634 152 RRVAIAGVLAMEPEVLVLDEPTAGLDpkgrKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQG 228
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
698-726 |
2.02e-07 |
|
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: 51.66 E-value: 2.02e-07
10 20
....*....|....*....|....*....
gi 6323278 698 AVIGPNGAGKSTLINVLTGELLPTSGEVY 726
Cdd:cd03216 30 ALLGENGAGKSTLMKILSGLYKPDSGEIL 58
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
461-604 |
2.26e-07 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 52.65 E-value: 2.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 461 ICGPNGCGKSTLMRAIANgqvdgfptQEECRTVYVEHDIDGTH--SDTSVLDfvfesGVGTKEAIKDKLiefgftdEMIA 538
Cdd:COG2401 61 IVGASGSGKSTLLRLLAG--------ALKGTPVAGCVDVPDNQfgREASLID-----AIGRKGDFKDAV-------ELLN 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 539 M-----------PISALSGGWKMKLALARAVLRNADILLLDEPTNHLDTVnVAWLVNY-----LNTCGITSITISHDSVF 602
Cdd:COG2401 121 AvglsdavlwlrRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQ-TAKRVARnlqklARRAGITLVVATHHYDV 199
|
..
gi 6323278 603 LD 604
Cdd:COG2401 200 ID 201
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
544-575 |
2.34e-07 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 54.83 E-value: 2.34e-07
10 20 30
....*....|....*....|....*....|..
gi 6323278 544 LSGGWKMKLALARAVLRNADILLLDEPTNHLD 575
Cdd:PRK11160 476 LSGGEQRRLGIARALLHDAPLLLLDEPTEGLD 507
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
698-951 |
2.42e-07 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 54.65 E-value: 2.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 698 AVIGPNGAGKSTLINVLTGELLPTSGEVYthencriayikqhafahieshldktpseyiqwrfqtgedretmdranrqin 777
Cdd:COG3845 35 ALLGENGAGKSTLMKILYGLYQPDSGEIL--------------------------------------------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 778 endaeamnkifkIEGTPRRIAG-IHSRRkfkntyeyecsflLGenIGMkserwV---PMmsvdnawiprgeLVESHSkmV 853
Cdd:COG3845 64 ------------IDGKPVRIRSpRDAIA-------------LG--IGM-----VhqhFM------------LVPNLT--V 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 854 AE-------------VDMKEAlasgqfrpltRKEIEEHCSMLGL--DPeivsHSRIRGLSGG--QKVKLVLAagTWQRPH 916
Cdd:COG3845 98 AEnivlgleptkggrLDRKAA----------RARIRELSERYGLdvDP----DAKVEDLSVGeqQRVEILKA--LYRGAR 161
|
250 260 270
....*....|....*....|....*....|....*....
gi 6323278 917 LIVLDEPTNYL---DRDSLGALSKALKEfEG-GVIIITH 951
Cdd:COG3845 162 ILILDEPTAVLtpqEADELFEILRRLAA-EGkSIIFITH 199
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
698-975 |
2.79e-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: 52.65 E-value: 2.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 698 AVIGPNGAGKSTLINVLTGellptsgevytHENCRIAYikqhafAHIeshldktpseyiqwRFQtGEDRETMdranrqin 777
Cdd:TIGR01978 30 AIMGPNGSGKSTLSKTIAG-----------HPSYEVTS------GTI--------------LFK-GQDLLEL-------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 778 ENDAEAMNKIFKIEGTPRRIAGIHSRRkfkntyeyecsFLlgenigmkserwvpmMSVDNAwiprgelveshskmVAEVD 857
Cdd:TIGR01978 70 EPDERARAGLFLAFQYPEEIPGVSNLE-----------FL---------------RSALNA--------------RRSAR 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 858 MKEALASGQFRPLTRKEIEehcsMLGLDPEIVSHSRIRGLSGGQKVKLVLaagtWQ----RPHLIVLDEPTNYLDRDSLG 933
Cdd:TIGR01978 110 GEEPLDLLDFEKLLKEKLA----LLDMDEEFLNRSVNEGFSGGEKKRNEI----LQmallEPKLAILDEIDSGLDIDALK 181
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 6323278 934 ALSK---ALKEFEGGVIIITHSAEFTKNLTEE-VWAVKDGRMTPSG 975
Cdd:TIGR01978 182 IVAEginRLREPDRSFLIITHYQRLLNYIKPDyVHVLLDGRIVKSG 227
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
542-577 |
3.04e-07 |
|
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: 52.62 E-value: 3.04e-07
10 20 30
....*....|....*....|....*....|....*.
gi 6323278 542 SALSGGWKMKLALARAVLRNADILLLDEPTNHLDTV 577
Cdd:cd03251 137 VKLSGGQRQRIAIARALLKDPPILILDEATSALDTE 172
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
463-599 |
3.39e-07 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 52.63 E-value: 3.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 463 GPNGCGKSTLMRAIA-----------NGQ-VDGFPTQEECR---------------TV--YVE-HDIDGTHSD--TSVLD 510
Cdd:PRK03695 29 GPNGAGKSTLLARMAgllpgsgsiqfAGQpLEAWSAAELARhraylsqqqtppfamPVfqYLTlHQPDKTRTEavASALN 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 511 FVFESgVGtkeaIKDKLiefgftdemiAMPISALSGG-WKmKLALARAVLR-------NADILLLDEPTNHLDTVNVAWL 582
Cdd:PRK03695 109 EVAEA-LG----LDDKL----------GRSVNQLSGGeWQ-RVRLAAVVLQvwpdinpAGQLLLLDEPMNSLDVAQQAAL 172
|
170 180
....*....|....*....|
gi 6323278 583 ---VNYLNTCGITSITISHD 599
Cdd:PRK03695 173 drlLSELCQQGIAVVMSSHD 192
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
872-976 |
3.72e-07 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 52.63 E-value: 3.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 872 RKEIEEHCSMLGLDPEIvsHSRIRGLSGG--QKVKLvlaAGT----WQR--PH--LIVLDEPTNYLDRDSLGALSKALKE 941
Cdd:PRK03695 104 ASALNEVAEALGLDDKL--GRSVNQLSGGewQRVRL---AAVvlqvWPDinPAgqLLLLDEPMNSLDVAQQAALDRLLSE 178
|
90 100 110
....*....|....*....|....*....|....*...
gi 6323278 942 FE---GGVIIITHSAEFTKNLTEEVWAVKDGRMTPSGH 976
Cdd:PRK03695 179 LCqqgIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGR 216
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
461-599 |
4.00e-07 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 52.71 E-value: 4.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 461 ICGPNGCGKSTLMRAIaNG---------QVDGFPTQEEcrTVY--------VEHDIDGTHSDTSVLD---FVFE-SGVGT 519
Cdd:PRK13635 38 IVGHNGSGKSTLAKLL-NGlllpeagtiTVGGMVLSEE--TVWdvrrqvgmVFQNPDNQFVGATVQDdvaFGLEnIGVPR 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 520 KEAIK---DKLIEFGFTDEMIAMPiSALSGGWKMKLALARAVLRNADILLLDEPTNHLDT---VNVAWLVNYLN-TCGIT 592
Cdd:PRK13635 115 EEMVErvdQALRQVGMEDFLNREP-HRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPrgrREVLETVRQLKeQKGIT 193
|
....*..
gi 6323278 593 SITISHD 599
Cdd:PRK13635 194 VLSITHD 200
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
698-726 |
4.24e-07 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 52.43 E-value: 4.24e-07
10 20
....*....|....*....|....*....
gi 6323278 698 AVIGPNGAGKSTLINVLTGELLPTSGEVY 726
Cdd:COG4674 40 VIIGPNGAGKTTLMDVITGKTRPDSGSVL 68
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
667-739 |
4.27e-07 |
|
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: 52.09 E-value: 4.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 667 VKVTNMEFQYPGTSKPQ--ITDINFQCSLSSRIAVIGPNGAGKSTLINVLTGELLPTSGEVY------THENCRIAYIKQ 738
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVtaLEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLvdgepvTGPGPDRGYVFQ 80
|
.
gi 6323278 739 H 739
Cdd:cd03293 81 Q 81
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
451-570 |
4.37e-07 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 52.06 E-value: 4.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 451 LRLKRARRYGICGPNGCGKSTLMRAIAngqvdGFPTQEECRTVYVEHDIDGTHSDT---SVLdF----------VFES-G 516
Cdd:COG3840 20 LTIAAGERVAILGPSGAGKSTLLNLIA-----GFLPPDSGRILWNGQDLTALPPAErpvSML-FqennlfphltVAQNiG 93
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6323278 517 VG----------TKEAIKDKLIEFGFTDEMIAMPiSALSGGWKMKLALARAVLRNADILLLDEP 570
Cdd:COG3840 94 LGlrpglkltaeQRAQVEQALERVGLAGLLDRLP-GQLSGGQRQRVALARCLVRKRPILLLDEP 156
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
667-975 |
4.55e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 52.74 E-value: 4.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 667 VKVTNMEFQY-PGT--SKPQITDINFQCSLSSRIAVIGPNGAGKSTLINVLTGELLPTSGEVYthencriayikqhafah 743
Cdd:PRK13637 3 IKIENLTHIYmEGTpfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKII----------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 744 ieshldktpseyiqwrfqtgedretmdranrqinendaeamnkIFKIEGTPRRIAGIHSRRKFKNTYEYECSFLLGENIg 823
Cdd:PRK13637 66 -------------------------------------------IDGVDITDKKVKLSDIRKKVGLVFQYPEYQLFEETI- 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 824 mkserwvpmmSVDNAWIPRgELVESHSKMVAEVdmKEALAsgqfrpltrkeieehcsMLGLDPEIVSHSRIRGLSGGQKV 903
Cdd:PRK13637 102 ----------EKDIAFGPI-NLGLSEEEIENRV--KRAMN-----------------IVGLDYEDYKDKSPFELSGGQKR 151
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6323278 904 KLVLAAGTWQRPHLIVLDEPTNYLD---RDSLGALSKAL-KEFEGGVIIITHSAEFTKNLTEEVWAVKDGRMTPSG 975
Cdd:PRK13637 152 RVAIAGVVAMEPKILILDEPTAGLDpkgRDEILNKIKELhKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQG 227
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
668-725 |
4.75e-07 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 52.06 E-value: 4.75e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 6323278 668 KVTNMEFQYPGtskpQITDINFQCSLSSRIAVIGPNGAGKSTLINVLTGELLPTSGEV 725
Cdd:COG3840 3 RLDDLTYRYGD----FPLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRI 56
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
664-954 |
5.22e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 52.40 E-value: 5.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 664 KAIVKVTNMEFQY----PGTSKPQITDINFQCSLSSRIAVIGPNGAGKSTLINVLTGELLPTSGEVYThencriayikqh 739
Cdd:PRK13633 2 NEMIKCKNVSYKYesneESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYV------------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 740 afahieshldktpseyiqwrfqtgEDRETMDranrqinendaeaMNKIFKIegtpRRIAGIhsrrKFKNTYEYECSFLLG 819
Cdd:PRK13633 70 ------------------------DGLDTSD-------------EENLWDI----RNKAGM----VFQNPDNQIVATIVE 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 820 ENIGMKSErwvpmmsvdNAWIPRGELVESHSKMVAEVDMKEalasgqFRpltrkeieEHCSMLgldpeivshsrirgLSG 899
Cdd:PRK13633 105 EDVAFGPE---------NLGIPPEEIRERVDESLKKVGMYE------YR--------RHAPHL--------------LSG 147
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 6323278 900 GQKVKLVLAAGTWQRPHLIVLDEPTNYLD----RDSLGALSKALKEFEGGVIIITHSAE 954
Cdd:PRK13633 148 GQKQRVAIAGILAMRPECIIFDEPTAMLDpsgrREVVNTIKELNKKYGITIILITHYME 206
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
443-610 |
5.59e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 51.97 E-value: 5.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 443 KILLNKTQLRLKRARRYGICGPNGCGKSTLMRAI------------ANG----------QVDGFPTQEECRTVYVEHDID 500
Cdd:PRK14246 23 KAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLnrlieiydskikVDGkvlyfgkdifQIDAIKLRKEVGMVFQQPNPF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 501 GTHSDTSVLDFVFES-GVGTKEAIK----DKLIEFGFTDEM---IAMPISALSGGWKMKLALARAVLRNADILLLDEPTN 572
Cdd:PRK14246 103 PHLSIYDNIAYPLKShGIKEKREIKkiveECLRKVGLWKEVydrLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTS 182
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 6323278 573 HLDTVN---VAWLVNYLNTcGITSITISHDSVFLDNVCEYI 610
Cdd:PRK14246 183 MIDIVNsqaIEKLITELKN-EIAIVIVSHNPQQVARVADYV 222
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
460-599 |
5.98e-07 |
|
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: 52.81 E-value: 5.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 460 GICGPNGCGKSTLMRAIA------------NGQV--DG----FPTQEECRTVYVEHDID-GTH-SDTSVLDF-VFESGVG 518
Cdd:TIGR02142 27 AIFGRSGSGKTTLIRLIAgltrpdegeivlNGRTlfDSrkgiFLPPEKRRIGYVFQEARlFPHlSVRGNLRYgMKRARPS 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 519 TKEAIKDKLIEFGFTDEMIAMPISALSGGWKMKLALARAVLRNADILLLDEPTNHLDTVNVAWLVNYLNTC----GITSI 594
Cdd:TIGR02142 107 ERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPYLERLhaefGIPIL 186
|
....*
gi 6323278 595 TISHD 599
Cdd:TIGR02142 187 YVSHS 191
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
463-571 |
6.79e-07 |
|
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: 51.52 E-value: 6.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 463 GPNGCGKSTLMRAIA------------NGQ-VDGFPTQEECR----------------TV--------YVEHDIDGTHSD 505
Cdd:COG0410 36 GRNGAGKTTLLKAISgllpprsgsirfDGEdITGLPPHRIARlgigyvpegrrifpslTVeenlllgaYARRDRAEVRAD 115
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6323278 506 tsvLDFVFESgvgtkeaikdkliefgFTD--EMIAMPISALSGGWKMKLALARAVLRNADILLLDEPT 571
Cdd:COG0410 116 ---LERVYEL----------------FPRlkERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPS 164
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
460-606 |
7.24e-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: 53.21 E-value: 7.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 460 GICGPNGCGKSTLMRAI------ANGQV--DGfptqeecrtvyveHDID-------GTH-----SDTSVLDfvfesgvGT 519
Cdd:COG4618 362 GVIGPSGSGKSTLARLLvgvwppTAGSVrlDG-------------ADLSqwdreelGRHigylpQDVELFD-------GT 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 520 keaIKDKLIEFGFTD--------------EMIA-MP------I----SALSGGWKMKLALARAVLRNADILLLDEPTNHL 574
Cdd:COG4618 422 ---IAENIARFGDADpekvvaaaklagvhEMILrLPdgydtrIgeggARLSGGQRQRIGLARALYGDPRLVVLDEPNSNL 498
|
170 180 190
....*....|....*....|....*....|....*
gi 6323278 575 DTVNVAWLVN---YLNTCGITSITISHDSVFLDNV 606
Cdd:COG4618 499 DDEGEAALAAairALKARGATVVVITHRPSLLAAV 533
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
666-726 |
7.47e-07 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 51.21 E-value: 7.47e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6323278 666 IVKVTNMEFQYPGtSKPQITDINFqcslssRIA------VIGPNGAGKSTLINVLTGELLPTSGEVY 726
Cdd:COG2884 1 MIRFENVSKRYPG-GREALSDVSL------EIEkgefvfLTGPSGAGKSTLLKLLYGEERPTSGQVL 60
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
437-575 |
7.77e-07 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 51.70 E-value: 7.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 437 SLAYGAKILLNKTQLRLKRARRYGICGPNGCGKSTLMRAIA------------NGQ-VDGFPTQE--ECRTVYVEHdidg 501
Cdd:PRK13548 9 SVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSgelspdsgevrlNGRpLADWSPAElaRRRAVLPQH---- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 502 thsdtSVLDFVF--------------ESGVGTKEAIKDKLIEFGFTDeMIAMPISALSGGWKMKLALAR--AVLRNAD-- 563
Cdd:PRK13548 85 -----SSLSFPFtveevvamgraphgLSRAEDDALVAAALAQVDLAH-LAGRDYPQLSGGEQQRVQLARvlAQLWEPDgp 158
|
170
....*....|....
gi 6323278 564 --ILLLDEPTNHLD 575
Cdd:PRK13548 159 prWLLLDEPTSALD 172
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
450-608 |
8.79e-07 |
|
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: 52.88 E-value: 8.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 450 QLRLKRARRYGICGPNGCGKSTLMRAIA------NGQVD-------------------------GFPTQEecRTVYVEHD 498
Cdd:TIGR03269 304 SLEVKEGEIFGIVGTSGAGKTTLSKIIAgvleptSGEVNvrvgdewvdmtkpgpdgrgrakryiGILHQE--YDLYPHRT 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 499 IDGTHSDTSVLDFVFESGVgTKEAIKDKLIefGFTDE-----MIAMPiSALSGGWKMKLALARAVLRNADILLLDEPTNH 573
Cdd:TIGR03269 382 VLDNLTEAIGLELPDELAR-MKAVITLKMV--GFDEEkaeeiLDKYP-DELSEGERHRVALAQVLIKEPRIVILDEPTGT 457
|
170 180 190
....*....|....*....|....*....|....*....
gi 6323278 574 LD---TVNVA-WLVNYLNTCGITSITISHDSVFLDNVCE 608
Cdd:TIGR03269 458 MDpitKVDVThSILKAREEMEQTFIIVSHDMDFVLDVCD 496
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
684-971 |
9.30e-07 |
|
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: 50.74 E-value: 9.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 684 ITDINFQCSLSSRIAVIGPNGAGKSTLINVLTGELLPTSGEVYThENCRIAYIKQHAFAHIeshldktPseyiqwrfqtg 763
Cdd:cd03269 16 LDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLF-DGKPLDIAARNRIGYL-------P----------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 764 EDRetmdranrqinendaeamnkifkiegtprriaGIHSRRKFKNTYEYecsflLGENIGMKSErwvpmmsvdnawiprg 843
Cdd:cd03269 77 EER--------------------------------GLYPKMKVIDQLVY-----LAQLKGLKKE---------------- 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 844 elveshskmvaevdmkEAlasgqfrpltRKEIEEHCSMLGLDPEivSHSRIRGLSGGQKVKLVLAAGTWQRPHLIVLDEP 923
Cdd:cd03269 104 ----------------EA----------RRRIDEWLERLELSEY--ANKRVEELSKGNQQKVQFIAAVIHDPELLILDEP 155
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 6323278 924 TNYLD---RDSLGALSKALKEFEGGVIIITHSAEFTKNLTEEVWAVKDGRM 971
Cdd:cd03269 156 FSGLDpvnVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRA 206
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
698-971 |
9.83e-07 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 52.71 E-value: 9.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 698 AVIGPNGAGKSTLINVLTGELLPTSGEVYthencriayikqhafahieshldktpseyiqwrfqtgedretmdranrqin 777
Cdd:COG1129 34 ALLGENGAGKSTLMKILSGVYQPDSGEIL--------------------------------------------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 778 endaeamnkifkIEGTPRRIAGIHSRRKfkntyeyecsflLGenIGMkserwV-------PMMSV-DNAWIPRgelvESH 849
Cdd:COG1129 63 ------------LDGEPVRFRSPRDAQA------------AG--IAI-----IhqelnlvPNLSVaENIFLGR----EPR 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 850 SKMVaeVDMKEalasgqfrplTRKEIEEHCSMLGL--DPeivsHSRIRGLSGGQKvKLV-LAAGTWQRPHLIVLDEPTNY 926
Cdd:COG1129 108 RGGL--IDWRA----------MRRRARELLARLGLdiDP----DTPVGDLSVAQQ-QLVeIARALSRDARVLILDEPTAS 170
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 6323278 927 LDR---DSLGALSKALKEfEG-GVIIITHsaeftkNLtEEVWAV-------KDGRM 971
Cdd:COG1129 171 LTErevERLFRIIRRLKA-QGvAIIYISH------RL-DEVFEIadrvtvlRDGRL 218
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
451-578 |
1.00e-06 |
|
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: 50.90 E-value: 1.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 451 LRLKRARRYGICGPNGCGKSTLMRAIA------NGQV--DGfptqeecrtvyveHDIDGthsdtsvLD------------ 510
Cdd:COG4181 33 LEVEAGESVAIVGASGSGKSTLLGLLAgldrptSGTVrlAG-------------QDLFA-------LDedararlrarhv 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 511 -FVFESG------------------VGTKEAIK---DKLIEFGFTDEMIAMPiSALSGGWKMKLALARAVLRNADILLLD 568
Cdd:COG4181 93 gFVFQSFqllptltalenvmlplelAGRRDARArarALLERVGLGHRLDHYP-AQLSGGEQQRVALARAFATEPAILFAD 171
|
170
....*....|
gi 6323278 569 EPTNHLDTVN 578
Cdd:COG4181 172 EPTGNLDAAT 181
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
460-575 |
1.01e-06 |
|
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: 50.97 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 460 GICGPNGCGKSTLMRAIAN------GQ--VDGFPTQEECRTVYVE------HDIdgTHSDTSVLDFVF-------ESGVG 518
Cdd:cd03263 32 GLLGHNGAGKTTTLKMLTGelrptsGTayINGYSIRTDRKAARQSlgycpqFDA--LFDELTVREHLRfyarlkgLPKSE 109
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 6323278 519 TKEAIKDKLIEFGFTDEMIAmPISALSGGWKMKLALARAVLRNADILLLDEPTNHLD 575
Cdd:cd03263 110 IKEEVELLLRVLGLTDKANK-RARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLD 165
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
463-595 |
1.08e-06 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 50.62 E-value: 1.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 463 GPNGCGKSTLMRAIA------NGQV--DGFPTQEECRT---VYVEHdIDGTHSDTSVLDFV-FESGVGTKEAIK---DKL 527
Cdd:PRK13543 44 GDNGAGKTTLLRVLAgllhveSGQIqiDGKTATRGDRSrfmAYLGH-LPGLKADLSTLENLhFLCGLHGRRAKQmpgSAL 122
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6323278 528 IEFGFTDEMIAMpISALSGGWKMKLALARAVLRNADILLLDEPTNHLDTVNVAwLVN-----YLNTCGITSIT 595
Cdd:PRK13543 123 AIVGLAGYEDTL-VRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGIT-LVNrmisaHLRGGGAALVT 193
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
463-575 |
1.13e-06 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 51.40 E-value: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 463 GPNGCGKSTLMRAIAngqvdGFPTQEECRTVYVEHDIDGTHSDTSVldfVFEsgvgtkeaiKDKL---------IEFGFT 533
Cdd:COG4525 40 GASGCGKTTLLNLIA-----GFLAPSSGEITLDGVPVTGPGADRGV---VFQ---------KDALlpwlnvldnVAFGLR 102
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6323278 534 -------------DEMIAM---------PISALSGGWKMKLALARAVLRNADILLLDEPTNHLD 575
Cdd:COG4525 103 lrgvpkaerraraEELLALvgladfarrRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALD 166
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
516-609 |
1.16e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 51.63 E-value: 1.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 516 GVGTKEAIK--DKLIEfgftdeMIAMPIS-------ALSGGWKMKLALARAVLRNADILLLDEPTNHLDTVNVAWLVN-- 584
Cdd:PRK13651 135 GVSKEEAKKraAKYIE------LVGLDESylqrspfELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEif 208
|
90 100
....*....|....*....|....*.
gi 6323278 585 -YLNTCGITSITISHDsvfLDNVCEY 609
Cdd:PRK13651 209 dNLNKQGKTIILVTHD---LDNVLEW 231
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
666-963 |
1.24e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 51.29 E-value: 1.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 666 IVKVTNMEFQYPGTSKPQITDINFQCSLSSRIAVIGPNGAGKSTLINVLTGELLPTSGEVYTHENCriayIKQHAFAHIE 745
Cdd:PRK13648 7 IIVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQA----ITDDNFEKLR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 746 SHldktpseyIQWRFQTGEDretmdranrqinendaeamnkifkiegtprRIAGihsrrkfkNTYEYECSFLLgenigmk 825
Cdd:PRK13648 83 KH--------IGIVFQNPDN------------------------------QFVG--------SIVKYDVAFGL------- 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 826 serwvpmmsvDNAWIPRGELVESHSKMVAEVDMkealasgqfrpLTRKEIEEHcsmlgldpeivshsrirGLSGGQKVKL 905
Cdd:PRK13648 110 ----------ENHAVPYDEMHRRVSEALKQVDM-----------LERADYEPN-----------------ALSGGQKQRV 151
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6323278 906 VLAAGTWQRPHLIVLDEPTNYLD---RDSLGALSKALKEFEGGVII-ITHsaeftkNLTEEV 963
Cdd:PRK13648 152 AIAGVLALNPSVIILDEATSMLDpdaRQNLLDLVRKVKSEHNITIIsITH------DLSEAM 207
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
823-950 |
1.29e-06 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 52.36 E-value: 1.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 823 GMKSERWvpMMSVDNAWIPRGEL------VESHSKMVAEVDMKEALASGQfrplTRKEIEEHCSMLGL----DPEIVSHS 892
Cdd:TIGR00955 89 GMPIDAK--EMRAISAYVQQDDLfiptltVREHLMFQAHLRMPRRVTKKE----KRERVDEVLQALGLrkcaNTRIGVPG 162
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 6323278 893 RIRGLSGGQKVKLVLAAGTWQRPHLIVLDEPTNYLDRDSLGALSKALKEF-EGGVIIIT 950
Cdd:TIGR00955 163 RVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLaQKGKTIIC 221
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
684-759 |
1.50e-06 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 50.88 E-value: 1.50e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6323278 684 ITDINFQCSLSSRIAVIGPNGAGKSTLINVLTGELLPTSGEVYTHENCRIAYIKQHafAHIESHLDKTPSEYIQWR 759
Cdd:PRK09544 20 LSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQK--LYLDTTLPLTVNRFLRLR 93
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
435-599 |
1.57e-06 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 50.26 E-value: 1.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 435 EFSLAY-GAKILLNKTQLRLKRARRYGICGPNGCGKSTLMRAIAngqvdGFPTQEECRTVYVEHDIDGTHS--------- 504
Cdd:PRK10908 6 HVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLIC-----GIERPSAGKIWFSGHDITRLKNrevpflrrq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 505 ------------DTSVLDFVF-------ESGVGTKEAIKDKLIEFGFTDEMIAMPISaLSGGWKMKLALARAVLRNADIL 565
Cdd:PRK10908 81 igmifqdhhllmDRTVYDNVAipliiagASGDDIRRRVSAALDKVGLLDKAKNFPIQ-LSGGEQQRVGIARAVVNKPAVL 159
|
170 180 190
....*....|....*....|....*....|....*..
gi 6323278 566 LLDEPTNHLD---TVNVAWLVNYLNTCGITSITISHD 599
Cdd:PRK10908 160 LADEPTGNLDdalSEGILRLFEEFNRVGVTVLMATHD 196
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
437-577 |
1.66e-06 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 50.94 E-value: 1.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 437 SLAYGAKILLNKTQLRLKRARRYGICGPNGCGKSTLMRAI--ANGQVDGFptQEECRTVYVEHDIDGTHSDTSVL----D 510
Cdd:PRK14243 17 NVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFnrLNDLIPGF--RVEGKVTFHGKNLYAPDVDPVEVrrriG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 511 FVFESGVGTKEAIKDKlIEFGF--------TDEMIAMPI-----------------SALSGGWKMKLALARAVLRNADIL 565
Cdd:PRK14243 95 MVFQKPNPFPKSIYDN-IAYGAringykgdMDELVERSLrqaalwdevkdklkqsgLSLSGGQQQRLCIARAIAVQPEVI 173
|
170
....*....|..
gi 6323278 566 LLDEPTNHLDTV 577
Cdd:PRK14243 174 LMDEPCSALDPI 185
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
446-611 |
1.68e-06 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 50.78 E-value: 1.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 446 LNKTQLRLKRARRYGICGPNGCGKSTLMRAIAnGQVDGFPTQEE-----CRTVYVE----HDIDGTHSDT---------- 506
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLS-GLITGDKSAGShiellGRTVQREgrlaRDIRKSRANTgyifqqfnlv 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 507 ---SVLDFVFESGVGTKEAIKDKLIEFGFTDEMIAMP--------------ISALSGGWKMKLALARAVLRNADILLLDE 569
Cdd:PRK09984 99 nrlSVLENVLIGALGSTPFWRTCFSWFTREQKQRALQaltrvgmvhfahqrVSTLSGGQQQRVAIARALMQQAKVILADE 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 6323278 570 PTNHLDTVNVAWLVNYL----NTCGITSITISHDSVFLDNVCEYII 611
Cdd:PRK09984 179 PIASLDPESARIVMDTLrdinQNDGITVVVTLHQVDYALRYCERIV 224
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
868-971 |
1.74e-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: 50.41 E-value: 1.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 868 RPLTRKEIEEH----CSMLGLDPeiVSHSRIRGLSGGQKVKLVLAAGTWQRPHLIVLDEPTNYLDRDSLGA----LSKAL 939
Cdd:cd03299 99 RKVDKKEIERKvleiAEMLGIDH--LLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKlreeLKKIR 176
|
90 100 110
....*....|....*....|....*....|..
gi 6323278 940 KEFEGGVIIITHSAEFTKNLTEEVWAVKDGRM 971
Cdd:cd03299 177 KEFGVTVLHVTHDFEEAWALADKVAIMLNGKL 208
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
534-576 |
1.77e-06 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 51.94 E-value: 1.77e-06
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 6323278 534 DEMIAMPISALSGGWKMKLALARAVLRNADILLLDEPTNHLDT 576
Cdd:PRK11176 471 DTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDT 513
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
542-576 |
2.01e-06 |
|
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: 51.64 E-value: 2.01e-06
10 20 30
....*....|....*....|....*....|....*
gi 6323278 542 SALSGGWKMKLALARAVLRNADILLLDEPTNHLDT 576
Cdd:TIGR02203 468 VLLSGGQRQRLAIARALLKDAPILILDEATSALDN 502
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
667-725 |
2.07e-06 |
|
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: 49.92 E-value: 2.07e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 6323278 667 VKVTNMEFQYPGTSKPQITDINFQCSLSSRIAVIGPNGAGKSTLINVLTGELLPTSGEV 725
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRI 59
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
434-599 |
2.29e-06 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 50.53 E-value: 2.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 434 CEFSLAYGAKILLNKTQLRLKRARRYGICGPNGCGKSTLMRAIAnGQV-----------DGFPTQEECRTVYVEHDID-- 500
Cdd:PRK11831 11 RGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIG-GQIapdhgeilfdgENIPAMSRSRLYTVRKRMSml 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 501 ----GTHSDTSVLDFV--------------FESGVGTK-EAIkdkliefGFTDEMIAMPiSALSGGWKMKLALARAVLRN 561
Cdd:PRK11831 90 fqsgALFTDMNVFDNVayplrehtqlpaplLHSTVMMKlEAV-------GLRGAAKLMP-SELSGGMARRAALARAIALE 161
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 6323278 562 ADILLLDEPTNHLDTVNVAWLV---NYLN-TCGITSITISHD 599
Cdd:PRK11831 162 PDLIMFDEPFVGQDPITMGVLVkliSELNsALGVTCVVVSHD 203
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
861-951 |
2.43e-06 |
|
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: 49.77 E-value: 2.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 861 ALASGQFRPLTRKE-----IEEHCSMLGLDPeiVSHSRIRGLSGGQKVKLVLAAGTWQRPHLIVLDEPTNYLDRDSLGAL 935
Cdd:TIGR01184 76 ALAVDRVLPDLSKSerraiVEEHIALVGLTE--AADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNL 153
|
90 100
....*....|....*....|
gi 6323278 936 SKAL----KEFEGGVIIITH 951
Cdd:TIGR01184 154 QEELmqiwEEHRVTVLMVTH 173
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
686-738 |
2.66e-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: 49.74 E-value: 2.66e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6323278 686 DINFQCSLSSRIAVIGPNGAGKSTLINVLTGELLPTSGEVY----------THENCR--IAYIKQ 738
Cdd:cd03224 18 GVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRfdgrditglpPHERARagIGYVPE 82
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
461-598 |
2.88e-06 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 51.26 E-value: 2.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 461 ICGPNGCGKSTLMRAIAN------GQV--DGFP-TQEECRTVYVEHDIDG----------THSDTSVLDFVFESGV--GT 519
Cdd:TIGR00958 512 LVGPSGSGKSTVAALLQNlyqptgGQVllDGVPlVQYDHHYLHRQVALVGqepvlfsgsvRENIAYGLTDTPDEEImaAA 591
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 520 KEAIKDKLIEfGFT---DEMIAMPISALSGGWKMKLALARAVLRNADILLLDEPTNHLDTVNVAWLVNYLNTCGITSITI 596
Cdd:TIGR00958 592 KAANAHDFIM-EFPngyDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQESRSRASRTVLLI 670
|
..
gi 6323278 597 SH 598
Cdd:TIGR00958 671 AH 672
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
667-975 |
2.98e-06 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 49.63 E-value: 2.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 667 VKVTNMEFQYpGTSKpQITDINFQCSLSSRIAVIGPNGAGKSTLINVLTGELLPTSGEVythencriaYIKQHAFahies 746
Cdd:PRK11124 3 IQLNGINCFY-GAHQ-ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTL---------NIAGNHF----- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 747 HLDKTPSEyiqwrfqtgedretmdranRQINEndaeamnkifkiegtprriagihsrrkfkntyeyecsflLGENIGMKS 826
Cdd:PRK11124 67 DFSKTPSD-------------------KAIRE---------------------------------------LRRNVGMVF 88
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 827 ER---WvPMMSV-DNawiprgeLVESHSKmVAEVDMKEALASGQfRPLTRKEIEEHCSMLGLDpeivshsrirgLSGGQK 902
Cdd:PRK11124 89 QQynlW-PHLTVqQN-------LIEAPCR-VLGLSKDQALARAE-KLLERLRLKPYADRFPLH-----------LSGGQQ 147
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6323278 903 VKLVLAAGTWQRPHLIVLDEPTNYLDRDSLGALSKALKEF-EGGV--IIITHSAEFTKNLTEEVWAVKDGRMTPSG 975
Cdd:PRK11124 148 QRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELaETGItqVIVTHEVEVARKTASRVVYMENGHIVEQG 223
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
441-610 |
3.16e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 50.19 E-value: 3.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 441 GAKILLNKTQLRLKRARRYGICGPNGCGKSTLMRAI------ANGQV--DGFP-TQEECRTVYVEHDIDGTHSDTSVLDF 511
Cdd:PRK13652 15 GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFngilkpTSGSVliRGEPiTKENIREVRKFVGLVFQNPDDQIFSP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 512 VFESGVG--------TKEAIKDKLIE----FGFTDEMIAMPiSALSGGWKMKLALARAVLRNADILLLDEPTNHLDTVNV 579
Cdd:PRK13652 95 TVEQDIAfgpinlglDEETVAHRVSSalhmLGLEELRDRVP-HHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGV 173
|
170 180 190
....*....|....*....|....*....|....*
gi 6323278 580 AWLVNYLN----TCGITSITISHDSVFLDNVCEYI 610
Cdd:PRK13652 174 KELIDFLNdlpeTYGMTVIFSTHQLDLVPEMADYI 208
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
542-598 |
3.94e-06 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 50.73 E-value: 3.94e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 6323278 542 SALSGGWKMKLALARAVLRNADILLLDEPTNHLDTVNVAWLVNYLNTC--GITSITISH 598
Cdd:PRK13657 470 RQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELmkGRTTFIIAH 528
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
667-975 |
4.43e-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: 48.73 E-value: 4.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 667 VKVTNMEFQYPGtsKPQITDINfqCSLSSRI-AVIGPNGAGKSTLINVLTGELLPTSGEVYTHencriayikqhafahie 745
Cdd:cd03264 1 LQLENLTKRYGK--KRALDGVS--LTLGPGMyGLLGPNGAGKTTLMRILATLTPPSSGTIRID----------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 746 shldktpseyiqwrfqtGEDretmDRANRQinendaeamnKIfkiegtpRRIAGihsrrkfkntyeyecsFLLGENigmk 825
Cdd:cd03264 60 -----------------GQD----VLKQPQ----------KL-------RRRIG----------------YLPQEF---- 81
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 826 seRWVPMMSVDnawiprgELVEsHSKMVAEVDMKEAlasgqfrpltRKEIEEHCSMLGLDPeiVSHSRIRGLSGGQKVKL 905
Cdd:cd03264 82 --GVYPNFTVR-------EFLD-YIAWLKGIPSKEV----------KARVDEVLELVNLGD--RAKKKIGSLSGGMRRRV 139
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6323278 906 VLAAGTWQRPHLIVLDEPTNYLD-------RDSLGALSKalkefEGGVIIITHSAEFTKNLTEEVWAVKDGRMTPSG 975
Cdd:cd03264 140 GIAQALVGDPSILIVDEPTAGLDpeerirfRNLLSELGE-----DRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
440-575 |
4.63e-06 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 49.31 E-value: 4.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 440 YGAKILLNKTQLRLKRARRYGICGPNGCGKSTLMRAIA-------------NGQVDGfPTQEecRTVYVEHDidGTHSDT 506
Cdd:PRK11248 11 YGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAgfvpyqhgsitldGKPVEG-PGAE--RGVVFQNE--GLLPWR 85
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6323278 507 SVLDFVfesGVGTKEAIKDKLIEFGFTDEMIAM---------PISALSGGWKMKLALARAVLRNADILLLDEPTNHLD 575
Cdd:PRK11248 86 NVQDNV---AFGLQLAGVEKMQRLEIAHQMLKKvglegaekrYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALD 160
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
544-570 |
4.94e-06 |
|
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: 48.62 E-value: 4.94e-06
10 20
....*....|....*....|....*..
gi 6323278 544 LSGGWKMKLALARAVLRNADILLLDEP 570
Cdd:cd03250 128 LSGGQKQRISLARAVYSDADIYLLDDP 154
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
696-726 |
6.08e-06 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 48.81 E-value: 6.08e-06
10 20 30
....*....|....*....|....*....|.
gi 6323278 696 RIAVIGPNGAGKSTLINVLTGELLPTSGEVY 726
Cdd:PRK10771 27 RVAILGPSGAGKSTLLNLIAGFLTPASGSLT 57
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
459-602 |
6.18e-06 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 48.42 E-value: 6.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 459 YGICGPNGCGKSTLMRAIA---NGQVDGFPTQEECRTVYveHDIDGThsdTSVlDFVFESGVGTKEAIKDKLIEF-GFT- 533
Cdd:cd03279 31 FLICGPTGAGKSTILDAITyalYGKTPRYGRQENLRSVF--APGEDT---AEV-SFTFQLGGKKYRVERSRGLDYdQFTr 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 534 ---------DEMIAMPISALSGG--WKMKLALARA---VLRNA-----DILLLDEPTNHLDTVN---VAWLVNYLNTCGI 591
Cdd:cd03279 105 ivllpqgefDRFLARPVSTLSGGetFLASLSLALAlseVLQNRggarlEALFIDEGFGTLDPEAleaVATALELIRTENR 184
|
170
....*....|.
gi 6323278 592 TSITISHDSVF 602
Cdd:cd03279 185 MVGVISHVEEL 195
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
439-575 |
6.39e-06 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 49.56 E-value: 6.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 439 AYGAKILLNKTQLRLKRARRYGICGPNGCGKSTLMRAIAngqvdGFPTQEECRTVYVEHDIDGTHSDTSVLDFVFES--- 515
Cdd:PRK09452 23 SFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIA-----GFETPDSGRIMLDGQDITHVPAENRHVNTVFQSyal 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 516 -----------------GVGTKEaIKDKLIE---FGFTDEMIAMPISALSGGWKMKLALARAVLRNADILLLDEPTNHLD 575
Cdd:PRK09452 98 fphmtvfenvafglrmqKTPAAE-ITPRVMEalrMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALD 176
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
687-726 |
6.55e-06 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 48.68 E-value: 6.55e-06
10 20 30 40
....*....|....*....|....*....|....*....|
gi 6323278 687 INFQCSLSSRIAVIGPNGAGKSTLINVLTGeLLPTSGEVY 726
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAG-LLPGQGEIL 53
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
440-580 |
7.25e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 48.68 E-value: 7.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 440 YGAKILLNKTQLRLKRARRYGICGPNGCGKSTLMRAI-----------ANGQVDGFPtqeecRTVYVEhDIDG------- 501
Cdd:PRK14267 14 YGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFnrllelneearVEGEVRLFG-----RNIYSP-DVDPievrrev 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 502 -------------THSDTSVLDFVFESGVGTKEAIkDKLIEFGFT---------DEMIAMPiSALSGGWKMKLALARAVL 559
Cdd:PRK14267 88 gmvfqypnpfphlTIYDNVAIGVKLNGLVKSKKEL-DERVEWALKkaalwdevkDRLNDYP-SNLSGGQRQRLVIARALA 165
|
170 180
....*....|....*....|.
gi 6323278 560 RNADILLLDEPTNHLDTVNVA 580
Cdd:PRK14267 166 MKPKILLMDEPTANIDPVGTA 186
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
671-975 |
7.39e-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: 48.64 E-value: 7.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 671 NMEFQYPGTSKPQITDINFQCSLSSRIAVIGPNGAGKSTLINVLTGELLPTSGEVYthencriayIKQHAFAHIEShldk 750
Cdd:cd03252 5 HVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVL---------VDGHDLALADP---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 751 tpseyiQW-RFQTGEDRETMDRANRQINENDA---EAMNKIFKIEGTprRIAGIHSrrkfkntyeyecsFLLgenigmks 826
Cdd:cd03252 72 ------AWlRRQVGVVLQENVLFNRSIRDNIAladPGMSMERVIEAA--KLAGAHD-------------FIS-------- 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 827 erwvpmmsvdnawiprgELVESHSKMVAEvdmkealasgqfrpltrkeieehcsmlgldpeivshsRIRGLSGGQKVKLV 906
Cdd:cd03252 123 -----------------ELPEGYDTIVGE-------------------------------------QGAGLSGGQRQRIA 148
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6323278 907 LAAGTWQRPHLIVLDEPTNYLDRDSLGALSKALKEFEGG--VIIITHSAEFTKNlTEEVWAVKDGRMTPSG 975
Cdd:cd03252 149 IARALIHNPRILIFDEATSALDYESEHAIMRNMHDICAGrtVIIIAHRLSTVKN-ADRIIVMEKGRIVEQG 218
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
436-575 |
7.41e-06 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 48.49 E-value: 7.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 436 FSLAYGAKILLNKTQLRLKRARRYGICGPNGCGKSTLMRAI-----------ANGQV--DG------------------- 483
Cdd:COG1117 17 LNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLnrmndlipgarVEGEIllDGediydpdvdvvelrrrvgm 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 484 -------FPTqeecrTVYvehD-------IDGTHsDTSVLDFVFES---GVGTKEAIKDKLIEFGFtdemiampisALSG 546
Cdd:COG1117 97 vfqkpnpFPK-----SIY---DnvayglrLHGIK-SKSELDEIVEEslrKAALWDEVKDRLKKSAL----------GLSG 157
|
170 180
....*....|....*....|....*....
gi 6323278 547 GWKMKLALARAVLRNADILLLDEPTNHLD 575
Cdd:COG1117 158 GQQQRLCIARALAVEPEVLLMDEPTSALD 186
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
664-725 |
7.42e-06 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 49.96 E-value: 7.42e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6323278 664 KAIVKVTNMEFQYPGtSKPQITDINFQCSLSSRIAVIGPNGAGKSTLINVLTGELLPTSGEV 725
Cdd:PRK13657 332 KGAVEFDDVSFSYDN-SRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRI 392
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
667-741 |
7.76e-06 |
|
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: 47.15 E-value: 7.76e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6323278 667 VKVTNMEFQYPgTSKPQITDINFQCSLSSRIAVIGPNGAGKSTLINVLtGELLP-TSGEVYTHENCRIAYIKQHAF 741
Cdd:cd03223 1 IELENLSLATP-DGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRAL-AGLWPwGSGRIGMPEGEDLLFLPQRPY 74
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
897-990 |
8.52e-06 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 48.43 E-value: 8.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 897 LSGGQKVKLVLAAGTWQRPHLIVLDEPTNYLDRDSLGALSKALKEF--EGG-VIIITHSAEFTKNLTEEVWAVKDGRMTP 973
Cdd:PRK10619 153 LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLaeEGKtMVVVTHEMGFARHVSSHVIFLHQGKIEE 232
|
90
....*....|....*...
gi 6323278 974 SGH-NWVSGQGAGPRIEK 990
Cdd:PRK10619 233 EGApEQLFGNPQSPRLQQ 250
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
441-577 |
8.69e-06 |
|
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: 48.70 E-value: 8.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 441 GAKILLNKTQLRLKRARRYGICGPNGCGKSTLMRAI-------ANGQVDG-----FPTQEECR--------------TVY 494
Cdd:cd03289 15 GGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFlrllnteGDIQIDGvswnsVPLQKWRKafgvipqkvfifsgTFR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 495 VEHDIDGTHSDTSVLDFVFESGVGTK-EAIKDKLiEFGFTDEMiampiSALSGGWKMKLALARAVLRNADILLLDEPTNH 573
Cdd:cd03289 95 KNLDPYGKWSDEEIWKVAEEVGLKSViEQFPGQL-DFVLVDGG-----CVLSHGHKQLMCLARSVLSKAKILLLDEPSAH 168
|
....
gi 6323278 574 LDTV 577
Cdd:cd03289 169 LDPI 172
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
461-586 |
9.04e-06 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 47.88 E-value: 9.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 461 ICGPNGCGKSTLMRAIA------NGQV--DGFPTQEeCRT------VYVEHdIDGTHSDTSV---LDFVFE-SGVGTKEA 522
Cdd:PRK13538 32 IEGPNGAGKTSLLRILAglarpdAGEVlwQGEPIRR-QRDeyhqdlLYLGH-QPGIKTELTAlenLRFYQRlHGPGDDEA 109
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6323278 523 IKDKLIEFG---FTDemiaMPISALSGGWKMKLALARAVLRNADILLLDEPTNHLDTVNVAWLVNYL 586
Cdd:PRK13538 110 LWEALAQVGlagFED----VPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARLEALL 172
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
680-954 |
9.30e-06 |
|
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: 47.90 E-value: 9.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 680 SKPQITDINFQCSLSSRIAVIGPNGAGKSTLINVLTGELLPTSGEVYthencriayikqhafahieshLDktpseyiqwr 759
Cdd:cd03259 12 SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEIL---------------------ID---------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 760 fqtGEDretmdranrqinendaeamnkifkIEGTPrriagIHSRrkfkntyeyecsfllgeNIGM--KSERWVPMMSV-D 836
Cdd:cd03259 61 ---GRD------------------------VTGVP-----PERR-----------------NIGMvfQDYALFPHLTVaE 91
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 837 NAWIPRGELVESHSKMVAEVDmkEALAsgqfrpltrkeieehcsMLGLDPEIvsHSRIRGLSGGQKVKLVLAAGTWQRPH 916
Cdd:cd03259 92 NIAFGLKLRGVPKAEIRARVR--ELLE-----------------LVGLEGLL--NRYPHELSGGQQQRVALARALAREPS 150
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 6323278 917 LIVLDEPTNYLD---RDSL-GALSKALKEFEGGVIIITHSAE 954
Cdd:cd03259 151 LLLLDEPLSALDaklREELrEELKELQRELGITTIYVTHDQE 192
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
659-791 |
9.40e-06 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 49.63 E-value: 9.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 659 VKTKQKAIVKVTNMEFQYPGTSKPQITDINFQCSLSSRIAVIGPNGAGKSTLINVLT-------GELLPTSGEV--YTHE 729
Cdd:PRK11176 334 VIERAKGDIEFRNVTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTrfydideGEILLDGHDLrdYTLA 413
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6323278 730 NCR--IAYIKQHAfahiesHL-DKTPSEYIQWRFQTGEDRETMDRANRQinendAEAMNKIFKIE 791
Cdd:PRK11176 414 SLRnqVALVSQNV------HLfNDTIANNIAYARTEQYSREQIEEAARM-----AYAMDFINKMD 467
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
698-725 |
9.82e-06 |
|
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: 48.05 E-value: 9.82e-06
10 20
....*....|....*....|....*...
gi 6323278 698 AVIGPNGAGKSTLINVLTGELLPTSGEV 725
Cdd:COG0410 33 ALLGRNGAGKTTLLKAISGLLPPRSGSI 60
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
897-970 |
9.99e-06 |
|
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: 47.60 E-value: 9.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 897 LSGGQKVKLVLA------------AGtwqrphLIVLDEPTNYLDRDSL-GALSKALKEFEGG----VIIITHSAEFtKNL 959
Cdd:cd03240 116 CSGGEKVLASLIirlalaetfgsnCG------ILALDEPTTNLDEENIeESLAEIIEERKSQknfqLIVITHDEEL-VDA 188
|
90
....*....|..
gi 6323278 960 TEEVWAV-KDGR 970
Cdd:cd03240 189 ADHIYRVeKDGR 200
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
459-575 |
1.05e-05 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 48.92 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 459 YGICGPNGCGKSTLMRAIA------NGQVDgfptqeecrtvyvehdIDGThsDTSVLD--------------F------- 511
Cdd:COG1135 34 FGIIGYSGAGKSTLIRCINllerptSGSVL----------------VDGV--DLTALSerelraarrkigmiFqhfnlls 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6323278 512 ---VFE--------SGVgTKEAIKDK---LIEF-GFTDEMIAMPiSALSGGWKMKLALARAVLRNADILLLDEPTNHLD 575
Cdd:COG1135 96 srtVAEnvalpleiAGV-PKAEIRKRvaeLLELvGLSDKADAYP-SQLSGGQKQRVGIARALANNPKVLLCDEATSALD 172
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
624-951 |
1.19e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 49.64 E-value: 1.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 624 NFTEFVKKCPAAKAYEELSNTDLEFKFPEpgylEGVKTKQKAIVKVTNMEFQYPGTSKPQI-TDINFQCSLSSRIAVIGP 702
Cdd:PTZ00265 344 NITEYMKSLEATNSLYEIINRKPLVENND----DGKKLKDIKKIQFKNVRFHYDTRKDVEIyKDLNFTLTEGKTYAFVGE 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 703 NGAGKSTLINVLTGELLPTSGEVYTHENcriayikqHAFAHIESHLdktpseyiqWRFQTGEDRETMDRANRQINEN--- 779
Cdd:PTZ00265 420 SGCGKSTILKLIERLYDPTEGDIIINDS--------HNLKDINLKW---------WRSKIGVVSQDPLLFSNSIKNNiky 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 780 ------DAEAMNKIFKIEGTPRriagiHSRRKFKNTYEYECSFLLGENIGMKSERWVPMMSVDNAWIPRGELVESHSKMV 853
Cdd:PTZ00265 483 slyslkDLEALSNYYNEDGNDS-----QENKNKRNSCRAKCAGDLNDMSNTTDSNELIEMRKNYQTIKDSEVVDVSKKVL 557
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 854 aevdmkealasgqfrpltrkeIEEHCSMLGLDPEIVSHSRIRGLSGGQKVKLVLAAGTWQRPHLIVLDEPTNYLDRDSLG 933
Cdd:PTZ00265 558 ---------------------IHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEY 616
|
330 340
....*....|....*....|..
gi 6323278 934 ALSKALKEFEGG----VIIITH 951
Cdd:PTZ00265 617 LVQKTINNLKGNenriTIIIAH 638
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
440-611 |
1.26e-05 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 48.04 E-value: 1.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 440 YGAKILLNKTQLRLKRARRYGICGPNGCGKSTLMRAI------------ANGQV-------DG---FPTQEECRTVYVEH 497
Cdd:PRK10619 15 YGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCInflekpsegsivVNGQTinlvrdkDGqlkVADKNQLRLLRTRL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 498 DIDGTH----SDTSVLDFVFESGVG----TKEAIKDKLIEF----GFTDEMIAMPISALSGGWKMKLALARAVLRNADIL 565
Cdd:PRK10619 95 TMVFQHfnlwSHMTVLENVMEAPIQvlglSKQEARERAVKYlakvGIDERAQGKYPVHLSGGQQQRVSIARALAMEPEVL 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 6323278 566 LLDEPTNHLD---TVNVAWLVNYLNTCGITSITISHDSVFLDNVCEYII 611
Cdd:PRK10619 175 LFDEPTSALDpelVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVI 223
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
872-951 |
1.28e-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: 47.21 E-value: 1.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 872 RKEIEEHCSMLGLDPEivSHSRIRGLSGGQKVKLVLAAGTWQRPHLIVLDEPTNYLDRDS---LGALSKALKEFEGGVII 948
Cdd:cd03268 104 KKRIDEVLDVVGLKDS--AKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGikeLRELILSLRDQGITVLI 181
|
...
gi 6323278 949 ITH 951
Cdd:cd03268 182 SSH 184
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
887-963 |
1.32e-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: 46.58 E-value: 1.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 887 EIVSHSRIRGLSGGQKVK----LVLAAGTWQRPHLIVLDEPTNYLDRDSLGALSKALKEFEGG---VIIITHSAEFTKNL 959
Cdd:cd03227 68 SAELIFTRLQLSGGEKELsalaLILALASLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKgaqVIVITHLPELAELA 147
|
....
gi 6323278 960 TEEV 963
Cdd:cd03227 148 DKLI 151
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
445-600 |
1.35e-05 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 47.47 E-value: 1.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 445 LLNKTQLRLKRARRYGICGPNGCGKSTLMRAIA------NGQVD--GFP---TQEECRTVYVEHDIDgthsdtsvldFVF 513
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAglddgsSGEVSlvGQPlhqMDEEARAKLRAKHVG----------FVF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 514 -----------------------ESGVGTKEAIKDKLIEFGFTDEMIAMPiSALSGGWKMKLALARAVLRNADILLLDEP 570
Cdd:PRK10584 95 qsfmliptlnalenvelpallrgESSRQSRNGAKALLEQLGLGKRLDHLP-AQLSGGEQQRVALARAFNGRPDVLFADEP 173
|
170 180 190
....*....|....*....|....*....|....
gi 6323278 571 TNHLDTVN---VAWLVNYLN-TCGITSITISHDS 600
Cdd:PRK10584 174 TGNLDRQTgdkIADLLFSLNrEHGTTLILVTHDL 207
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
446-598 |
1.44e-05 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 48.86 E-value: 1.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 446 LNKTQLRLKRARRYGICGPNGCGKSTLMRAIAngqvdGfptqeecrtVYvEHD-----IDGT-HSDTSVLDfVFESGVGT 519
Cdd:COG1129 20 LDGVSLELRPGEVHALLGENGAGKSTLMKILS-----G---------VY-QPDsgeilLDGEpVRFRSPRD-AQAAGIAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 520 --------------------KEAIKdklieFGFTD--EMIA----------------MPISALSGGWKMKLALARAVLRN 561
Cdd:COG1129 84 ihqelnlvpnlsvaeniflgREPRR-----GGLIDwrAMRRrarellarlgldidpdTPVGDLSVAQQQLVEIARALSRD 158
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 6323278 562 ADILLLDEPTNHLDTVNVAWL---VNYLNTCGITSITISH 598
Cdd:COG1129 159 ARVLILDEPTASLTEREVERLfriIRRLKAQGVAIIYISH 198
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
446-599 |
1.45e-05 |
|
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: 47.71 E-value: 1.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 446 LNKTQLRLKRARRYGICGPNGCGKSTLMRaIANGQVdgFPTQEECRtvyVEHDIDGTHSDTSV--LDFVF---------- 513
Cdd:cd03267 37 LKGISFTIEKGEIVGFIGPNGAGKTTTLK-ILSGLL--QPTSGEVR---VAGLVPWKRRKKFLrrIGVVFgqktqlwwdl 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 514 ---ES--------GVGTKEAIK--DKLIEFGFTDEMIAMPISALSGGWKMKLALARAVLRNADILLLDEPTNHLDTV--- 577
Cdd:cd03267 111 pviDSfyllaaiyDLPPARFKKrlDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVaqe 190
|
170 180
....*....|....*....|...
gi 6323278 578 NV-AWLVNYLNTCGITSITISHD 599
Cdd:cd03267 191 NIrNFLKEYNRERGTTVLLTSHY 213
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
869-975 |
1.46e-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: 48.57 E-value: 1.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 869 PLTRKEIEEHCSMLGLDPEIVShsRIRGLSGGQKVKLVLAAGTWQRPHLIVLDEPTNYLDRDS----LGALSKALKEFEG 944
Cdd:TIGR02142 106 SERRISFERVIELLGIGHLLGR--LPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRkyeiLPYLERLHAEFGI 183
|
90 100 110
....*....|....*....|....*....|.
gi 6323278 945 GVIIITHSAEFTKNLTEEVWAVKDGRMTPSG 975
Cdd:TIGR02142 184 PILYVSHSLQEVLRLADRVVVLEDGRVAAAG 214
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
542-575 |
1.46e-05 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 49.07 E-value: 1.46e-05
10 20 30
....*....|....*....|....*....|....
gi 6323278 542 SALSGGWKMKLALARAVLRNADILLLDEPTNHLD 575
Cdd:PRK11174 484 AGLSVGQAQRLALARALLQPCQLLLLDEPTASLD 517
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
440-570 |
1.48e-05 |
|
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: 47.54 E-value: 1.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 440 YGAKILLNKTQLRLKRARRYGICGPNGCGKSTLMRAIA------NGQVD-------------------GFPTQEEC--RT 492
Cdd:cd03218 10 YGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVglvkpdSGKILldgqditklpmhkrarlgiGYLPQEASifRK 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6323278 493 VYVEHDIDgthsdtSVLDFVFESGVGTKEAIKDKLIEFGFTdEMIAMPISALSGGWKMKLALARAVLRNADILLLDEP 570
Cdd:cd03218 90 LTVEENIL------AVLEIRGLSKKEREEKLEELLEEFHIT-HLRKSKASSLSGGERRRVEIARALATNPKFLLLDEP 160
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
664-743 |
1.50e-05 |
|
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: 47.47 E-value: 1.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 664 KAIVKVTNMEFQYPGTSKPQI-TDINFQCSLSSRIAVIGPNGAGKSTLINVLTGELLPTSGEVYTHENCRIAYikQHAFA 742
Cdd:cd03248 9 KGIVKFQNVTFAYPTRPDTLVlQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQY--EHKYL 86
|
.
gi 6323278 743 H 743
Cdd:cd03248 87 H 87
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
684-950 |
1.57e-05 |
|
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: 47.27 E-value: 1.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 684 ITDINFQCSLSSRIAVIGPNGAGKSTLINVLTGELLP---TSGEVYthencriayikqhafahieshldktpseyiqwrf 760
Cdd:cd03234 23 LNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggtTSGQIL---------------------------------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 761 qtgedretmdranrqinendaeamnkifkIEGTPRriagihSRRKFKntyeYECSFLLgenigmKSERWVPMMSVdnawi 840
Cdd:cd03234 69 -----------------------------FNGQPR------KPDQFQ----KCVAYVR------QDDILLPGLTV----- 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 841 prgelvESHSKMVAEVDMKEALASGQfrpltRKEIEEHCSMLGLDPEIVSHSRIRGLSGGQKVKLVLAAGTWQRPHLIVL 920
Cdd:cd03234 99 ------RETLTYTAILRLPRKSSDAI-----RKKRVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLIL 167
|
250 260 270
....*....|....*....|....*....|...
gi 6323278 921 DEPTNYLdrDSLGALS--KALKEF-EGGVIIIT 950
Cdd:cd03234 168 DEPTSGL--DSFTALNlvSTLSQLaRRNRIVIL 198
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
667-729 |
1.65e-05 |
|
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: 47.10 E-value: 1.65e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6323278 667 VKVTNMEFQYpgtskpQITDINFQCSLSS--RIAVIGPNGAGKSTLINVLTGELLPTSGEVYTHE 729
Cdd:cd03298 1 VRLDKIRFSY------GEQPMHFDLTFAQgeITAIVGPSGSGKSTLLNLIAGFETPQSGRVLING 59
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
667-726 |
1.87e-05 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 47.39 E-value: 1.87e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 667 VKVTNMEFQYpgTSKPQITDINFQCSLSSRIAVIGPNGAGKSTLINVLTGELLPTSGEVY 726
Cdd:COG4604 2 IEIKNVSKRY--GGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVL 59
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
897-975 |
1.89e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 47.42 E-value: 1.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 897 LSGGQKVKLVLAAGTWQRPHLIVLDEPTNYLD---RDSLGALSKALKEFEGGVIIITHSAEFTKNLTEEVWAVKDGRMTP 973
Cdd:PRK13647 139 LSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDprgQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLA 218
|
..
gi 6323278 974 SG 975
Cdd:PRK13647 219 EG 220
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
893-952 |
1.93e-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: 46.39 E-value: 1.93e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6323278 893 RIRGLSGGQKVKLVLAAGTWQRPHLIVLDEPTNYLDRDSLGALSKALKEF-EGG--VIIITHS 952
Cdd:cd03213 108 KLRGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLaDTGrtIICSIHQ 170
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
542-576 |
1.94e-05 |
|
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: 47.08 E-value: 1.94e-05
10 20 30
....*....|....*....|....*....|....*
gi 6323278 542 SALSGGWKMKLALARAVLRNADILLLDEPTNHLDT 576
Cdd:cd03248 149 SQLSGGQKQRVAIARALIRNPQVLILDEATSALDA 183
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
664-970 |
2.08e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 47.42 E-value: 2.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 664 KAIVKVTNMEFQY-PGTSKPQITDINFQCSLSSRIAVIGPNGAGKSTLINVLTGELLPTSGEVYthencriayikqhafa 742
Cdd:PRK13650 2 SNIIEVKNLTFKYkEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQII---------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 743 hIESHLdktpseyiqwrfqtgedretmdranrQINENDAEAMNKIFKIegtprriagihsrrkFKN--------TYEYEC 814
Cdd:PRK13650 66 -IDGDL--------------------------LTEENVWDIRHKIGMV---------------FQNpdnqfvgaTVEDDV 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 815 SFLLgENIGMkserwvpmmsvdnawiprgelveSHSKMVAEVDmkEALASGQFRPLTRKEieehcsmlgldPeivshSRi 894
Cdd:PRK13650 104 AFGL-ENKGI-----------------------PHEEMKERVN--EALELVGMQDFKERE-----------P-----AR- 140
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 895 rgLSGGQKVKLVLAAGTWQRPHLIVLDEPTNYLD----RDSLGALSKALKEFEGGVIIITHSAEFTKnLTEEVWAVKDGR 970
Cdd:PRK13650 141 --LSGGQKQRVAIAGAVAMRPKIIILDEATSMLDpegrLELIKTIKGIRDDYQMTVISITHDLDEVA-LSDRVLVMKNGQ 217
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
686-975 |
2.30e-05 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 46.93 E-value: 2.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 686 DINFQCSLSSRIAVIGPNGAGKSTLINVLTGELLPTSGEVythencriayikqhafaHIESHldktpseyiQWRFQtged 765
Cdd:COG4161 20 DINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQL-----------------NIAGH---------QFDFS---- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 766 retmdranRQINENDAEAMnkifkiegtprriagihsRRKfkntyeyecsfllgenIGMKSER---WvPMMSV-DNawip 841
Cdd:COG4161 70 --------QKPSEKAIRLL------------------RQK----------------VGMVFQQynlW-PHLTVmEN---- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 842 rgeLVESHSKmVAEVDMKEAlasgqfrpltRKEIEEHCSMLGLDPEivSHSRIRGLSGGQKVKLVLAAGTWQRPHLIVLD 921
Cdd:COG4161 103 ---LIEAPCK-VLGLSKEQA----------REKAMKLLARLRLTDK--ADRFPLHLSGGQQQRVAIARALMMEPQVLLFD 166
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 6323278 922 EPTNYLDRDSLGALSKALKEF-EGGV--IIITHSAEFTKNLTEEVWAVKDGRMTPSG 975
Cdd:COG4161 167 EPTAALDPEITAQVVEIIRELsQTGItqVIVTHEVEFARKVASQVVYMEKGRIIEQG 223
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
436-599 |
2.35e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 47.40 E-value: 2.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 436 FSLAYGAKILLNKTQLRLKRARRYGICGPNGCGKSTLMRAI--ANGQVDGFPTQEEC----RTVYVEHDI---------- 499
Cdd:PRK14271 27 LTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLnrMNDKVSGYRYSGDVllggRSIFNYRDVlefrrrvgml 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 500 --DGTHSDTSVLDFVFE---------------------SGVGTKEAIKDKLIEFGFTdemiampisaLSGGWKMKLALAR 556
Cdd:PRK14271 107 fqRPNPFPMSIMDNVLAgvrahklvprkefrgvaqarlTEVGLWDAVKDRLSDSPFR----------LSGGQQQLLCLAR 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 6323278 557 AVLRNADILLLDEPTNHLDTVNVAWLVNYLNTCG--ITSITISHD 599
Cdd:PRK14271 177 TLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLAdrLTVIIVTHN 221
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
673-728 |
2.38e-05 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 48.17 E-value: 2.38e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 6323278 673 EFQYPGTSKPQITDINFQCSLSSRIAVIGPNGAGKSTLINVLTGELLPTSGEVYTH 728
Cdd:PRK10789 320 QFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFH 375
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
442-598 |
2.38e-05 |
|
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: 47.10 E-value: 2.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 442 AKILLNKTQLRLKRARRYGICGPNGCGKSTLMRAIAngqvdGFPTQEECRTVYVEHDIdGTHSDTSV---LDFVFESGVG 518
Cdd:cd03252 14 GPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQ-----RFYVPENGRVLVDGHDL-ALADPAWLrrqVGVVLQENVL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 519 TKEAIKD------------KLIEF----GFTDEMIAMPI----------SALSGGWKMKLALARAVLRNADILLLDEPTN 572
Cdd:cd03252 88 FNRSIRDnialadpgmsmeRVIEAaklaGAHDFISELPEgydtivgeqgAGLSGGQRQRIAIARALIHNPRILIFDEATS 167
|
170 180
....*....|....*....|....*...
gi 6323278 573 HLDTVNV-AWLVNYLNTC-GITSITISH 598
Cdd:cd03252 168 ALDYESEhAIMRNMHDICaGRTVIIIAH 195
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
869-951 |
2.41e-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: 46.76 E-value: 2.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 869 PLTRKEIEEHCSMLGLDPEIVS-----HSRI--RG--LSGGQKVKLVLAAGTWQRPHLIVLDEPTNYLDRDSLGALSKAL 939
Cdd:cd03249 103 DATDEEVEEAAKKANIHDFIMSlpdgyDTLVgeRGsqLSGGQKQRIAIARALLRNPKILLLDEATSALDAESEKLVQEAL 182
|
90
....*....|....
gi 6323278 940 KEFEGG--VIIITH 951
Cdd:cd03249 183 DRAMKGrtTIVIAH 196
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
446-609 |
2.42e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 47.47 E-value: 2.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 446 LNKTQLRLKRARRYGICGPNGCGKSTLMRAIaNGQVDgfPTqeecrTVYVEHDIDGTHSDTS-------------VLDF- 511
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNI-NALLK--PT-----TGTVTVDDITITHKTKdkyirpvrkrigmVFQFp 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 512 ---VFESGV------GTK------EAIKDK----LIEFGFTDEMIAMPISALSGGWKMKLALARAVLRNADILLLDEPTN 572
Cdd:PRK13646 95 esqLFEDTVereiifGPKnfkmnlDEVKNYahrlLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTA 174
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 6323278 573 HLD---TVNVAWLVNYLNT-CGITSITISHDsvfLDNVCEY 609
Cdd:PRK13646 175 GLDpqsKRQVMRLLKSLQTdENKTIILVSHD---MNEVARY 212
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
681-971 |
2.50e-05 |
|
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: 47.11 E-value: 2.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 681 KPQITDINFQCSLSSRIAVIGPNGAGKSTLINVLTGELLPTSGEVythencriayikqhafahieshldktpseyiqwRF 760
Cdd:TIGR02769 24 APVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTV---------------------------------SF 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 761 QtGEDRETMDRAnrqinendaeamnkifkiegtprriagihSRRKFKNTYEyecsFLLGENIGMKSerwvPMMSVDnaWI 840
Cdd:TIGR02769 71 R-GQDLYQLDRK-----------------------------QRRAFRRDVQ----LVFQDSPSAVN----PRMTVR--QI 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 841 pRGELVESHSkmvaevDMKEAlasgqfrplTRKE-IEEHCSMLGLDPEIVShSRIRGLSGGQKVKLVLAAGTWQRPHLIV 919
Cdd:TIGR02769 111 -IGEPLRHLT------SLDES---------EQKArIAELLDMVGLRSEDAD-KLPRQLSGGQLQRINIARALAVKPKLIV 173
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 6323278 920 LDEPTNYLDR---DSLGALSKALKEfEGGV--IIITHSAEFTKNLTEEVWAVKDGRM 971
Cdd:TIGR02769 174 LDEAVSNLDMvlqAVILELLRKLQQ-AFGTayLFITHDLRLVQSFCQRVAVMDKGQI 229
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
862-975 |
2.50e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 47.54 E-value: 2.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 862 LASGQFRPLTRKEIEEHCSMLGLDPEIVSHSRIrGLSGGQKVKLVLAAGTWQRPHLIVLDEPTNYLD---RDSLGALSKA 938
Cdd:PRK13631 143 VALGVKKSEAKKLAKFYLNKMGLDDSYLERSPF-GLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDpkgEHEMMQLILD 221
|
90 100 110
....*....|....*....|....*....|....*..
gi 6323278 939 LKEFEGGVIIITHSAEFTKNLTEEVWAVKDGRMTPSG 975
Cdd:PRK13631 222 AKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTG 258
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
446-599 |
2.64e-05 |
|
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: 46.69 E-value: 2.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 446 LNKTQLRLKRARRYGICGPNGCGKSTLMRAIAngqvdGFpTQEECRTVYVE-HDIDGTHSDTSVldfVFES--------- 515
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLIS-----GL-AQPTSGGVILEgKQITEPGPDRMV---VFQNysllpwltv 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 516 ---------------GVGTKEAIKDKLIEFGFTDEMIAMPISALSGGWKMKLALARAVLRNADILLLDEPTNHLDTVNVA 580
Cdd:TIGR01184 72 renialavdrvlpdlSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRG 151
|
170 180
....*....|....*....|...
gi 6323278 581 ----WLVNYLNTCGITSITISHD 599
Cdd:TIGR01184 152 nlqeELMQIWEEHRVTVLMVTHD 174
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
697-725 |
2.79e-05 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 46.91 E-value: 2.79e-05
10 20
....*....|....*....|....*....
gi 6323278 697 IAVIGPNGAGKSTLINVLTGELLPTSGEV 725
Cdd:PRK11300 34 VSLIGPNGAGKTTVFNCLTGFYKPTGGTI 62
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
697-762 |
2.86e-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: 46.63 E-value: 2.86e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6323278 697 IAVIGPNGAGKSTLINVLTGELLPTSGEVYThENCRIAYIKQHAFAHIESHLD-----KTPSEYIQWRFQT 762
Cdd:cd03237 28 IGILGPNGIGKTTFIKMLAGVLKPDEGDIEI-ELDTVSYKPQYIKADYEGTVRdllssITKDFYTHPYFKT 97
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
667-725 |
2.94e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 47.13 E-value: 2.94e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6323278 667 VKVTNMEFQY-PGTS--KPQITDINFQCSLSSRIAVIGPNGAGKSTLINVLTGELLPTSGEV 725
Cdd:PRK13641 3 IKFENVDYIYsPGTPmeKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTI 64
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
896-951 |
3.13e-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: 45.98 E-value: 3.13e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 6323278 896 GLSGGQKVKLVLAAGTWQRPHLIVLDEPTNYLDRDSLGALSKALKEF--EG-GVIIITH 951
Cdd:cd03217 104 GFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKLreEGkSVLIITH 162
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
544-576 |
3.29e-05 |
|
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: 47.89 E-value: 3.29e-05
10 20 30
....*....|....*....|....*....|...
gi 6323278 544 LSGGWKMKLALARAVLRNADILLLDEPTNHLDT 576
Cdd:COG5265 495 LSGGEKQRVAIARTLLKNPPILIFDEATSALDS 527
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
460-570 |
3.38e-05 |
|
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: 47.40 E-value: 3.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 460 GICGPNGCGKSTLMRAIA------NG--QVDGFPTQEECRTV----------YV-------EHdidgthsdTSV---LDF 511
Cdd:COG4148 29 ALFGPSGSGKTTLLRAIAglerpdSGriRLGGEVLQDSARGIflpphrrrigYVfqearlfPH--------LSVrgnLLY 100
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6323278 512 vfesgvGTKEAIKDK-LIEFgftDEMIAM---------PISALSGGWKMKLALARAVLRNADILLLDEP 570
Cdd:COG4148 101 ------GRKRAPRAErRISF---DEVVELlgighlldrRPATLSGGERQRVAIGRALLSSPRLLLMDEP 160
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
441-575 |
3.49e-05 |
|
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: 46.41 E-value: 3.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 441 GAKILLNKTQLRLKRARRYGICGPNGCGKSTLMRAIaNGQVDgfPT------QEECRTVYVEHDIDGTHSDT-------- 506
Cdd:cd03256 12 NGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCL-NGLVE--PTsgsvliDGTDINKLKGKALRQLRRQIgmifqqfn 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 507 -----SVLDFVFESGVGTKEAIK---------DKLIEFGFTD-----EMIAMPISALSGGWKMKLALARAVLRNADILLL 567
Cdd:cd03256 89 lierlSVLENVLSGRLGRRSTWRslfglfpkeEKQRALAALErvgllDKAYQRADQLSGGQQQRVAIARALMQQPKLILA 168
|
....*...
gi 6323278 568 DEPTNHLD 575
Cdd:cd03256 169 DEPVASLD 176
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
435-575 |
3.59e-05 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 47.78 E-value: 3.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 435 EFSLAYGAKILLNKTQLRLKRARRYGICGPNGCGKSTLMrAIANGQVDgfPTQEECRTvyveHDI-------DGTHSDTS 507
Cdd:PRK10789 320 QFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLL-SLIQRHFD--VSEGDIRF----HDIpltklqlDSWRSRLA 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 508 VLD---FVFESGVG----------TKEAIKDKLIEFGFTDEMIAMPIS----------ALSGGWKMKLALARAVLRNADI 564
Cdd:PRK10789 393 VVSqtpFLFSDTVAnnialgrpdaTQQEIEHVARLASVHDDILRLPQGydtevgergvMLSGGQKQRISIARALLLNAEI 472
|
170
....*....|.
gi 6323278 565 LLLDEPTNHLD 575
Cdd:PRK10789 473 LILDDALSAVD 483
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
883-975 |
3.72e-05 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 47.78 E-value: 3.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 883 GLDPEivshSRIR---GLSGGQKVKLVLAAGTWQRPHLIVLDEPTNYLDRD---SLGALSKALKE-FEGGVIIITHSAEF 955
Cdd:PRK15134 413 GLDPE----TRHRypaEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTvqaQILALLKSLQQkHQLAYLFISHDLHV 488
|
90 100
....*....|....*....|
gi 6323278 956 TKNLTEEVWAVKDGRMTPSG 975
Cdd:PRK15134 489 VRALCHQVIVLRQGEVVEQG 508
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
895-975 |
3.93e-05 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 46.28 E-value: 3.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 895 RGLSGGQKVKLVLAAGTWQRPHLIVLDEPTNYLDRDSLG---ALSKALKEFEGGVIIITHSAEFTKNLTEEVWAVKDGRM 971
Cdd:PRK11264 143 RRLSGGQQQRVAIARALAMRPEVILFDEPTSALDPELVGevlNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRI 222
|
....
gi 6323278 972 TPSG 975
Cdd:PRK11264 223 VEQG 226
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
893-975 |
4.09e-05 |
|
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: 45.82 E-value: 4.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 893 RIRGLSGGQKVKLVLAAGTWQRPHLIVLDEPTNYLDRDSLGALSKALKEF-EGG--VIIITHSAEFTKNLTEEVWAVKDG 969
Cdd:cd03266 133 RVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLrALGkcILFSTHIMQEVERLCDRVVVLHRG 212
|
....*.
gi 6323278 970 RMTPSG 975
Cdd:cd03266 213 RVVYEG 218
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
519-598 |
4.23e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 47.72 E-value: 4.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 519 TKEAIKdKLIEFGFTDEMI-AMPIS----------ALSGGWKMKLALARAVLRNADILLLDEPTNHLDTVNVAW----LV 583
Cdd:PTZ00265 1324 TREDVK-RACKFAAIDEFIeSLPNKydtnvgpygkSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLiektIV 1402
|
90
....*....|....*
gi 6323278 584 NYLNTCGITSITISH 598
Cdd:PTZ00265 1403 DIKDKADKTIITIAH 1417
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
651-726 |
4.43e-05 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 47.41 E-value: 4.43e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6323278 651 PEPGYLEGVKTKQKAIVKVTNMEFQYpGTSKPQITDINFQCSLSSRIAVIGPNGAGKSTLINVLTGELLPTSGEVY 726
Cdd:PRK10790 325 PRQQYGNDDRPLQSGRIDIDNVSFAY-RDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIR 399
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
686-972 |
4.87e-05 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 45.96 E-value: 4.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 686 DINFQCSLSSRIAVIGPNGAGKSTLINVLTGELLPTSGEVYthencriayikqhafahieshldktpseyiqwrFQtGED 765
Cdd:PRK11629 27 NVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVI---------------------------------FN-GQP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 766 RETMDRANRqinendAEAMNkifkiegtpRRIAGIhsrrkfkntyeYECSFLLG-----ENIGMkserwvPMMSvdnAWI 840
Cdd:PRK11629 73 MSKLSSAAK------AELRN---------QKLGFI-----------YQFHHLLPdftalENVAM------PLLI---GKK 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 841 PRGELVESHSKMVAEVdmkealasgqfrpltrkeieehcsmlGLDPEivSHSRIRGLSGGQKVKLVLAAGTWQRPHLIVL 920
Cdd:PRK11629 118 KPAEINSRALEMLAAV--------------------------GLEHR--ANHRPSELSGGERQRVAIARALVNNPRLVLA 169
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 6323278 921 DEPTNYLDR---DSLGALSKALKEFEG-GVIIITHSAEFTKNLTEEVwAVKDGRMT 972
Cdd:PRK11629 170 DEPTGNLDArnaDSIFQLLGELNRLQGtAFLVVTHDLQLAKRMSRQL-EMRDGRLT 224
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
676-725 |
4.98e-05 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 47.21 E-value: 4.98e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 6323278 676 YPGTSKpqITDINFQCSLSSRIAVIGPNGAGKSTLINVLTGELLPTSGEV 725
Cdd:PRK11288 14 FPGVKA--LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSI 61
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
441-611 |
5.29e-05 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 47.01 E-value: 5.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 441 GAKILLNKTQLRLKRARRYGICGPNGCGKST----LMRAIAN-GQV--DGFPTQEECR--TVYVEHDIDGTHSDT----- 506
Cdd:PRK15134 297 DHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINSqGEIwfDGQPLHNLNRrqLLPVRHRIQVVFQDPnssln 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 507 ---SVLDFVFE---------SGVGTKEAIKDKLIEFGFTDEMIAMPISALSGGWKMKLALARAVLRNADILLLDEPTNHL 574
Cdd:PRK15134 377 prlNVLQIIEEglrvhqptlSAAQREQQVIAVMEEVGLDPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSL 456
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 6323278 575 D-TVN---VAWLVNYLNTCGITSITISHDSVFLDNVCEYII 611
Cdd:PRK15134 457 DkTVQaqiLALLKSLQQKHQLAYLFISHDLHVVRALCHQVI 497
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
441-621 |
5.36e-05 |
|
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: 47.60 E-value: 5.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 441 GAKILLNKTQLRLKRARRYGICGPNGCGKSTLMRAI-----ANG--QVDGFP----TQEECRTVY--VEHDI---DGT-- 502
Cdd:TIGR01271 1230 AGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALlrllsTEGeiQIDGVSwnsvTLQTWRKAFgvIPQKVfifSGTfr 1309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 503 --------HSDTSVLDFVFEsgVGTKEAIK---DKLiEFGFTDEMIAmpisaLSGGWKMKLALARAVLRNADILLLDEPT 571
Cdd:TIGR01271 1310 knldpyeqWSDEEIWKVAEE--VGLKSVIEqfpDKL-DFVLVDGGYV-----LSNGHKQLMCLARSILSKAKILLLDEPS 1381
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 6323278 572 NHLDTVNVAWLVNYL-NTCGITSITISHDSVFLDNVCEYIINYEGLKLRKY 621
Cdd:TIGR01271 1382 AHLDPVTLQIIRKTLkQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQY 1432
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
686-725 |
5.50e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 45.25 E-value: 5.50e-05
10 20 30 40
....*....|....*....|....*....|....*....|
gi 6323278 686 DINFQCSLSSRIAVIGPNGAGKSTLINVLTGELLPTSGEV 725
Cdd:PRK13539 20 GLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTI 59
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
693-951 |
5.77e-05 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 45.39 E-value: 5.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 693 LSSRIAVI-GPNGAGKSTLINVLTGELLptsGEVYTHENCRIAYIKQHA-FAHIESHLDKTPSEYIQWRFQtGEDRETMD 770
Cdd:COG0419 21 FDDGLNLIvGPNGAGKSTILEAIRYALY---GKARSRSKLRSDLINVGSeEASVELEFEHGGKRYRIERRQ-GEFAEFLE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 771 RANRQInendAEAMNKIFKIEgtprriagihsrrkfknTYEyecsfllgenigmKSERWVpmmsvdnawiprGELVESHS 850
Cdd:COG0419 97 AKPSER----KEALKRLLGLE-----------------IYE-------------ELKERL------------KELEEALE 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 851 KMVAEVDMKEALASGQFRPLTrkeieehcsmlGLDPeivshsrIRGLSGGQKVKLVLAagtwqRPHLIVLDepTNYLDRD 930
Cdd:COG0419 131 SALEELAELQKLKQEILAQLS-----------GLDP-------IETLSGGERLRLALA-----DLLSLILD--FGSLDEE 185
|
250 260
....*....|....*....|.
gi 6323278 931 SLGALSKALKEfeggVIIITH 951
Cdd:COG0419 186 RLERLLDALEE----LAIITH 202
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
534-575 |
5.84e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 47.33 E-value: 5.84e-05
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 6323278 534 DEMIAMPISALSGGWKMKLALARAVLRNADILLLDEPTNHLD 575
Cdd:PTZ00265 570 ETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLD 611
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
439-607 |
6.13e-05 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 46.85 E-value: 6.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 439 AYGAKILLNKTQLRLKRARRYGICGPNGCGKSTLMRAIA--------NGQV--DGFPTQ------EECRTVYVEHDIDGT 502
Cdd:PRK13549 14 TFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSgvyphgtyEGEIifEGEELQasnirdTERAGIAIIHQELAL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 503 HSDTSVLDFVFesgvgtkeaIKDKLIEFGFTD--EMI----------------AMPISALSGGWKMKLALARAVLRNADI 564
Cdd:PRK13549 94 VKELSVLENIF---------LGNEITPGGIMDydAMYlraqkllaqlkldinpATPVGNLGLGQQQLVEIAKALNKQARL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 6323278 565 LLLDEPTNHLDTVNVAWLVNY---LNTCGITSITISH--DSVF--LDNVC 607
Cdd:PRK13549 165 LILDEPTASLTESETAVLLDIirdLKAHGIACIYISHklNEVKaiSDTIC 214
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
831-975 |
6.31e-05 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 46.77 E-value: 6.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 831 PMMSVdNAWIPRGELVESHSKMVAEVDMKEALASGQfRPLTRKEIEEHCSMLGLDPeivsHSrirgLSGGQKVKLVLAAG 910
Cdd:PRK10261 113 PMTSL-NPVFTVGEQIAESIRLHQGASREEAMVEAK-RMLDQVRIPEAQTILSRYP----HQ----LSGGMRQRVMIAMA 182
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6323278 911 TWQRPHLIVLDEPTNYLD---RDSLGALSKAL-KEFEGGVIIITHSAEFTKNLTEEVWAVKDGRMTPSG 975
Cdd:PRK10261 183 LSCRPAVLIADEPTTALDvtiQAQILQLIKVLqKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETG 251
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
897-972 |
6.60e-05 |
|
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: 44.34 E-value: 6.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 897 LSGGQKVKLVLAAGTWQRPHLIVLDEPTNYLDR---DSLGALSKALKEFEGGVIIITHsaeftkNLtEEVWAV------- 966
Cdd:cd03216 83 LSVGERQMVEIARALARNARLLILDEPTAALTPaevERLFKVIRRLRAQGVAVIFISH------RL-DEVFEIadrvtvl 155
|
....*.
gi 6323278 967 KDGRMT 972
Cdd:cd03216 156 RDGRVV 161
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
544-630 |
6.61e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 47.28 E-value: 6.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 544 LSGGWKMKLALARAVLRNADILLLDEPTNHLDTvNVAWLVnyLNTC------GITSITISHDSVFLDNVCEYIINYEGLK 617
Cdd:PLN03232 741 ISGGQKQRVSMARAVYSNSDIYIFDDPLSALDA-HVAHQV--FDSCmkdelkGKTRVLVTNQLHFLPLMDRIILVSEGMI 817
|
90
....*....|...
gi 6323278 618 lrKYKGNFTEFVK 630
Cdd:PLN03232 818 --KEEGTFAELSK 828
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
537-571 |
6.66e-05 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 46.55 E-value: 6.66e-05
10 20 30
....*....|....*....|....*....|....*
gi 6323278 537 IAMPISALSGGWKMKLALARAVLRNADILLLDEPT 571
Cdd:COG1129 388 PEQPVGNLSGGNQQKVVLAKWLATDPKVLILDEPT 422
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
850-975 |
7.10e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 45.88 E-value: 7.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 850 SKMVAEVDMKEALASGQFRPLTRKEIE----EHCSMLGLDPEIVSHSRIRgLSGGQKVKLVLAAGTWQRPHLIVLDEPTN 925
Cdd:PRK13643 95 SQLFEETVLKDVAFGPQNFGIPKEKAEkiaaEKLEMVGLADEFWEKSPFE-LSGGQMRRVAIAGILAMEPEVLVLDEPTA 173
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 6323278 926 YLD---RDSLGALSKALKEFEGGVIIITHSAEFTKNLTEEVWAVKDGRMTPSG 975
Cdd:PRK13643 174 GLDpkaRIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCG 226
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
641-741 |
7.12e-05 |
|
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: 47.25 E-value: 7.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 641 LSNTDLEfkfPEPGYLEGVKTKQKAIVKVTNMEFQYPGTSKPQITDINFQCSLSSRIAVIGPNGAGKSTLINVLTGELLP 720
Cdd:TIGR00957 614 LSHEELE---PDSIERRTIKPGEGNSITVHNATFTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDK 690
|
90 100
....*....|....*....|.
gi 6323278 721 TSGEVytHENCRIAYIKQHAF 741
Cdd:TIGR00957 691 VEGHV--HMKGSVAYVPQQAW 709
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
666-725 |
7.13e-05 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 45.85 E-value: 7.13e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 666 IVKVTNMEFQYPGtsKPQITDINFQCSLSSRIAVIGPNGAGKSTLINVLTGELLPTSGEV 725
Cdd:PRK11248 1 MLQISHLYADYGG--KPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSI 58
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
441-575 |
7.43e-05 |
|
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: 45.71 E-value: 7.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 441 GAKILLNKTQLRLKRARRYGICGPNGCGKSTLMRAIaNGQVDgfPTQEEcrtVYVEHDIDGTHSDTSVLDF-------VF 513
Cdd:cd03294 35 GQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCI-NRLIE--PTSGK---VLIDGQDIAAMSRKELRELrrkkismVF 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 514 ES--------------------GVGTKEAIK---DKLIEFGFTDEMIAMPiSALSGGWKMKLALARAVLRNADILLLDEP 570
Cdd:cd03294 109 QSfallphrtvlenvafglevqGVPRAEREEraaEALELVGLEGWEHKYP-DELSGGMQQRVGLARALAVDPDILLMDEA 187
|
....*
gi 6323278 571 TNHLD 575
Cdd:cd03294 188 FSALD 192
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
873-975 |
7.57e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 45.77 E-value: 7.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 873 KEIEEHCSMLGLDPEIVSHSRIRgLSGGQKVKLVLAAGTWQRPHLIVLDEPTNYLD----RDSLGALSKALKEFEGGVII 948
Cdd:PRK13645 128 KKVPELLKLVQLPEDYVKRSPFE-LSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDpkgeEDFINLFERLNKEYKKRIIM 206
|
90 100
....*....|....*....|....*..
gi 6323278 949 ITHSAEFTKNLTEEVWAVKDGRMTPSG 975
Cdd:PRK13645 207 VTHNMDQVLRIADEVIVMHEGKVISIG 233
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
666-725 |
8.03e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 45.75 E-value: 8.03e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6323278 666 IVKVTNMEFQYP-GTskPQITDINFQCSLSSRIAVIGPNGAGKSTLINVLTGELLPTSGEV 725
Cdd:PRK13644 1 MIRLENVSYSYPdGT--PALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKV 59
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
446-606 |
8.32e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 45.49 E-value: 8.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 446 LNKTQLRLKRARRYGICGPNGCGKSTLMRAI------ANGQ--VDGFPTQEEcrTVY-VEHDI-------DGTHSDTSVL 509
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIdglleaESGQiiIDGDLLTEE--NVWdIRHKIgmvfqnpDNQFVGATVE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 510 D---FVFES-GVGTKEAIK--DKLIEF-GFTDEMIAMPiSALSGGWKMKLALARAVLRNADILLLDEPTNHLDTVNVAWL 582
Cdd:PRK13650 101 DdvaFGLENkGIPHEEMKErvNEALELvGMQDFKEREP-ARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLEL 179
|
170 180
....*....|....*....|....*...
gi 6323278 583 VNYLNTC----GITSITISHDsvfLDNV 606
Cdd:PRK13650 180 IKTIKGIrddyQMTVISITHD---LDEV 204
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
461-591 |
8.37e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 44.86 E-value: 8.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 461 ICGPNGCGKSTLMRAIANGQ--VDGFPTQEECRT--------VYVEHDIdGTHSDTSVLD-FVFESGVGTKEAIKDKLIE 529
Cdd:PRK13541 31 IKGANGCGKSSLLRMIAGIMqpSSGNIYYKNCNInniakpycTYIGHNL-GLKLEMTVFEnLKFWSEIYNSAETLYAAIH 109
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6323278 530 FGFTDEMIAMPISALSGGWKMKLALARAVLRNADILLLDEPTNHLDTVNVAWLVNYL----NTCGI 591
Cdd:PRK13541 110 YFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLIvmkaNSGGI 175
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
435-600 |
8.74e-05 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 44.78 E-value: 8.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 435 EFSLAYGAKILLNKTQLRLKRARRYGICGPNGCGKSTLMRAIANGQVDGFPTQEECRtvyvehdIDGTHSDT-------- 506
Cdd:COG4136 6 NLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAFSASGEVL-------LNGRRLTAlpaeqrri 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 507 -------------SV---LDFVFESGVGT---KEAIKDKLIEFGFTDEMIAMPISaLSGGWKMKLALARAVLRNADILLL 567
Cdd:COG4136 79 gilfqddllfphlSVgenLAFALPPTIGRaqrRARVEQALEEAGLAGFADRDPAT-LSGGQRARVALLRALLAEPRALLL 157
|
170 180 190
....*....|....*....|....*....|....*..
gi 6323278 568 DEPTNHLDT---VNV-AWLVNYLNTCGITSITISHDS 600
Cdd:COG4136 158 DEPFSKLDAalrAQFrEFVFEQIRQRGIPALLVTHDE 194
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
451-599 |
8.97e-05 |
|
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: 45.02 E-value: 8.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 451 LRLKRARRYGICGPNGCGKSTLMRAIAngqvdGFPTQEECRTVYVEHDIDGTHSDTSVLDFVFESGV------------- 517
Cdd:cd03299 20 LEVERGDYFVILGPTGSGKSVLLETIA-----GFIKPDSGKILLNGKDITNLPPEKRDISYVPQNYAlfphmtvykniay 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 518 ------GTKEAIKDKLIE---FGFTDEMIAMPISALSGGWKMKLALARAVLRNADILLLDEPTNHLDTVNVAWLVNYLNT 588
Cdd:cd03299 95 glkkrkVDKKEIERKVLEiaeMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREELKK 174
|
170
....*....|....*
gi 6323278 589 C----GITSITISHD 599
Cdd:cd03299 175 IrkefGVTVLHVTHD 189
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
463-618 |
9.09e-05 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 45.64 E-value: 9.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 463 GPNGCGKSTLMRAI------ANGQVD--GFPTQEECRTVYVEHDIDGTHSDTS----VLDFVFESGVG-----------T 519
Cdd:PRK15056 40 GVNGSGKSTLFKALmgfvrlASGKISilGQPTRQALQKNLVAYVPQSEEVDWSfpvlVEDVVMMGRYGhmgwlrrakkrD 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 520 KEAIKDKLIEFGFTdEMIAMPISALSGGWKMKLALARAVLRNADILLLDEPTNHLDTVNVAWLVNYLNTC---GITSITI 596
Cdd:PRK15056 120 RQIVTAALARVDMV-EFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELrdeGKTMLVS 198
|
170 180
....*....|....*....|..
gi 6323278 597 SHDSVFLDNVCEYIINYEGLKL 618
Cdd:PRK15056 199 THNLGSVTEFCDYTVMVKGTVL 220
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
463-589 |
9.22e-05 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 44.56 E-value: 9.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 463 GPNGCGKSTLMRAIAN-----GQVDGfptqeecRTVYVEHDIDGTHSD-TSVLDFVFESGVGTKEAIKDKLIEFGFT--- 533
Cdd:cd03233 40 GRPGSGCSTLLKALANrtegnVSVEG-------DIHYNGIPYKEFAEKyPGEIIYVSEEDVHFPTLTVRETLDFALRckg 112
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 6323278 534 DEMIampiSALSGGWKMKLALARAVLRNADILLLDEPTNHLDTVNVAWLVNYLNTC 589
Cdd:cd03233 113 NEFV----RGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEILKCIRTM 164
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
436-577 |
1.05e-04 |
|
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: 46.44 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 436 FSLaYGAKILLNkTQLRLKRARRYGICGPNGCGKSTLMRAIAnGQVDgfPTQEECR-------TVYVEHDIDGTHSDTSV 508
Cdd:TIGR01271 434 FSL-YVTPVLKN-ISFKLEKGQLLAVAGSTGSGKSSLLMMIM-GELE--PSEGKIKhsgrisfSPQTSWIMPGTIKDNII 508
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 509 L-----DFVFESGVG--------TKEAIKDK--LIEFGFTdemiampisaLSGGWKMKLALARAVLRNADILLLDEPTNH 573
Cdd:TIGR01271 509 FglsydEYRYTSVIKacqleediALFPEKDKtvLGEGGIT----------LSGGQRARISLARAVYKDADLYLLDSPFTH 578
|
....
gi 6323278 574 LDTV 577
Cdd:TIGR01271 579 LDVV 582
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
431-615 |
1.19e-04 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 45.16 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 431 LCNCEFSLAygAKILLNKTQLRLKRARRYGICGPNGCGKSTLMR------------AIANGQ-VDGFPTQEECRTV-YVE 496
Cdd:PRK10575 14 LRNVSFRVP--GRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKmlgrhqppsegeILLDAQpLESWSSKAFARKVaYLP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 497 HDIDGTHSDTsVLDFVfesGVGtKEAIKDKLIEFGFTD-----EMIAM----P-----ISALSGGWKMKLALARAVLRNA 562
Cdd:PRK10575 92 QQLPAAEGMT-VRELV---AIG-RYPWHGALGRFGAADrekveEAISLvglkPlahrlVDSLSGGERQRAWIAMLVAQDS 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 6323278 563 DILLLDEPTNHLD---TVNVAWLVNYLNTC-GITSITISHDSVFLDNVCEYIINYEG 615
Cdd:PRK10575 167 RCLLLDEPTSALDiahQVDVLALVHRLSQErGLTVIAVLHDINMAARYCDYLVALRG 223
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
863-975 |
1.20e-04 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 45.16 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 863 ASGQFRPLTRKEIEEHCSMLGLDPeiVSHSRIRGLSGGQKVKLVLAAGTWQRPHLIVLDEPTNYLD----RDSLgALSKA 938
Cdd:PRK10575 116 ALGRFGAADREKVEEAISLVGLKP--LAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDiahqVDVL-ALVHR 192
|
90 100 110
....*....|....*....|....*....|....*...
gi 6323278 939 LKEFEG-GVIIITHSAEFTKNLTEEVWAVKDGRMTPSG 975
Cdd:PRK10575 193 LSQERGlTVIAVLHDINMAARYCDYLVALRGGEMIAQG 230
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
666-726 |
1.22e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 45.22 E-value: 1.22e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6323278 666 IVKVTNMEFQYP-GTSKpqITDINFQCSLSSRIAVIGPNGAGKSTLINVLTGELLPTSGEVY 726
Cdd:PRK13636 5 ILKVEELNYNYSdGTHA--LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRIL 64
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
876-975 |
1.38e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 45.12 E-value: 1.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 876 EEHCSMLGLDPEIVSHSRIRgLSGGQKVKLVLAAGTWQRPHLIVLDEPTNYLD---RDSLGALSKALKEFEGGVIIITHS 952
Cdd:PRK13649 126 REKLALVGISESLFEKNPFE-LSGGQMRRVAIAGILAMEPKILVLDEPTAGLDpkgRKELMTLFKKLHQSGMTIVLVTHL 204
|
90 100
....*....|....*....|...
gi 6323278 953 AEFTKNLTEEVWAVKDGRMTPSG 975
Cdd:PRK13649 205 MDDVANYADFVYVLEKGKLVLSG 227
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
897-957 |
1.50e-04 |
|
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: 43.30 E-value: 1.50e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6323278 897 LSGGQKVKLVLAAGTWQRPHLIVLDEPTNYLDRDSLGALSKALKEFEGGVIIITHSAEFTK 957
Cdd:cd03223 92 LSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKELGITVISVGHRPSLWK 152
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
433-645 |
1.52e-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: 46.09 E-value: 1.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 433 NCEFSLAYGAKILLNKTQLRLKRARRYGICGPNGCGKSTLMRAI------------ANGQVDGFPTQEECRTVYVEHDID 500
Cdd:TIGR00957 641 NATFTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALlaemdkveghvhMKGSVAYVPQQAWIQNDSLRENIL 720
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 501 GTHSdtsVLDFVFESGVGTKEAIKDKLIEFGFTDEMIAMPISALSGGWKMKLALARAVLRNADILLLDEPTNHLDT-VNV 579
Cdd:TIGR00957 721 FGKA---LNEKYYQQVLEACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAhVGK 797
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6323278 580 AWLVNYLNTCGI----TSITISHDSVFLDNVcEYIINYEGLK---------LRKYKGNFTEFVkkCPAAKAYEELSNTD 645
Cdd:TIGR00957 798 HIFEHVIGPEGVlknkTRILVTHGISYLPQV-DVIIVMSGGKisemgsyqeLLQRDGAFAEFL--RTYAPDEQQGHLED 873
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
667-975 |
1.57e-04 |
|
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: 45.56 E-value: 1.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 667 VKVTNMEFQYPGtsKPQITDINFQCSLSSRIAVIGPNGAGKSTLINVLTG--ELLPTSGEVYTH----ENCriAYIKQHA 740
Cdd:TIGR03269 1 IEVKNLTKKFDG--KEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPTSGRIIYHvalcEKC--GYVERPS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 741 FA-----HIESHLDKTPSEYIqwrfqtgedretmdranrqineNDAEAMNKIFKiegtpRRIAgIHSRRKFKnTYEYECS 815
Cdd:TIGR03269 77 KVgepcpVCGGTLEPEEVDFW----------------------NLSDKLRRRIR-----KRIA-IMLQRTFA-LYGDDTV 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 816 FllgENIgmkserwvpMMSVDNAWIPRGELVESHSKMVAEVDMkealasgqfrpltrkeieEHcsmlgldpeivshsRI- 894
Cdd:TIGR03269 128 L---DNV---------LEALEEIGYEGKEAVGRAVDLIEMVQL------------------SH--------------RIt 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 895 ---RGLSGGQKVKLVLAAGTWQRPHLIVLDEPTNYLDRDSL----GALSKALKEFEGGVIIITHSAEFTKNLTEEVWAVK 967
Cdd:TIGR03269 164 hiaRDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAklvhNALEEAVKASGISMVLTSHWPEVIEDLSDKAIWLE 243
|
....*...
gi 6323278 968 DGRMTPSG 975
Cdd:TIGR03269 244 NGEIKEEG 251
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
446-597 |
1.58e-04 |
|
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: 45.59 E-value: 1.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 446 LNKTQLRLKRARRYGICGPNGCGKSTLMRAI---------ANGQVDGFPTQEECRTVYVEHDIDGTHSDTSVLDFVFESG 516
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALfgaypgkfeGNVFINGKPVDIRNPAQAIRAGIAMVPEDRKRHGIVPILG 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 517 VG-----------TKEAIKDKLIEFGFTDEMIA----------MPISALSGGWKMKLALARAVLRNADILLLDEPTNHLD 575
Cdd:TIGR02633 356 VGknitlsvlksfCFKMRIDAAAELQIIGSAIQrlkvktaspfLPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVD 435
|
170 180
....*....|....*....|....*
gi 6323278 576 T---VNVAWLVNYLNTCGITSITIS 597
Cdd:TIGR02633 436 VgakYEIYKLINQLAQEGVAIIVVS 460
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
684-738 |
1.60e-04 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 45.51 E-value: 1.60e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 6323278 684 ITDINFQCSLSSRIAVIGPNGAGKSTLINVLtGELLPTSGEVYTH-ENCRIAYIKQ 738
Cdd:TIGR00954 468 IESLSFEVPSGNNLLICGPNGCGKSSLFRIL-GELWPVYGGRLTKpAKGKLFYVPQ 522
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
537-575 |
1.64e-04 |
|
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: 43.57 E-value: 1.64e-04
10 20 30
....*....|....*....|....*....|....*....
gi 6323278 537 IAMPISaLSGGWKMKLALARAVLRNADILLLDEPTNHLD 575
Cdd:cd03215 99 IALSSL-LSGGNQQKVVLARWLARDPRVLILDEPTRGVD 136
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
872-975 |
1.72e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 44.65 E-value: 1.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 872 RKEIEEHCSMLGLDPEIvsHSRIRG----LSGGQKVKLVLAAGTWQRPHLIVLDEPTNYLDRDSLGALSKALKEF--EGG 945
Cdd:PRK14246 127 KKIVEECLRKVGLWKEV--YDRLNSpasqLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELknEIA 204
|
90 100 110
....*....|....*....|....*....|
gi 6323278 946 VIIITHSAEFTKNLTEEVWAVKDGRMTPSG 975
Cdd:PRK14246 205 IVIVSHNPQQVARVADYVAFLYNGELVEWG 234
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
544-575 |
1.74e-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: 44.85 E-value: 1.74e-04
10 20 30
....*....|....*....|....*....|..
gi 6323278 544 LSGGWKMKLALARAVLRNADILLLDEPTNHLD 575
Cdd:cd03291 160 LSGGQRARISLARAVYKDADLYLLDSPFGYLD 191
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
645-725 |
2.16e-04 |
|
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: 45.39 E-value: 2.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 645 DLEFKFPEPGYLEGVKTKQkaIVKVtnmefqYPGTSKPQITDINFQCSLSSRIAVIGPNGAGKSTLINVLTGELLPTSGE 724
Cdd:TIGR01257 915 DSFFERELPGLVPGVCVKN--LVKI------FEPSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGT 986
|
.
gi 6323278 725 V 725
Cdd:TIGR01257 987 V 987
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
461-575 |
2.22e-04 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 44.31 E-value: 2.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 461 ICGPNGCGKSTLMRAIA------------NGQ-VDGFPtqEECRTVY---VEHD-IDGTHSDTSVLD-----------FV 512
Cdd:COG1101 37 VIGSNGAGKSTLLNAIAgslppdsgsiliDGKdVTKLP--EYKRAKYigrVFQDpMMGTAPSMTIEEnlalayrrgkrRG 114
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6323278 513 FESGVGTK--EAIKDKLIEFGFTDE-MIAMPISALSGGWKMKLALARAVLRNADILLLDEPTNHLD 575
Cdd:COG1101 115 LRRGLTKKrrELFRELLATLGLGLEnRLDTKVGLLSGGQRQALSLLMATLTKPKLLLLDEHTAALD 180
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
698-725 |
2.60e-04 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 44.33 E-value: 2.60e-04
10 20
....*....|....*....|....*...
gi 6323278 698 AVIGPNGAGKSTLINVLTGELLPTSGEV 725
Cdd:COG4152 31 GLLGPNGAGKTTTIRIILGILAPDSGEV 58
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
446-612 |
2.65e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 43.91 E-value: 2.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 446 LNKTQLRLKRARRYGICGPNGCGKSTLMRAI------ANGQV--DGFPTQE------ECRT----VYVEHDiDGTHSDTS 507
Cdd:PRK13639 18 LKGINFKAEKGEMVALLGPNGAGKSTLFLHFngilkpTSGEVliKGEPIKYdkksllEVRKtvgiVFQNPD-DQLFAPTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 508 VLDFVF----------ESGVGTKEAIKDKLIEfGFTDEmiamPISALSGGWKMKLALARAVLRNADILLLDEPTNHLDTV 577
Cdd:PRK13639 97 EEDVAFgplnlglskeEVEKRVKEALKAVGME-GFENK----PPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPM 171
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 6323278 578 NVAWLVNY---LNTCGITSITISHD----SVFLDNVceYIIN 612
Cdd:PRK13639 172 GASQIMKLlydLNKEGITIIISTHDvdlvPVYADKV--YVMS 211
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
667-725 |
2.85e-04 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 44.45 E-value: 2.85e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 6323278 667 VKVTNMEFQYPGTskPQITDINFQCSLSSRIAVIGPNGAGKSTLINVLTGELLPTSGEV 725
Cdd:PRK09536 4 IDVSDLSVEFGDT--TVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTV 60
|
|
| MMR_HSR1 |
pfam01926 |
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ... |
696-722 |
3.12e-04 |
|
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete activity of the protein of interacting with the 50S ribosome and binding of both adenine and guanine nucleotides, with a preference for guanine nucleotide.
Pssm-ID: 460387 [Multi-domain] Cd Length: 113 Bit Score: 41.45 E-value: 3.12e-04
10 20
....*....|....*....|....*...
gi 6323278 696 RIAVIG-PNgAGKSTLINVLTGELLPTS 722
Cdd:pfam01926 1 RVALVGrPN-VGKSTLINALTGAKAIVS 27
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
890-971 |
3.19e-04 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 43.85 E-value: 3.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 890 SHSRIRGLSGGQKVKLVLAAGTWQRPHLIVLDEPTNYLDRDSLGALSKALKEF---EGGVIIIT-HSAEFTKNLTEEVWA 965
Cdd:PRK09984 146 AHQRVSTLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDInqnDGITVVVTlHQVDYALRYCERIVA 225
|
....*.
gi 6323278 966 VKDGRM 971
Cdd:PRK09984 226 LRQGHV 231
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
897-959 |
3.30e-04 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 43.41 E-value: 3.30e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6323278 897 LSGGQKVKLVLAAGTWQRPHLIVLDEPTNYLDRDSLG----ALSKALKEFEGGVIIITHSAEFTKNL 959
Cdd:COG2401 137 LSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKrvarNLQKLARRAGITLVVATHHYDVIDDL 203
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
681-738 |
3.34e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 44.73 E-value: 3.34e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 6323278 681 KPQITDINFQCSLSSRIAVIGPNGAGKSTLINVLTGELLPTSGEVYTHENcRIAYIKQ 738
Cdd:PLN03130 630 RPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDASVVIRG-TVAYVPQ 686
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
697-726 |
3.40e-04 |
|
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: 43.26 E-value: 3.40e-04
10 20 30
....*....|....*....|....*....|
gi 6323278 697 IAVIGPNGAGKSTLINVLTGELLPTSGEVY 726
Cdd:cd03261 29 LAIIGPSGSGKSTLLRLIVGLLRPDSGEVL 58
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
679-720 |
3.44e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 44.97 E-value: 3.44e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 6323278 679 TSKPQITDINFQCSLSSRIAVIGPNGAGKSTLINVLTGELLP 720
Cdd:PLN03232 628 TSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSH 669
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
671-726 |
4.31e-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: 42.99 E-value: 4.31e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 6323278 671 NMEFQYPgTSKPQITDINFQCSLSSRIAVIGPNGAGKSTLINVLTGELLPTSGEVY 726
Cdd:cd03253 5 NVTFAYD-PGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSIL 59
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
699-726 |
4.99e-04 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 42.48 E-value: 4.99e-04
10 20
....*....|....*....|....*...
gi 6323278 699 VIGPNGAGKSTLINVLTGELLPTSGEVY 726
Cdd:PRK13538 32 IEGPNGAGKTSLLRILAGLARPDAGEVL 59
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
544-728 |
5.11e-04 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 44.00 E-value: 5.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 544 LSGGWKMKLALARAVLRNADILLLDEPTNHLDTVNVAWL---VNYLNTCGITSITISHDSVFLDNVCEyiiNYEGLKLRK 620
Cdd:PRK09700 146 LSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLfliMNQLRKEGTAIVYISHKLAEIRRICD---RYTVMKDGS 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 621 YKGnfTEFVKKCPAAKAYEELSNTDLEFKFpePGYLEGVKT-KQKAIVKVTNMefqypgTSK--PQITDINFQCSLSSRI 697
Cdd:PRK09700 223 SVC--SGMVSDVSNDDIVRLMVGRELQNRF--NAMKENVSNlAHETVFEVRNV------TSRdrKKVRDISFSVCRGEIL 292
|
170 180 190
....*....|....*....|....*....|.
gi 6323278 698 AVIGPNGAGKSTLINVLTGELLPTSGEVYTH 728
Cdd:PRK09700 293 GFAGLVGSGRTELMNCLFGVDKRAGGEIRLN 323
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
666-741 |
5.30e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 42.24 E-value: 5.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 666 IVKVTNMEFQYpgTSKPQITDINFQCSLSSRIAVIGPNGAGKSTLINVLTGELLPTSGEVY----THENCRIAYIKQHAF 741
Cdd:PRK13540 1 MLDVIELDFDY--HDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILferqSIKKDLCTYQKQLCF 78
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
540-575 |
5.75e-04 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 43.32 E-value: 5.75e-04
10 20 30
....*....|....*....|....*....|....*.
gi 6323278 540 PISaLSGGWKMKLALARAVLRNADILLLDEPTNHLD 575
Cdd:PRK11144 126 PGS-LSGGEKQRVAIGRALLTAPELLLMDEPLASLD 160
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
892-975 |
6.22e-04 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 43.26 E-value: 6.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 892 SRIRGLSGGQKVKLVLAAGTWQRPHLIVLDEPTNYLDRDSLGALSKALKEF--EGGVIII-THSAEFTKNLTEEVWAVKD 968
Cdd:PRK13537 134 AKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLlaRGKTILLtTHFMEEAERLCDRLCVIEE 213
|
....*..
gi 6323278 969 GRMTPSG 975
Cdd:PRK13537 214 GRKIAEG 220
|
|
| SbcC_Walker_B |
pfam13558 |
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from ... |
885-941 |
6.25e-04 |
|
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: 39.91 E-value: 6.25e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 885 DPEIVSHSRIRGLSGGQKVKLV---LAAG-------TWQRPH---LIVLDEPTNYLDRDSLGALSKALKE 941
Cdd:pfam13558 21 GSEVETYRRSGGLSGGEKQLLAylpLAAAlaaqygsAEGRPPaprLVFLDEAFAKLDEENIRTALELLRA 90
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
882-971 |
6.74e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 42.84 E-value: 6.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 882 LGLDPEIVSHSRIRgLSGGQKVKLVLAAGTWQRPHLIVLDEPTNYLD---RDSLGALSKALKEFEGGVII-ITHSAEFTK 957
Cdd:PRK13646 132 LGFSRDVMSQSPFQ-MSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDpqsKRQVMRLLKSLQTDENKTIIlVSHDMNEVA 210
|
90
....*....|....
gi 6323278 958 NLTEEVWAVKDGRM 971
Cdd:PRK13646 211 RYADEVIVMKEGSI 224
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
667-726 |
6.92e-04 |
|
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: 42.10 E-value: 6.92e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 667 VKVTNMEFQYPGTSKPQITDINFQCSLSSRIAVIGPNGAGKSTLINVLTGELLPTSGEVY 726
Cdd:cd03244 3 IEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSIL 62
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
653-725 |
7.01e-04 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 43.56 E-value: 7.01e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6323278 653 PGYLEGVktkqkaiVKVTNMEFQYPG-TSKPQITDINFQCSLSSRIAVIGPNGAGKSTLINVLTGELLPTSGEV 725
Cdd:TIGR00958 472 PLNLEGL-------IEFQDVSFSYPNrPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQV 538
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
461-599 |
8.20e-04 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 43.17 E-value: 8.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 461 ICGPNGCGKSTLMRAIanGQVDGfPTQEECRtvyvehdIDGThsDTSVLD-------------FVFE------------- 514
Cdd:PRK10535 39 IVGASGSGKSTLMNIL--GCLDK-PTSGTYR-------VAGQ--DVATLDadalaqlrrehfgFIFQryhllshltaaqn 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 515 -------SGVGTKEAIK---DKLIEFGFTDEMIAMPiSALSGGWKMKLALARAVLRNADILLLDEPTNHLDT---VNVAW 581
Cdd:PRK10535 107 vevpavyAGLERKQRLLraqELLQRLGLEDRVEYQP-SQLSGGQQQRVSIARALMNGGQVILADEPTGALDShsgEEVMA 185
|
170
....*....|....*...
gi 6323278 582 LVNYLNTCGITSITISHD 599
Cdd:PRK10535 186 ILHQLRDRGHTVIIVTHD 203
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
697-725 |
8.74e-04 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 43.26 E-value: 8.74e-04
10 20
....*....|....*....|....*....
gi 6323278 697 IAVIGPNGAGKSTLINVLTGELLPTSGEV 725
Cdd:PRK13409 102 TGILGPNGIGKTTAVKILSGELIPNLGDY 130
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
682-738 |
8.88e-04 |
|
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: 43.36 E-value: 8.88e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 6323278 682 PQITDINFQCSLSSRIAVIGPNGAGKSTLINVLTGELLPTSGEVytHENCRIAYIKQ 738
Cdd:TIGR01271 440 PVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKI--KHSGRISFSPQ 494
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
897-976 |
9.07e-04 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 42.00 E-value: 9.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 897 LSGGQKVKLVLAAGTWQRPHLIVLDEPTNYLD---RDSLGALSKALKEfEG-GVIIITHSAEFTKNLTEEVWAVKDGRMT 972
Cdd:PRK09493 137 LSGGQQQRVAIARALAVKPKLMLFDEPTSALDpelRHEVLKVMQDLAE-EGmTMVIVTHEIGFAEKVASRLIFIDKGRIA 215
|
....
gi 6323278 973 PSGH 976
Cdd:PRK09493 216 EDGD 219
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
699-725 |
9.16e-04 |
|
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: 41.71 E-value: 9.16e-04
10 20
....*....|....*....|....*..
gi 6323278 699 VIGPNGAGKSTLINVLTGELLPTSGEV 725
Cdd:cd03231 31 VTGPNGSGKTTLLRILAGLSPPLAGRV 57
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
688-806 |
9.52e-04 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 41.33 E-value: 9.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 688 NFQCSLSSRIAVI-GPNGAGKSTLIN----VLTGELLPTSGEvythencriayIKQHAFAH-IESHLDKTPSEYIQWRFQ 761
Cdd:pfam13476 11 DQTIDFSKGLTLItGPNGSGKTTILDaiklALYGKTSRLKRK-----------SGGGFVKGdIRIGLEGKGKAYVEITFE 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 6323278 762 TGEDRETmdranRQINENDAEAMNKIFKIEGTPRRIAGIHSRRKF 806
Cdd:pfam13476 80 NNDGRYT-----YAIERSRELSKKKGKTKKKEILEILEIDELQQF 119
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
897-970 |
1.02e-03 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 42.77 E-value: 1.02e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6323278 897 LSGGQKVKLVLAAGTWQRPHLIVLDEPTNYLDRDSLGALSKALKEFEG----GVIIITHSAEFTKNLTEEVWAVKDGR 970
Cdd:PRK15134 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQelnmGLLFITHNLSIVRKLADRVAVMQNGR 234
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
542-599 |
1.05e-03 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 41.73 E-value: 1.05e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6323278 542 SALSGGWKMKLALARAVLRNADILLLDEPTNHLDTVN---VAWLVNYLNTC-GITSITISHD 599
Cdd:PRK11629 144 SELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNadsIFQLLGELNRLqGTAFLVVTHD 205
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
666-726 |
1.05e-03 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 42.06 E-value: 1.05e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6323278 666 IVKVTNMEFQYpgTSKPQITDINFQCSLSSRIAVIGPNGAGKSTLINVLTGELLPTSGEVY 726
Cdd:PRK11831 7 LVDMRGVSFTR--GNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEIL 65
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
697-730 |
1.06e-03 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 41.92 E-value: 1.06e-03
10 20 30
....*....|....*....|....*....|....
gi 6323278 697 IAVIGPNGAGKSTLINVLTGELLPTSGEVYTHEN 730
Cdd:PRK11231 31 TALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDK 64
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
682-741 |
1.19e-03 |
|
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: 42.15 E-value: 1.19e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 682 PQITDINFQCSLSSRIAVIGPNGAGKSTLINVLTGELLPTSGEVytHENCRIAYIKQHAF 741
Cdd:cd03291 51 PVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKI--KHSGRISFSSQFSW 108
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
892-975 |
1.25e-03 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 42.13 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 892 SRIRGLSGGQKVKLVLAAGTWQRPHLIVLDEPTNYLDRDSLGALSKALKEF--EGGVIII-THSAEFTKNLTEEVWAVKD 968
Cdd:PRK13536 168 ARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLlaRGKTILLtTHFMEEAERLCDRLCVLEA 247
|
....*..
gi 6323278 969 GRMTPSG 975
Cdd:PRK13536 248 GRKIAEG 254
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
697-725 |
1.35e-03 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 41.70 E-value: 1.35e-03
10 20
....*....|....*....|....*....
gi 6323278 697 IAVIGPNGAGKSTLINVLTGELLPTSGEV 725
Cdd:PRK15112 42 LAIIGENGSGKSTLAKMLAGMIEPTSGEL 70
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
868-928 |
1.39e-03 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 42.56 E-value: 1.39e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6323278 868 RPLTRKE----IEEHCSMLGL---DPEIVSHSRIRGLSGGQKVKLVLAAGTWQRPHLIVLDEPTNYLD 928
Cdd:PLN03211 171 KSLTKQEkilvAESVISELGLtkcENTIIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLD 238
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
667-726 |
1.46e-03 |
|
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: 41.52 E-value: 1.46e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 667 VKVTNMEFQYPGtSKPQITDINFQCSLSSRIAVIGPNGAGKSTLINVLTGELLPTSGEVY 726
Cdd:cd03295 1 IEFENVTKRYGG-GKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIF 59
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
697-725 |
1.50e-03 |
|
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: 42.46 E-value: 1.50e-03
10 20
....*....|....*....|....*....
gi 6323278 697 IAVIGPNGAGKSTLINVLTGELLPTSGEV 725
Cdd:COG1245 102 TGILGPNGIGKSTALKILSGELKPNLGDY 130
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
891-952 |
1.56e-03 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 41.68 E-value: 1.56e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6323278 891 HSRIRGLSGGQKVKLVLAAGTWQRPHLIVLDEPTNYLDRDSLGALSKALKEFEGG--VIIITHS 952
Cdd:PRK14239 143 HDSALGLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDytMLLVTRS 206
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
699-726 |
1.78e-03 |
|
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: 42.09 E-value: 1.78e-03
10 20
....*....|....*....|....*...
gi 6323278 699 VIGPNGAGKSTLINVLTGELLPTSGEVY 726
Cdd:COG4615 363 IVGGNGSGKSTLAKLLTGLYRPESGEIL 390
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
897-975 |
1.87e-03 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 41.62 E-value: 1.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 897 LSGGQKVKLVLAAGTWQRPHLIVLDEPTNYLDRDSLGALSKALKEFEG--GVIIITHSAEFTKNLTEEVWAVKDGRMTPS 974
Cdd:PRK14271 164 LSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADrlTVIIVTHNLAQAARISDRAALFFDGRLVEE 243
|
.
gi 6323278 975 G 975
Cdd:PRK14271 244 G 244
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
544-575 |
1.94e-03 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 42.46 E-value: 1.94e-03
10 20 30
....*....|....*....|....*....|..
gi 6323278 544 LSGGWKMKLALARAVLRNADILLLDEPTNHLD 575
Cdd:PTZ00243 783 LSGGQKARVSLARAVYANRDVYLLDDPLSALD 814
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
637-726 |
1.96e-03 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 41.88 E-value: 1.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 637 AYEELSNTDL---EFKFPEPGYLEGVKTkqkaiVKVTNMEFQYPGTS---KPqitdINFQCSLSSRIAVIGPNGAGKSTL 710
Cdd:PRK10522 295 AFNKLNKLALapyKAEFPRPQAFPDWQT-----LELRNVTFAYQDNGfsvGP----INLTIKRGELLFLIGGNGSGKSTL 365
|
90
....*....|....*.
gi 6323278 711 INVLTGELLPTSGEVY 726
Cdd:PRK10522 366 AMLLTGLYQPQSGEIL 381
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
666-941 |
2.13e-03 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 41.74 E-value: 2.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 666 IVKVTNMEFQYPGtsKPQITDINFQCSLSSRIAVIGPNGAGKSTLINVLTGELLPTSGEVYthencriayikqhafahie 745
Cdd:PRK11607 19 LLEIRNLTKSFDG--QHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIM------------------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 746 shLDktpseyiqwrfqtGEDRETMDRANRQINendaeamnKIFKiegtprriagihSRRKFKN-TYEYECSFllgeniGM 824
Cdd:PRK11607 78 --LD-------------GVDLSHVPPYQRPIN--------MMFQ------------SYALFPHmTVEQNIAF------GL 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 825 KSERwvpmmsvdnawIPRGELVESHSKMVAEVDMKEALAsgqfrpltRKeieehcsmlgldpeivSHSrirgLSGGQKVK 904
Cdd:PRK11607 117 KQDK-----------LPKAEIASRVNEMLGLVHMQEFAK--------RK----------------PHQ----LSGGQRQR 157
|
250 260 270
....*....|....*....|....*....|....*..
gi 6323278 905 LVLAAGTWQRPHLIVLDEPtnyldrdsLGALSKALKE 941
Cdd:PRK11607 158 VALARSLAKRPKLLLLDEP--------MGALDKKLRD 186
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
697-725 |
2.13e-03 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 41.06 E-value: 2.13e-03
10 20
....*....|....*....|....*....
gi 6323278 697 IAVIGPNGAGKSTLINVLTGELLPTSGEV 725
Cdd:PRK11701 35 LGIVGESGSGKTTLLNALSARLAPDAGEV 63
|
|
| Der |
COG1160 |
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis]; |
696-717 |
2.14e-03 |
|
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440774 [Multi-domain] Cd Length: 438 Bit Score: 41.93 E-value: 2.14e-03
10 20
....*....|....*....|...
gi 6323278 696 RIAVIG-PNgAGKSTLINVLTGE 717
Cdd:COG1160 177 KIAIVGrPN-VGKSSLINALLGE 198
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
666-725 |
2.16e-03 |
|
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: 41.03 E-value: 2.16e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6323278 666 IVKVTNMEFQYPGTSK--PQITDINFQCSLSSRIAVIGPNGAGKSTLINVLTGELLPTSGEV 725
Cdd:cd03258 1 MIELKNVSKVFGDTGGkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSV 62
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
667-725 |
2.22e-03 |
|
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: 40.47 E-value: 2.22e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 6323278 667 VKVTNMEFQYPGTSKPQITDINFQCSLSSRIAVIGPNGAGKSTLINVLTGELLPTSGEV 725
Cdd:cd03369 7 IEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKI 65
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
446-569 |
2.27e-03 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 41.80 E-value: 2.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 446 LNKTQLRLKRARRYGICGPNGCGKSTLMRAIA------NGQVDgfpTQEECRTVYVEHDIDGTHSDTSVLDFVFESGVGT 519
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAgvtmpnKGTVD---IKGSAALIAISSGLNGQLTGIENIELKGLMMGLT 116
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 6323278 520 KEAIKD---KLIEFGFTDEMIAMPISALSGGWKMKLALARAVLRNADILLLDE 569
Cdd:PRK13545 117 KEKIKEiipEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDE 169
|
|
| RsgA_GTPase |
pfam03193 |
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ... |
693-725 |
2.33e-03 |
|
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are broadly conserved in bacteria and are indispensable for growth. The GTPase domain of RsgA is very similar to several P-loop GTPases, but differs in having a circular permutation of the GTPase structure described by a G4-G1-G3 pattern.
Pssm-ID: 427191 [Multi-domain] Cd Length: 174 Bit Score: 40.22 E-value: 2.33e-03
10 20 30
....*....|....*....|....*....|....
gi 6323278 693 LSSRIAV-IGPNGAGKSTLINVLTGELLPTSGEV 725
Cdd:pfam03193 104 LKGKTTVlAGQSGVGKSTLLNALLPELDLRTGEI 137
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
544-633 |
2.33e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 42.03 E-value: 2.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 544 LSGGWKMKLALARAVLRNADILLLDEPTNHLDTvNVAWLVnyLNTC------GITSITISHDSVFLDNVCEYIINYEGLK 617
Cdd:PLN03130 741 ISGGQKQRVSMARAVYSNSDVYIFDDPLSALDA-HVGRQV--FDKCikdelrGKTRVLVTNQLHFLSQVDRIILVHEGMI 817
|
90
....*....|....*.
gi 6323278 618 lrKYKGNFTEFVKKCP 633
Cdd:PLN03130 818 --KEEGTYEELSNNGP 831
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
520-599 |
2.41e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 40.89 E-value: 2.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 520 KEAIKDKLIEFGFTDEMIAMPiSALSGGWKMKLALARAVLRNADILLLDEPTNHLD---TVNVAWLVNYLN-TCGITSIT 595
Cdd:PRK13648 120 HRRVSEALKQVDMLERADYEP-NALSGGQKQRVAIAGVLALNPSVIILDEATSMLDpdaRQNLLDLVRKVKsEHNITIIS 198
|
....
gi 6323278 596 ISHD 599
Cdd:PRK13648 199 ITHD 202
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
693-725 |
2.92e-03 |
|
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 40.07 E-value: 2.92e-03
10 20 30
....*....|....*....|....*....|....
gi 6323278 693 LSSRIAV-IGPNGAGKSTLINVLTGELLPTSGEV 725
Cdd:cd01854 83 LKGKTSVlVGQSGVGKSTLLNALLPELVLATGEI 116
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
897-952 |
2.95e-03 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 40.60 E-value: 2.95e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 6323278 897 LSGGQKVKLVLAAGTWQRPHLIVLDEPTNYLDRDSLGALSKALKEF--EGGVIIITHS 952
Cdd:PRK14267 150 LSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELkkEYTIVLVTHS 207
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
538-597 |
2.97e-03 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 41.45 E-value: 2.97e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6323278 538 AMPISALSGGWKMKLALARAVLRNADILLLDEPTNHLDtVNVAW----LVNYLNTCGITSITIS 597
Cdd:PRK13549 400 ELAIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGID-VGAKYeiykLINQLVQQGVAIIVIS 462
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
693-733 |
3.18e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 39.85 E-value: 3.18e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 6323278 693 LSSRIAVI-GPNGAGKSTLINVLTGELLPTSGEVYTHeNCRI 733
Cdd:PRK13541 24 LPSAITYIkGANGCGKSSLLRMIAGIMQPSSGNIYYK-NCNI 64
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
913-966 |
3.25e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 41.07 E-value: 3.25e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 6323278 913 QRPHLIVLDEPTNYLDRDSLGALSKALKEF--EGGVIIITHSAEFTKNLT-EEVWAV 966
Cdd:COG4637 277 RPPPLLCIEEPENGLHPDLLPALAELLREAseRTQVIVTTHSPALLDALEpEEVLVL 333
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
678-733 |
3.44e-03 |
|
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: 40.11 E-value: 3.44e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6323278 678 GTSKPQITDINF-----QCslssrIAVIGPNGAGKSTLINVLTGELLPTSGEV-YTHENCRI 733
Cdd:COG4778 21 GKRLPVLDGVSFsvaagEC-----VALTGPSGAGKSTLLKCIYGNYLPDSGSIlVRHDGGWV 77
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
698-725 |
3.52e-03 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 40.83 E-value: 3.52e-03
10 20 30
....*....|....*....|....*....|
gi 6323278 698 AVIGPNGAGKSTLINVLTgeLL--PTSGEV 725
Cdd:COG1135 35 GIIGYSGAGKSTLIRCIN--LLerPTSGSV 62
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
667-744 |
3.76e-03 |
|
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: 40.40 E-value: 3.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 667 VKVTNMEFQYPGTskPQITDINFQCSLSSRIAVIGPNGAGKSTLINVLTGELLPTSGEVY------THENCR---IAYIK 737
Cdd:cd03296 3 IEVRNVSKRFGDF--VALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILfggedaTDVPVQernVGFVF 80
|
....*....
gi 6323278 738 QH--AFAHI 744
Cdd:cd03296 81 QHyaLFRHM 89
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
677-716 |
3.82e-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: 39.53 E-value: 3.82e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 6323278 677 PGTSKPQITDINFQCSLSSRIAVIGPNGAGKSTLINVLTG 716
Cdd:cd03232 16 KGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAG 55
|
|
| PRK00093 |
PRK00093 |
GTP-binding protein Der; Reviewed |
696-717 |
4.10e-03 |
|
GTP-binding protein Der; Reviewed
Pssm-ID: 234628 [Multi-domain] Cd Length: 435 Bit Score: 40.80 E-value: 4.10e-03
10 20
....*....|....*....|...
gi 6323278 696 RIAVIG-PNgAGKSTLINVLTGE 717
Cdd:PRK00093 175 KIAIIGrPN-VGKSSLINALLGE 196
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
686-726 |
4.78e-03 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 39.98 E-value: 4.78e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 6323278 686 DINFQCSLSSRIAVIGPNGAGKSTLINVLTGELLPTSGEVY 726
Cdd:COG1126 19 GISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIT 59
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
891-970 |
5.29e-03 |
|
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: 39.44 E-value: 5.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 891 HSRIRGLSGGQKVKLVLAAGTWQRPHLIVLDEPTNYLD----RDSLGALsKALKEfEG-GVIIITHSAEFTKNLTEEVWA 965
Cdd:cd03262 130 DAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDpelvGEVLDVM-KDLAE-EGmTMVVVTHEMGFAREVADRVIF 207
|
....*
gi 6323278 966 VKDGR 970
Cdd:cd03262 208 MDDGR 212
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
534-631 |
5.52e-03 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 40.07 E-value: 5.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 534 DEMIAM---------PISALSGGWKMKLALARAVLRNADILLLDEPTNHLDtVNV-----AWLVNYLNTCGITSITISHD 599
Cdd:COG4586 136 DELVELldlgelldtPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLD-VVSkeairEFLKEYNRERGTTILLTSHD 214
|
90 100 110
....*....|....*....|....*....|....
gi 6323278 600 SVFLDNVCE--YIINyEGLKLrkYKGNFTEFVKK 631
Cdd:COG4586 215 MDDIEALCDrvIVID-HGRII--YDGSLEELKER 245
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
446-609 |
5.59e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 39.83 E-value: 5.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 446 LNKTQLRLKRARRYGICGPNGCGKSTLMRAI------ANGQV--DGFPTQEECRTVY--------VEHDIDGTHSDTSVL 509
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLngilkpSSGRIlfDGKPIDYSRKGLMklresvgmVFQDPDNQLFSASVY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 510 DFV----FESGVGTKEAIK--DKLIEFGFTDEMIAMPISALSGGWKMKLALARAVLRNADILLLDEPTNHLDTVNVA--- 580
Cdd:PRK13636 102 QDVsfgaVNLKLPEDEVRKrvDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSeim 181
|
170 180 190
....*....|....*....|....*....|
gi 6323278 581 -WLVNYLNTCGITSITISHDsvfLDNVCEY 609
Cdd:PRK13636 182 kLLVEMQKELGLTIIIATHD---IDIVPLY 208
|
|
| EngA2 |
cd01895 |
EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second ... |
696-717 |
5.98e-03 |
|
EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second GTPase domain of EngA and its orthologs, which are composed of two adjacent GTPase domains. Since the sequences of the two domains are more similar to each other than to other GTPases, it is likely that an ancient gene duplication, rather than a fusion of evolutionarily distinct GTPases, gave rise to this family. Although the exact function of these proteins has not been elucidated, studies have revealed that the E. coli EngA homolog, Der, and Neisseria gonorrhoeae EngA are essential for cell viability. A recent report suggests that E. coli Der functions in ribosome assembly and stability.
Pssm-ID: 206682 [Multi-domain] Cd Length: 174 Bit Score: 38.95 E-value: 5.98e-03
10 20
....*....|....*....|...
gi 6323278 696 RIAVIG-PNgAGKSTLINVLTGE 717
Cdd:cd01895 4 KIAIIGrPN-VGKSSLLNALLGE 25
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
684-728 |
6.20e-03 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 39.80 E-value: 6.20e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 6323278 684 ITDINFQCSLSSRIAVIGPNGAGKSTLINVLTGELLPTSGEVYTH 728
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRN 84
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
436-575 |
6.85e-03 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 39.78 E-value: 6.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 436 FSLAYGAKILLNKTQLRLKRARRYGICGPNGCGKSTLMRAI------ANGQ--VDG-----FPTQE-------------- 488
Cdd:PRK11153 11 FPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCInllerpTSGRvlVDGqdltaLSEKElrkarrqigmifqh 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 489 ----ECRTVY------VEhdIDGThsdtsvldfvfesgvgTKEAIKDKLIEF----GFTDEMIAMPiSALSGGWKMKLAL 554
Cdd:PRK11153 91 fnllSSRTVFdnvalpLE--LAGT----------------PKAEIKARVTELlelvGLSDKADRYP-AQLSGGQKQRVAI 151
|
170 180
....*....|....*....|.
gi 6323278 555 ARAVLRNADILLLDEPTNHLD 575
Cdd:PRK11153 152 ARALASNPKVLLCDEATSALD 172
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
885-951 |
7.49e-03 |
|
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: 38.93 E-value: 7.49e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6323278 885 DPEIVSHSRIRG----LSGGQKVKLVLAAGTWQRPHLIVLDEPTNYLDRDSLGALSKAL-KEFEGG-VIIITH 951
Cdd:cd03369 110 DEEIYGALRVSEgglnLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQKTIrEEFTNStILTIAH 182
|
|
| HolB |
COG0470 |
DNA polymerase III, delta prime subunit [Replication, recombination and repair]; |
446-573 |
7.67e-03 |
|
DNA polymerase III, delta prime subunit [Replication, recombination and repair];
Pssm-ID: 440238 [Multi-domain] Cd Length: 289 Bit Score: 39.57 E-value: 7.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 446 LNKTQLRLKRARRYG-------ICGPNGCGKSTLMRAIAN----GQVDGFPTQEECRTVYVEHdidGTHSDTSVLDFVFE 514
Cdd:COG0470 1 QEEAWEQLLAAAESGrlphallLHGPPGIGKTTLALALARdllcENPEGGKACGQCHSRLMAA---GNHPDLLELNPEEK 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6323278 515 SGVGTKEAIKDkLIEFgftdemiaMPISALSGGWK---------MKLALARAVLRnadilLLDEPTNH 573
Cdd:COG0470 78 SDQIGIDQIRE-LGEF--------LSLTPLEGGRKvviideadaMNEAAANALLK-----TLEEPPKN 131
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
461-520 |
7.98e-03 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 38.63 E-value: 7.98e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6323278 461 ICGPNGCGKSTLMRAIA---NGQVDGFPTQEECRTVYVEHDIDGTHSDTSVLDFVFESGVGTK 520
Cdd:pfam13476 23 ITGPNGSGKTTILDAIKlalYGKTSRLKRKSGGGFVKGDIRIGLEGKGKAYVEITFENNDGRY 85
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
461-601 |
8.20e-03 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 39.83 E-value: 8.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 461 ICGPNGCGKSTLMRAIA------------NGQVdgfPTQEECRtvyvEHDIdgthsdtsvlDFVFES------------- 515
Cdd:PRK11650 35 LVGPSGCGKSTLLRMVAgleritsgeiwiGGRV---VNELEPA----DRDI----------AMVFQNyalyphmsvrenm 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 516 -------GVGtKEAIKD------KLIEFGftdEMIAMPISALSGGWKMKLALARAVLRNADILLLDEPTNHLDT------ 576
Cdd:PRK11650 98 ayglkirGMP-KAEIEErvaeaaRILELE---PLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAklrvqm 173
|
170 180
....*....|....*....|....*.
gi 6323278 577 -VNVAWLVNYLNTcgiTSITISHDSV 601
Cdd:PRK11650 174 rLEIQRLHRRLKT---TSLYVTHDQV 196
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
701-726 |
8.57e-03 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 39.24 E-value: 8.57e-03
10 20
....*....|....*....|....*.
gi 6323278 701 GPNGAGKSTLINVLTGELLPTSGEVY 726
Cdd:COG1137 36 GPNGAGKTTTFYMIVGLVKPDSGRIF 61
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
460-569 |
9.08e-03 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 39.03 E-value: 9.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323278 460 GICGPNGCGKSTLMRAIA------NGQVDgfpTQEECRTVYVEHDIDGTHSDTSVLDF-VFESGVGTKE--AIKDKLIEF 530
Cdd:PRK13546 54 GLVGINGSGKSTLSNIIGgslsptVGKVD---RNGEVSVIAISAGLSGQLTGIENIEFkMLCMGFKRKEikAMTPKIIEF 130
|
90 100 110
....*....|....*....|....*....|....*....
gi 6323278 531 GFTDEMIAMPISALSGGWKMKLALARAVLRNADILLLDE 569
Cdd:PRK13546 131 SELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDE 169
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
697-726 |
9.78e-03 |
|
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: 38.68 E-value: 9.78e-03
10 20 30
....*....|....*....|....*....|
gi 6323278 697 IAVIGPNGAGKSTLINVLTGELLPTSGEVY 726
Cdd:cd03218 29 VGLLGPNGAGKTTTFYMIVGLVKPDSGKIL 58
|
|
| |
