ID E9AQ74_LEIMU Unreviewed; 2679 AA.
AC E9AQ74;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE SubName: Full=ABC1 transporter-like protein {ECO:0000313|EMBL:CBZ25093.1};
GN ORFNames=LMXM_15_0760 {ECO:0000313|EMBL:CBZ25093.1};
OS Leishmania mexicana (strain MHOM/GT/2001/U1103).
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX NCBI_TaxID=929439 {ECO:0000313|EMBL:CBZ25093.1, ECO:0000313|Proteomes:UP000007259};
RN [1] {ECO:0000313|Proteomes:UP000007259}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MHOM/GT/2001/U1103 {ECO:0000313|Proteomes:UP000007259};
RX PubMed=22038252; DOI=10.1101/gr.122945.111;
RA Rogers M.B., Hilley J.D., Dickens N.J., Wilkes J., Bates P.A.,
RA Depledge D.P., Harris D., Her Y., Herzyk P., Imamura H., Otto T.D.,
RA Sanders M., Seeger K., Dujardin J.C., Berriman M., Smith D.F.,
RA Hertz-Fowler C., Mottram J.C.;
RT "Chromosome and gene copy number variation allow major structural change
RT between species and strains of Leishmania.";
RL Genome Res. 21:2129-2142(2011).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; FR799568; CBZ25093.1; -; Genomic_DNA.
DR RefSeq; XP_003873601.1; XM_003873552.1.
DR GeneID; 13449809; -.
DR KEGG; lmi:LMXM_15_0760; -.
DR VEuPathDB; TriTrypDB:LmxM.15.0760; -.
DR OMA; SWNMYRG; -.
DR OrthoDB; 6951at2759; -.
DR PhylomeDB; E9AQ74; -.
DR Proteomes; UP000007259; Chromosome 15.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0004601; F:peroxidase activity; IEA:InterPro.
DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR CDD; cd03263; ABC_subfamily_A; 2.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR013525; ABC2_TM.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR026082; ABCA.
DR InterPro; IPR002016; Haem_peroxidase.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR19229; ATP-BINDING CASSETTE TRANSPORTER SUBFAMILY A ABCA; 1.
DR PANTHER; PTHR19229:SF266; TRANSPORTER, PUTATIVE-RELATED; 1.
DR Pfam; PF12698; ABC2_membrane_3; 2.
DR Pfam; PF00005; ABC_tran; 2.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 2.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
DR PROSITE; PS50873; PEROXIDASE_4; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 178..201
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 505..527
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 555..583
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 589..613
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 620..638
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 644..666
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 687..707
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1453..1472
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1637..1659
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1679..1706
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1718..1739
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1751..1774
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 794..1027
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT DOMAIN 2119..2396
FT /note="Plant heme peroxidase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50873"
FT DOMAIN 2125..2356
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 746..786
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1142..1167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1188..1280
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1313..1333
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1347..1395
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1909..1944
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2090..2116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2363..2415
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2556..2633
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2651..2679
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 757..772
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1248..1262
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2100..2114
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2388..2415
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2560..2602
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2661..2679
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2679 AA; 291486 MW; 643553DEF059B1D3 CRC64;
MQPTTKGSRV AATRQSDGGV KTDAVAVAAA SPGASPSPPL QNYAFPTVEE LVSPAAPFRS
SKSEDVLELE TPSPVAAAAR QPPAAAVRRA SRVRFSLASE QFFEPPLPPP SDGLWNRADG
DLASFGHGNE LHRTLSVSAT RLEPYSVITK TGGVHISRWT QVLALLQRTG QQYTRQKLLI
IAEVVSPLLF VVLLIILNVA FGTDSIPETV FTAPTVYSYQ LNLHDYMTYI CYNDTTRPIN
GLHPCTHLQV PYSCDGDESD IPVYGLCYLS SFKKPAAVVK QYVDSFMGVI ISLPSLDSII
VHQWMAKKAG LAKDSRSRTA LAALSNVGIG LSATTRFDSI SYSGLLYFAP AANTPAALIE
YFHKHCATFG YVYGGVLDTV EEAHATIKAN GSDEVLNSTW GLIIVNDITD GFDVQVQLHS
SALPSLSSPT VSLEFRGGFT YDGTDMFLAS GFLSLQQMLY TYFYESRAEA GALPNLHSGA
VSPYTFKEIY PVISSYPTIA AHTPYLLSLS PSLVALVMVM SFLYPFAQVT KRVVLEKELS
IQESVCIMGL RRSSLWVNFL LVIFFEYVLI SILLTALLCA VVAPRSNPFA VFIILFVYSL
TLIPLCGLVS AFLSRARMAT LMTPLLYVVL STPIFAMATP SRGIVVGLSL LSPAALASLL
TDVFIVEAGG GFQIHHFMSP HFNAEPYLIM IILACDCVLY LLLMVYLNAV LPQEWGTRKH
PLFFIIEPWV WLKDTCGTCC SCPTNAPRGS ASEPVAGATG ATATSQKSQR PGSLAFDPRI
SRDASTDDKK DIGVRISHLC KYFQRNAKRF AAVDNVSWNM YRGEIAVLLG PNGAGKSTAI
KMITGILAAD SGDCFIEGYS ITQNVAEARH EIGYCPQHNI LWPDLTCREH LEFYGKIKGL
RGAELEDAVV DILRAVDLEE KVDAIPGQMS GGQKRKLSVA IAFVGRNRVV LLDEPTAGMD
AAARRHTWCL LRAMTQHHTI LLTTHFMDEA DLLGDNIAIV TEGVLQCAGS TAFLRQYAGV
GYTLRFDLSP VPTQKDGDAA RQPRVAAVWA KLHQLVMSHL PDSTLVLQTD AEVEYELRLG
TDARLPGFLK DMESRGNQQL HIRGYALRAP TLENVFMRVV EHQIAPSPQV AVVRAADEAV
AREQVDGKKD GGRTNSGPPT APSSPLVHHF MSRRMSRASL HYLNNESTLN YGNNAEPGDG
DEDPIPDFAA ASPTQHQTPS DVVGARSMAA AGPDGGNAGG VHVAGVAENN NASVTGLRQR
ESRSRSPNYH ESAEGPPSLS AQFPQEVVGL EDFCAAANRS LAGAAPSVRR TTTAALTAQQ
HQGSTTTGVS DSDIPGVATV AARVRRPDRA PCPPLSEAMV SESHARTSAV SAPSNAAPVP
AAAPPPAPAA TAAGTNPSVR SEAFLYKLVT DHHLTKVWES RQTSQRWHLW GLQLRGMMYK
RFLCAIRDPR MHFFQIICPI LCILLVMSLQ LVKGGGDEGR LYLSPSVFGV ESAMQVSGCT
NYMGDVAHMH KYGHNFSTLS FSDPNFVSST DMSSELLDTW FTHSRNRFMS LQCGDPDVEL
YLTFFYPNVI GTRQVNTLLY NTSSRNSLPI AMHIMHAMAY FGALGTSTDA AAATYTMTLA
GLPQDAKATQ ATSAISSILI GTIFLIPFTF LPANPVAWVA KEYESRARHL QTASGLLYLV
YWIGNFLFDF TAYVVSMLFI VVTFLIFQRW EYVGCEAIGA TIASFSIYGI CYCWCSYMVS
FAFTEHTTAQ IVVLGVSFLT GFLCVMLVFV LSLLEKTLSA SNALRWVFRL LPPYSIGEVI
LNLALLEQKK VTDPSLTAWS MSITGWPDIY MAVEAPIFAA ITLLWDHPNR RSVIDQLSVW
WAARWCRCCG GSGFWRRHRT QKTDQQGRRA TMPGAVAVTV DDTSATPISA AAASPRSSPP
NALSPIRRSH DNGSPTVGGN GTAEVAPTET SVLMQGPPLR AKVIVPDTYR SPHKQWGEEP
VGSNASPFPM TPISSADANV GGGVVGLAGP TLMGVTGAQQ SQQQLMSGQP VSDRANGPTL
PEMVYPPPRW YMAEVLRRRQ EEEDSDVEEE RGAVYQAEQQ HLAEQEALSI RAASSRHHSP
QQKGSDKEEK CQQQTEPTVE SCDAVRLVDL HKVYHAPRKV AVRALTLSVM HGEVFGFLGT
NGAGKSSALA IITQEQLPTS GRAYVCGNDV VRESRRAARS LGYCPQFDAC LDLLTVTEHL
RLYAIVRGVP VGQLESLATS LLIICNLTQY RHVSARQLSG GNRRRLSVAI ALIGAPKVLC
LDEPTSGMDP LARQLLWRAI DRVSRKCCIL LTTHHLDEVE ALADCVGIMV DGGLRCFGDM
PHLKHKYASN AYELTLRVSP GARRCAQKRR EEQRQRTTAE AGVSPVADLQ RSSPSTPHGL
SNKNQGGTIN SALGRRTSTS YAGNDLIDTS DDIFQFMLKA FPSALLIDVF NNERYIYTLP
ATPDVANAMQ QLLQQQQSRC SMQLVQTPLV SAKNYVGQHS ATNAPKTLPP IVRLSEVFET
LRAAQAELGI TEYSVSQVSL EQVFLRVCSA EETLNQDRRH NRATTTSPTS QSTTFVVNSN
TSSSATPHAH LLQRQGSRAS FIARSSPAAM RDSGASPSRR RLSMPSYGNL PGATAAPRVT
FAEYRRQRAL GGLRTEAAEP HLTTAKQQRA AQPDHESTP
//
