ID W7K4H6_PLAFO Unreviewed; 1654 AA.
AC W7K4H6;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=ATP synthase F1 complex delta/epsilon subunit N-terminal domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=PFNF54_03507 {ECO:0000313|EMBL:EWC87700.1};
OS Plasmodium falciparum (isolate NF54).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX NCBI_TaxID=5843 {ECO:0000313|EMBL:EWC87700.1, ECO:0000313|Proteomes:UP000030673};
RN [1] {ECO:0000313|EMBL:EWC87700.1, ECO:0000313|Proteomes:UP000030673}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NF54 {ECO:0000313|EMBL:EWC87700.1,
RC ECO:0000313|Proteomes:UP000030673};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Neafsey D., Cheeseman I., Volkman S., Adams J., Walker B., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A.,
RA Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Plasmodium falciparum NF54.";
RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
CC -!- SIMILARITY: Belongs to the ATPase epsilon chain family.
CC {ECO:0000256|ARBA:ARBA00005712}.
CC -!- SIMILARITY: Belongs to the apicomplexan parasites AMA1 family.
CC {ECO:0000256|ARBA:ARBA00007098}.
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DR EMBL; KE123838; EWC87700.1; -; Genomic_DNA.
DR EnsemblProtists; EWC87700; EWC87700; PFNF54_03507.
DR OMA; KCPPRFP; -.
DR Proteomes; UP000030673; Unassembled WGS sequence.
DR GO; GO:0045261; C:proton-transporting ATP synthase complex, catalytic core F(1); IEA:InterPro.
DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:InterPro.
DR CDD; cd12152; F1-ATPase_delta; 1.
DR Gene3D; 1.10.1740.170; Erythrocyte binding antigen 175 region VI; 1.
DR Gene3D; 2.60.15.10; F0F1 ATP synthase delta/epsilon subunit, N-terminal; 1.
DR Gene3D; 3.50.4.10; Hepatocyte Growth Factor; 2.
DR InterPro; IPR003298; Apmem_Ag1.
DR InterPro; IPR001469; ATP_synth_F1_dsu/esu.
DR InterPro; IPR020546; ATP_synth_F1_dsu/esu_N.
DR InterPro; IPR036771; ATPsynth_dsu/esu_N.
DR InterPro; IPR021620; EBA-175_C.
DR InterPro; IPR043057; EBA-175_C_sf.
DR PANTHER; PTHR21024:SF0; ELECTRON TRANSFER FLAVOPROTEIN REGULATORY FACTOR 1; 1.
DR PANTHER; PTHR21024; GROWTH HORMONE-INDUCIBLE SOLUBLE PROTEIN-RELATED; 1.
DR Pfam; PF02430; AMA-1; 2.
DR Pfam; PF02823; ATP-synt_DE_N; 1.
DR Pfam; PF11556; EBA-175_VI; 1.
DR SUPFAM; SSF51344; Epsilon subunit of F1F0-ATP synthase N-terminal domain; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000030673};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT TRANSMEM 1587..1604
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 20..84
FT /note="ATP synthase F1 complex delta/epsilon subunit N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF02823"
FT DOMAIN 1501..1579
FT /note="Erythrocyte binding antigen 175 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11556"
FT REGION 1425..1445
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1303..1391
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1654 AA; 194261 MW; FBF6AFF58AC2E45F CRC64;
MFYRTRRIFF STAKNSNLYL SISSSSESIF RNQVIKRASF PGIEGYFTVT NNHSPLVTLL
RNGIITVEFD DKEKKQFFIS DGIFIYKKSN DNNSSNNAEI VGVEIVPLEY LDKNKTIKVL
QEMCAINDAT DDKWRKIKTL LGKELCSSIL QERDVLSEGN ESEKSTICPN HVKEGTYKLG
CPDYGKTFLM GFEDNKYSEE FLNEISFGFL NKKYKLPIEI PLNKSGLSMY QGLFKRCPYN
KKHYSMIKNE NEYDMCFRKF YNNSNISTRI YKRGKQNRKY IYFSSHGLGG RLGANIEEPL
HKYKNDEHYV TKKMRYPEKI KNLFDCSIYS HCIGPCLYKD FNNSCFLNLP ILFNHQTKEC
VIIGTHEEKR IHNCQSGSTD QNIQRCFLPV KKEKGNQWTY ASSFIRTDYM TKCPPRFPLN
HTMFGYFNYS TGKCETYYMN HEKRTLSFSK CIETLFNNIK KQDDVNNSSF LWGVWTIENN
ANEKTNLASM DNTGSCYFLK KKPTCVLKKE NHFSFTILTA NSFNLNQNII YPELKNNSSK
EGSSLIHFKD PKQTNKRVLY ENNKKSKRNV RTKINSVNPF TIPSTLNTNE KEEYNKNEVK
NYPNNNISYI QKVHSSFVNN RFNIHSDSSF KPIHKMIQMN IYTDNKLYNN NNQKIKDSNN
NMNGMSVTQR SPSIGENQNG NPQQKYMERF DIPNNHIFIE WQKEGEYGND EFKYNIISNK
TAGTSQSLFH NYKDKTCPNH VYEGRAHGSC PNYGKAIIVQ NLLGEEYDKN FNLNFLNEIR
TGYLNKYFKK DVEISYENSG IAMHNNMLRS CPVHENEEKL FSVKTDYNYK MCKSKIFSNR
FTMKEYDPKT RLFMYYGLYG LGGRLGANIK RDKQKEKKYE DNITLPMKNP SLIKNLFDCS
IYSYCLGPCL ENSFGNKCFR NLPAYYNHLT NECVILGTHE QERTNSCRRT KEEKKKPNCQ
ILRKTTDSKD WTYVSSFIRP DYETKCPPRY PLKSKVFGTF DQKTGKCKSL MDKAYEVGIN
KFSVCLEYLF LVSPKDLYNS GRNNYWGIWA ADHSVNENNI EIANGKCYHL VVKPTCVIDK
ENHFSFTALT ANTVDFNQSV NIRKIEELTE YGNNDDVLKE KEINNEPIDN VNETKINRKS
HVNSMERNKP SYKENEYDQM EKNVEDETYS EEFGLFEEAR KTETGRIEEE SKKKEAMKRA
EDARRIEEAR RAEDARRIEE ARRAEDARRV EIARRVEDAR RIEISRRAED AKRIEAARRA
IEVRRAELRK AEDARRIEAA RRYENERRIE EARRYEDEKR IEAVKRAEEV RKDEEEAKRA
EKERNNEEIR KFEEARMAHF ARRQAAIKAE EKKEKEAVIE EELKKEDEKR RMEVEKKIKD
TKDNFENIQE GNNKNTPYIN KEMFDSEIKE VVITKNMQLN EADAFEKHNS ENSKSSNKNA
DFSKEKDLLE DDIENILETD ENEKINKDDI ERSNNNMKGN NNDIIYTKLD VEEYKKRDVN
ETREKIIKIS KKNMCNNDFS SKYCDYMKDN ISSGTCSNEE RKSLCCSISD FCLKYFDHNS
NKYYDCTKIE FADPLYRCFK KKEFSNMVYF AGAGIVLILL FVIGSKMIIG KWFEEATFDE
MDLNYDKIYT LAMINNEETQ VSNPLSYSEE NIIK
//