ID   YCF2_MESVI              Reviewed;         890 AA.
AC   Q9MUP8;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 62.
DE   RecName: Full=Protein Ycf2;
DE            Short=RF2;
GN   Name=ycf2;
OS   Mesostigma viride (Green alga).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Mesostigmatophyceae;
OC   Mesostigmatales; Mesostigmataceae; Mesostigma.
OX   NCBI_TaxID=41882;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIES-296 / KY-14 / CCMP 2046;
RX   PubMed=10688199; DOI=10.1038/35001059;
RA   Lemieux C., Otis C., Turmel M.;
RT   "Ancestral chloroplast genome in Mesostigma viride reveals an early branch
RT   of green plant evolution.";
RL   Nature 403:649-652(2000).
CC   -!- FUNCTION: Probable ATPase of unknown function. Its presence in a non-
CC       photosynthetic plant (Epifagus virginiana) and experiments in tobacco
CC       indicate that it has an essential function which is probably not
CC       related to photosynthesis.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma {ECO:0000250}.
CC   -!- MISCELLANEOUS: The protein in this organism is about half the size it
CC       is in other chloroplasts.
CC   -!- SIMILARITY: Belongs to the Ycf2 family. {ECO:0000305}.
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DR   EMBL; AF166114; AAF43852.1; -; Genomic_DNA.
DR   RefSeq; NP_038412.1; NC_002186.1.
DR   AlphaFoldDB; Q9MUP8; -.
DR   SMR; Q9MUP8; -.
DR   PRIDE; Q9MUP8; -.
DR   GeneID; 800888; -.
DR   GO; GO:0009570; C:chloroplast stroma; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0004176; F:ATP-dependent peptidase activity; IEA:InterPro.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   Gene3D; 1.20.58.760; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR003960; ATPase_AAA_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR000642; Peptidase_M41.
DR   InterPro; IPR037219; Peptidase_M41-like.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF01434; Peptidase_M41; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF140990; SSF140990; 2.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS00674; AAA; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Chloroplast; Nucleotide-binding; Plastid.
FT   CHAIN           1..890
FT                   /note="Protein Ycf2"
FT                   /id="PRO_0000223058"
FT   BINDING         385..392
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   890 AA;  103936 MW;  43CAEEE991AF2C4B CRC64;
     MQQNHMSLSN MIKEVKEVFF HVPALLIPTR YREIYREIDR APKLLEQSFY TIFIKVWNIT
     EKVTVTDVFY YSSVEDPLGL QSPRHSRWAQ NTDEEQRKQA RIIIQSVYKP NSFIRITSNK
     FTRVLITSLF VLTYFQSNGV FQSFPYFESQ INGFLFKKMN NINQLEINST NTCIIKITDL
     LTHQKSKELL GNSLPTNSIL RWKMHSKISD IKTIFNMPEK WIYLPLGLGL ENSEQIFSYR
     NFDICNLTKN SSNIMKIKNN RTILDPKIDK YPLVLKNKEN ILFFHKLPIQ FFLFPYIVLR
     IWLAPVFVLW WSYQFNSEEK ENIKNNLKNI HDIEISTIQK FVAKAITFRD IGGMESLKQE
     LATVAFLLKQ KNYSNSYPMG YLFAGPPGTG KTLMAKAMSY EAETPYLYVE GSQFRCREEG
     VANARVDDLF KQIQNISPCI LYIDEIDSIA ERREEANKQL EQLKTIGDSI EGSNINIDQK
     PSDTVLMQFL IYMDGYKKRN DLIIIGATNR IETLDDAIMR PGRFDRQIVF SPPFFEERKD
     ILRIFLRNTK ALVDDTTKTM MAERSIGLNG CDLRLLADNI LLLSALESRN QQKTIPVINE
     DTFDRALERV SRIRHIISNY ELAFGKYDFY RTAYHEAGIA LIHTLLPECR PVYSVKLFPK
     PLNDRYLEIE RENLKVPSSD IISTNNIDYF VQKIVGLLAG RAAESILFDF YPGQISTYLN
     KTYDPNIQGA YNIAHHIVEF GLLDSVTGVI HYLNSENENN IKDPFVTKIN DLIQNKVTLK
     TNRELRKYSQ AASILDFNEF WYEQDYPWQF DFIKKQYIYS NESSRNLDME IVSILHTLFQ
     YTYDFLKSNE QLLDHLASLV LKNKSISQKE IHLVVNSYGI KIPTKTWKAW