ID   YCF2_OENPI              Reviewed;         721 AA.
AC   P31568;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   03-AUG-2022, entry version 62.
DE   RecName: Full=Protein Ycf2;
DE   Flags: Fragment;
GN   Name=ycf2;
OS   Oenothera picensis (Evening primrose).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Myrtales; Onagraceae; Onagroideae; Onagreae; Oenothera.
OX   NCBI_TaxID=3946;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8435856; DOI=10.1007/bf00351505;
RA   Nimzyk R., Schoendorf T., Hachtel W.;
RT   "In-frame length mutations associated with short tandem repeats are located
RT   in unassigned open reading frames of Oenothera chloroplast DNA.";
RL   Curr. Genet. 23:265-270(1993).
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   -!- SIMILARITY: Belongs to the Ycf2 family. {ECO:0000305}.
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DR   EMBL; X64616; CAA45898.1; -; Genomic_DNA.
DR   PIR; S29795; S29795.
DR   AlphaFoldDB; P31568; -.
DR   GO; GO:0009570; C:chloroplast stroma; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   Gene3D; 2.150.10.10; -; 1.
DR   InterPro; IPR011049; Serralysin-like_metalloprot_C.
PE   3: Inferred from homology;
KW   ATP-binding; Chloroplast; Nucleotide-binding; Plastid.
FT   CHAIN           <1..721
FT                   /note="Protein Ycf2"
FT                   /id="PRO_0000223061"
FT   REGION          176..424
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          492..592
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        184..407
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        492..589
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         174..181
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   NON_TER         1
SQ   SEQUENCE   721 AA;  82900 MW;  279A3FC1AA06F9C9 CRC64;
     EFESTILGPS VPDLVALTNE ALSISITQKK SIIDTTTIRY ALHRKTWDLE ADRNLSPAKE
     HGTLFYQVGR AFAHTVLLRN CSIDPISIYI KKNLCEAGDS SLYKWYFELG TSMKKLTILL
     YLLTCSAGSI AQDLLSPPGP DEQNLITSYG LVENDSDLVH GLSDIVHGLL ELEGALVGSS
     PTEEEVEGTE EEVEGTEEEV EGTEEEVEGT EDEEVEGTEE EVEGTEEEVE GTEEEVEGTE
     EEVEGTEDEE VEGTEDEEVE GTEEEVEGTE EEVEGTEEEV EGTEEEVEGT EDEEVEGTEE
     EVEGTEEEVE GTEDEEVEGT EEEVEGTEEE VEGTEDEEVE GTEEEVEGTE EEVEGTEEEV
     EGTEEEVEGT EEEVEGTEEE VEGTEEEVEG TEEEVEGTED EEVEGTEKDS SQFDNDRVTL
     LLRPKPRNPL DIQRLIYQHQ KYESELEEDD DDDEDVFAPQ KMLEDLFSEL VWSPRIWHPW
     DFLLDCEAEI PAEEIPEEED ELPEDALETE VAVWGVEEEG EADDEEDVLL EAQQEDELLE
     EEDEELDEEE DELDEEEEEP KEEEDELHEE EEEEEEEEEE EEEDELQEND SEFFRVKPII
     PRHRWIFRKK KDVFEVLSYP EEATEISKEL LRLLNPKTKR DAPKRPRQRW WTKKKQDKHY
     ELLLDRQRWL ITKRSLSKSN GFFRSNTPSE SYQYLSNLFL SNRRLLDQMT KTFFRKMAFP
     G