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Database: UniProt
Entry: L0BDL8_9ASPA
LinkDB: L0BDL8_9ASPA
Original site: L0BDL8_9ASPA 
ID   L0BDL8_9ASPA            Unreviewed;       714 AA.
AC   L0BDL8;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   22-FEB-2023, entry version 20.
DE   RecName: Full=Protein TIC 214 {ECO:0000256|RuleBase:RU364085};
DE   AltName: Full=Translocon at the inner envelope membrane of chloroplasts 214 {ECO:0000256|RuleBase:RU364085};
DE   Flags: Fragment;
GN   Name=ycf1 {ECO:0000313|EMBL:AFZ85925.1};
GN   Synonyms=TIC214 {ECO:0000256|RuleBase:RU364085};
OS   Zephyranthes immaculata.
OG   Plastid; Chloroplast {ECO:0000313|EMBL:AFZ85925.1}.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Asparagales; Amaryllidaceae;
OC   Amaryllidoideae; Hippeastreae; Zephyranthes;
OC   Zephyranthes subgen. Habranthus.
OX   NCBI_TaxID=146428 {ECO:0000313|EMBL:AFZ85925.1};
RN   [1] {ECO:0000313|EMBL:AFZ85925.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Garcia N., Meerow A.W., Soltis D.E., Soltis P.S.;
RT   "Testing Deep Reticulate Evolution in Amaryllidaceae Tribe Hippeastreae
RT   (Asparagales) with ITS and Chloroplast Sequence Data.";
RL   Syst. Bot. 39:75-89(2014).
CC   -!- FUNCTION: Involved in protein precursor import into chloroplasts. May
CC       be part of an intermediate translocation complex acting as a protein-
CC       conducting channel at the inner envelope.
CC       {ECO:0000256|RuleBase:RU364085}.
CC   -!- SUBUNIT: Part of the Tic complex. {ECO:0000256|RuleBase:RU364085}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast inner membrane
CC       {ECO:0000256|RuleBase:RU364085}.
CC   -!- SIMILARITY: Belongs to the TIC214 family.
CC       {ECO:0000256|RuleBase:RU364085}.
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DR   EMBL; KC207496; AFZ85925.1; -; Genomic_DNA.
DR   AlphaFoldDB; L0BDL8; -.
DR   GO; GO:0009706; C:chloroplast inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   InterPro; IPR008896; TIC214.
DR   PANTHER; PTHR33163:SF40; PROTEIN TIC 214; 1.
DR   PANTHER; PTHR33163; PROTEIN TIC 214-RELATED; 1.
DR   Pfam; PF05758; Ycf1; 1.
PE   3: Inferred from homology;
KW   Chloroplast {ECO:0000256|RuleBase:RU364085, ECO:0000313|EMBL:AFZ85925.1};
KW   Membrane {ECO:0000256|RuleBase:RU364085};
KW   Plastid {ECO:0000256|RuleBase:RU364085, ECO:0000313|EMBL:AFZ85925.1};
KW   Plastid inner membrane {ECO:0000256|RuleBase:RU364085};
KW   Protein transport {ECO:0000256|RuleBase:RU364085};
KW   Transport {ECO:0000256|RuleBase:RU364085}.
FT   REGION          13..39
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        13..37
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AFZ85925.1"
FT   NON_TER         714
FT                   /evidence="ECO:0000313|EMBL:AFZ85925.1"
SQ   SEQUENCE   714 AA;  85864 MW;  8968CC4CFF7A0C0A CRC64;
     EIRSRKGKRV VIYTDNDQST NSRASNNTTN NTNTSDEEEE VALIRYSQQS DFRRGIIKGS
     MRAQRRKTVT WKIFQANVHS PLFLDRIDKI FFFSFFDISE TINLVFRNWV GEPPELQISY
     FDEEEETKEK EKTNEEKEGE SERIAISEAW DTFIFTQAIR GFMLVTQSFL RKYVTLPLLI
     IAKNIGRMLL LQFPEWYEDL KEWNREMHVK CTYNGVQLSE TEFPQNWLTD GIQIKILFPF
     CLKPWRRSKI RSHHRDQQMT KKEKKDHFCF LTVWGREAEL PFGSPRKRPS FFEPILKELK
     KKMIRLKKKI FQLIRVFKER KKRFLKVSKE KTRWVAKIVL VINLIMKELE KRNRFFLSKL
     RKVEVYESNE NGKDSNINNK IIRESTIRIR STSCVNENYS LIEKKMKDLA NKTTTIRTQI
     EGITKDKKKI VLNKKSESQK DFWQKFKRKN IRLIRKSYYF MKSFIEKIYT DILLCIIKIP
     RINAQLFFEL TKKIINKSIF TNETNQEGIE NTNQNTMNFI STIKKSFSNT NINNNSYWDL
     SSLSQAYVFY KLSQNQLLNK YRLRSVLQHH GTYSFLKDII KNYCTTRGIF YSKSRHKKID
     KYGMNKWKIW LRGHYQYNFS QTKWSHLVAK KWRNRVNQCR MIQKKNSMKL DLYKKEKDQL
     IHYMKENYYA VDSLMSQKDK LKKHYGYDLL SYKYIYYGDS KDSYISGSAL QVED
//
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