ID A0AA88R807_9ASTE Unreviewed; 340 AA.
AC A0AA88R807;
DT 27-MAR-2024, integrated into UniProtKB/TrEMBL.
DT 27-MAR-2024, sequence version 1.
DT 28-JAN-2026, entry version 9.
DE RecName: Full=Protein TIC 20 {ECO:0000256|RuleBase:RU367003};
GN ORFNames=RJ640_015901 {ECO:0000313|EMBL:KAK2976925.1};
OS Escallonia rubra.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Escalloniales; Escalloniaceae; Escallonia.
OX NCBI_TaxID=112253 {ECO:0000313|EMBL:KAK2976925.1, ECO:0000313|Proteomes:UP001187471};
RN [1] {ECO:0000313|EMBL:KAK2976925.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=UCBG92.1500 {ECO:0000313|EMBL:KAK2976925.1};
RC TISSUE=Leaf {ECO:0000313|EMBL:KAK2976925.1};
RA Chanderbali A., Dervinis C., Anghel I., Soltis D., Soltis P., Zapata F.;
RT "Draft genome assemblies for two species of Escallonia (Escalloniales).";
RL Submitted (DEC-2022) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in protein precursor import into chloroplasts.
CC {ECO:0000256|RuleBase:RU367003}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}. Plastid,
CC chloroplast inner membrane {ECO:0000256|ARBA:ARBA00004478}; Multi-pass
CC membrane protein {ECO:0000256|ARBA:ARBA00004478}. Plastid, chloroplast
CC membrane {ECO:0000256|RuleBase:RU367003}; Multi-pass membrane protein
CC {ECO:0000256|RuleBase:RU367003}.
CC -!- SIMILARITY: Belongs to the Tic20 family.
CC {ECO:0000256|ARBA:ARBA00009596, ECO:0000256|RuleBase:RU367003}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|RuleBase:RU367003}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KAK2976925.1}.
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DR EMBL; JAVXUO010002025; KAK2976925.1; -; Genomic_DNA.
DR AlphaFoldDB; A0AA88R807; -.
DR Proteomes; UP001187471; Unassembled WGS sequence.
DR GO; GO:0009706; C:chloroplast inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR Gene3D; 2.40.330.10; DNA-binding pseudobarrel domain; 1.
DR InterPro; IPR015300; DNA-bd_pseudobarrel_sf.
DR InterPro; IPR005691; Tic20.
DR PANTHER; PTHR36264; SET DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR36264:SF5; SET DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF16166; TIC20; 1.
PE 3: Inferred from homology;
KW Chloroplast {ECO:0000256|RuleBase:RU367003};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU367003};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Plastid {ECO:0000256|RuleBase:RU367003};
KW Plastid inner membrane {ECO:0000256|ARBA:ARBA00022780};
KW Reference proteome {ECO:0000313|Proteomes:UP001187471};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU367003};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU367003}.
FT TRANSMEM 182..202
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367003"
FT TRANSMEM 264..284
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367003"
FT TRANSMEM 290..312
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367003"
SQ SEQUENCE 340 AA; 39508 MW; 0D4319E100969C90 CRC64;
MKKILFYSFI PTKSEEEAAK ASNTQFKASR ALVEIRDLSP PPPPPDPNHP WQIRKRLTAS
DVAHRRLALS HNDTFDHIFR YWTTDMVNYV LMGTKAPVVL WDITDENHPL RYRTENIYLE
RGSSDEFYVL GWMDLISNRL VNPGDEIGLY WDVRSGTLQF KWTDRVILTE QKLVNPLKFH
EFIYLVQNIL LEKILFSSIF LLRQYKDCNM FGLKAQTMVS ENMILSGCSM KSGVGCMSYK
PDTFRFFSSA GVVKRKEWPH FFRFHVIMGM LLEIVMQVVM YARMSIPPAF YWGKVGMHLF
SAFTYAYLFT ALECTRCSLA GMHAEVPFLC DAACIQISYE
//
