ID   A4RXP4_OSTLU            Unreviewed;       492 AA.
AC   A4RXP4;
DT   15-MAY-2007, integrated into UniProtKB/TrEMBL.
DT   15-MAY-2007, sequence version 1.
DT   02-SEP-2026, entry version 114.
DE   RecName: Full=Glycoprotease 1 {ECO:0000256|HAMAP-Rule:MF_03179};
GN   Name=GCP1 {ECO:0000256|HAMAP-Rule:MF_03179};
GN   ORFNames=OSTLU_31766 {ECO:0000313|EMBL:ABO96086.1};
OS   Ostreococcus lucimarinus (strain CCE9901).
OC   Eukaryota; Viridiplantae; Chlorophyta; Mamiellophyceae; Mamiellales;
OC   Bathycoccaceae; Ostreococcus.
OX   NCBI_TaxID=436017 {ECO:0000313|EMBL:ABO96086.1, ECO:0000313|Proteomes:UP000001568};
RN   [1] {ECO:0000313|EMBL:ABO96086.1, ECO:0000313|Proteomes:UP000001568}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCE9901 {ECO:0000313|EMBL:ABO96086.1,
RC   ECO:0000313|Proteomes:UP000001568};
RX   PubMed=17460045; DOI=10.1073/pnas.0611046104;
RA   Palenik B., Grimwood J., Aerts A., Rouze P., Salamov A., Putnam N.,
RA   Dupont C., Jorgensen R., Derelle E., Rombauts S., Zhou K., Otillar R.,
RA   Merchant S.S., Podell S., Gaasterland T., Napoli C., Gendler K.,
RA   Manuell A., Tai V., Vallon O., Piganeau G., Jancek S., Heijde M.,
RA   Jabbari K., Bowler C., Lohr M., Robbens S., Werner G., Dubchak I.,
RA   Pazour G.J., Ren Q., Paulsen I., Delwiche C., Schmutz J., Rokhsar D.,
RA   Van de Peer Y., Moreau H., Grigoriev I.V.;
RT   "The tiny eukaryote Ostreococcus provides genomic insights into the paradox
RT   of plankton speciation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:7705-7710(2007).
CC   -!- FUNCTION: Required for the formation of a threonylcarbamoyl group on
CC       adenosine at position 37 (t(6)A37) in mitochondrial tRNAs that read
CC       codons beginning with adenine. Probably involved in the transfer of the
CC       threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6
CC       group of A37. Involved in mitochondrial genome maintenance.
CC       {ECO:0000256|HAMAP-Rule:MF_03179}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-threonylcarbamoyladenylate + adenosine(37) in tRNA = N(6)-L-
CC         threonylcarbamoyladenosine(37) in tRNA + AMP + H(+);
CC         Xref=Rhea:RHEA:37059, Rhea:RHEA-COMP:10162, Rhea:RHEA-COMP:10163,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:73682, ChEBI:CHEBI:74411,
CC         ChEBI:CHEBI:74418, ChEBI:CHEBI:456215; EC=2.3.1.234;
CC         Evidence={ECO:0000256|ARBA:ARBA00048117, ECO:0000256|HAMAP-
CC         Rule:MF_03179};
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_03179};
CC       Note=Binds 1 divalent metal cation per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_03179};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_03179}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03179}.
CC   -!- SIMILARITY: Belongs to the KAE1 / TsaD family. {ECO:0000256|HAMAP-
CC       Rule:MF_03179}.
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DR   EMBL; CP000585; ABO96086.1; -; Genomic_DNA.
DR   RefSeq; XP_001417793.1; XM_001417756.1.
DR   AlphaFoldDB; A4RXP4; -.
DR   STRING; 436017.A4RXP4; -.
DR   GeneID; 5002106; -.
DR   Gramene; ABO96086; ABO96086; OSTLU_31766.
DR   KEGG; olu:OSTLU_31766; -.
DR   eggNOG; KOG2707; Eukaryota.
DR   HOGENOM; CLU_023208_1_1_1; -.
DR   OMA; NAAMIGC; -.
DR   OrthoDB; 10259622at2759; -.
DR   Proteomes; UP000001568; Chromosome 5.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0061711; F:tRNA N(6)-L-threonylcarbamoyladenine synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0002949; P:tRNA threonylcarbamoyladenosine modification; IEA:UniProtKB-UniRule.
DR   CDD; cd24134; ASKHA_NBD_OSGEPL1_QRI7_euk; 1.
DR   FunFam; 3.30.420.40:FF:000012; tRNA N6-adenosine threonylcarbamoyltransferase; 1.
DR   Gene3D; 3.30.420.40; -; 2.
DR   HAMAP; MF_01445; TsaD; 1.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR000905; Gcp-like_dom.
DR   InterPro; IPR017861; KAE1/TsaD.
DR   InterPro; IPR022450; TsaD.
DR   NCBIfam; TIGR00329; gcp_kae1; 1.
DR   NCBIfam; TIGR03723; T6A_TsaD_YgjD; 1.
DR   PANTHER; PTHR11735; TRNA N6-ADENOSINE THREONYLCARBAMOYLTRANSFERASE; 1.
DR   PANTHER; PTHR11735:SF6; TRNA N6-ADENOSINE THREONYLCARBAMOYLTRANSFERASE, MITOCHONDRIAL; 1.
DR   Pfam; PF00814; TsaD; 1.
DR   PRINTS; PR00789; OSIALOPTASE.
DR   SUPFAM; SSF53067; Actin-like ATPase domain; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315, ECO:0000256|HAMAP-
KW   Rule:MF_03179};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_03179}; Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03179};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001568};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_03179};
KW   tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW   Rule:MF_03179}.
FT   DOMAIN          103..405
FT                   /note="Gcp-like"
FT                   /evidence="ECO:0000259|Pfam:PF00814"
FT   REGION          451..492
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   492 AA;  51559 MW;  3C956D5A339E709C CRC64;
     MTTLAVGHRA ACRRAPRVRA RVAAASETSH AAAGSFGFAS RRRRAVVAAG RDRVADVSSG
     IFLGSGRLDE GAPRAVDANT VVLGIETSCD DTAAAVVRGD GVVLGEAIAS QAAIHGPWGG
     VVPNLARAAH EEVIDDVVRR ALTEAGVSAA DLSAVAVTCG PGLSMCLRVG VRKAQRMSAE
     YGIPIAPVHH VEAHALVSRL CAGTETVKFP FLALLVSGGH NLLIKARGVG DYTILGTTLD
     DALGEAYDKT ARLLGLPVGG GGGPALEKLA LEGDEKRFKF PVPLRQRKNC DFSYAGLKTA
     ARMAIDAEIG GEDVEWDGVD KRQTRADIAA SFQAKAVKHL EERMRRALTW ALEDTPDLSC
     VVVAGGVAAN ATVRSTLVKV VEETGLPLVF PPPKWCTDNG VMVAWTGCER LALGLAEAPV
     DAELEAKHAM MDPRDVHVNL LPRWPLGEKD ARATGDIKSG KKARIADPLT GAGHRDSGIA
     VSRDAVSNNS DD
//