QRI7_SCHPO
ID QRI7_SCHPO Reviewed; 412 AA.
AC O94710;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=tRNA N6-adenosine threonylcarbamoyltransferase, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03179};
DE EC=2.3.1.234 {ECO:0000255|HAMAP-Rule:MF_03179};
DE AltName: Full=N6-L-threonylcarbamoyladenine synthase {ECO:0000255|HAMAP-Rule:MF_03179};
DE Short=t(6)A synthase {ECO:0000255|HAMAP-Rule:MF_03179};
DE AltName: Full=Pombe glycoprotease 1;
DE AltName: Full=t(6)A37 threonylcarbamoyladenosine biosynthesis protein pgp1 {ECO:0000255|HAMAP-Rule:MF_03179};
DE AltName: Full=tRNA threonylcarbamoyladenosine biosynthesis protein pgp1 {ECO:0000255|HAMAP-Rule:MF_03179};
DE Flags: Precursor;
GN Name=pgp1; ORFNames=SPCC1259.10;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP GENE NAME.
RX PubMed=11115118; DOI=10.1046/j.1365-2958.2000.02180.x;
RA Ladds G., Davey J.;
RT "Identification of proteases with shared functions to the proprotein
RT processing protease Krp1 in the fission yeast Schizosaccharomyces pombe.";
RL Mol. Microbiol. 38:839-853(2000).
RN [3]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
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:0000255|HAMAP-Rule:MF_03179}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=adenosine(37) in tRNA + L-threonylcarbamoyladenylate = AMP +
CC H(+) + N(6)-L-threonylcarbamoyladenosine(37) in tRNA;
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:0000255|HAMAP-Rule:MF_03179};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03179};
CC Note=Binds 1 divalent metal cation per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_03179};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_03179}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03179,
CC ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the KAE1 / TsaD family. {ECO:0000255|HAMAP-
CC Rule:MF_03179}.
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DR EMBL; CU329672; CAA22548.1; -; Genomic_DNA.
DR PIR; T40899; T40899.
DR RefSeq; NP_588066.1; NM_001023058.2.
DR AlphaFoldDB; O94710; -.
DR SMR; O94710; -.
DR BioGRID; 275646; 4.
DR STRING; 4896.SPCC1259.10.1; -.
DR iPTMnet; O94710; -.
DR SwissPalm; O94710; -.
DR MaxQB; O94710; -.
DR PaxDb; O94710; -.
DR EnsemblFungi; SPCC1259.10.1; SPCC1259.10.1:pep; SPCC1259.10.
DR GeneID; 2539074; -.
DR KEGG; spo:SPCC1259.10; -.
DR PomBase; SPCC1259.10; pgp1.
DR VEuPathDB; FungiDB:SPCC1259.10; -.
DR eggNOG; KOG2707; Eukaryota.
DR HOGENOM; CLU_023208_4_1_1; -.
DR InParanoid; O94710; -.
DR OMA; HLEGHIY; -.
DR PhylomeDB; O94710; -.
DR PRO; PR:O94710; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0005739; C:mitochondrion; HDA:PomBase.
DR GO; GO:0061711; F:N(6)-L-threonylcarbamoyladenine synthase activity; ISO:PomBase.
DR GO; GO:0008270; F:zinc ion binding; ISM:PomBase.
DR GO; GO:0072670; P:mitochondrial tRNA threonylcarbamoyladenosine modification; ISO:PomBase.
DR HAMAP; MF_01445; TsaD; 1.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR000905; Gcp-like_dom.
DR InterPro; IPR017861; KAE1/TsaD.
DR InterPro; IPR017860; Peptidase_M22_CS.
DR InterPro; IPR022450; TsaD.
DR PANTHER; PTHR11735; PTHR11735; 1.
DR PANTHER; PTHR11735:SF6; PTHR11735:SF6; 1.
DR Pfam; PF00814; TsaD; 1.
DR PRINTS; PR00789; OSIALOPTASE.
DR SUPFAM; SSF53067; SSF53067; 1.
DR TIGRFAMs; TIGR00329; gcp_kae1; 1.
DR PROSITE; PS01016; GLYCOPROTEASE; 1.
PE 3: Inferred from homology;
KW Acyltransferase; Metal-binding; Mitochondrion; Reference proteome;
KW Transferase; Transit peptide; tRNA processing.
FT TRANSIT 1..78
FT /note="Mitochondrion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03179"
FT CHAIN 79..412
FT /note="tRNA N6-adenosine threonylcarbamoyltransferase,
FT mitochondrial"
FT /id="PRO_0000255599"
FT BINDING 157
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03179"
FT BINDING 161
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03179"
FT BINDING 179..183
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03179"
FT BINDING 212
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03179"
FT BINDING 228
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03179"
FT BINDING 232
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03179"
FT BINDING 328..329
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03179"
FT BINDING 363
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03179"
FT BINDING 364
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03179"
SQ SEQUENCE 412 AA; 45973 MW; 17D28729FCD50009 CRC64;
MLCLVYNSIL CKQRRISLKV LQQFRCWNIS KTFLSYRTLT ALAIETSCDD TSVSVVRTSD
SSSHCQNEII CLNTHRTISK YEAYGGIHPT IVIHEHQKNL AKVIQRTISD AARSGITDFD
LIAVTRGPGM IGPLAVGLNT AKGLAVGLQK PLLAVHHMQA HALAVQLEKS IDFPYLNILV
SGGHTMLVYS NSLLNHEIIV TTSDIAVGDY LDKCAKYLGI PWDNEMPAAA LEQFASPEIN
STSYSLKPPI PLNTREKVHS ASFSFSGLES YACRIIRKTP LNLSEKKFFA YQLQYAAFQH
ICQKTLLALK RLDLSKVKYL VCSGGVARNE LLKKMLNDTL MVLQFEHQPT DIKLVYPSPD
ICSDNAAMIG YTAIQMFKAG YTSSFDVEPI RKWPINQILT VEGWLTKKNK KV
