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Database: UniProt
Entry: C8VQH2_EMENI
LinkDB: C8VQH2_EMENI
Original site: C8VQH2_EMENI 
ID   C8VQH2_EMENI            Unreviewed;       235 AA.
AC   C8VQH2;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   24-JAN-2024, entry version 66.
DE   RecName: Full=tRNA(His) guanylyltransferase {ECO:0000256|ARBA:ARBA00015443, ECO:0000256|PIRNR:PIRNR028980};
DE            EC=2.7.7.79 {ECO:0000256|ARBA:ARBA00012511, ECO:0000256|PIRNR:PIRNR028980};
DE   AltName: Full=tRNA-histidine guanylyltransferase {ECO:0000256|ARBA:ARBA00032480, ECO:0000256|PIRNR:PIRNR028980};
GN   ORFNames=ANIA_00804 {ECO:0000313|EMBL:CBF88750.1};
OS   Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS   M139) (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Nidulantes.
OX   NCBI_TaxID=227321 {ECO:0000313|EMBL:CBF88750.1, ECO:0000313|Proteomes:UP000000560};
RN   [1] {ECO:0000313|Proteomes:UP000000560}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139
RC   {ECO:0000313|Proteomes:UP000000560};
RX   PubMed=16372000; DOI=10.1038/nature04341;
RA   Galagan J.E., Calvo S.E., Cuomo C., Ma L.J., Wortman J.R., Batzoglou S.,
RA   Lee S.I., Basturkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA   Jurka J., Scazzocchio C., Farman M., Butler J., Purcell S., Harris S.,
RA   Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA   Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA   Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA   Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA   Denning D.W., Caddick M., Hynes M., Paoletti M., Fischer R., Miller B.,
RA   Dyer P., Sachs M.S., Osmani S.A., Birren B.W.;
RT   "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT   fumigatus and A. oryzae.";
RL   Nature 438:1105-1115(2005).
RN   [2] {ECO:0000313|Proteomes:UP000000560}
RP   GENOME REANNOTATION.
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139
RC   {ECO:0000313|Proteomes:UP000000560};
RX   PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA   Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA   Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA   Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA   Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA   Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA   Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA   Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA   van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA   Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA   Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA   Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA   Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA   Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA   van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA   Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA   Oliver S.G., Turner G.;
RT   "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT   effort.";
RL   Fungal Genet. Biol. 46:S2-13(2009).
CC   -!- FUNCTION: Adds a GMP to the 5'-end of tRNA(His) after transcription and
CC       RNase P cleavage. {ECO:0000256|PIRNR:PIRNR028980}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 5'-end ribonucleotide-tRNA(His) + ATP + GTP + H2O = a 5'-end
CC         phospho-guanosine-ribonucleotide-tRNA(His) + AMP + 2 diphosphate +
CC         H(+); Xref=Rhea:RHEA:54564, Rhea:RHEA-COMP:14193, Rhea:RHEA-
CC         COMP:14917, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:37565, ChEBI:CHEBI:138282,
CC         ChEBI:CHEBI:141847, ChEBI:CHEBI:456215; EC=2.7.7.79;
CC         Evidence={ECO:0000256|PIRNR:PIRNR028980};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|PIRSR:PIRSR028980-2};
CC       Note=Binds 2 magnesium ions per subunit.
CC       {ECO:0000256|PIRSR:PIRSR028980-2};
CC   -!- SIMILARITY: Belongs to the tRNA(His) guanylyltransferase family.
CC       {ECO:0000256|ARBA:ARBA00010113, ECO:0000256|PIRNR:PIRNR028980}.
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DR   EMBL; BN001308; CBF88750.1; -; Genomic_DNA.
DR   AlphaFoldDB; C8VQH2; -.
DR   STRING; 227321.C8VQH2; -.
DR   EnsemblFungi; CBF88750; CBF88750; ANIA_00804.
DR   VEuPathDB; FungiDB:AN0804; -.
DR   eggNOG; KOG2721; Eukaryota.
DR   HOGENOM; CLU_044271_1_1_1; -.
DR   InParanoid; C8VQH2; -.
DR   OMA; WKQHTEI; -.
DR   Proteomes; UP000000560; Chromosome VIII.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0042802; F:identical protein binding; IEA:EnsemblFungi.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008193; F:tRNA guanylyltransferase activity; IBA:GO_Central.
DR   GO; GO:0006400; P:tRNA modification; IEA:UniProtKB-UniRule.
DR   GO; GO:0008033; P:tRNA processing; IBA:GO_Central.
DR   Gene3D; 3.30.70.3000; -; 1.
DR   InterPro; IPR025845; Thg1_C_dom.
DR   InterPro; IPR024956; tRNAHis_GuaTrfase_cat.
DR   InterPro; IPR007537; tRNAHis_GuaTrfase_Thg1.
DR   InterPro; IPR038469; tRNAHis_GuaTrfase_Thg1_sf.
DR   PANTHER; PTHR12729:SF6; TRNA(HIS) GUANYLYLTRANSFERASE-RELATED; 1.
DR   PANTHER; PTHR12729; UNCHARACTERIZED; 1.
DR   Pfam; PF04446; Thg1; 1.
DR   Pfam; PF14413; Thg1C; 1.
DR   PIRSF; PIRSF028980; tRNAHis_guanylyltransferase; 1.
PE   3: Inferred from homology;
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|PIRNR:PIRNR028980};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRNR:PIRNR028980};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRNR:PIRNR028980};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|PIRNR:PIRNR028980};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW   ECO:0000256|PIRNR:PIRNR028980};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000560};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR028980};
KW   tRNA processing {ECO:0000256|ARBA:ARBA00022694,
KW   ECO:0000256|PIRNR:PIRNR028980}.
FT   DOMAIN          1..84
FT                   /note="tRNAHis guanylyltransferase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF04446"
FT   DOMAIN          88..213
FT                   /note="Thg1 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF14413"
FT   REGION          172..192
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         22..23
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR028980-1"
FT   BINDING         23
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR028980-2"
FT   BINDING         23
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR028980-2"
SQ   SEQUENCE   235 AA;  27356 MW;  57739888CC9F9D24 CRC64;
     MNAAAVEVLK DLPDLAIAYG VSDEYSFVFH PTCELFERRS AKLVTTIVST FTAHYIYLWG
     NYFPDTPLQP PHLPSFDGRA VVYPTIRNLR DYMSWRQVDC HINNLYNTTF WMMVLKGGMS
     NTDAENELKG TLSSDKNEIL FKRFGINYNN EEEIYKKGSV VYRQYQLEER KPLKAPEEEG
     PTVQESISKS QQEKLRKLRR KAQVIVEHVD IIKDEFWERR PWILSGKPGR LPAEA
//
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