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Database: UniProt
Entry: H3B1G7_LATCH
LinkDB: H3B1G7_LATCH
Original site: H3B1G7_LATCH 
ID   H3B1G7_LATCH            Unreviewed;       488 AA.
AC   H3B1G7;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 2.
DT   27-MAR-2024, entry version 68.
DE   RecName: Full=tRNA dimethylallyltransferase {ECO:0000256|PIRNR:PIRNR039110};
DE            EC=2.5.1.75 {ECO:0000256|PIRNR:PIRNR039110};
GN   Name=TRIT1 {ECO:0000313|Ensembl:ENSLACP00000015738.2};
OS   Latimeria chalumnae (Coelacanth).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Coelacanthiformes; Coelacanthidae; Latimeria.
OX   NCBI_TaxID=7897 {ECO:0000313|Ensembl:ENSLACP00000015738.2, ECO:0000313|Proteomes:UP000008672};
RN   [1] {ECO:0000313|Proteomes:UP000008672}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Wild caught {ECO:0000313|Proteomes:UP000008672};
RA   Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA   MacCallum I., Young S., Walker B.J., Lander E., Lindblad-Toh K.;
RT   "The draft genome of Latimeria chalumnae.";
RL   Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSLACP00000015738.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- FUNCTION: Catalyzes the transfer of a dimethylallyl group onto the
CC       adenine at position 37. {ECO:0000256|PIRNR:PIRNR039110}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=adenosine(37) in tRNA + dimethylallyl diphosphate =
CC         diphosphate + N(6)-dimethylallyladenosine(37) in tRNA;
CC         Xref=Rhea:RHEA:26482, Rhea:RHEA-COMP:10162, Rhea:RHEA-COMP:10375,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:57623, ChEBI:CHEBI:74411,
CC         ChEBI:CHEBI:74415; EC=2.5.1.75;
CC         Evidence={ECO:0000256|PIRNR:PIRNR039110};
CC   -!- SIMILARITY: Belongs to the IPP transferase family.
CC       {ECO:0000256|ARBA:ARBA00005842, ECO:0000256|PIRNR:PIRNR039110,
CC       ECO:0000256|RuleBase:RU003785}.
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DR   EMBL; AFYH01052431; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AFYH01052432; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AFYH01052433; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AFYH01052434; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_014342668.1; XM_014487182.1.
DR   AlphaFoldDB; H3B1G7; -.
DR   STRING; 7897.ENSLACP00000015738; -.
DR   Ensembl; ENSLACT00000015848.2; ENSLACP00000015738.2; ENSLACG00000013861.2.
DR   GeneID; 102360123; -.
DR   KEGG; lcm:102360123; -.
DR   CTD; 54802; -.
DR   eggNOG; KOG1384; Eukaryota.
DR   GeneTree; ENSGT00390000015214; -.
DR   HOGENOM; CLU_032616_2_1_1; -.
DR   InParanoid; H3B1G7; -.
DR   OMA; WGLHLKS; -.
DR   OrthoDB; 11270at2759; -.
DR   TreeFam; TF315069; -.
DR   Proteomes; UP000008672; Unassembled WGS sequence.
DR   Bgee; ENSLACG00000013861; Expressed in chordate pharynx and 4 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0052381; F:tRNA dimethylallyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.20.140; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   HAMAP; MF_00185; IPP_trans; 1.
DR   InterPro; IPR039657; Dimethylallyltransferase.
DR   InterPro; IPR030666; IPP_transferase_euk.
DR   InterPro; IPR018022; IPT.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR022755; Znf_C2H2_jaz.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   NCBIfam; TIGR00174; miaA; 1.
DR   PANTHER; PTHR11088; TRNA DIMETHYLALLYLTRANSFERASE; 1.
DR   PANTHER; PTHR11088:SF95; TRNA DIMETHYLALLYLTRANSFERASE; 1.
DR   Pfam; PF01715; IPPT; 1.
DR   Pfam; PF12171; zf-C2H2_jaz; 1.
DR   PIRSF; PIRSF039110; IPP_transferase; 1.
DR   SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR039110};
KW   Cytoplasm {ECO:0000256|PIRNR:PIRNR039110};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|PIRNR:PIRNR039110};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008672};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR039110};
KW   tRNA processing {ECO:0000256|PIRNR:PIRNR039110};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT   DOMAIN          424..446
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS00028"
FT   REGION          443..488
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        456..478
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   488 AA;  55795 MW;  41D9716A5A923AE8 CRC64;
     MCGTTQSRIL HYYGNRHAFS HQATLCCSRM AAACQRVRSS LPLLVILGAT GTGKSKLAIE
     LGQRLGGEII SADSMQIYKG LDIITNKVTP EEQQLCKHHM ISIVDPLVST YTVVEFRNKA
     LSLIEDIFGR KKIPIVVGGT NYYIESLLWK VLIDQKERNI SPSETWEDTV KASPPNLKKE
     LETLDSQELH RRLREVDPEM AARLHPHDKR KVARSLQVYE ETGIPHSKLI HQQQQADGGG
     PLGGPLRFQD PCILWLNADL AALDKRLDQR VDDMLDAGLL DELKDFHDRY NQEKVVNKSQ
     DYEHGIFQSI GFKEFHEYLT MGDHFTEEDR QKLLKKGIEA LKQATKRYAR KQNKWVRNRF
     LKRPGVSVLP VYGLDVTDVA QWKESVLKPA LHIVESFMKG EKPALEPVKV DYDKNENKRS
     HHVCELCDKI ILGDREWTAH LKSKSHLHHT RKRRKLEAKE CPAEQKRDAQ RAEATRENPD
     GADTLTTV
//
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