ID G3TTP2_LOXAF Unreviewed; 736 AA.
AC G3TTP2;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=TRMT1-like protein {ECO:0000256|ARBA:ARBA00015939};
GN Name=TRMT1L {ECO:0000313|Ensembl:ENSLAFP00000018950.1};
OS Loxodonta africana (African elephant).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta.
OX NCBI_TaxID=9785 {ECO:0000313|Ensembl:ENSLAFP00000018950.1, ECO:0000313|Proteomes:UP000007646};
RN [1] {ECO:0000313|Ensembl:ENSLAFP00000018950.1, ECO:0000313|Proteomes:UP000007646}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000018950.1,
RC ECO:0000313|Proteomes:UP000007646};
RA Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Loxodonta africana (African elephant).";
RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLAFP00000018950.1}
RP IDENTIFICATION.
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000018950.1};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: May play a role in motor coordination and exploratory
CC behavior. {ECO:0000256|ARBA:ARBA00003652}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. Trm1 family. {ECO:0000256|PROSITE-ProRule:PRU00958}.
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DR AlphaFoldDB; G3TTP2; -.
DR STRING; 9785.ENSLAFP00000018950; -.
DR Ensembl; ENSLAFT00000036126.1; ENSLAFP00000018950.1; ENSLAFG00000004339.2.
DR eggNOG; KOG1253; Eukaryota.
DR GeneTree; ENSGT00530000063646; -.
DR InParanoid; G3TTP2; -.
DR OMA; HLPCHPV; -.
DR TreeFam; TF300851; -.
DR Proteomes; UP000007646; Unassembled WGS sequence.
DR GO; GO:0160102; F:tRNA (guanine(10)-N2)-methyltransferase activity; IEA:InterPro.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0007610; P:behavior; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
DR Gene3D; 3.30.56.70; N2,N2-dimethylguanosine tRNA methyltransferase, C-terminal domain; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR002905; Trm1.
DR InterPro; IPR042296; tRNA_met_Trm1_C.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR10631; N 2 ,N 2 -DIMETHYLGUANOSINE TRNA METHYLTRANSFERASE; 1.
DR PANTHER; PTHR10631:SF1; TRMT1-LIKE PROTEIN; 1.
DR Pfam; PF02005; TRM; 2.
DR SMART; SM00355; ZnF_C2H2; 2.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS51626; SAM_MT_TRM1; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
PE 3: Inferred from homology;
KW Behavior {ECO:0000256|ARBA:ARBA00022610};
KW Isopeptide bond {ECO:0000256|ARBA:ARBA00022499};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW ProRule:PRU00958}; Reference proteome {ECO:0000313|Proteomes:UP000007646};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW ProRule:PRU00958};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW ECO:0000256|PROSITE-ProRule:PRU00958};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW ProRule:PRU00958}; tRNA processing {ECO:0000256|PROSITE-ProRule:PRU00958};
KW tRNA-binding {ECO:0000256|ARBA:ARBA00022555, ECO:0000256|PROSITE-
KW ProRule:PRU00958}; Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00042}.
FT DOMAIN 187..214
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT REGION 577..604
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 577..592
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 736 AA; 82752 MW; DCFCD347898FEF6E CRC64;
MENMAEEELL PLAKAEVEVA QVQVPTPAPD AAQVSSLPTS IADCLFMLIR SEFSSSRECM
LPPPFQSLPL RIISVLQKKE KKRHISIQRQ LADLEKLAFV SERDFDSASS LNSDNLDTGN
KQACPLCPKE KLRACNSHKL RRHLQNLHWK VSVEFEGYRM CICHLPCRPV KPSVIGEQIS
SKMGAHYHCI ICSATITRRT DMLGHVRRHV NKGETQSRYI AASAAKPPNE ILKEADTDIQ
VCPNYSIPQK TDSYFNPKMK LNRQLIFCTL AALAEERKPL ECLDAFGATG IMGLQWAKHL
GNAVKVTIND LNENSVTLIQ ENCHLNKLKV VVDSKEKAEG DDGLEEGEEH LGDVKVTKMD
ANVLMHLRSF DFIHLDPFGT SVNYLDSAFR NIRNLGIVSV TSTDISSLYA KAQHVARRHY
GCNIVRTEYY KELAARIVVA AVARAAARCN KGIEVLFAVA LEHFVLVVVR VLRGPTSADE
TAKKIQYLIH CQWCEERIFQ KDGNMVEENP YRQLPCNCHG SMPGKTAIEL GPLWSSSLFN
TGFLKRMLFE SLHHGLDDIQ TLIKTLIFES ECTPQSQFSL HPSSNLNKQE ESGVHTKTTD
DTTTDNYIAQ GKRKSNEMIT NLAKRQKADT STEHPPFYYN IHRHSIKGMN MPKLKKFLCY
LSQAGFRVSR THFDPMGVRT DAPLMQFKSI LLKYSTPTYT GGQSEGQVQS APEDTVADRV
EISVNEKAEA SSCRRW
//
