ID H3AIV7_LATCH Unreviewed; 680 AA.
AC H3AIV7;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, 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:ENSLACP00000009578.1};
OS Latimeria chalumnae (Coelacanth).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Coelacanthiformes; Coelacanthidae; Latimeria.
OX NCBI_TaxID=7897 {ECO:0000313|Ensembl:ENSLACP00000009578.1, 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:ENSLACP00000009578.1}
RP IDENTIFICATION.
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 EMBL; AFYH01082522; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01082523; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01082524; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01082525; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; H3AIV7; -.
DR STRING; 7897.ENSLACP00000009578; -.
DR Ensembl; ENSLACT00000009651.1; ENSLACP00000009578.1; ENSLACG00000008447.1.
DR eggNOG; KOG1253; Eukaryota.
DR GeneTree; ENSGT00530000063646; -.
DR HOGENOM; CLU_010862_3_0_1; -.
DR InParanoid; H3AIV7; -.
DR OMA; HLPCHPV; -.
DR TreeFam; TF300851; -.
DR Proteomes; UP000008672; Unassembled WGS sequence.
DR Bgee; ENSLACG00000008447; Expressed in chordate pharynx and 1 other cell type or tissue.
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 CDD; cd02440; AdoMet_MTases; 1.
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:UP000008672};
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 142..169
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 659..680
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..35
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 680 AA; 76308 MW; E898E72BF3F850BE CRC64;
VDSLIQNGLS PCEKKEDEST DVEMQKQSLD EETKQTKHIS IQKELGDLEN LADIDGGELS
AGSVLMIAHL LAPGKKPCPL CPEEKFKSCY SYKLRRHLQN LHWKVSVEFE GHRMCICHLP
CRQMKPNLNG EQQPSSRLGA HYHCIVCSAT IARRTDMISH IKRHVNKGET EAGYTGGFAG
QQSSYEIVKE ADTDVQVLPN HSTPQKTDSY FNPKMKSNRL LVFCSLATLA EERSPLECLD
AFGATGIMGL QWAKHLGTAV KVTINDINDN CVKMIRENCQ LNRIKVTPIL KEEEEMEEEP
EEAEDTLGTV KVTNMDANVI LHLRAFDFIH LDPFGTAVNY LDAAFRNVRN HGIVSITSTD
TSSLYSKAVN VAIRHYGCNI VRTEYYKELA ARVVITAVAR AAARCNKGIE VLFSLCLEHF
ALVVVRVLRG PTQADETVKK IRHLIHCQWC EERVFQKEGN MLEESPYRQL PCDCHDSMPG
KTAAELGPMW SGTLFNTGFL KRMLFEAIQH GIDDIQPLIK SLLCEAECTT SKQLSLHGSG
FHSSQEECGV YIKTAAPQNP EDVTTEYAIA QGKRKGKEVI GSQLKRQKSE VHVEHPPFYY
SIHRHSIRGM NIPKLNKFLQ YLTEAGFRVS RTHFDPTGVR TDATLEQFKS VLMTYSVPTY
TGGQSGTHSH STEDVKSDHE
//
