ID A0A452ILK7_9SAUR Unreviewed; 422 AA.
AC A0A452ILK7;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=N6-adenosine-methyltransferase non-catalytic subunit {ECO:0000256|ARBA:ARBA00026130, ECO:0000256|RuleBase:RU369092};
DE AltName: Full=Methyltransferase-like protein 14 {ECO:0000256|ARBA:ARBA00032942, ECO:0000256|RuleBase:RU369092};
OS Gopherus agassizii (Agassiz's desert tortoise).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Testudinoidea; Testudinidae; Gopherus.
OX NCBI_TaxID=38772 {ECO:0000313|Ensembl:ENSGAGP00000028790.1, ECO:0000313|Proteomes:UP000291020};
RN [1] {ECO:0000313|Proteomes:UP000291020}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=28562605;
RA Tollis M., DeNardo D.F., Cornelius J.A., Dolby G.A., Edwards T.,
RA Henen B.T., Karl A.E., Murphy R.W., Kusumi K.;
RT "The Agassiz's desert tortoise genome provides a resource for the
RT conservation of a threatened species.";
RL PLoS ONE 12:e0177708-e0177708(2017).
RN [2] {ECO:0000313|Ensembl:ENSGAGP00000028790.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: The METTL3-METTL14 heterodimer forms a N6-methyltransferase
CC complex that methylates adenosine residues at the N(6) position of some
CC mRNAs and regulates the circadian clock, differentiation of embryonic
CC stem cells and cortical neurogenesis. In the heterodimer formed with
CC mettl3, mettl14 constitutes the RNA-binding scaffold that recognizes
CC the substrate rather than the catalytic core. N6-methyladenosine (m6A),
CC which takes place at the 5'-[AG]GAC-3' consensus sites of some mRNAs,
CC plays a role in mRNA stability and processing.
CC {ECO:0000256|RuleBase:RU369092}.
CC -!- SUBUNIT: Heterodimer; heterodimerizes with mettl3 to form an
CC antiparallel heterodimer that constitutes an active methyltransferase.
CC {ECO:0000256|RuleBase:RU369092}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU369092}.
CC -!- SIMILARITY: Belongs to the MT-A70-like family. {ECO:0000256|PROSITE-
CC ProRule:PRU00489, ECO:0000256|RuleBase:RU369092}.
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DR AlphaFoldDB; A0A452ILK7; -.
DR Ensembl; ENSGAGT00000032705.1; ENSGAGP00000028790.1; ENSGAGG00000020861.1.
DR Proteomes; UP000291020; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0036396; C:RNA N6-methyladenosine methyltransferase complex; IEA:UniProtKB-UniRule.
DR GO; GO:0003729; F:mRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0080009; P:mRNA methylation; IEA:UniProtKB-UniRule.
DR InterPro; IPR045123; METTL14-like.
DR InterPro; IPR007757; MT-A70-like.
DR PANTHER; PTHR13107; N6-ADENOSINE-METHYLTRANSFERASE NON-CATALYTIC SUBUNIT; 1.
DR PANTHER; PTHR13107:SF0; N6-ADENOSINE-METHYLTRANSFERASE NON-CATALYTIC SUBUNIT; 1.
DR Pfam; PF05063; MT-A70; 2.
DR PROSITE; PS51143; MT_A70; 1.
DR PROSITE; PS51592; SAM_MTA70L_2; 1.
PE 3: Inferred from homology;
KW Differentiation {ECO:0000256|RuleBase:RU369092};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU369092};
KW Reference proteome {ECO:0000313|Proteomes:UP000291020};
KW RNA-binding {ECO:0000256|RuleBase:RU369092}.
FT REGION 355..422
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 387..410
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 422 AA; 48023 MW; 3B7C89CB801FEBF1 CRC64;
MAMNSRLQEI RERQKLRRQL LAQQLGAESA DSIGAILNSK DDQREIAETR ETCRASYDTL
APNAKRKYPD EGEADEEEIE EYKDEVELHQ DEENLPYEEE IYKDSSTFLK GTQSLNPHND
YCQHFVDTGH RPQNFIRDVG LADRFEEYPK LRELIRLKDE LISKSNTPPM YLQADLEAFD
TRELKSKFDV ILLEPPLEEY YRETGITANE KCWTWDDIMK LEIEEIAASR SFVFLWCGSG
EGLDLGRVEH CLMGIKGTVR RSTDGDFIHA NVDIDLIITE EPEIGNIEKP VEIFHIIEHF
CLGRRRLHLF GRDSTIRPGW LTVGPTLTNS NFNAETYASY FTAPNSHLTG CTEEIERLRP
KSPPPKSKSD RGGGAPRGGG RGGTSAGRGE RGRERNRTNF RGERGGFRGG RGGTHRGGFP
PR
//
