ID A0A1U7LNP0_NEOID Unreviewed; 483 AA.
AC A0A1U7LNP0;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=N6-adenosine-methyltransferase subunit METTL14 {ECO:0000313|EMBL:OLL24141.1};
GN ORFNames=NEOLI_002927 {ECO:0000313|EMBL:OLL24141.1};
OS Neolecta irregularis (strain DAH-3).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina; Neolectales;
OC Neolectaceae; Neolecta.
OX NCBI_TaxID=1198029 {ECO:0000313|EMBL:OLL24141.1, ECO:0000313|Proteomes:UP000186594};
RN [1] {ECO:0000313|EMBL:OLL24141.1, ECO:0000313|Proteomes:UP000186594}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DAH-3 {ECO:0000313|EMBL:OLL24141.1,
RC ECO:0000313|Proteomes:UP000186594};
RA Cisse O., Nguyen A., Hewitt D.A., Jedd G., Stajich J.E.;
RT "Evolutionary innovation and constraint leading to complex multicellularity
RT in the Ascomycota.";
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
CC -!- SIMILARITY: Belongs to the ATPase inhibitor family.
CC {ECO:0000256|ARBA:ARBA00010901}.
CC -!- SIMILARITY: Belongs to the MT-A70-like family. {ECO:0000256|PROSITE-
CC ProRule:PRU00489}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OLL24141.1}.
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DR EMBL; LXFE01000968; OLL24141.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1U7LNP0; -.
DR STRING; 1198029.A0A1U7LNP0; -.
DR OrthoDB; 179166at2759; -.
DR Proteomes; UP000186594; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0042030; F:ATPase inhibitor activity; IEA:InterPro.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0090304; P:nucleic acid metabolic process; IEA:UniProt.
DR CDD; cd00890; Prefoldin; 1.
DR Gene3D; 1.20.5.500; Single helix bin; 1.
DR InterPro; IPR007648; ATPase_inhibitor_mt.
DR InterPro; IPR045123; METTL14-like.
DR InterPro; IPR007757; MT-A70-like.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR13107; N6-ADENOSINE-METHYLTRANSFERASE NON-CATALYTIC SUBUNIT; 1.
DR PANTHER; PTHR13107:SF0; N6-ADENOSINE-METHYLTRANSFERASE NON-CATALYTIC SUBUNIT; 1.
DR Pfam; PF04568; IATP; 1.
DR Pfam; PF05063; MT-A70; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS51143; MT_A70; 1.
DR PROSITE; PS51592; SAM_MTA70L_2; 1.
PE 3: Inferred from homology;
KW Methyltransferase {ECO:0000313|EMBL:OLL24141.1};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000186594};
KW Transferase {ECO:0000313|EMBL:OLL24141.1}.
FT REGION 460..483
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 483 AA; 55373 MW; 2975534735397ADD CRC64;
MDPIPRPETS PSDFNYSVSE DAILHLLNDR AVQRALIFKL TKPEPVIVKT TSKHTDEENL
RDNSIRKVPT YRQSYQTSDS VVNDLSTSYI STRSRPQNYI QKRTPQTRFE GYPKLQHLVS
LKQGFVTARA HPPISVQWDY NRNLLEMLNS PTSINKFNVI VIGSKTEGVD LYSLPISELS
QTPCFLFLWI GTQLDLETGR LLLKHHGFRR AEDVVWVKTT VGPDTKQMNR FNQGVFVTTK
EHCLMGIKGT VRRSSDGRLI HCNVDTDIIV ADEEPADSTK KPEEIYQIIE NFCQGRKRLE
LFGSDDNLRR GWVTVGRTMS VSNYCPDTYN RFFQDGTLLG PHAEIEMLRP KSPQQRMQNG
GQFQQRGQFK SASFVNQPLT STSRQFKMLR TFNHIPRNVS LSMRMGSRYM SDNPGSVGGI
RPAGSHYGDA FSNREKAMED QAIRQREIEK LAQLRKKLER QQQDLDEAKS QLDEIEQKHN
GTQ
//
