ID   METL9_CHICK             Reviewed;         321 AA.
AC   Q5ZMH6;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 65.
DE   RecName: Full=Protein-L-histidine N-pros-methyltransferase;
DE            EC=2.1.1.- {ECO:0000250|UniProtKB:Q9H1A3};
DE   AltName: Full=Methyltransferase-like protein 9 {ECO:0000250|UniProtKB:Q9H1A3};
DE   Flags: Precursor;
GN   Name=METTL9 {ECO:0000250|UniProtKB:Q9H1A3};
GN   ORFNames=RCJMB04_2a9 {ECO:0000303|PubMed:15642098};
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=CB; TISSUE=Bursa of Fabricius;
RX   PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA   Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA   Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA   Hayashizaki Y., Buerstedde J.-M.;
RT   "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT   function analysis.";
RL   Genome Biol. 6:R6.1-R6.9(2005).
CC   -!- FUNCTION: Protein-histidine N-methyltransferase that specifically
CC       catalyzes 1-methylhistidine (pros-methylhistidine) methylation of
CC       target proteins (By similarity). Mediates methylation of proteins with
CC       a His-x-His (HxH) motif (where 'x' is preferably a small amino acid);
CC       1-methylhistidine modification may affect the binding of zinc and other
CC       metals to its target proteins (By similarity).
CC       {ECO:0000250|UniProtKB:Q9H1A3}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-histidyl-[protein] + S-adenosyl-L-methionine = H(+) +
CC         N(pros)-methyl-L-histidyl-[protein] + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:67076, Rhea:RHEA-COMP:9745, Rhea:RHEA-COMP:17184,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29979, ChEBI:CHEBI:43903,
CC         ChEBI:CHEBI:57856, ChEBI:CHEBI:59789;
CC         Evidence={ECO:0000250|UniProtKB:Q9H1A3};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67077;
CC         Evidence={ECO:0000250|UniProtKB:Q9H1A3};
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC       {ECO:0000250|UniProtKB:Q9H1A3}. Mitochondrion
CC       {ECO:0000250|UniProtKB:Q9H1A3}. Note=Colocalizes with membranous
CC       compartments such as the endoplasmic reticulum and mitochondria.
CC       {ECO:0000250|UniProtKB:Q9H1A3}.
CC   -!- SIMILARITY: Belongs to the METTL9 family. {ECO:0000305}.
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DR   EMBL; AJ719408; CAG31067.1; -; mRNA.
DR   RefSeq; NP_001006172.1; NM_001006172.1.
DR   AlphaFoldDB; Q5ZMH6; -.
DR   SMR; Q5ZMH6; -.
DR   STRING; 9031.ENSGALP00000011398; -.
DR   PaxDb; Q5ZMH6; -.
DR   GeneID; 416623; -.
DR   KEGG; gga:416623; -.
DR   CTD; 51108; -.
DR   VEuPathDB; HostDB:geneid_416623; -.
DR   eggNOG; KOG3987; Eukaryota.
DR   InParanoid; Q5ZMH6; -.
DR   OrthoDB; 899076at2759; -.
DR   PhylomeDB; Q5ZMH6; -.
DR   PRO; PR:Q5ZMH6; -.
DR   Proteomes; UP000000539; Unplaced.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0106370; F:protein-L-histidine N-pros-methyltransferase activity; ISS:UniProtKB.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR007884; METL9.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR12890; PTHR12890; 1.
DR   Pfam; PF05219; DREV; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
PE   2: Evidence at transcript level;
KW   Endoplasmic reticulum; Glycoprotein; Methyltransferase; Mitochondrion;
KW   Reference proteome; Signal; Transferase.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..321
FT                   /note="Protein-L-histidine N-pros-methyltransferase"
FT                   /id="PRO_0000317492"
FT   CARBOHYD        89
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   321 AA;  37009 MW;  E902B221D3EC9622 CRC64;
     MRLWLCWLGC YTLLLWALRR RMWAGPARYL RSPLSRSLYA NMMGSHGPPA PGAGENHQWY
     VCNTEQLSES LQPIFVQSYL DQGTQIFLNN SIEKSGWLFI QLYHSFVSSI FSLFMSRTSI
     NGLLGRGSMF VFSPEQFQRL LKINPEWKSH RLLDLGAGDG EVTKVMSPHF EEIYATELSE
     TMIWQLQKKK YRVLGINEWQ NTGFQYDVIS CLNLLDRCDQ PLTVLKDTRS VLEPTRGRVI
     LALVLPFHPY VENVGGKWEK PSEVLEIKGH TWEEQVNSLP EVFGKAGFAI EAFTRLPYLC
     EGDMYNDYYV LDDAVFVLKP V