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Database: UniProt
Entry: A0A2K3QKM4_9HYPO
LinkDB: A0A2K3QKM4_9HYPO
Original site: A0A2K3QKM4_9HYPO 
ID   A0A2K3QKM4_9HYPO        Unreviewed;       462 AA.
AC   A0A2K3QKM4;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   SubName: Full=Methyltransferase OMS1, mitochondrial {ECO:0000313|EMBL:PNY28081.1};
GN   ORFNames=TCAP_01998 {ECO:0000313|EMBL:PNY28081.1};
OS   Tolypocladium capitatum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Tolypocladium.
OX   NCBI_TaxID=45235 {ECO:0000313|EMBL:PNY28081.1, ECO:0000313|Proteomes:UP000236621};
RN   [1] {ECO:0000313|EMBL:PNY28081.1, ECO:0000313|Proteomes:UP000236621}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 113982 {ECO:0000313|EMBL:PNY28081.1,
RC   ECO:0000313|Proteomes:UP000236621};
RA   Quandt C.A., Patterson W., Spatafora J.W.;
RT   "Harnessing the power of phylogenomics to disentangle the directionality
RT   and signatures of interkingdom host jumping in the parasitic fungal genus
RT   Tolypocladium.";
RL   Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
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:PNY28081.1}.
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DR   EMBL; NRSZ01000306; PNY28081.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2K3QKM4; -.
DR   STRING; 45235.A0A2K3QKM4; -.
DR   OrthoDB; 35684at2759; -.
DR   Proteomes; UP000236621; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR42912; METHYLTRANSFERASE; 1.
DR   PANTHER; PTHR42912:SF60; METHYLTRANSFERASE OMS1, MITOCHONDRIAL; 1.
DR   Pfam; PF13489; Methyltransf_23; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Methyltransferase {ECO:0000313|EMBL:PNY28081.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000236621};
KW   Transferase {ECO:0000313|EMBL:PNY28081.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        130..149
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REGION          1..121
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        55..72
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        73..87
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        106..120
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   462 AA;  50340 MW;  91B45733F8BD4EEF CRC64;
     MARAVPTSGN KPDVVFRPSC DSSLSSTRDR RNNYTRDATS MIRPTRGIAR AARSQWRLAS
     SSARASRQTT RASPPKQPPP LPPRIARPYK PSSCLHDRSG RRRADTPPPS SPPPPPPKSD
     TLLTLWRRSW LPLTGAALLA GFLGFYVFGT AAASFRTCPC EGACKHAAPT GRPPALTGEN
     AEQFDKELDF GEWWMGISGL RRKLAGHATG HVLELAMGTG RNLEYYNWEP LSAAAEVANT
     GGKKAVAPQG VMSFTGLDIS ADMLDVARRR LVKTVPPMFS SGPMVKASTM ADDTGGQLPY
     LDGHLRLINA DAHHPLPPPA AATPDSKYDT VIQTFGLCSV SDPVAVLSNL ASAVKPRTGR
     IILLEHGKGW YGIVNGLLDK NAVKHYEKYG CWWNRDIEAL VVEAVRKTPG LEVVKLDRPN
     LLQMGTLVWV ELRVADKAER KCTERCRIMA RPVMNTAPEV EA
//
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