ID A0A176VF81_MARPO Unreviewed; 576 AA.
AC A0A176VF81;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=SET domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=AXG93_3756s1140 {ECO:0000313|EMBL:OAE19608.1};
OS Marchantia polymorpha subsp. ruderalis.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Marchantiophyta;
OC Marchantiopsida; Marchantiidae; Marchantiales; Marchantiaceae; Marchantia.
OX NCBI_TaxID=1480154 {ECO:0000313|EMBL:OAE19608.1, ECO:0000313|Proteomes:UP000077202};
RN [1] {ECO:0000313|EMBL:OAE19608.1, ECO:0000313|Proteomes:UP000077202}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Tak-1 and cv. Tak-2 {ECO:0000313|Proteomes:UP000077202};
RC TISSUE=Whole gametophyte {ECO:0000313|EMBL:OAE19608.1};
RA Honkanen S., Jones V.A., Morieri G., Champion C., Hetherington A.J.,
RA Kelly S., Saint-Marcoux D., Proust H., Prescott H., Dolan L.;
RT "Mechanisms controlling the formation of the plant cell surface in tip-
RT growing cells are functionally conserved among land plants.";
RL Submitted (MAR-2016) 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:OAE19608.1}.
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DR EMBL; LVLJ01003810; OAE19608.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A176VF81; -.
DR OrthoDB; 362650at2759; -.
DR Proteomes; UP000077202; Unassembled WGS sequence.
DR Gene3D; 3.90.1420.10; Rubisco LSMT, substrate-binding domain; 1.
DR Gene3D; 3.90.1410.10; set domain protein methyltransferase, domain 1; 2.
DR InterPro; IPR015353; Rubisco_LSMT_subst-bd.
DR InterPro; IPR036464; Rubisco_LSMT_subst-bd_sf.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR PANTHER; PTHR13271:SF134; OS01G0976450 PROTEIN; 1.
DR PANTHER; PTHR13271; UNCHARACTERIZED PUTATIVE METHYLTRANSFERASE; 1.
DR Pfam; PF09273; Rubis-subs-bind; 1.
DR Pfam; PF00856; SET; 1.
DR SUPFAM; SSF82199; SET domain; 1.
PE 4: Predicted;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW Reference proteome {ECO:0000313|Proteomes:UP000077202};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 215..375
FT /note="SET"
FT /evidence="ECO:0000259|Pfam:PF00856"
FT DOMAIN 407..558
FT /note="Rubisco LSMT substrate-binding"
FT /evidence="ECO:0000259|Pfam:PF09273"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 42..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 119..143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 42..56
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 125..143
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 576 AA; 63736 MW; 774FDA9C24C5ABCA CRC64;
MAAEQSAGER SAGLMNARAS DRAMDGSIDR WARAGAEFRY EDGDWSDWRG GRGGEAEAED
EDEEQSDDDS LEAAAGRESE CLPTSPGELR LIAAPFAGFL VWTACAWNSL RGISNGVEDT
GGAGKVSRGS ERELKSHKRE TKETMWGTLS RARRSMICLP HPTAVCSNVR TRIAGPIVQV
QPVSYKEQVE FLDWLKERGQ RDAYLSTTVG ISTHGRALFA TRPIQAGERV LRVSRDLLIT
PDKLPKEVTK LLPQDVSEWA RLALFLLAEQ HKGQESTWSP YISCLPPLGA IHSTVFWKKE
ELELVRHSSL HRETVQRKAI IGAEFAAVQP VPFVDFFNHE SYCQALLSYD EEQGYAEVIA
DRDYAVGSQV VLSYGRLPNS ILALDFGFTL PENPHDQVEV WMGVSRRDEL RKLKLQLLHA
HDMPTFLHAD GSDSGGSGFN IRFVKSAIGR GKGIPHALRA FARVLCVDNA QELTEMAAEA
TKLDGRLARR PLKDKNREAQ AMSLLLARLE SMMQQRHSAL LTLRLVETCR GSNSGSKSPV
TVHVHMAGAV VSGEMRVLRS AIAWLRNHCS PSTVLT
//
