ID A0A168GD72_CORDF Unreviewed; 524 AA.
AC A0A168GD72;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Protein arginine methyltransferase RmtB {ECO:0000313|EMBL:OAA76337.1};
GN ORFNames=LEL_06021 {ECO:0000313|EMBL:OAA76337.1};
OS Akanthomyces lecanii RCEF 1005.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Akanthomyces;
OC Cordyceps confragosa.
OX NCBI_TaxID=1081108 {ECO:0000313|EMBL:OAA76337.1, ECO:0000313|Proteomes:UP000076881};
RN [1] {ECO:0000313|EMBL:OAA76337.1, ECO:0000313|Proteomes:UP000076881}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RCEF 1005 {ECO:0000313|EMBL:OAA76337.1,
RC ECO:0000313|Proteomes:UP000076881};
RX PubMed=27071652; DOI=10.1093/gbe/evw082;
RA Shang Y., Xiao G., Zheng P., Cen K., Zhan S., Wang C.;
RT "Divergent and convergent evolution of fungal pathogenicity.";
RL Genome Biol. Evol. 8:1374-1387(2016).
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:OAA76337.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AZHF01000004; OAA76337.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A168GD72; -.
DR STRING; 1081108.A0A168GD72; -.
DR OrthoDB; 197898at2759; -.
DR Proteomes; UP000076881; Unassembled WGS sequence.
DR GO; GO:0016274; F:protein-arginine N-methyltransferase activity; IEA:InterPro.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 2.70.160.11; Hnrnp arginine n-methyltransferase1; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR049482; ANM3-like_C2H2_Zf.
DR InterPro; IPR025799; Arg_MeTrfase.
DR InterPro; IPR041698; Methyltransf_25.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR PANTHER; PTHR11006; PROTEIN ARGININE N-METHYLTRANSFERASE; 1.
DR PANTHER; PTHR11006:SF116; PROTEIN METHYLTRANSFERASE; 1.
DR Pfam; PF21137; ANM3_C2H2_Zf; 1.
DR Pfam; PF13649; Methyltransf_25; 1.
DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS51678; SAM_MT_PRMT; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW ProRule:PRU01015}; Reference proteome {ECO:0000313|Proteomes:UP000076881};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW ECO:0000256|PROSITE-ProRule:PRU01015};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW ProRule:PRU01015}.
FT DOMAIN 58..102
FT /note="Protein arginine N-methyltransferase 3-like C2H2
FT zinc finger"
FT /evidence="ECO:0000259|Pfam:PF21137"
FT DOMAIN 228..325
FT /note="Methyltransferase"
FT /evidence="ECO:0000259|Pfam:PF13649"
FT REGION 120..141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 524 AA; 59184 MW; B20DD69BB8FFA592 CRC64;
MSVSSDSENS DAAGWLDVEP DQEQITFVSL FDAETFSSIE DLLTHCKTQH AFDLVATIHR
LGLEFHDAIK LVNFIRACTL EKKSLPQVVS VHDFSDDKYL KPVLENDALL FSLDEILPEV
PENTENASPE KSSSPETRNK ELEAELAAVN ERFASYRMAV EETLDKRWGD ENEAGKPGSE
KKKDSSDYYF ESYAYNDIHE TMLKDEVRTD AYRDFIYENK QLFQGKIVLD IGCGTGILSM
FCARAGAAQV IAVDKSDIID KARENVFNNG LAGTITCLRG AIEDVKLPVD QVDIIVSEWM
GYCLLYEAML PSVLYARDKY LRPDGLLVPS SATIWVAPVR DSEFVTDTVS FWRDVYGFDM
KAMQECIYDE TRILNMPPAA VCGTPYPFKV LDLHTVKPED LFFTATWESQ VNRDIDSLDG
FLIWFDNFFA NCRADKLPAP ETTPEVFVKQ KSGYVAFTTG PFGKATHWKQ GLLLQPPTEL
KASQPKLTGQ IVFSALEENA RALDIRLTWA EEGREEESRS WKLK
//
