ID A0A095CDT5_CRYGR Unreviewed; 856 AA.
AC A0A095CDT5;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 47.
DE RecName: Full=Protein arginine N-methyltransferase {ECO:0000256|PIRNR:PIRNR015894};
GN ORFNames=CNBG_3482 {ECO:0000313|EMBL:KGB77644.1};
OS Cryptococcus gattii serotype B (strain R265) (Filobasidiella gattii)
OS (Cryptococcus bacillisporus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus;
OC Cryptococcus gattii species complex.
OX NCBI_TaxID=294750 {ECO:0000313|EMBL:KGB77644.1, ECO:0000313|Proteomes:UP000029445};
RN [1] {ECO:0000313|EMBL:KGB77644.1, ECO:0000313|Proteomes:UP000029445}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R265 {ECO:0000313|EMBL:KGB77644.1};
RX PubMed=21304167; DOI=10.1128/mBio.00342-10;
RA D'Souza C.A., Kronstad J.W., Taylor G., Warren R., Yuen M., Hu G.,
RA Jung W.H., Sham A., Kidd S.E., Tangen K., Lee N., Zeilmaker T., Sawkins J.,
RA McVicker G., Shah S., Gnerre S., Griggs A., Zeng Q., Bartlett K., Li W.,
RA Wang X., Heitman J., Stajich J.E., Fraser J.A., Meyer W., Carter D.,
RA Schein J., Krzywinski M., Kwon-Chung K.J., Varma A., Wang J., Brunham R.,
RA Fyfe M., Ouellette B.F., Siddiqui A., Marra M., Jones S., Holt R.,
RA Birren B.W., Galagan J.E., Cuomo C.A.;
RT "Genome variation in Cryptococcus gattii, an emerging pathogen of
RT immunocompetent hosts.";
RL MBio 2:E342-E342(2011).
RN [2] {ECO:0000313|EMBL:KGB77644.1, ECO:0000313|Proteomes:UP000029445}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R265 {ECO:0000313|EMBL:KGB77644.1};
RX PubMed=29507212;
RA Yadav V., Sun S., Billmyre R.B., Thimmappa B.C., Shea T., Lintner R.,
RA Bakkeren G., Cuomo C.A., Heitman J., Sanyal K.;
RT "RNAi is a critical determinant of centromere evolution in closely related
RT fungi.";
RL Proc. Natl. Acad. Sci. 115:3108-3113(2018).
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. {ECO:0000256|PIRNR:PIRNR015894}.
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DR EMBL; CP025759; KGB77644.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A095CDT5; -.
DR STRING; 294750.A0A095CDT5; -.
DR VEuPathDB; FungiDB:CNBG_3482; -.
DR HOGENOM; CLU_010247_0_0_1; -.
DR OMA; WEFSHPI; -.
DR Proteomes; UP000029445; Chromosome 1.
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; 3.20.20.150; Divalent-metal-dependent TIM barrel enzymes; 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; IPR025799; Arg_MeTrfase.
DR InterPro; IPR007857; Arg_MeTrfase_PRMT5.
DR InterPro; IPR035075; PRMT5.
DR InterPro; IPR035248; PRMT5_C.
DR InterPro; IPR035247; PRMT5_TIM.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR10738; PROTEIN ARGININE N-METHYLTRANSFERASE 5; 1.
DR PANTHER; PTHR10738:SF0; PROTEIN ARGININE N-METHYLTRANSFERASE 5; 1.
DR Pfam; PF05185; PRMT5; 1.
DR Pfam; PF17286; PRMT5_C; 1.
DR Pfam; PF17285; PRMT5_TIM; 1.
DR PIRSF; PIRSF015894; Skb1_MeTrfase; 2.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS51678; SAM_MT_PRMT; 1.
PE 3: Inferred from homology;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000256|PIRNR:PIRNR015894};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW ECO:0000256|PIRNR:PIRNR015894};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR015894}.
FT DOMAIN 40..414
FT /note="PRMT5 TIM barrel"
FT /evidence="ECO:0000259|Pfam:PF17285"
FT DOMAIN 438..596
FT /note="PRMT5 arginine-N-methyltransferase"
FT /evidence="ECO:0000259|Pfam:PF05185"
FT DOMAIN 599..853
FT /note="PRMT5 oligomerisation"
FT /evidence="ECO:0000259|Pfam:PF17286"
FT REGION 213..246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 567
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR015894-1"
FT ACT_SITE 576
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR015894-1"
FT BINDING 461
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR015894-2"
FT BINDING 470..471
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR015894-2"
FT BINDING 524
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR015894-2"
FT BINDING 551..552
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR015894-2"
FT SITE 464
FT /note="Critical for specifying symmetric addition of methyl
FT groups"
FT /evidence="ECO:0000256|PIRSR:PIRSR015894-3"
SQ SEQUENCE 856 AA; 92625 MW; E5D731E5D4B025A3 CRC64;
MPRHNVALYL PHPLPSLPIE PPPTPSPLQQ VIASTLSTTD YDHVSLPLTN TAWQARWEKL
CLRPIEEEGL SEEELERRAI EERKVDQEAD VWRRDGGLKR SEVVVSRLEE SQGVIPLASE
WLELDSPDEG IRFDSELALR AEFAHALYLS LPVLILPAPS LANRAFLPSY ARAICNLLQM
GGQSAVTNIS IRIPVSNPLE LIAPESVVPN GLAGSHSSVA PPSASGAPQM DKKHKRLSSL
STRPQSMQTS LFGQPANQGT NQNQQQGMRI TSGASSLISA NTAYGSVAGS GQASLSVTAH
GGDLSSTWEM WDCIRTLCGY HPRLSVTLDL TNPLPPSAGA LARWSAEPVN YIWLPASSFI
PNAKGYPVLS KACQAFIREM GKQNPTYILS QTTMKRHSAG GHNAYLQYIR HITSTPQPGP
NTQPRAIMAL PAGASEKFQG YSDYLQAPLQ PLMDDLGSMT YNIFENDPVK YAQYETAITQ
ALLDLPANKK HVVTVVGAGR GPLVDCTLRA LLHSGRQASI YAVEKNTNAF VTLQERKELE
WRDKVHIISG DMRVIDVPEK CDILVSELLG SFGDNELSPE CLDGALRLMK STGVSIPSSY
TAHIAPLSTS KLYQETHSPS RGPSSAETPY VVMLSQVDPI SGDNNVPGVS ARCGERIQQC
WQFVHPNRDI TVDSNGIPLS NSHNARASTH TFHIPHAATL HGFGGYFEAH LYGDVGLSIH
PENAHAVSPD LTSWFPLFFP LKEPMYLPSG SELQVNLWRM GDGKGKKVWY EWAVESYLPV
VQSVSSAPGA VTVPGSRNVS SASGSGIGFG GQPSPLMDAP FSPGMGHIGL PGGLGRVKIG
QSTLHNPGGI HSWVGL
//
