ID A0A0P1BFB1_9BASI Unreviewed; 1635 AA.
AC A0A0P1BFB1;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Protein kinase inhibitor {ECO:0000313|EMBL:CEH14590.1};
OS Ceraceosorus bombacis.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Exobasidiomycetes; Ceraceosorales; Ceraceosoraceae; Ceraceosorus.
OX NCBI_TaxID=401625 {ECO:0000313|EMBL:CEH14590.1, ECO:0000313|Proteomes:UP000054845};
RN [1] {ECO:0000313|EMBL:CEH14590.1, ECO:0000313|Proteomes:UP000054845}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Magalhaes I.L.F., Oliveira U., Santos F.R., Vidigal T.H.D.A.,
RA Brescovit A.D., Santos A.J.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CCYA01000243; CEH14590.1; -; Genomic_DNA.
DR STRING; 401625.A0A0P1BFB1; -.
DR OrthoDB; 5489665at2759; -.
DR Proteomes; UP000054845; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
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; 3.20.20.70; Aldolase class I; 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; IPR013785; Aldolase_TIM.
DR InterPro; IPR025799; Arg_MeTrfase.
DR InterPro; IPR001155; OxRdtase_FMN_N.
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; PF00724; Oxidored_FMN; 1.
DR Pfam; PF05185; PRMT5; 1.
DR Pfam; PF17286; PRMT5_C; 1.
DR Pfam; PF17285; PRMT5_TIM; 1.
DR SUPFAM; SSF51395; FMN-linked oxidoreductases; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS51678; SAM_MT_PRMT; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW ProRule:PRU01015}; Reference proteome {ECO:0000313|Proteomes:UP000054845};
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}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1611..1630
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 298..570
FT /note="PRMT5 TIM barrel"
FT /evidence="ECO:0000259|Pfam:PF17285"
FT DOMAIN 579..744
FT /note="PRMT5 arginine-N-methyltransferase"
FT /evidence="ECO:0000259|Pfam:PF05185"
FT DOMAIN 747..946
FT /note="PRMT5 oligomerisation"
FT /evidence="ECO:0000259|Pfam:PF17286"
FT DOMAIN 1138..1406
FT /note="NADH:flavin oxidoreductase/NADH oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00724"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 41..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 173..201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 213..301
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 432..451
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1435..1465
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 213..228
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 265..291
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1440..1457
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1635 AA; 175293 MW; A99FB5DFCCD4C657 CRC64;
MSAPAPVGVE SGPPLPIGQF VDFNSHGPQP VKAFPYASLA AVESQARRGP PSASGSTSGR
ATPGGLEPLP EASHINALSE ASGPSPAGLP GPKGSASATS RSNGKAASSR LEGLSADIDA
ALAGLTQVQR LRAILRSEGY DKVVVPLTNE KWKDRWERMC LAPATPVMNG HMAGDGPAPA
HDSPGASAWD QPKHAMSNPG AMGESWEILT REQGMKRSTS RPHVALPDDS PRRGGTAPEG
APKSGGGSGP AATFKRKLKS PMMSGHGSGG SSKSPPSEAS APSTAFAFSS ETEEQARMRE
AEDWRRAPAF RRNEVNIAKI DETDGLVAVI SPWLELDSPD EGVRLDSEIA LRQEVAYAAF
LGIPQVVLPA PSSSPSHVPF LPFYARAISG LLSSGGTETA PAGSWMQLSL RLPVSSVHAA
RIWLNKQSGA KSSKSTESLD SGFTSGTERD RGAAVRSDND WAWSVWELMR QITGYPTRLS
VALDLGVPLP SAASLSHWAA EPVGLVLMPA GSFLANAKGF PVLSKAAQSL CRSLMRRKPL
FVLSGIQEPP PRHTRGTPSG YLQYLRHIER SAPAESAVDT FARGYADWLQ APLQPLMDNL
ESQTYEVFER DPIKYQLYEE AVAQALADRS VVGVISVWVC GAGRGPLVSR VLAAATKARR
NVKVIALEKN ANALVTLQER IVNEWGDKVE LRFGDMRTMP APSDVRQRAD IVVSELLGSF
GDNELSPECL DGAMRFLKPD GVSIPSSYTP FLTPLSSAKL HSEVLNVGGS TGNAPSSGSL
TERLTKASET PYVVLFQAVQ LLAAHGGRGN WEQVQHAWTF EHAPLESTPT VRGHDGLPIT
NQHNVRSTTH TFHIPEAGTC HGLAGYFEAH LYGNVFCSIH PDPERTSTDM LSWFPIFFPF
KEPLYLPAKS ELDVSMWRLT SDRKVWYEWC AQAYLSGAAL AIQTEAEVRP SARRQASIPG
LRTVSAASND SHDAGANGAF VNAPNTPGMP SVLLPSSSDE VHSHSAAAAA MGRPKSVAGN
HVATSNIIIP QRIYIAGTAL HNPGGSPSVR ILHSLRLAPV IQTKVVSLSV VCSLDINPRV
FYCYHLGHRS FSAFTRAVTY RLSNTSPRPN AGSTGAAPAS LPDQKMSESV KILSQKLDFG
NGKVAPNRLV KAPMEEMLGR FGGSAPTPAL LKLYRHWAKA GWGMVITGNV AVDRTHLGFP
WDISFPSPPH SDALISDFKA YAEASSGRDN SSIDEADRPL VVVQLVHAGR QSLRGSGRAP
WKPALAPSAV PMRPSEGMGV VGKALDWLLW GTPRAMTLPE IQEMVNRFAA AAEACSRAGF
DGIELHASHG YQLSAFLSPR TNLRADAYGG DAQRRARILL EIVTEARKRV PREFLIGVKL
NSSDYIQGGL TEDDALLNVR WLAEHGGVDF VEISGGNYEN PSFMTEGFNA EEEMRKLQGD
TSVSAPQRGT EASQRQKDQG ARSARSHARE AFFHNFAKKA RDNLPASSST RLIVTGGLKT
RAGMASAIEN SHVDGVGIGR MAAVYPDLPR RVLDQNVVDD EDPRANGPKY VIPGSGLLGY
IPIKFVGAGW GTAWHNGMMS YLVLDRKPDV HASTPRILLG IFAPSVLQLR IHAFIAAILV
FLVAFLPGVA RQKTV
//
