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Database: UniProt
Entry: J3KBB1_COCIM
LinkDB: J3KBB1_COCIM
Original site: J3KBB1_COCIM 
ID   J3KBB1_COCIM            Unreviewed;       555 AA.
AC   J3KBB1;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 2.
DT   27-MAR-2024, entry version 54.
DE   SubName: Full=Protein arginine methyltransferase RmtB {ECO:0000313|EMBL:EAS32393.3};
GN   ORFNames=CIMG_03417 {ECO:0000313|EMBL:EAS32393.3};
OS   Coccidioides immitis (strain RS) (Valley fever fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX   NCBI_TaxID=246410 {ECO:0000313|EMBL:EAS32393.3, ECO:0000313|Proteomes:UP000001261};
RN   [1] {ECO:0000313|Proteomes:UP000001261}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RS {ECO:0000313|Proteomes:UP000001261};
RX   PubMed=19717792; DOI=10.1101/gr.087551.108;
RA   Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA   Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA   McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA   Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA   Henn M.R., Birren B.W., Taylor J.W.;
RT   "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT   and their relatives.";
RL   Genome Res. 19:1722-1731(2009).
RN   [2] {ECO:0000313|Proteomes:UP000001261}
RP   GENOME REANNOTATION.
RC   STRAIN=RS {ECO:0000313|Proteomes:UP000001261};
RX   PubMed=20516208; DOI=10.1101/gr.103911.109;
RA   Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J.,
RA   Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D.,
RA   Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A.,
RA   FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J.,
RA   Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R.,
RA   Taylor J.W., Rounsley S.D.;
RT   "Population genomic sequencing of Coccidioides fungi reveals recent
RT   hybridization and transposon control.";
RL   Genome Res. 20:938-946(2010).
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR   EMBL; GG704916; EAS32393.3; -; Genomic_DNA.
DR   RefSeq; XP_001243976.2; XM_001243975.2.
DR   AlphaFoldDB; J3KBB1; -.
DR   STRING; 246410.J3KBB1; -.
DR   GeneID; 4564562; -.
DR   KEGG; cim:CIMG_03417; -.
DR   VEuPathDB; FungiDB:CIMG_03417; -.
DR   InParanoid; J3KBB1; -.
DR   OMA; DGWAVWF; -.
DR   OrthoDB; 197898at2759; -.
DR   Proteomes; UP000001261; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW   ProRule:PRU01015}; Reference proteome {ECO:0000313|Proteomes:UP000001261};
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          81..125
FT                   /note="Protein arginine N-methyltransferase 3-like C2H2
FT                   zinc finger"
FT                   /evidence="ECO:0000259|Pfam:PF21137"
FT   DOMAIN          258..355
FT                   /note="Methyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF13649"
FT   REGION          1..45
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          150..177
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1..18
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   555 AA;  62753 MW;  3A16AF4F45A64FE0 CRC64;
     MTDSELPARP REAVDDVEDS SSESSPSECL DLTKDDGWED VEPDEEVNPV VDLFSDKVFP
     DTRSMLQHCK ENFNFDLVKV QKQLGLDFLG TIKLVNYIRS EVQSGNTKPD VSSSAPFEDD
     KYLKPVLEDD ALLYTLEDIS DGDEDLGQQA ANPTSRIRDL EEELSRLREE FVEYKNMVQR
     SLSKQLGSEV ENGSQIPPNQ NQNEHVTETR RYKDAEAGYF TSYAYNTIHE SMLKDTVRTD
     SYRDFIYDNK SIFKDKVVLD VGCGSGILSM FCAKAGAKMV IAVDNSDIID KARQIVYENG
     FGDVIKCIRG KIEEVVLPVK QVDVIVSEWM GYCLLFEAML DSVLFARDRY LAPGGLMVPS
     HATLRIAPIA DSDFIDEHIS FWNSVYGFKM SGMLENVYDE VLIQTISPSA MVADSALFLS
     LPLHTITVEE LTFVKEFKVA ITKDADTLDG WLVWFDMFFM PSCESKLADN ATPGEMKKSG
     YVAFTTGPDG KETHWQQGVF LINRGKHQER PLKKGQVIKG KIGYKKKEEQ SRLLDIDIEW
     AVDEEPPVHQ EWALQ
//
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