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Database: UniProt
Entry: A0A2V0P2P9_9CHLO
LinkDB: A0A2V0P2P9_9CHLO
Original site: A0A2V0P2P9_9CHLO 
ID   A0A2V0P2P9_9CHLO        Unreviewed;       873 AA.
AC   A0A2V0P2P9;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Alkylated DNA repair protein {ECO:0000313|EMBL:GBF93859.1};
GN   ORFNames=Rsub_06858 {ECO:0000313|EMBL:GBF93859.1};
OS   Raphidocelis subcapitata.
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC   CS clade; Sphaeropleales; Selenastraceae; Raphidocelis.
OX   NCBI_TaxID=307507 {ECO:0000313|EMBL:GBF93859.1, ECO:0000313|Proteomes:UP000247498};
RN   [1] {ECO:0000313|EMBL:GBF93859.1, ECO:0000313|Proteomes:UP000247498}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIES-35 {ECO:0000313|EMBL:GBF93859.1,
RC   ECO:0000313|Proteomes:UP000247498};
RX   PubMed=29795299; DOI=10.1038/s41598-018-26331-6;
RA   Suzuki S., Yamaguchi H., Nakajima N., Kawachi M.;
RT   "Raphidocelis subcapitata (=Pseudokirchneriella subcapitata) provides an
RT   insight into genome evolution and environmental adaptations in the
RT   Sphaeropleales.";
RL   Sci. Rep. 8:8058-8058(2018).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC       Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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:GBF93859.1}.
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DR   EMBL; BDRX01000045; GBF93859.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2V0P2P9; -.
DR   STRING; 307507.A0A2V0P2P9; -.
DR   InParanoid; A0A2V0P2P9; -.
DR   Proteomes; UP000247498; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:InterPro.
DR   GO; GO:0008175; F:tRNA methyltransferase activity; IEA:UniProt.
DR   GO; GO:0043412; P:macromolecule modification; IEA:UniProt.
DR   GO; GO:0008033; P:tRNA processing; IEA:UniProt.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   Gene3D; 2.60.120.590; Alpha-ketoglutarate-dependent dioxygenase AlkB-like; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR027450; AlkB-like.
DR   InterPro; IPR037151; AlkB-like_sf.
DR   InterPro; IPR013216; Methyltransf_11.
DR   InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR13069:SF21; ALKYLATED DNA REPAIR PROTEIN ALKB HOMOLOG 8; 1.
DR   PANTHER; PTHR13069; UNCHARACTERIZED; 1.
DR   Pfam; PF13532; 2OG-FeII_Oxy_2; 1.
DR   Pfam; PF08241; Methyltransf_11; 1.
DR   SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS51471; FE2OG_OXY; 1.
PE   4: Predicted;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00022516};
KW   Reference proteome {ECO:0000313|Proteomes:UP000247498};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          276..377
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51471"
FT   REGION          79..99
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          226..245
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          406..481
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          651..822
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        664..683
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        719..734
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        781..800
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   873 AA;  89698 MW;  63F0B6680F2498BB CRC64;
     MAAAPREFRR PPNSEPTRHL RITRANAGAT EPLSPADAAA VAAALAAPPA LAPALRAAAD
     GPRLYLSFAS EADATAARAR LSSDAPETGG AEAGAAVDGA DGAGAGATAL WPLDVRYCIR
     HESRSPEPPP PEAATTSAAA GVPGLLLLPH YVSVGEEAAM LAAIDANAAG WVALSRRRVQ
     HYGFRFEYAL RSVDPAAAAA EPLPPWLSAL VARIASDPRI TKLARTTEAP AASDPARLPA
     SGAPPAASGA AAAATGAAVA AASAARAPAS DGGALVFDQA TVNEYEAGVG LSPHVDTHSA
     FQGPILSLSL AGGAVMEFRR GGERRALMLP PRSLLVMAGE ARYAWQHYIP HRKRDTVEGI
     TLPRPPRRVS VTLRRVRRPE AGPCRCAWPD CCDCQEGVLP PTRLQVLQPG AEPGDECAAG
     DARPCSAAGS PAGSPTLKPR GGAAEAGHRD GDDDDDAGAQ NGVAASDGEA RAPDGEGASA
     SELAARRLEA LHVHSVYDAI APHFSATRFA IWPKVREFLE SLPPGAVVAD VGCGNGKYFG
     VRRDLAVIGS DRSAGLAAVA ARRIRPSGLP SLYVPAADVL VADGLSPPYR RGCADAALCI
     AVLHHLSSAP RRRRMLEALV RLLRPGGRAL VTVWAAEQED PRRTIQKWTP FGGAQQEQEQ
     QQAQAGRREQ REQQQREEGE QQEQQQEQQE QQQGEEGEEA AALDSASSCG DGGAESGARN
     GSGASTSDGS GSGGSGGSGG GGGGGGGGGG GGGDFLVPWH LPFHRAGGAA ASAAATPAAA
     RAHQPSQQPQ QQQNNGEHER GQDGAAQGTG AAPTAAPHGA PRLDASKGAV VFQRYYHLFK
     KGELEALVAT VPGATLAGSF YDRSNWCAVV ERL
//
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