ID A0A1W0A934_9STRA Unreviewed; 1540 AA.
AC A0A1W0A934;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Alkylated DNA repair protein alkB homolog 8 {ECO:0008006|Google:ProtNLM};
GN ORFNames=THRCLA_01232 {ECO:0000313|EMBL:OQS06738.1};
OS Thraustotheca clavata.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC Thraustotheca.
OX NCBI_TaxID=74557 {ECO:0000313|EMBL:OQS06738.1, ECO:0000313|Proteomes:UP000243217};
RN [1] {ECO:0000313|EMBL:OQS06738.1, ECO:0000313|Proteomes:UP000243217}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 34112 {ECO:0000313|EMBL:OQS06738.1,
RC ECO:0000313|Proteomes:UP000243217};
RX PubMed=25527045; DOI=10.1093/gbe/evu276;
RA Misner I., Blouin N., Leonard G., Richards T.A., Lane C.E.;
RT "The secreted proteins of Achlya hypogyna and Thraustotheca clavata
RT identify the ancestral oomycete secretome and reveal gene acquisitions by
RT horizontal gene transfer.";
RL Genome Biol. Evol. 7:120-135(2014).
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:OQS06738.1}.
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DR EMBL; JNBS01000310; OQS06738.1; -; Genomic_DNA.
DR STRING; 74557.A0A1W0A934; -.
DR OrthoDB; 54820at2759; -.
DR Proteomes; UP000243217; 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; 3.40.250.10; Rhodanese-like domain; 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; IPR000195; Rab-GAP-TBC_dom.
DR InterPro; IPR001763; Rhodanese-like_dom.
DR InterPro; IPR036873; Rhodanese-like_dom_sf.
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; SSF52821; Rhodanese/Cell cycle control phosphatase; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS51471; FE2OG_OXY; 1.
DR PROSITE; PS50206; RHODANESE_3; 1.
DR PROSITE; PS50086; TBC_RABGAP; 1.
PE 4: Predicted;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Reference proteome {ECO:0000313|Proteomes:UP000243217};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 21..124
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
FT DOMAIN 633..837
FT /note="Rab-GAP TBC"
FT /evidence="ECO:0000259|PROSITE:PS50086"
FT DOMAIN 1025..1145
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
FT REGION 432..451
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 467..488
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 511..614
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 915..950
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1203..1224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1337..1383
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 467..481
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 511..533
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 541..556
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 567..586
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 598..614
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1339..1353
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1540 AA; 168747 MW; 94001FD4406DC909 CRC64;
MPNFCKNIAE TMHALRPDLD LPDQCTINEY IPGQGIAPHV DTADVFTEYI ASLSLGSDIV
MDFRLASNPS IVKHVHLKRG SLCLMVAEAR YHWKHGIAYR KHDRIAGKIT SRSRRVSMTF
RKVLNERNSS RMNQSVQKPS EIEMEHVHGV YDSIASHFSH TRHHPWPLVA DFLNGLPSGS
MVADIGCGNG KYLGVNSDLM MIGSDRSIPL LTVCSQRSHE VFGCDGLAVP LRTGAFDAAI
CIAVLHHMST IEHRLQILRE LSRIVKVGGQ IYIVAWAFEQ DERSKRKFET QDVMVEWKLQ
QKYIDTREPL PNHVQLDKEK KWAIYQRYCH VYRDLELEML VRQIPGLTVT KVEMMRTAPM
SSLDDIFGDC NEFLASTSAA PSSSFSLEGL GLDDLGLGEL KPSGDVLSPT TAAITSDPSD
FLSWLDAKPT SPVGNEPKLD GPASESFNFD SPLTVPAKAS VDTTFVLDDE PKEDKEIPAT
PVPPVDKRVE NEFAVPPPAP QVKEIQVEAN STGNPFLNPA PAAKTNSKPA TPISSVRKEE
PKPLTPTSSF SMSPPAPGGD KTTPPPTNID GDKTAPFQSN RSVPPAIETK EESRGSSFEN
AKSPANLPTY SSQDGTKVIA NDELRAHYRA LNKIPIEERL QAWCTLLEAP LLETKSIELG
SSEQIRRDAE AVCSLLFADG VFCKGLEKDG VSPDTARLSL TDQVEALILN ECEKHTIAYT
PGLALAFAPL IFLGGADPLR SDLFGIMNMI TVRMFPHLIA HVPMSHVALA RRPLLKLLLL
YHDPTIALHL DHTFPSWSEP GLIPDQWLAS LLEGTDHTTA IGLEVASRVW DCCVVNASST
YPAIIMIFVL LAAILGSKKR LLSLTNGPNL RSCMLQLFVE TMSRHQTLIA NVHELIEKTP
FSFCTKLCDA GMETQTSSPV EESRSGSFTR TGSSSSVVSP KPRTASKESL EVKTTSKFSL
GQLSSINTKI LAQASHLKSS ITGKAEDSRS DSFHLETPCT YFSMTISACE VIPSVFRSFK
SSCTEKIRYF IVDCRPQESL ALGRIPTSFH FNSESLLDPA AFDTVMATLE PMKSSVHICI
MGHGHSRYAS SMVKDLNYNK SDVADMIAKD AAQINDTVMF LTKKGFPYVS IIDGGYASAH
RYLAKSRLFT LSDLCDHDPN NCNLCHHGQT LKAKGRTSST ASLMSDEENE HIQRSEGGVC
LGRFGPDGRV RSKPTTPSEV TSPSSYFSSM TTALKDGGKT LTAVSGKTLN AVPGSALMSG
AFKDSKNWMM KKKDSIDIGG KLSDAKAHLH LNEINMPSMT SVRSAVDAAV KRDSTLNPAN
MLKKAASSFA ATMGPMEPAA TMGNSTSGVH SPPIATSPGA KKPAVKPASE AVFSIDDDDE
DEVDRALNST DGGYDEAEAP AVEHIVEKGQ IQLLKKGMQI HMHQLLPLVS SPLFSCYKKK
IRNGGSTLVP RYIVIAEGHI IVLRPDKGQE DASSVRSCHH LSHVARMTCM KKNALMVTMY
YKFDGKEKQN SYEVQQRDAF IKVVRSSMEE LAAQQRQREE
//
