ID L1J438_GUITC Unreviewed; 1194 AA.
AC L1J438;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=SWIRM domain-containing protein {ECO:0000259|PROSITE:PS50934};
GN ORFNames=GUITHDRAFT_110688 {ECO:0000313|EMBL:EKX43273.1};
OS Guillardia theta (strain CCMP2712) (Cryptophyte).
OC Eukaryota; Cryptophyceae; Pyrenomonadales; Geminigeraceae; Guillardia.
OX NCBI_TaxID=905079 {ECO:0000313|EMBL:EKX43273.1};
RN [1] {ECO:0000313|EMBL:EKX43273.1, ECO:0000313|Proteomes:UP000011087}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CCMP2712 {ECO:0000313|EMBL:EKX43273.1,
RC ECO:0000313|Proteomes:UP000011087};
RX PubMed=23201678; DOI=10.1038/nature11681;
RG DOE Joint Genome Institute;
RA Curtis B.A., Tanifuji G., Burki F., Gruber A., Irimia M., Maruyama S.,
RA Arias M.C., Ball S.G., Gile G.H., Hirakawa Y., Hopkins J.F., Kuo A.,
RA Rensing S.A., Schmutz J., Symeonidi A., Elias M., Eveleigh R.J.,
RA Herman E.K., Klute M.J., Nakayama T., Obornik M., Reyes-Prieto A.,
RA Armbrust E.V., Aves S.J., Beiko R.G., Coutinho P., Dacks J.B.,
RA Durnford D.G., Fast N.M., Green B.R., Grisdale C.J., Hempel F.,
RA Henrissat B., Hoppner M.P., Ishida K., Kim E., Koreny L., Kroth P.G.,
RA Liu Y., Malik S.B., Maier U.G., McRose D., Mock T., Neilson J.A.,
RA Onodera N.T., Poole A.M., Pritham E.J., Richards T.A., Rocap G., Roy S.W.,
RA Sarai C., Schaack S., Shirato S., Slamovits C.H., Spencer D.F., Suzuki S.,
RA Worden A.Z., Zauner S., Barry K., Bell C., Bharti A.K., Crow J.A.,
RA Grimwood J., Kramer R., Lindquist E., Lucas S., Salamov A., McFadden G.I.,
RA Lane C.E., Keeling P.J., Gray M.W., Grigoriev I.V., Archibald J.M.;
RT "Algal genomes reveal evolutionary mosaicism and the fate of
RT nucleomorphs.";
RL Nature 492:59-65(2012).
RN [2] {ECO:0000313|Proteomes:UP000011087}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CCMP2712 {ECO:0000313|Proteomes:UP000011087};
RA Kuo A., Curtis B.A., Tanifuji G., Burki F., Gruber A., Irimia M.,
RA Maruyama S., Arias M.C., Ball S.G., Gile G.H., Hirakawa Y., Hopkins J.F.,
RA Rensing S.A., Schmutz J., Symeonidi A., Elias M., Eveleigh R.J.,
RA Herman E.K., Klute M.J., Nakayama T., Obornik M., Reyes-Prieto A.,
RA Armbrust E.V., Aves S.J., Beiko R.G., Coutinho P., Dacks J.B.,
RA Durnford D.G., Fast N.M., Green B.R., Grisdale C., Hempe F., Henrissat B.,
RA Hoppner M.P., Ishida K.-I., Kim E., Koreny L., Kroth P.G., Liu Y.,
RA Malik S.-B., Maier U.G., McRose D., Mock T., Neilson J.A., Onodera N.T.,
RA Poole A.M., Pritham E.J., Richards T.A., Rocap G., Roy S.W., Sarai C.,
RA Schaack S., Shirato S., Slamovits C.H., Spencer D.F., Suzuki S.,
RA Worden A.Z., Zauner S., Barry K., Bell C., Bharti A.K., Crow J.A.,
RA Grimwood J., Kramer R., Lindquist E., Lucas S., Salamov A., McFadden G.I.,
RA Lane C.E., Keeling P.J., Gray M.W., Grigoriev I.V., Archibald J.M.;
RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblProtists:EKX43273}
RP IDENTIFICATION.
RG EnsemblProtists;
RL Submitted (JUN-2015) to UniProtKB.
CC -!- SIMILARITY: Belongs to the flavin monoamine oxidase family.
CC {ECO:0000256|ARBA:ARBA00005995}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JH993011; EKX43273.1; -; Genomic_DNA.
DR RefSeq; XP_005830253.1; XM_005830196.1.
DR AlphaFoldDB; L1J438; -.
DR STRING; 905079.L1J438; -.
DR PaxDb; 55529-EKX43273; -.
DR EnsemblProtists; EKX43273; EKX43273; GUITHDRAFT_110688.
DR GeneID; 17300001; -.
DR KEGG; gtt:GUITHDRAFT_110688; -.
DR eggNOG; KOG0029; Eukaryota.
DR HOGENOM; CLU_271536_0_0_1; -.
DR OrthoDB; 5402444at2759; -.
DR Proteomes; UP000011087; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0140993; F:histone modifying activity; IEA:UniProt.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:UniProt.
DR GO; GO:0010558; P:negative regulation of macromolecule biosynthetic process; IEA:UniProt.
DR CDD; cd04508; Tudor_SF; 3.
DR Gene3D; 2.30.30.140; -; 2.
DR Gene3D; 3.90.660.10; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR InterPro; IPR002937; Amino_oxidase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR007526; SWIRM.
DR InterPro; IPR002999; Tudor.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR PANTHER; PTHR10742; FLAVIN MONOAMINE OXIDASE; 1.
DR PANTHER; PTHR10742:SF386; LYSINE-SPECIFIC HISTONE DEMETHYLASE 1A; 1.
DR Pfam; PF01593; Amino_oxidase; 2.
DR Pfam; PF12831; FAD_oxidored; 1.
DR Pfam; PF04433; SWIRM; 1.
DR SMART; SM00333; TUDOR; 3.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
DR SUPFAM; SSF46689; Homeodomain-like; 1.
DR PROSITE; PS50934; SWIRM; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000011087}.
FT DOMAIN 59..157
FT /note="SWIRM"
FT /evidence="ECO:0000259|PROSITE:PS50934"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 237..264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 464..484
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 618..652
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 688..756
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 795..891
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 940..959
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 237..260
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 621..640
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 708..751
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 810..824
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 825..868
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 869..891
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1194 AA; 132996 MW; AAB1B85F8419A4A7 CRC64;
MPVRNIKKQD KIVSQQRIET SPQEFLKDDE AKECNDVSLD GCKHEKEPQG CDDESVICEG
GLENFIWLPV KGMTLLEEQE LPLLATSPIS YVKLRNHILS TWHKNPSQEL THEAAALDAP
IVFHRREAQA EAIRLIHEFL SCHGHINVGV FAPKTPTLMS NSSTATAGSE DGGAGVEGGK
GEAYDVIVVG GGIAGLAAAS QLKRRGHKVV VLEAQSFIGG RARAGGWNNR DEFLTSRQKS
LKKKKTAEPP ADHRPHEEGT DGGASTALDF GAMIITGIWG NPIAMLCRQL GIKMQQIKNA
CPLLDAEPQG SFKDVSCRKL SPPESPEPQQ GALLHHSIPK DVDNKIQSIF NKALTAACNK
RKHLADDQDL SLGEELLRVL HNYKFSQVET RVLNWHIANL EYGCGAPLDE VSLRFWDQDD
AFGFGGPHCL IPGGYQRIAE ELAKEVEEIR LNAEVARVRW TGRGGEKKRK EEGEETQELS
PPSAESKIES LLCVGAFVGK LNAGTQEVRA MESVRTKHKV PEGWRIFSTM KRVSTSCFSL
SGGGGIDCDV VFQTERGVKL RSIGDAKREI KRMRSGSWEE EKQQEALHDV NKVLRDMCRL
EAEDGQRREC ERQILQSLGL SYEEEDEEED EDDEEEAETT SEVSDRAGEW EEGMEVEMYF
SDGMWYRGRV TSLEDKVAVI DFEDGDRQTV RLPDPDVRPV RALGSSYMQS KEEEKETEEE
EKMKCGSHWK RKGEGERRKN SQGEQKRPRR SAVDQQLQVG DEAEVLFSDG VWYRGRVTAR
KENLIHVAFA DGDRQSFLLP DPDVRPATAP SASDMSSPST DDRSVQTTLK DDEESEKVEN
MDREDKQDKE ESESEEKREK ENEKSEKSNS VEASTSLNDM DIGSAGQSTL GRGSKLKYHV
GMQVEMFFDD GVWYRGRVAS LLQDVATVFF EDGDVQQVSL PHPDVRPARP PPPVRVHTRD
GQTLRSRAVL LCVPMGVIQQ GAMKFEPSLP SWKHEAIRRA GNGLINKLTI EYREVFWDPQ
VDFFGTTSSV VEERGAFFLV WSLFRFTGRP ILIAVLSGAA ARKYESLPDD TVVRRFHEAI
TSIFGHVPQP ERSHVTRWGS NPHARGAYSF VKASHLPASP PSPAHVQVMQ VGSKGGPDYD
LLAEPVAGQV FFAGEGTCRE HPATAAGAYL TGLREAARLH RLLSEMKGEA RDDR
//
