ID K0R313_THAOC Unreviewed; 1554 AA.
AC K0R313;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN ORFNames=THAOC_34699 {ECO:0000313|EMBL:EJK46625.1};
OS Thalassiosira oceanica (Marine diatom).
OC Eukaryota; Sar; Stramenopiles; Ochrophyta; Bacillariophyta;
OC Coscinodiscophyceae; Thalassiosirophycidae; Thalassiosirales;
OC Thalassiosiraceae; Thalassiosira.
OX NCBI_TaxID=159749 {ECO:0000313|EMBL:EJK46625.1, ECO:0000313|Proteomes:UP000266841};
RN [1] {ECO:0000313|EMBL:EJK46625.1, ECO:0000313|Proteomes:UP000266841}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCMP1005 {ECO:0000313|EMBL:EJK46625.1,
RC ECO:0000313|Proteomes:UP000266841};
RX PubMed=22835381; DOI=10.1186/gb-2012-13-7-r66;
RA Lommer M., Specht M., Roy A.S., Kraemer L., Andreson R., Gutowska M.A.,
RA Wolf J., Bergner S.V., Schilhabel M.B., Klostermeier U.C., Beiko R.G.,
RA Rosenstiel P., Hippler M., Laroche J.;
RT "Genome and low-iron response of an oceanic diatom adapted to chronic iron
RT limitation.";
RL Genome Biol. 13:R66-R66(2012).
CC -!- COFACTOR:
CC Name=L-ascorbate; Xref=ChEBI:CHEBI:38290;
CC Evidence={ECO:0000256|ARBA:ARBA00001961};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the BRE1 family.
CC {ECO:0000256|ARBA:ARBA00005555}.
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:EJK46625.1}.
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DR EMBL; AGNL01047634; EJK46625.1; -; Genomic_DNA.
DR EnsemblProtists; EJK46625; EJK46625; THAOC_34699.
DR eggNOG; KOG0978; Eukaryota.
DR eggNOG; KOG3710; Eukaryota.
DR OMA; ACAQRFD; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000266841; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0031418; F:L-ascorbic acid binding; IEA:InterPro.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR CDD; cd16499; RING-HC_Bre1-like; 1.
DR Gene3D; 2.60.120.620; q2cbj1_9rhob like domain; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR013956; E3_ubiquit_lig_Bre1.
DR InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR InterPro; IPR006620; Pro_4_hyd_alph.
DR InterPro; IPR044862; Pro_4_hyd_alph_FE2OG_OXY.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR23163:SF0; E3 UBIQUITIN-PROTEIN LIGASE BRE1; 1.
DR PANTHER; PTHR23163; RING FINGER PROTEIN-RELATED; 1.
DR Pfam; PF13640; 2OG-FeII_Oxy_3; 1.
DR Pfam; PF13920; zf-C3HC4_3; 1.
DR SMART; SM00702; P4Hc; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS51471; FE2OG_OXY; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Dioxygenase {ECO:0000256|ARBA:ARBA00022964};
KW Iron {ECO:0000256|ARBA:ARBA00023004}; Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000266841};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT TRANSMEM 1531..1552
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 897..935
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 1405..1512
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
FT REGION 1..120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 227..252
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 334..355
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 401..433
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 618..703
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 497..524
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 48..69
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 87..101
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 334..349
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 635..667
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 669..703
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1554 AA; 169399 MW; B941327D990DB376 CRC64;
MKRALAERVK QEFGDPVLQA PASSPSAYGN GVAPHHHGHH SKVPKLEAGQ IASSSSASRH
TSLSGSMTAQ GHAPPLIPPV SKKRPRSPPN ADSSGNVEAY QSTGKARGGK PGASDDDEDD
KSAFFLKHQN SALASELYAY RRRIYLLERE REYRRKECRA VDGLVREVRS SWRGLEEAIG
QDLRPIGVGT TNGHTTSGPN CTGTGADVES STHILHSLLD LVSNPNQIST KMDHDDPEDP
QTGPQPNDFE SYTRGITVKL EPDEKAEFLS EKILLDDMEG FVGDLAARTR SLKDGILNLL
RNSAKGDPGD GGASESASSA DIVELKARVS SLQSRLSSTT SQLEEMANSR NEAGASERRV
RRALYRLASG RMTLEEIMAA VEKDDGGASF SETLADIDAV ASKPPSPGSV HAKAVTADST
PENGCDAGES SANPEEIAQL KKSLQDVQAV AESRDEKISE LLSEREHHLK QINDLVLSKK
SAETCLREES IRKSPLFVET LSRLNEAERK SQELESQTSK IMAKWSAAKG DLDLAKKRLN
RAPNGKGESS TNDAAIQEGA NPFSNARRTA ELELHLRQAL EGNKRTEKLR ESLDQAHKMN
EQLQAKFEEM KAKNAKMVAE KVAARGRSKE SGTDPTAAPP PQSGDKSMSP HSSSSSLRRS
ISSSDPAVEK LQRDYRRARK EVSAAVLSKD QAKLKQERAE KERDTLLKTN ARLLQQSSTK
DDMNAQSLSN ILHLQQKKKE LEKEKVILLQ KTKAAEQLGI AARLASNARD KVGEELLKEK
EALDEKVKQQ QGECQQIRAE KDAMQCELAK AKEALTSVSE DLAVARKRCD DLVSEGNAKE
QGRKSMMESL AVLRKEASES AKLASASGCT EHGGGDGSFT MEQMQTQVKY LSSRVTCPVC
NVREKNVILL RCRHMFCQQC VDVNIKNRSR KCPACAQRFD MKDVAEIWLQ PHLYPHDLPS
SSKHLTCFVT WTSSVGVSLL AVFASVDPDL HRGMSCSCKS RLHVARLVPE REELRQSEHA
YDFTHVIVIV VAAHDDGSAN NHVMSGGIAL FKPPLLFHFE VCWEAMVSPL PDRWKGRRDG
RVVLALAVGT AEVVHHFIVG EWRAEDHQRI YQSHQHEGFI GAQVNYTDQE CQRSRSPCGA
RVRRGAVYFG LDLFFACRPS RIGGRRGPSA RGGGGGALRP EADVDRGRSG IAVEDLVTPS
PLVAVLRCGL ARSVRPRVSF AHQSSTDQNT GVSARVKMRA NAILSAMAVL AALTAETSLA
FTVRPGAQRG STSSNIELRA ALATTASPTI LSPQDMKKLA DDGFVIIHDF IKQDLIGELR
NDVLTLREND AFRQAKIGQD STNNLNTEIR IAETCFLGRN RNELLTIEAA GGKDSVRDRS
GGLYDILDNL RVALEGVSET GLDSSLTELL FAYYPKGGFY RRHRDAIPNS ASLLRKYSLL
LYLNQDWSEK DGGQLRIHLD GGGDECPAGV APKFIDVEPK GGTLVLFKSD AIPHEVLNTN
SERFAVVGWY NRGVSAADIG NLGESAGGGD LLGIGMLAVS AALVTVGLVM VFNG
//
