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Database: UniProt
Entry: B8CG52_THAPS
LinkDB: B8CG52_THAPS
Original site: B8CG52_THAPS 
ID   B8CG52_THAPS            Unreviewed;       566 AA.
AC   B8CG52;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 58.
DE   RecName: Full=RING-type domain-containing protein {ECO:0000259|PROSITE:PS50089};
GN   ORFNames=THAPSDRAFT_11988 {ECO:0000313|EMBL:EED87428.1};
OS   Thalassiosira pseudonana (Marine diatom) (Cyclotella nana).
OC   Eukaryota; Sar; Stramenopiles; Ochrophyta; Bacillariophyta;
OC   Coscinodiscophyceae; Thalassiosirophycidae; Thalassiosirales;
OC   Thalassiosiraceae; Thalassiosira.
OX   NCBI_TaxID=35128 {ECO:0000313|EMBL:EED87428.1, ECO:0000313|Proteomes:UP000001449};
RN   [1] {ECO:0000313|EMBL:EED87428.1, ECO:0000313|Proteomes:UP000001449}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCMP1335 {ECO:0000313|EMBL:EED87428.1};
RX   PubMed=15459382; DOI=10.1126/science.1101156;
RA   Armbrust E.V., Berges J.A., Bowler C., Green B.R., Martinez D.,
RA   Putnam N.H., Zhou S., Allen A.E., Apt K.E., Bechner M., Brzezinski M.A.,
RA   Chaal B.K., Chiovitti A., Davis A.K., Demarest M.S., Detter J.C.,
RA   Glavina T., Goodstein D., Hadi M.Z., Hellsten U., Hildebrand M.,
RA   Jenkins B.D., Jurka J., Kapitonov V.V., Kroger N., Lau W.W., Lane T.W.,
RA   Larimer F.W., Lippmeier J.C., Lucas S., Medina M., Montsant A., Obornik M.,
RA   Parker M.S., Palenik B., Pazour G.J., Richardson P.M., Rynearson T.A.,
RA   Saito M.A., Schwartz D.C., Thamatrakoln K., Valentin K., Vardi A.,
RA   Wilkerson F.P., Rokhsar D.S.;
RT   "The genome of the diatom Thalassiosira pseudonana: ecology, evolution, and
RT   metabolism.";
RL   Science 306:79-86(2004).
RN   [2] {ECO:0000313|EMBL:EED87428.1, ECO:0000313|Proteomes:UP000001449}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCMP1335 {ECO:0000313|EMBL:EED87428.1};
RX   PubMed=18923393; DOI=10.1038/nature07410;
RA   Bowler C., Allen A.E., Badger J.H., Grimwood J., Jabbari K., Kuo A.,
RA   Maheswari U., Martens C., Maumus F., Otillar R.P., Rayko E., Salamov A.,
RA   Vandepoele K., Beszteri B., Gruber A., Heijde M., Katinka M., Mock T.,
RA   Valentin K., Verret F., Berges J.A., Brownlee C., Cadoret J.P.,
RA   Chiovitti A., Choi C.J., Coesel S., De Martino A., Detter J.C., Durkin C.,
RA   Falciatore A., Fournet J., Haruta M., Huysman M.J., Jenkins B.D.,
RA   Jiroutova K., Jorgensen R.E., Joubert Y., Kaplan A., Kroger N., Kroth P.G.,
RA   La Roche J., Lindquist E., Lommer M., Martin-Jezequel V., Lopez P.J.,
RA   Lucas S., Mangogna M., McGinnis K., Medlin L.K., Montsant A.,
RA   Oudot-Le Secq M.P., Napoli C., Obornik M., Parker M.S., Petit J.L.,
RA   Porcel B.M., Poulsen N., Robison M., Rychlewski L., Rynearson T.A.,
RA   Schmutz J., Shapiro H., Siaut M., Stanley M., Sussman M.R., Taylor A.R.,
RA   Vardi A., von Dassow P., Vyverman W., Willis A., Wyrwicz L.S.,
RA   Rokhsar D.S., Weissenbach J., Armbrust E.V., Green B.R., Van de Peer Y.,
RA   Grigoriev I.V.;
RT   "The Phaeodactylum genome reveals the evolutionary history of diatom
RT   genomes.";
RL   Nature 456:239-244(2008).
CC   -!- PATHWAY: Protein modification. {ECO:0000256|ARBA:ARBA00043952}.
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DR   EMBL; CM000654; EED87428.1; -; Genomic_DNA.
DR   RefSeq; XP_002295124.1; XM_002295088.1.
DR   AlphaFoldDB; B8CG52; -.
DR   STRING; 35128.B8CG52; -.
DR   PaxDb; 35128-Thaps11988; -.
DR   EnsemblProtists; EED87428; EED87428; THAPSDRAFT_11988.
DR   GeneID; 7442706; -.
DR   KEGG; tps:THAPSDRAFT_11988; -.
DR   eggNOG; ENOG502SXMH; Eukaryota.
DR   HOGENOM; CLU_481948_0_0_1; -.
DR   InParanoid; B8CG52; -.
DR   Proteomes; UP000001449; Chromosome 23.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016740; F:transferase activity; IEA:InterPro.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:InterPro.
DR   CDD; cd16454; RING-H2_PA-TM-RING; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR044602; ATL10/ATL75-79-like.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR46905; RING-H2 FINGER PROTEIN ATL78; 1.
DR   PANTHER; PTHR46905:SF7; RING-H2 FINGER PROTEIN ATL78; 1.
DR   Pfam; PF13639; zf-RING_2; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00175};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001449};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00175};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00175}.
FT   TRANSMEM        78..99
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          454..501
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          38..68
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          261..392
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          413..435
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        261..276
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        307..332
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        346..360
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        375..389
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   566 AA;  62753 MW;  DFC5D8A63860C6DF CRC64;
     MSSSASYLRH VAARPLHQPS ALSIHRVLNT LFDGATATTN QDQDSYPTLQ QTTSSSSSST
     PQAPQIDNYD NASWDTRATI LFIEAIVLTV IVLCVLIACT RRHFRRMDLA SQRAASLQEW
     AAVRMPAGSG GSMEVSDATE DIENGVVANN ASADATNTTT DNTNLSNERT PLRQLTSLPS
     TILSILLSPL RMLDSAINDW STERVRTNNY DISYYRSMVE RWEREKEAGR EKEDERGERL
     RRAFEKGCMV WEIEEEDFVK PKNKGEINDD NMEEHNDNNN NNGSESGDFE IGLDETGSDD
     EAAATGEKSI TETTTADTTD EGESLSNEIT EATTELKDSD VCEDEVSHQQ QMNNAKNSVQ
     HDNGVDKETR AEPNNTEEAS SNTPITSDED SAPGYLYLNR QRANTTGSLT TITASTSQST
     LPESHSTHSM PSSFTTQLPF TPEVSSGRTI PNQCAICLCD YEKGDTVVVS CNKLCPHAFH
     QECIVEWLAK MQEGTPCPCC RRTFVELDEY LPGNKNTNVA TGTNVITSSQ QSPEEAERLR
     QIRRRRHIEL GLQRGRAFNA SVISMW
//
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