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Database: UniProt
Entry: C3YRY2_BRAFL
LinkDB: C3YRY2_BRAFL
Original site: C3YRY2_BRAFL 
ID   C3YRY2_BRAFL            Unreviewed;       527 AA.
AC   C3YRY2;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 81.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EEN56887.1};
GN   ORFNames=BRAFLDRAFT_75840 {ECO:0000313|EMBL:EEN56887.1};
OS   Branchiostoma floridae (Florida lancelet) (Amphioxus).
OC   Eukaryota; Metazoa; Chordata; Cephalochordata; Leptocardii; Amphioxiformes;
OC   Branchiostomatidae; Branchiostoma.
OX   NCBI_TaxID=7739;
RN   [1] {ECO:0000313|EMBL:EEN56887.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S238N-H82 {ECO:0000313|EMBL:EEN56887.1};
RC   TISSUE=Testes {ECO:0000313|EMBL:EEN56887.1};
RX   PubMed=18563158; DOI=10.1038/nature06967;
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Putnam N.H., Butts T., Ferrier D.E.K., Furlong R.F., Hellsten U.,
RA   Kawashima T., Robinson-Rechavi M., Shoguchi E., Terry A., Yu J.-K.,
RA   Benito-Gutierrez E.L., Dubchak I., Garcia-Fernandez J., Gibson-Brown J.J.,
RA   Grigoriev I.V., Horton A.C., de Jong P.J., Jurka J., Kapitonov V.V.,
RA   Kohara Y., Kuroki Y., Lindquist E., Lucas S., Osoegawa K., Pennacchio L.A.,
RA   Salamov A.A., Satou Y., Sauka-Spengler T., Schmutz J., Shin-I T.,
RA   Toyoda A., Bronner-Fraser M., Fujiyama A., Holland L.Z., Holland P.W.H.,
RA   Satoh N., Rokhsar D.S.;
RT   "The amphioxus genome and the evolution of the chordate karyotype.";
RL   Nature 453:1064-1071(2008).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR   EMBL; GG666548; EEN56887.1; -; Genomic_DNA.
DR   RefSeq; XP_002600875.1; XM_002600829.1.
DR   AlphaFoldDB; C3YRY2; -.
DR   eggNOG; KOG0123; Eukaryota.
DR   eggNOG; KOG2177; Eukaryota.
DR   InParanoid; C3YRY2; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006513; P:protein monoubiquitination; IBA:GO_Central.
DR   Gene3D; 4.10.830.40; -; 1.
DR   Gene3D; 1.10.1900.10; c-terminal domain of poly(a) binding protein; 1.
DR   Gene3D; 3.30.160.60; Classic Zinc Finger; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR036053; PABP-dom.
DR   InterPro; IPR002004; PABP_HYD.
DR   InterPro; IPR047153; TRIM45/56/19.
DR   InterPro; IPR027370; Znf-RING_euk.
DR   InterPro; IPR000315; Znf_B-box.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   PANTHER; PTHR25462; BONUS, ISOFORM C-RELATED; 1.
DR   PANTHER; PTHR25462:SF229; NHL (RING FINGER B-BOX COILED COIL) DOMAIN CONTAINING; 1.
DR   Pfam; PF00658; PABP; 1.
DR   Pfam; PF00643; zf-B_box; 2.
DR   Pfam; PF13445; zf-RING_UBOX; 1.
DR   SMART; SM00336; BBOX; 2.
DR   SMART; SM00517; PolyA; 1.
DR   SMART; SM00184; RING; 1.
DR   SUPFAM; SSF57845; B-box zinc-binding domain; 1.
DR   SUPFAM; SSF63570; PABC (PABP) domain; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS51309; PABC; 1.
DR   PROSITE; PS50119; ZF_BBOX; 2.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00024}.
FT   DOMAIN          17..59
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   DOMAIN          95..142
FT                   /note="B box-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50119"
FT   DOMAIN          157..200
FT                   /note="B box-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50119"
FT   DOMAIN          439..516
FT                   /note="PABC"
FT                   /evidence="ECO:0000259|PROSITE:PS51309"
SQ   SEQUENCE   527 AA;  59026 MW;  C4A5DBC25B8E1496 CRC64;
     MATAAFPEKV SDDSTQCTIC FYTFKNPKVL PCLHTFCEHC LREWVQKNDG DTIPCPICRQ
     PVSLPQNGVE GLKDNFFIAS LVKAVTEHNK VRHGKDELLC TSCEEGKPAT SRCSECAEFL
     CESCESAHRL VRATRGHTLF TFEELKTGKY DNVVRARKAP PCSKHPGEIL KLYCRTCETP
     ICNECALFEH RDSQHDYTRI EEVAAEKRDT ILDLTPQCQA RMQFFRQTEE AQKRLREQLQ
     LNVEGARQNV HRTVQTLTAL VKEEGERLLT CIHTEESSRK KQIEAEIEGA QISLASAKST
     CEFAKTLARE GGDYEVASFS QDMAARLNEL TKPPMEKVNF KLANITIDYS VMVQKLTKNR
     PKTAHYSLPK STERELCSLL KRARQSGVSS STGPPLGRYG DRVLVNGGGL RPGYRYTANM
     RNPPSGDRPL HQAVYIQGEE PLTASMLAAA PPQEQKQMLG ERLFPLIQNS HPDLAGKITG
     MLLELENPEL LHMLESREAL KAKVEEAVAV LQAHEAKERA ARAGLAE
//
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