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Database: UniProt
Entry: C3XXM8_BRAFL
LinkDB: C3XXM8_BRAFL
Original site: C3XXM8_BRAFL 
ID   C3XXM8_BRAFL            Unreviewed;       752 AA.
AC   C3XXM8;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   24-JAN-2024, entry version 82.
DE   RecName: Full=RanBP-type and C3HC4-type zinc finger-containing protein 1 {ECO:0000256|ARBA:ARBA00017887};
GN   ORFNames=BRAFLDRAFT_63887 {ECO:0000313|EMBL:EEN67488.1};
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:EEN67488.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S238N-H82 {ECO:0000313|EMBL:EEN67488.1};
RC   TISSUE=Testes {ECO:0000313|EMBL:EEN67488.1};
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).
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DR   EMBL; GG666471; EEN67488.1; -; Genomic_DNA.
DR   RefSeq; XP_002611478.1; XM_002611432.1.
DR   AlphaFoldDB; C3XXM8; -.
DR   STRING; 7739.C3XXM8; -.
DR   eggNOG; KOG4185; Eukaryota.
DR   InParanoid; C3XXM8; -.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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:0016567; P:protein ubiquitination; IBA:GO_Central.
DR   CDD; cd19756; Bbox2; 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; IPR027370; Znf-RING_euk.
DR   InterPro; IPR000315; Znf_B-box.
DR   InterPro; IPR001876; Znf_RanBP2.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   PANTHER; PTHR47156; PROTEIN CBG20824; 1.
DR   PANTHER; PTHR47156:SF10; RING-TYPE DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00643; zf-B_box; 1.
DR   Pfam; PF13445; zf-RING_UBOX; 1.
DR   SMART; SM00336; BBOX; 1.
DR   SMART; SM00184; RING; 1.
DR   SMART; SM00547; ZnF_RBZ; 2.
DR   SUPFAM; SSF57845; B-box zinc-binding domain; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS50119; ZF_BBOX; 1.
DR   PROSITE; PS01358; ZF_RANBP2_1; 1.
DR   PROSITE; PS50199; ZF_RANBP2_2; 1.
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:PRU00322}.
FT   DOMAIN          21..68
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   DOMAIN          107..149
FT                   /note="B box-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50119"
FT   DOMAIN          685..717
FT                   /note="RanBP2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50199"
FT   REGION          367..570
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          643..677
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        410..434
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        454..507
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        515..538
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        643..667
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   752 AA;  82666 MW;  C373B8BE0C2A3A9A CRC64;
     MLSLESTLDV RSIDEPRGHC CAICYHPFSR DGLFVPRNLS CGHSYCTECL VKLVNHGQRG
     HICCPTCKTT TKIPGLSNDA TRLPKNFGVL EILAGEEDKY GRTLGIQPCL ACDEHENEPK
     KVYCLSDQEI ICIYCQVYGK HKGHDCALVK DVAAKERQNL RQLAEALIKH KQQLSEVRRG
     VHEMCTAVRF KEEKLMREIS HHFELLRKRL YKRENQLKAQ VKNQTIIRVA TLEKQERELS
     DVVSKAEELE GHCHFLIQRS DRTVLEKKGQ VQETYKQVEE LVSECVVHPQ AVDTLSCKFV
     GDILDLLSDY GYIGEPPGEE NNKSEVKLNA EAVAILETSS SEEHEGENQQ GAKEVLADIM
     CCRVSRQRSP ADDGSSDLAL SELDDPHDIN ANRPPVGTKP RHLHSCRRLS NDNSDNYSES
     QSSCLATSET SSSEDELEAV SDLEEGRGAS ALAESPRQQP SHDSQRSTIT RITSSSNIVI
     EVTIGQTQTT DRQETSSGQT TQAKGEGSNP CRGAHKVDPW DKPASHVHFS RGRETKVKSQ
     TSRLLSTVLG RRKKHRSPSY ASTTSLATAQ SSGKPKCSVV NCPGPAIVKC KHCNRAFCKE
     CATNSLSAKR CYKRPRGHSL IHVDNFPRPP KVGVDNAAFA KSSGTVQSQP LSDAATVGSN
     DQESVSEKTA AGGAAGKGQG LQQLQASPLR KWKCLRCAAI NRCSSKVCSR CNLPRGAPIP
     EPVPVGNVCP ACTLLNPMAA LKCELCETEL LL
//
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