ID C3Z9P1_BRAFL Unreviewed; 316 AA.
AC C3Z9P1;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 24-JAN-2024, entry version 61.
DE RecName: Full=RING-type domain-containing protein {ECO:0000259|PROSITE:PS50089};
GN ORFNames=BRAFLDRAFT_281265 {ECO:0000313|EMBL:EEN50737.1};
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:EEN50737.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S238N-H82 {ECO:0000313|EMBL:EEN50737.1};
RC TISSUE=Testes {ECO:0000313|EMBL:EEN50737.1};
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; GG666600; EEN50737.1; -; Genomic_DNA.
DR RefSeq; XP_002594726.1; XM_002594680.1.
DR AlphaFoldDB; C3Z9P1; -.
DR STRING; 7739.C3Z9P1; -.
DR eggNOG; KOG0800; Eukaryota.
DR InParanoid; C3Z9P1; -.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd16677; RING-H2_RNF32_rpt1; 1.
DR Gene3D; 1.20.5.190; -; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR InterPro; IPR042862; RNF32.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR14991; RING FINGER PROTEIN 32; 1.
DR PANTHER; PTHR14991:SF0; RING FINGER PROTEIN 32; 1.
DR Pfam; PF00612; IQ; 1.
DR Pfam; PF13639; zf-RING_2; 1.
DR SMART; SM00015; IQ; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50096; IQ; 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:PRU00175}.
FT DOMAIN 150..192
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 60..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..81
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 82..101
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 316 AA; 36848 MW; 8D9E85EA84452379 CRC64;
MSNKLSDIKM NQYRNVSAPL STSTGGKAKS SPTTSSTTLA AVAFQDHIMR NLSLSDPLRA
RRPLPVKGHH QRPKHIRPVV DTRRRRPSSD TKTRKEEIEE KEYVLDPKPQ PLSLAQKLGL
VEAPKQPLTE EEWQSVKHRA SRRDDHIQPC VICKEDFGTQ EQVLLSCSHV FHKACLQAFE
RFSGKKTCPL CRRDQYQTRV IHEGARHHRV KCATRIQACW RGYVVRCWYR KLRQTVPPKD
PKLRQKFYED KFQSITDRIV QSCAYNIDDF LSEIDRSVQA SRDVFKFFDE NSWKPLSEEE
WEKIQLRVSM IGLYIS
//