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
//