ID Q4H2N4_CIOIN Unreviewed; 743 AA.
AC Q4H2N4; A0A1W2VS13;
DT 30-AUG-2005, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2005, sequence version 1.
DT 03-MAY-2023, entry version 118.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN Name=Ci-UHRF2 {ECO:0000313|EMBL:BAE06743.1};
OS Ciona intestinalis (Transparent sea squirt) (Ascidia intestinalis).
OC Eukaryota; Metazoa; Chordata; Tunicata; Ascidiacea; Phlebobranchia;
OC Cionidae; Ciona.
OX NCBI_TaxID=7719 {ECO:0000313|EMBL:BAE06743.1};
RN [1] {ECO:0000313|EMBL:BAE06743.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=12736827; DOI=10.1007/s00427-003-0330-z;
RA Satou Y., Satoh N.;
RT "Genomewide surveys of developmentally relevant genes in Ciona
RT intestinalis.";
RL Dev. Genes Evol. 213:211-212(2003).
RN [2] {ECO:0000313|EMBL:BAE06743.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=15269171; DOI=10.1242/dev.01270;
RA Imai K.S., Hino K., Yagi K., Satoh N., Satou Y.;
RT "Gene expression profiles of transcription factors and signaling molecules
RT in the ascidian embryo: towards a comprehensive understanding of gene
RT networks.";
RL Development 131:4047-4058(2004).
RN [3] {ECO:0000313|EMBL:BAE06743.1}
RP NUCLEOTIDE SEQUENCE.
RA Satou Y.;
RT "Expressed genes in Ciona intestinalis.";
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27; Evidence={ECO:0000256|ARBA:ARBA00000900};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|PROSITE-ProRule:PRU00358}.
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DR EMBL; AB210738; BAE06743.1; -; mRNA.
DR RefSeq; NP_001071846.1; NM_001078378.1.
DR AlphaFoldDB; Q4H2N4; -.
DR GeneID; 778788; -.
DR KEGG; cin:778788; -.
DR CTD; 115426; -.
DR OrthoDB; 5481936at2759; -.
DR UniPathway; UPA00143; -.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR CDD; cd15525; PHD_UHRF1_2; 1.
DR CDD; cd16613; RING-HC_UHRF; 1.
DR CDD; cd20387; Tudor_UHRF_rpt1; 1.
DR CDD; cd20388; Tudor_UHRF_rpt2; 1.
DR CDD; cd01797; Ubl_UHRF; 1.
DR Gene3D; 2.30.30.1150; -; 1.
DR Gene3D; 2.30.30.140; -; 1.
DR Gene3D; 2.30.280.10; SRA-YDG; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR015947; PUA-like_sf.
DR InterPro; IPR036987; SRA-YDG_sf.
DR InterPro; IPR003105; SRA_YDG.
DR InterPro; IPR021991; TTD_dom.
DR InterPro; IPR000626; Ubiquitin-like_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR InterPro; IPR045134; UHRF1/2-like.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR14140; E3 UBIQUITIN-PROTEIN LIGASE UHRF-RELATED; 1.
DR PANTHER; PTHR14140:SF45; RING-TYPE E3 UBIQUITIN TRANSFERASE; 1.
DR Pfam; PF00628; PHD; 1.
DR Pfam; PF02182; SAD_SRA; 1.
DR Pfam; PF12148; TTD; 1.
DR Pfam; PF00240; ubiquitin; 1.
DR Pfam; PF13920; zf-C3HC4_3; 1.
DR SMART; SM00249; PHD; 1.
DR SMART; SM00184; RING; 2.
DR SMART; SM00466; SRA; 1.
DR SMART; SM00213; UBQ; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF88697; PUA domain-like; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR SUPFAM; SSF54236; Ubiquitin-like; 1.
DR PROSITE; PS50053; UBIQUITIN_2; 1.
DR PROSITE; PS51015; YDG; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 2: Evidence at transcript level;
KW Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PROSITE-
KW ProRule:PRU00358}; Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 1..75
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000259|PROSITE:PS50053"
FT DOMAIN 291..342
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 395..558
FT /note="YDG"
FT /evidence="ECO:0000259|PROSITE:PS51015"
FT DOMAIN 675..714
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 80..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 598..625
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..99
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 599..613
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 743 AA; 84112 MW; E91A7591174E636E CRC64;
MWIRVRTMDG KRSEQVDGLS KLTKIEDLRE LIMEKFSVEP SLQRLFFRGK QLEDGYSLFD
YDVGLNALVQ LLERKVIKEV ETQQENETPA SPSDTDSGIE TAENVQEVVE DTPSTSCEGL
YKINALIDAQ DTDVGAWFEA KVVNVTKGKT DGLDYHIKFD DYGDDGVKVV GEKLIRPRAR
KLLEWNEIEV TSKVMANYNM DHPKERGFWY DCVVLDKKNK RKKNELTVQL LLGENRTLEP
CNITFVEEVF VIETVGSESG PLSADTAVTR KTEKEADCGH CRDNPDKDCK ECGCHVCGEK
RAFDKTLLCD ECNLPFHTFC LNPPLDNLPE EDDWYCPLCC QDRSKVVKAG EKLKENKKKN
KMKSMTSDTQ RDWGKGMACV GRSKICTIVP SNHFGAIPGV PVGSLWKFRV QVSESGIHRP
HVSGIHGKEN EGAYSIVLAG GYEDDEDNGD EFTYTGSGGR DLSGNKRTAE QSCDQVLTKN
NMAIARTCDV KADAKNGAEA KDWKKSRPIR VVRNYKGAKH SDYAPEEGNR YDGLYKVVKY
WPEKGKSGFI VWRYLFRRDD KEPAPWTKAG KKRSKELGIT IKYPEGYLEA QAQKLANEEA
AGPKKKGKRS LSNDDASTPK STPKKIKINE FEVSQELMKM IKTDKLNSKL WSEGLKSRKE
GQTKFYQIIQ DLFMCVCCQD VVHQPITTPC KHNLCKTCLQ RSFKADIYSC PVCREDLEKE
NIEINIPLQK VLLKLFPGYT SGR
//
