ID A7S739_NEMVE Unreviewed; 776 AA.
AC A7S739;
DT 02-OCT-2007, integrated into UniProtKB/TrEMBL.
DT 02-OCT-2007, sequence version 1.
DT 27-MAR-2024, entry version 101.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN ORFNames=NEMVEDRAFT_v1g226911 {ECO:0000313|EMBL:EDO40465.1};
OS Nematostella vectensis (Starlet sea anemone).
OC Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria;
OC Edwardsiidae; Nematostella.
OX NCBI_TaxID=45351 {ECO:0000313|EMBL:EDO40465.1, ECO:0000313|Proteomes:UP000001593};
RN [1] {ECO:0000313|EMBL:EDO40465.1, ECO:0000313|Proteomes:UP000001593}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CH2 X CH6 {ECO:0000313|Proteomes:UP000001593};
RX PubMed=17615350; DOI=10.1126/science.1139158;
RA Putnam N.H., Srivastava M., Hellsten U., Dirks B., Chapman J., Salamov A.,
RA Terry A., Shapiro H., Lindquist E., Kapitonov V.V., Jurka J.,
RA Genikhovich G., Grigoriev I.V., Lucas S.M., Steele R.E., Finnerty J.R.,
RA Technau U., Martindale M.Q., Rokhsar D.S.;
RT "Sea anemone genome reveals ancestral eumetazoan gene repertoire and
RT genomic organization.";
RL Science 317:86-94(2007).
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; DS469591; EDO40465.1; -; Genomic_DNA.
DR RefSeq; XP_001632528.1; XM_001632478.1.
DR AlphaFoldDB; A7S739; -.
DR STRING; 45351.A7S739; -.
DR EnsemblMetazoa; EDO40465; EDO40465; NEMVEDRAFT_v1g226911.
DR GeneID; 5512127; -.
DR KEGG; nve:5512127; -.
DR eggNOG; ENOG502QRDQ; Eukaryota.
DR HOGENOM; CLU_022357_0_0_1; -.
DR InParanoid; A7S739; -.
DR OMA; QIVMVNY; -.
DR OrthoDB; 5481936at2759; -.
DR PhylomeDB; A7S739; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000001593; Unassembled WGS sequence.
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:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR CDD; cd15525; PHD_UHRF1_2; 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; IPR019786; Zinc_finger_PHD-type_CS.
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 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; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
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}; Reference proteome {ECO:0000313|Proteomes:UP000001593};
KW 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..78
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000259|PROSITE:PS50053"
FT DOMAIN 323..374
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 427..590
FT /note="YDG"
FT /evidence="ECO:0000259|PROSITE:PS51015"
FT DOMAIN 707..746
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 74..122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 625..664
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EDO40465.1"
SQ SEQUENCE 776 AA; 87387 MW; C78718CF5BDDCCE0 CRC64;
MWIQVRTFDG KQEQQINNLS KQTKIEDLKE RIAEAFLVDT TQERLFFRGK QLEDGHTLFD
YNVGLNEIVQ LMIKAPPPTN DNNNNDDRKS NNEESEALVN GSVENGHSSM DEDSVENNSS
KDKSVIKSIY KKGEFIDAKD PSMGAWFEAE IVDISLKDES DPESVLYHVK YDGYEEDEIN
KLPGRDIRPR ARKRLQWDQL SVGQVVMANY CPDEPKERGF WYDVQITKKH SKQITQGGAE
SRSGSGRELH AKLILSNEED SHAPVAQECR LIFLDEIFKI EAPPAYDENG ERIQSSNDGP
SVKRQNKPDC RFCKDDKMKK CKQCACHQCG GKEDPDKQLL CDECDMAYHI YCLDPPLESI
PDDEDWYCPL CKTDASEVVQ AGEKLKASKK KSKMASANST SNRDWGKGMA CVGRSKVCSI
VPPNHFGPIP GVPVGSAWKF RVQASESGIH RPHVSGIHGR DSEGAYSIVL AGGYEDDLDS
GEEFIYTGSG GRDLSGNKRT AEQSCDQKLT KMNRALARNC AAPLNDKEGA EAEDWKKGKP
VRVIRSSKLR KHSEYAPEDG NRYDGIYKVV KYWPAKGKSG FIVWRYLFKR DDESPAPWTK
EGKKNIESLG LTMVYPEGFL EAQAKKQEES AENGKNKGKG KRKRDEEVPS PSKSPVKKKK
ASQILSDEQK GLIAEDKENV KLWEELLTDT TLDYTAFHQK VEELFACVCC QDLVLYPVTT
KCLHNICKGC LQRSFKAEVF TCPYCRTDLG KTYKLSVNSA LDAILNDLFP GYSKGR
//
