ID V4C4J8_LOTGI Unreviewed; 762 AA.
AC V4C4J8;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN ORFNames=LOTGIDRAFT_206317 {ECO:0000313|EMBL:ESO96469.1};
OS Lottia gigantea (Giant owl limpet).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Patellogastropoda; Lottioidea; Lottiidae; Lottia.
OX NCBI_TaxID=225164 {ECO:0000313|EMBL:ESO96469.1, ECO:0000313|Proteomes:UP000030746};
RN [1] {ECO:0000313|EMBL:ESO96469.1, ECO:0000313|Proteomes:UP000030746}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23254933; DOI=10.1038/nature11696;
RA Simakov O., Marletaz F., Cho S.J., Edsinger-Gonzales E., Havlak P.,
RA Hellsten U., Kuo D.H., Larsson T., Lv J., Arendt D., Savage R.,
RA Osoegawa K., de Jong P., Grimwood J., Chapman J.A., Shapiro H., Aerts A.,
RA Otillar R.P., Terry A.Y., Boore J.L., Grigoriev I.V., Lindberg D.R.,
RA Seaver E.C., Weisblat D.A., Putnam N.H., Rokhsar D.S.;
RT "Insights into bilaterian evolution from three spiralian genomes.";
RL Nature 493:526-531(2013).
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}.
CC -!- SIMILARITY: Belongs to the Polycomblike family.
CC {ECO:0000256|ARBA:ARBA00008084}.
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DR EMBL; KB201459; ESO96469.1; -; Genomic_DNA.
DR RefSeq; XP_009052828.1; XM_009054580.1.
DR AlphaFoldDB; V4C4J8; -.
DR STRING; 225164.V4C4J8; -.
DR EnsemblMetazoa; LotgiT206317; LotgiP206317; LotgiG206317.
DR GeneID; 20245907; -.
DR KEGG; lgi:LOTGIDRAFT_206317; -.
DR CTD; 20245907; -.
DR HOGENOM; CLU_022357_0_0_1; -.
DR OMA; QIVMVNY; -.
DR OrthoDB; 5481936at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000030746; 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: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; 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; IPR002999; Tudor.
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 SMART; SM00249; PHD; 1.
DR SMART; SM00184; RING; 2.
DR SMART; SM00466; SRA; 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; PS50304; TUDOR; 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 3: Inferred from homology;
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:UP000030746};
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..76
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000259|PROSITE:PS50053"
FT DOMAIN 121..194
FT /note="Tudor"
FT /evidence="ECO:0000259|PROSITE:PS50304"
FT DOMAIN 307..358
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 411..574
FT /note="YDG"
FT /evidence="ECO:0000259|PROSITE:PS51015"
FT DOMAIN 692..731
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 82..116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 610..643
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 87..105
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 762 AA; 86472 MW; 01BF7F5CCF39FA0F CRC64;
MWIQVRSIDG KKTVRVDSLS KLTKVEDLRE KLVEPFEADV DCQKLFFRGK ILVDGHSLFD
YDVGLNDLVQ IMVRKPVIME TNNNNTDDLE SSDKENQKPE SPVKMEENDI EEEEVDTEGS
AFKVGDIIDA RDISNGAWFE AKITKVSKDK SPAEKDGEQN EEENDGFVYH VQYEGYEETE
QLKMNNIRPR CKNLIKFNDL KVGQKVVANY NCEDPAERGF WYDCVITDKK ENKSKGILAT
VFAGVDLTPL EDCKILFPNE IFTIEKAGSQ INEKDIDLND ATSTPTMRKN KIDCNKCKDN
PRVKCKECAC SVCGGKQEPE KQILCDECNK AYHLFCMDPP LTKVPEEDEW YCSDCKNDVT
EVVRAGERLK QSKKKSKMAS ATSKSSRDWG KGMACVGRTT MCTIVPPNHF GPIPGIEVGM
LWKFRVQVSE AGVHRPHVAG IHGREDEGAY SIVLSGGYED DHDDGDKFTY TGSGGRDLSG
NKRTAEQSCD QLLTRMNKAL AKNCNAPINA KDGAEAKDWK GGKPVRVVRN CKGRKHSKYA
PEEGNRYDGI YKMVKYWPEK GKSGFIVWRY LLKRDDENPA PWTKEGKKKI KSLGLEIKYP
EGYLETLKEK EREKEEKSEK GKKRKRSDVE DSPEKSPKKT KKVQAEAYKL PKDVKKFVDE
DEQNKKLWEE TFPSMGDGKP KFLQKVEDVF TCICCQEIVF KPVTLDCSHN VCKLCLSRSF
KAQVYSCPAC RHDLGEKYSM KVNENLSKAL SALYPGYEAG RT
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