ID V3ZS26_LOTGI Unreviewed; 707 AA.
AC V3ZS26;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 60.
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_118698 {ECO:0000313|EMBL:ESO94243.1};
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:ESO94243.1, ECO:0000313|Proteomes:UP000030746};
RN [1] {ECO:0000313|EMBL:ESO94243.1, 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 -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000256|ARBA:ARBA00004245}.
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DR EMBL; KB201847; ESO94243.1; -; Genomic_DNA.
DR RefSeq; XP_009055088.1; XM_009056840.1.
DR AlphaFoldDB; V3ZS26; -.
DR STRING; 225164.V3ZS26; -.
DR EnsemblMetazoa; LotgiT118698; LotgiP118698; LotgiG118698.
DR GeneID; 20231646; -.
DR KEGG; lgi:LOTGIDRAFT_118698; -.
DR CTD; 20231646; -.
DR HOGENOM; CLU_013137_19_2_1; -.
DR OMA; EAIVHRY; -.
DR OrthoDB; 5383069at2759; -.
DR Proteomes; UP000030746; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd19803; Bbox1_TRIM9-like_C-I; 1.
DR CDD; cd19764; Bbox2_TRIM9-like; 1.
DR CDD; cd00063; FN3; 1.
DR CDD; cd16576; RING-HC_TRIM9-like_C-I; 1.
DR CDD; cd12889; SPRY_PRY_TRIM67_9; 1.
DR Gene3D; 1.20.5.170; -; 1.
DR Gene3D; 2.60.120.920; -; 1.
DR Gene3D; 4.10.830.40; -; 1.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR001870; B30.2/SPRY.
DR InterPro; IPR043136; B30.2/SPRY_sf.
DR InterPro; IPR003649; Bbox_C.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR017903; COS_domain.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003877; SPRY_dom.
DR InterPro; IPR027370; Znf-RING_euk.
DR InterPro; IPR000315; Znf_B-box.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR24099; E3 UBIQUITIN-PROTEIN LIGASE TRIM36-RELATED; 1.
DR PANTHER; PTHR24099:SF15; E3 UBIQUITIN-PROTEIN LIGASE TRIM9; 1.
DR Pfam; PF00622; SPRY; 1.
DR Pfam; PF00643; zf-B_box; 1.
DR Pfam; PF13445; zf-RING_UBOX; 1.
DR SMART; SM00502; BBC; 1.
DR SMART; SM00336; BBOX; 2.
DR SMART; SM00060; FN3; 1.
DR SMART; SM00184; RING; 1.
DR SMART; SM00449; SPRY; 1.
DR SUPFAM; SSF57845; B-box zinc-binding domain; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF49265; Fibronectin type III; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50188; B302_SPRY; 1.
DR PROSITE; PS51262; COS; 1.
DR PROSITE; PS50853; FN3; 1.
DR PROSITE; PS50119; ZF_BBOX; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000030746};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
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:PRU00024}.
FT DOMAIN 7..57
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 224..266
FT /note="B box-type"
FT /evidence="ECO:0000259|PROSITE:PS50119"
FT DOMAIN 374..433
FT /note="COS"
FT /evidence="ECO:0000259|PROSITE:PS51262"
FT DOMAIN 437..531
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 513..696
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000259|PROSITE:PS50188"
SQ SEQUENCE 707 AA; 78782 MW; 2EBF0B17A286FEFB CRC64;
MEEELKCPVC RRWYSKPLLL PCSHSICTAC AVAGQEPTQN MVSSSVGGTG AQCPSENGVG
VNGTNCPSEA DTVSIMEMDK LSLISEADSG VVCNSRPSSY LGTPSVENIF TPSTVQTYPY
GLRCPVCSKI VLLDDFGALS LPINKVLEAI IEKYTQPKEP KKVEVRCELC INKAEIATTM
CEQCEVFYCD TCRDGCHPAR GSLAKHNLVD PTQGQNIIES KKKRKEVKCK EHSEEVLNMF
CVGCKLPVCY VCSQDGRHIN HDVQSLVSIC KQQKNELSQN LQSLSEKAKS GTEFIQRLKT
MAEKINGNCS EFEATVIAQC DALIERIKLR KVELLASVKE EKDMKTVTMK EQVSDCTSLL
QRTTGLLQFC IEVLKESNQS SFLQISSGLI YRVSEAKGNF NKEMEFAPRI SPEFEMTLDN
KPSLRAIENM NFFQMKAPGE PYILPEECSA ENNSVTIVWQ PFCNTTVVEA YTLELDDGNG
GDFRVVYVGR ETICTVDGLH FNSIYNARVK GHNHAGESPY SEIVSLQTAE VAWFTFDPVT
THQDIIFANN NQSITCNSFD HRVALGNVGF SKGVHYWEIR IDRYDSHTDP SIGIARFDVD
KNTMLGKDEK AWSMYIDNQR SWFINHDEHT NRTDGGIQPS DTIGLLLDLN HHTLSYFIND
HPHGPIAFTD LHGVFFPAVS INRNVQVTLR SGLEPPVDSE VGESDVD
//
