ID A0A1S3K8Y0_LINUN Unreviewed; 1496 AA.
AC A0A1S3K8Y0;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|RuleBase:RU369009};
DE EC=2.3.2.26 {ECO:0000256|RuleBase:RU369009};
GN Name=LOC106179840 {ECO:0000313|RefSeq:XP_013419080.1};
OS Lingula unguis.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Brachiopoda; Linguliformea;
OC Lingulata; Lingulida; Linguloidea; Lingulidae; Lingula.
OX NCBI_TaxID=7574 {ECO:0000313|Proteomes:UP000085678, ECO:0000313|RefSeq:XP_013419080.1};
RN [1] {ECO:0000313|RefSeq:XP_013419080.1}
RP IDENTIFICATION.
RC TISSUE=Gonads {ECO:0000313|RefSeq:XP_013419080.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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=2.3.2.26; Evidence={ECO:0000256|ARBA:ARBA00000885,
CC ECO:0000256|RuleBase:RU369009};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|RuleBase:RU369009}.
CC -!- SIMILARITY: Belongs to the UPL family. K-HECT subfamily.
CC {ECO:0000256|RuleBase:RU369009}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_013419080.1; XM_013563626.1.
DR STRING; 7574.A0A1S3K8Y0; -.
DR EnsemblMetazoa; g20164.t1; g20164.t1; g20164.
DR EnsemblMetazoa; XM_013563626.1; XP_013419080.1; LOC106179840.
DR GeneID; 106179840; -.
DR KEGG; lak:106179840; -.
DR InParanoid; A0A1S3K8Y0; -.
DR OMA; GHEIFFA; -.
DR OrthoDB; 1093891at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000085678; Unplaced.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.720.50; -; 1.
DR Gene3D; 3.90.1750.10; Hect, E3 ligase catalytic domains; 1.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR InterPro; IPR045322; HECTD1/TRIP12-like.
DR InterPro; IPR004170; WWE-dom.
DR InterPro; IPR018123; WWE-dom_subgr.
DR InterPro; IPR037197; WWE_dom_sf.
DR PANTHER; PTHR45670; E3 UBIQUITIN-PROTEIN LIGASE TRIP12; 1.
DR PANTHER; PTHR45670:SF1; E3 UBIQUITIN-PROTEIN LIGASE TRIP12; 1.
DR Pfam; PF02825; WWE; 1.
DR SMART; SM00678; WWE; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF56204; Hect, E3 ligase catalytic domain; 1.
DR SUPFAM; SSF117839; WWE domain; 1.
DR PROSITE; PS50918; WWE; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000085678};
KW Transferase {ECO:0000256|RuleBase:RU369009};
KW Ubl conjugation pathway {ECO:0000256|RuleBase:RU369009}.
FT DOMAIN 506..582
FT /note="WWE"
FT /evidence="ECO:0000259|PROSITE:PS50918"
FT REGION 724..898
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1239..1271
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 727..782
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 818..832
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 850..898
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1254..1269
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1496
FT /evidence="ECO:0000313|RefSeq:XP_013419080.1"
SQ SEQUENCE 1496 AA; 164578 MW; 475D593D90F517CF CRC64;
MSGNENYGDV VGDAEKVKYV LEAITATQLA NKPVCKRLRQ PRQDGTPRPI LVTLGSESLR
RDILQKLAQR NGGQGELQIP HVNDTLRIKR DQHPAIRAEW GRMFRALDTE KQKPENMGHE
IFFAKKKRVI TKDASSSALG ASAMATSESE SEEADMGRLQ ALLEARGLPP HLFGALGSRM
HQLLHRSMSG GTITKAQHLL QGLQAVGDEG QQLTAAIEMC QLLVMGNEDT LAGFPVKQVV
PALITLLQMD HNFDIMNNSC RALTYMMEAL PRSSAVVVDA VPVFLEKLQV IQCMDVAEQA
LTALEMLSRR HSKSILQAGG IAACLMFLDF FSITAQRCAL AITANCCQNM NSDEFHYVRD
SLPLLSGRLS HHDKKSVESV CLCFSRLVDN FQTDERILKE ISAHGLLTNI LQLLVVTPPV
VNTGTFVTVL RMLAVMCASC PDLAVVLLKS NIADTLCYLL VGTSETASQG VELVTRTPQE
LYEIVCLIGE LMPSLPNDGV FSVDSLLRKG CTTNTDAVIW QWRDDRGIWH PYSLIDSRII
EASHQSGEDE VSLSTMGRNY SIDFNSMQQI NEDTGTSRPV QRKLNPLAAH GSAAASNNCG
VVRSDSRAEI LKEDMDLASS FIKALFAVLY EVYSSSAGPA VRHKCLQAIL RMVYYATPEL
LKDVLQNHAV SSHIAAMLAS QDLKVVVGAM QMAEILMQKL ANIFGIYFRR EGVMHQVKRL
ADPANWEPSP QKSTDSASTP VSQTSREELR AAATSVSSSL GSSLEKVDLD NNSTTPNTVA
GGATAATPEA ALDRSPGSSQ MRLSDVLKRK KPPKRSSRSS RSSSSGKTDE SPSAMETVFA
RLGGGGGGGS NNRPTPSSRG KTGKDTSKSG GATPKSSFLA NLNPARWGRA STSATPERPV
STRIIVHQQE TFIVKSTSNP NLVSNREKVK TWIREQAARF IEQYFSDETQ GSSHPAMDVL
KRLSVATEQL ANLEEDAGLE CLQVLSTIMK DSDVSPFEII HSGFVGKLLK YISSAHGVVS
REVKIRRFLH VFLNCPPPDV TTVSQVEFSE NPPFSPLISK LVGCLHQLEQ FQVKVHDLPG
GGTGNSRGSS AIKFFNTHQL KCNLVRHPAC TNLRQWRGGP VKIDPLALVQ AIERYLVMRG
YGRIRPDADD ENSDDENSDD DLDDTRAAVF LTQGTGRHKL EFLMGDRVLP YNWTVYQAIK
QYGSLEGRDG SETDTDTENP FGHAGIWVQT HTIWYRPAPE EDTNASQPTS PKKTKAEGKS
HKASPKGKKG DDLWLGGQCP PVVLPLDRYL SPSLPDSVLV QDPSLEVLAL LRVLHAINIY
WGALYETSSY DPLVSSLEFS SSKLIAKANR QLQDPLVIMT GNLPQWLPEI AAACPFLFPF
DTRQMLFYAT AFDRDRAMMR LQDATQDAAN NDTSERVAPR LDRRKRVVSR DDLLKQAEKV
MEEMGNSKAL LEIQYENEVG TGLGPTLEFY SLVSRELRRS DLDIWRGEAT KLKDSS
//
