ID   A0A1S3IKK3_LINUN        Unreviewed;      1034 AA.
AC   A0A1S3IKK3;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=Ubiquitin conjugation factor E4 A {ECO:0000256|ARBA:ARBA00040077};
DE            EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN   Name=LOC106164917 {ECO:0000313|RefSeq:XP_013398421.1};
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_013398421.1};
RN   [1] {ECO:0000313|RefSeq:XP_013398421.1}
RP   IDENTIFICATION.
RC   TISSUE=Gonads {ECO:0000313|RefSeq:XP_013398421.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- FUNCTION: Ubiquitin-protein ligase that probably functions as an E3
CC       ligase in conjunction with specific E1 and E2 ligases. May also
CC       function as an E4 ligase mediating the assembly of polyubiquitin chains
CC       on substrates ubiquitinated by another E3 ubiquitin ligase. Mediates
CC       'Lys-48'-linked polyubiquitination of substrates.
CC       {ECO:0000256|ARBA:ARBA00037624}.
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: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the ubiquitin conjugation factor E4 family.
CC       {ECO:0000256|ARBA:ARBA00007434}.
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DR   RefSeq; XP_013398421.1; XM_013542967.1.
DR   AlphaFoldDB; A0A1S3IKK3; -.
DR   STRING; 7574.A0A1S3IKK3; -.
DR   EnsemblMetazoa; XM_013542967.1; XP_013398421.1; LOC106164917.
DR   GeneID; 106164917; -.
DR   KEGG; lak:106164917; -.
DR   InParanoid; A0A1S3IKK3; -.
DR   OrthoDB; 1554at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000085678; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0000151; C:ubiquitin ligase complex; IEA:InterPro.
DR   GO; GO:0034450; F:ubiquitin-ubiquitin ligase activity; IEA:InterPro.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IEA:InterPro.
DR   CDD; cd16658; RING-Ubox_UBE4B; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR019474; Ub_conjug_fac_E4_core.
DR   InterPro; IPR045132; UBE4.
DR   InterPro; IPR003613; Ubox_domain.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR13931:SF16; UBIQUITIN CONJUGATION FACTOR E4 A; 1.
DR   PANTHER; PTHR13931; UBIQUITINATION FACTOR E4; 1.
DR   Pfam; PF04564; U-box; 1.
DR   Pfam; PF10408; Ufd2P_core; 1.
DR   SMART; SM00504; Ubox; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS51698; U_BOX; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Reference proteome {ECO:0000313|Proteomes:UP000085678}.
FT   DOMAIN          962..1034
FT                   /note="U-box"
FT                   /evidence="ECO:0000259|PROSITE:PS51698"
SQ   SEQUENCE   1034 AA;  118627 MW;  9DF2C4085F8725EF CRC64;
     MSRMSGPDLK NNPFTALFPS VLDAQQFAAG VKDALATSDQ DISESIFSDQ GKAEEVVHLN
     NLIERIFLIT LDQTCTSDKF RPAKAVFMAE FQLTLGGQDW LDLEILETCL FERLVFEEPD
     KHIVKTSKTG EPDRTVTEGR VLFYLYYAYV RAVQETKKIE DESYLSFVTV IKDIIIRNGK
     TSLQTAPLFV GQDPGQQFLD IFMEEHRNSD SEIMMEFLEL VASEIDSHQE DGSLAQILRP
     VLDQVTTTFH KELGLNNPRT FDFVEFVLFM TRTECLGKVF MDYTTPRDIK TAKNFEMSLL
     GCTLSISCIP ENPQGPFQFF TEPSTMRPSE VEMTMHSLWQ PIAILNEKVH KMIYNLLKLS
     EELKHRTLEW LGNCLTANQG RAKLWSNHLP PELLNRMYCS DGFFINLCAV LLRLCKPFCA
     AQSPKLLKIQ LSYCAVEMKT VEEGRERNMH LKGLNKETSL IPPPEGSVPY PGEDKFNFLT
     ECFMMTHYCL HLGIHVIHEK FMRLNQEMGQ LEGAYRDLVN SGAEGSAIGR QLKDRFEKRM
     SMFQCVRAAL LEPQIVQMSL QLHVASATLL VNLAAGGVES FLQEICFPLP DPVPDVLTVV
     PEFLVENMVD LVVFIRRFRD ETFEIIGGDI SHFASLILVF MGSPQRMKNP HLRAKLAQTL
     ENLMPVQNEM KAGLIANYHR EQLFVKHPLI QHLAETLLHV FVSIEMTGQA VQFEQKFNYR
     RPMYKILDYI WNIEIHHEAL KRLSAHAEEH IEDSDAPLFL RFINLLVNDA TFLLDEALMY
     MSQIKEQQEE KDSGAWQNLP EDQQREKESN LQQLTMLSRF HNLMSRDTIH ILELLTRDIQ
     TLFIHNIMVD RIAAMLNYFL IHLVGPKKKN LKVKNFEEFE FKPQLIVSDI CQIYLNLGSH
     EAFCLAVTAD GRSYSPDLLP QAERVLQRIG KPVQMISEFA GLAEEIKSVA SQQKEEEELL
     GDVPEEFQDA IMGTVMKDPV ILPSGQVVDR STIARHLLSD QTDPFNRSPL TMEMLKPHDE
     LREKIKLWIQ DNKK
//