ID   A0A0R3QUD2_9BILA        Unreviewed;       416 AA.
AC   A0A0R3QUD2;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=E3 ubiquitin-protein transferase MAEA {ECO:0000256|ARBA:ARBA00014384};
DE   AltName: Full=Macrophage erythroblast attacher {ECO:0000256|ARBA:ARBA00029678};
OS   Brugia timori.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Brugia.
OX   NCBI_TaxID=42155 {ECO:0000313|Proteomes:UP000050602, ECO:0000313|WBParaSite:BTMF_0001133401-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:BTMF_0001133401-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Nucleus matrix {ECO:0000256|ARBA:ARBA00004109}.
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DR   AlphaFoldDB; A0A0R3QUD2; -.
DR   STRING; 42155.A0A0R3QUD2; -.
DR   WBParaSite; BTMF_0001133401-mRNA-1; BTMF_0001133401-mRNA-1; BTMF_0001133401.
DR   Proteomes; UP000050602; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0016363; C:nuclear matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR   GO; GO:0043249; P:erythrocyte maturation; IEA:UniProtKB-KW.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR   CDD; cd16659; RING-Ubox_Emp; 1.
DR   InterPro; IPR013144; CRA_dom.
DR   InterPro; IPR024964; CTLH/CRA.
DR   InterPro; IPR006595; CTLH_C.
DR   InterPro; IPR045098; Fyv10_fam.
DR   InterPro; IPR006594; LisH.
DR   InterPro; IPR044063; ZF_RING_GID.
DR   PANTHER; PTHR12170:SF2; E3 UBIQUITIN-PROTEIN TRANSFERASE MAEA; 1.
DR   PANTHER; PTHR12170; MACROPHAGE ERYTHROBLAST ATTACHER-RELATED; 1.
DR   Pfam; PF10607; CTLH; 1.
DR   SMART; SM00757; CRA; 1.
DR   SMART; SM00668; CTLH; 1.
DR   SMART; SM00667; LisH; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS50897; CTLH; 1.
DR   PROSITE; PS50896; LISH; 1.
DR   PROSITE; PS51867; ZF_RING_GID; 1.
PE   4: Predicted;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Erythrocyte maturation {ECO:0000256|ARBA:ARBA00023057};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU01215}.
FT   DOMAIN          181..238
FT                   /note="CTLH"
FT                   /evidence="ECO:0000259|PROSITE:PS50897"
FT   DOMAIN          333..401
FT                   /note="RING-Gid-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51867"
FT   ZN_FING         333..401
FT                   /note="RING-Gid-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01215"
FT   REGION          9..28
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        10..28
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   416 AA;  48362 MW;  64274A7060666B1B CRC64;
     LKEKKVYKFM MSSSSPSQDS TQSSEPLKPD EITALEYTSL KVPYEMFNKR FRSSQKTMEK
     NNYFLKETAD LVAKAMKGDG TKPIYKRDIK EKMDLYFGRF DELFGTFKQI TDEEMELIDL
     LDTRVKYLQQ ANTTDALKQE TWRSQRISRL IIDYLLRSGY FETAQKLAEQ ANVEDMCNKT
     VFMIAKQVED SLSRHETDRC LEWIADNKSK LRRLKSTLET TVRLQDCIEL VRRGDRLEAV
     HYARKFLANL PKDQWSEQVV KVMGLIGFGI PSKSRAYNEY FSEKRWDQLI ELFKQENARV
     YKLMEYSSFN ACLCMGLSAY KSPQCHPDPD SRCPTCRPDM HELAEDLPHS HVSNSRLMCA
     YSGEPMDDDN EPFMLPNGYV YGANSIEKLL NASDEIVCPR TGEIYPANQL LRVFVL
//