ID A0A016T363_9BILA Unreviewed; 361 AA.
AC A0A016T363;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=E3 ubiquitin-protein transferase MAEA {ECO:0000256|ARBA:ARBA00014384};
DE AltName: Full=Macrophage erythroblast attacher {ECO:0000256|ARBA:ARBA00029678};
GN Name=Acey_s0143.g2403 {ECO:0000313|EMBL:EYB97122.1};
GN Synonyms=Acey-maea-1 {ECO:0000313|EMBL:EYB97122.1};
GN ORFNames=Y032_0143g2403 {ECO:0000313|EMBL:EYB97122.1};
OS Ancylostoma ceylanicum.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Ancylostomatidae;
OC Ancylostomatinae; Ancylostoma.
OX NCBI_TaxID=53326 {ECO:0000313|EMBL:EYB97122.1, ECO:0000313|Proteomes:UP000024635};
RN [1] {ECO:0000313|Proteomes:UP000024635}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=HY135 {ECO:0000313|Proteomes:UP000024635};
RX PubMed=25730766; DOI=10.1038/ng.3237;
RA Schwarz E.M., Hu Y., Antoshechkin I., Miller M.M., Sternberg P.W.,
RA Aroian R.V.;
RT "The genome and transcriptome of the zoonotic hookworm Ancylostoma
RT ceylanicum identify infection-specific gene families.";
RL Nat. Genet. 47:416-422(2015).
CC -!- SUBCELLULAR LOCATION: Nucleus matrix {ECO:0000256|ARBA:ARBA00004109}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EYB97122.1}.
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DR EMBL; JARK01001479; EYB97122.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A016T363; -.
DR Proteomes; UP000024635; Unassembled WGS sequence.
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 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 Reference proteome {ECO:0000313|Proteomes:UP000024635};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU01215}.
FT DOMAIN 128..185
FT /note="CTLH"
FT /evidence="ECO:0000259|PROSITE:PS50897"
FT DOMAIN 279..346
FT /note="RING-Gid-type"
FT /evidence="ECO:0000259|PROSITE:PS51867"
FT ZN_FING 279..346
FT /note="RING-Gid-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01215"
SQ SEQUENCE 361 AA; 41333 MW; FB5AE010FDC0DAA4 CRC64;
MERAGAGLKR SITSLRSALS EKDGCVSVAT AREAFRDFKL KLEQLDLEKR EAVRKQRQFI
KNMQSRIQFL RNEDISSEKA QRDLEMWRRD RQQVARLICT QMLRCGHVES AKALANEMEI
SNIVDLEVFA KVERVINALL SKDTTPCLEW IGEHRSKLRR MNSKLEQVVR VQNAVELVRD
GRVKEALMYI RKHLGASKDG WCEDAMKVMG LIALRSHNDI PAYKELLSDQ RWQRLADLFR
EEVFALYQLP RQSAFAMCLQ CGLSAYKTPH CSPGGVERCP TCQPCAYALA EGLPYAHTVN
SRLICSYSGE ALNEENHPMM MPDGRVYGEK AIRELQVDNM VRCPRTGSMI PIDHVLKLYV
L
//
