ID A0A0J7P3E8_LASNI Unreviewed; 391 AA.
AC A0A0J7P3E8;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=E3 ubiquitin-protein transferase MAEA {ECO:0000256|ARBA:ARBA00014384};
DE AltName: Full=Macrophage erythroblast attacher {ECO:0000256|ARBA:ARBA00029678};
GN ORFNames=RF55_701 {ECO:0000313|EMBL:KMR04459.1};
OS Lasius niger (Black garden ant).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Formicinae; Lasius; Lasius.
OX NCBI_TaxID=67767 {ECO:0000313|EMBL:KMR04459.1, ECO:0000313|Proteomes:UP000036403};
RN [1] {ECO:0000313|EMBL:KMR04459.1, ECO:0000313|Proteomes:UP000036403}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Whole {ECO:0000313|EMBL:KMR04459.1};
RA Konorov E.A., Nikitin M.A., Kirill M.V., Chang P.;
RT "Lasius niger genome sequencing.";
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
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:KMR04459.1}.
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DR EMBL; LBMM01000214; KMR04459.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0J7P3E8; -.
DR STRING; 67767.A0A0J7P3E8; -.
DR PaxDb; 67767-A0A0J7P3E8; -.
DR OrthoDB; 1429623at2759; -.
DR Proteomes; UP000036403; 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 InterPro; IPR027370; Znf-RING_euk.
DR PANTHER; PTHR12170:SF2; E3 UBIQUITIN-PROTEIN TRANSFERASE MAEA; 1.
DR PANTHER; PTHR12170; MACROPHAGE ERYTHROBLAST ATTACHER-RELATED; 1.
DR Pfam; PF10607; CTLH; 1.
DR Pfam; PF13445; zf-RING_UBOX; 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 Reference proteome {ECO:0000313|Proteomes:UP000036403};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU01215}.
FT DOMAIN 152..209
FT /note="CTLH"
FT /evidence="ECO:0000259|PROSITE:PS50897"
FT DOMAIN 307..376
FT /note="RING-Gid-type"
FT /evidence="ECO:0000259|PROSITE:PS51867"
FT ZN_FING 307..376
FT /note="RING-Gid-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01215"
SQ SEQUENCE 391 AA; 44925 MW; ED7BF2E34C643161 CRC64;
MSDVKSLEHP TLKVPYELLN KKFRSAQKTL DREVSHVQAV SNELEKSLKT DGSYVATGEI
SKLLGGVVAR LQVLKRKAQE SIAEELQAGM VCKRRLDHLK EHANTSPSAV NQWRRQRLDR
MLVEYFLRKG YYKTATKLAD SNELRDLTNI DVFMVSREVE KSLANHETAR CIGWCHDNRS
KLRKLGSTME FNLRVQEFIE LVRTDRRLDA VKHARKYFSN YDDYQLQEIQ CCMGQLAFPA
HAYLSPYKDL LDEKRWDKLI ETFRQENYRL FQLASQSVFT VALQAGLSAL KTPQCYSANK
EGRNPSCPVC NEALNELAAP LPFAHCSQSR LVCSISGKPL NEYNQPMMMP NGYVYGEQAL
EKMAQENNGT VICPKTKEVF PYKKIEKVYV M
//
