ID F4WII5_ACREC Unreviewed; 391 AA.
AC F4WII5;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=E3 ubiquitin-protein transferase MAEA {ECO:0000256|ARBA:ARBA00014384};
DE AltName: Full=Macrophage erythroblast attacher {ECO:0000256|ARBA:ARBA00029678};
GN ORFNames=G5I_05509 {ECO:0000313|EMBL:EGI66116.1};
OS Acromyrmex echinatior (Panamanian leafcutter ant) (Acromyrmex octospinosus
OS echinatior).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Acromyrmex.
OX NCBI_TaxID=103372 {ECO:0000313|Proteomes:UP000007755};
RN [1] {ECO:0000313|EMBL:EGI66116.1}
RP NUCLEOTIDE SEQUENCE.
RA Nygaard S., Zhang G.;
RT "The genome of the leaf-cutting ant Acromyrmex echinatior suggests key
RT adaptations to social evolution and fungus farming.";
RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus matrix {ECO:0000256|ARBA:ARBA00004109}.
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DR EMBL; GL888175; EGI66116.1; -; Genomic_DNA.
DR RefSeq; XP_011053492.1; XM_011055190.1.
DR AlphaFoldDB; F4WII5; -.
DR STRING; 103372.F4WII5; -.
DR EnsemblMetazoa; XM_011055190.1; XP_011053492.1; LOC105145552.
DR GeneID; 105145552; -.
DR KEGG; aec:105145552; -.
DR eggNOG; KOG0396; Eukaryota.
DR InParanoid; F4WII5; -.
DR OrthoDB; 1429623at2759; -.
DR Proteomes; UP000007755; 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:UP000007755};
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; 44843 MW; 0AEC1ACEF2BB6AFE CRC64;
MSDVKSLEHP TLKVPYELLN KKFRSAQKTL DREVSHVQAV SNELEKSLKT DGTYVASGEI
SKLLGGVVAR LQVLKRKAQE SIAEELQAGM VCKRRLDHLK DHANTSSSAV NQWRRQRLDR
MLVEYFLRKG YYKTATKLAD SSELRDLTNI DVFMVSREVE KSLANHESAR CIGWCHDNRS
KLRKLGSTME FNLRVQEFIE LVRTDRRLDA VKHARKYFAN YDDYQLQEIQ CCMGQLAFPA
HAYLSPYKDL LDEKRWDKLI ETFRQENYRL FQLASQSVFT VALQAGLSAL KTPQCYSANK
EGRNPSCPVC NEALNELAAP LPFAHCSQSR LVCSISGKPL NEYNQPMMMP NGYVYGEQAL
EKMAQENNGT VICPKTKEVF PYKKIEKVYV M
//
