ID A0A093HZ98_STRCA Unreviewed; 411 AA.
AC A0A093HZ98;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, 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};
DE Flags: Fragment;
GN ORFNames=N308_13996 {ECO:0000313|EMBL:KFV86996.1};
OS Struthio camelus australis.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Palaeognathae; Struthioniformes; Struthionidae;
OC Struthio.
OX NCBI_TaxID=441894 {ECO:0000313|EMBL:KFV86996.1, ECO:0000313|Proteomes:UP000053584};
RN [1] {ECO:0000313|EMBL:KFV86996.1, ECO:0000313|Proteomes:UP000053584}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N308 {ECO:0000313|EMBL:KFV86996.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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 -!- SUBCELLULAR LOCATION: Nucleus matrix {ECO:0000256|ARBA:ARBA00004109}.
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DR EMBL; KL206928; KFV86996.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093HZ98; -.
DR STRING; 441894.ENSSCUP00000021074; -.
DR Proteomes; UP000053584; 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:0003779; F:actin binding; IEA:UniProtKB-KW.
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 Reference proteome {ECO:0000313|Proteomes:UP000053584};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU01215}.
FT DOMAIN 136..231
FT /note="CTLH"
FT /evidence="ECO:0000259|PROSITE:PS50897"
FT DOMAIN 329..396
FT /note="RING-Gid-type"
FT /evidence="ECO:0000259|PROSITE:PS51867"
FT ZN_FING 329..396
FT /note="RING-Gid-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01215"
FT REGION 167..192
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFV86996.1"
FT NON_TER 411
FT /evidence="ECO:0000313|EMBL:KFV86996.1"
SQ SEQUENCE 411 AA; 47160 MW; 201B8A2DD5017662 CRC64;
VPYETLNKRF RAAQKNIDRE TSHVTMVVAE LEKTLSSCPA VDSVVSLLDG VVEKLSVLKR
KVVESIQAED ESAKLCKRRI EHLKEHSSDQ PAAANMWKKK RMDRMMVEHL LRCGYYNTAV
KLARQSGIED LVNIEMFLTA KEVEESLERQ ETMTCLAWCH DNKSRLRKMK GRQNENEPKM
GRKSKSASDY SKENDDLVME TIKGKPELSC LEFSLRIQEF IELIRQNKRL DAVRHARKHF
SQAEGSQLDE VRQVMGMLAF PSDTHISPYK DLLDPARWRM LIQQFRYDNY RLHQLGNNSV
FTITLQAGLS AIKTPQCYKE DGSSKNPDCP VCSKSLNKLA QPLPMAHCAN SRLVCKISGD
VMNENNPPMM LPNGYVYGYN SLLSIRQDDK VICPRTKEVF NFSQAEKVYI M
//
