ID U6ME12_EIMMA Unreviewed; 661 AA.
AC U6ME12;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN ORFNames=EMWEY_00007510 {ECO:0000313|EMBL:CDJ60679.1};
OS Eimeria maxima (Coccidian parasite).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Eimeriidae; Eimeria.
OX NCBI_TaxID=5804 {ECO:0000313|EMBL:CDJ60679.1};
RN [1] {ECO:0000313|EMBL:CDJ60679.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Weybridge {ECO:0000313|EMBL:CDJ60679.1};
RA Reid A.J., Blake D., Billington K., Browne H., Dunn M., Hung S.,
RA Kawahara F., Miranda-Saavedra D., Mourier T., Nagra H., Otto T.D.,
RA Rawlings N., Sanchez A., Sanders M., Subramaniam C., Tay Y., Dear P.,
RA Doerig C., Gruber A., Parkinson J., Shirley M., Wan K.L., Berriman M.,
RA Tomley F., Pain A.;
RT "Genomic analysis of the causative agents of coccidiosis in chickens.";
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CDJ60679.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Weybridge {ECO:0000313|EMBL:CDJ60679.1};
RA Aslett M.;
RL Submitted (OCT-2013) 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};
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DR EMBL; HG721904; CDJ60679.1; -; Genomic_DNA.
DR RefSeq; XP_013337329.1; XM_013481875.1.
DR AlphaFoldDB; U6ME12; -.
DR EnsemblProtists; CDJ60679; CDJ60679; EMWEY_00007510.
DR GeneID; 25334737; -.
DR VEuPathDB; ToxoDB:EMWEY_00007510; -.
DR OrthoDB; 216971at2759; -.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR045194; MGRN1/RNF157-like.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR22996; MAHOGUNIN; 1.
DR PANTHER; PTHR22996:SF0; RING-TYPE E3 UBIQUITIN TRANSFERASE; 1.
DR Pfam; PF13920; zf-C3HC4_3; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Signal {ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00175}.
FT SIGNAL 1..45
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 46..661
FT /note="RING-type E3 ubiquitin transferase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004676077"
FT DOMAIN 496..533
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 229..249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 568..590
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 172..202
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 568..586
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 661 AA; 69107 MW; 9681330C80B8BB6D CRC64;
MAASAATAAA AAAAAAGAAV SRSRRGLSLV VVVAVLLLLL RPSAANAAAA ASGAESGGMT
PAAAMSAAAA AAGGSSISSS SRSNDNNNDS SSNSSSLIYD VELSPGAHNV MEALLLAGFG
RYRYELQQLM RVHFTKLLQH NKPAAAAAMP LVEVKVYCYD PLPLNQGEVQ ENEEHQQQLL
LMQQQQQQQQ ELQQELQQEM LLLHQTDSTG HSSSHNSFFS PIVAAYSSSS SRRERNSNNS
NLQQREALLS SPSSTAAAAA AASTSAAAAA AAALAGGGFE VSVDAAATAA VRAYWGVGQK
AMETFIKGNN NSDGQSLLSG SARRLARLLP SSSSDSSSSR RFNTGTFAAD SAAMPWGPDG
CCLMSAPQIV PAGRGHRLRF FTHDRDNTAG RLSPFTEAVF PLVIVASVGG SSATCHLLLL
RCRPLPPPPP STSSRSRVSA AEAAAAAAAA PLPACYVSHR YEVYRQLLAG GSLDKPQEKG
DIFGVSSSSG TLDLECLVCM TNPKNVVLYP CRHCALCLEC LQALHQEKCP VCRSHFFGFI
TFPLSKNLTA AESVSVAPAA AVADSRNGVV SSGSSNNGST NVQHHRGGSR VVPAETQMET
VTKYAALFRL LVVLQEAAAA TYFVTVSMPL EARQEAGTVQ QKQQQQHCST QLHNVRYSAV
A
//