ID U6N242_9EIME Unreviewed; 693 AA.
AC U6N242;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN ORFNames=ENH_00068120 {ECO:0000313|EMBL:CDJ69378.1};
OS Eimeria necatrix.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Eimeriidae; Eimeria.
OX NCBI_TaxID=51315 {ECO:0000313|EMBL:CDJ69378.1};
RN [1] {ECO:0000313|EMBL:CDJ69378.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Houghton {ECO:0000313|EMBL:CDJ69378.1};
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:CDJ69378.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Houghton {ECO:0000313|EMBL:CDJ69378.1};
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};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
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DR EMBL; HG725707; CDJ69378.1; -; Genomic_DNA.
DR RefSeq; XP_013437845.1; XM_013582391.1.
DR AlphaFoldDB; U6N242; -.
DR GeneID; 25476945; -.
DR VEuPathDB; ToxoDB:ENH_00068120; -.
DR OrthoDB; 5487971at2759; -.
DR UniPathway; UPA00143; -.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0007219; P:Notch signaling pathway; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.30.390.130; -; 1.
DR Gene3D; 3.30.720.50; -; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR039396; Deltex_C.
DR InterPro; IPR039399; Deltex_C_sf.
DR InterPro; IPR039398; Deltex_fam.
DR InterPro; IPR004170; WWE-dom.
DR InterPro; IPR037197; WWE_dom_sf.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR12622; DELTEX-RELATED; 1.
DR PANTHER; PTHR12622:SF36; E3 UBIQUITIN-PROTEIN LIGASE DTX3-RELATED; 1.
DR Pfam; PF18102; DTC; 1.
DR Pfam; PF02825; WWE; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR SUPFAM; SSF117839; WWE domain; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 208..247
FT /note="WWE"
FT /evidence="ECO:0000259|Pfam:PF02825"
FT DOMAIN 548..680
FT /note="Deltex C-terminal"
FT /evidence="ECO:0000259|Pfam:PF18102"
FT REGION 1..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 170..208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 340..359
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 410..502
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..29
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 41..63
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 170..189
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 435..498
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 693 AA; 76687 MW; A1CC3A8B8A3FA2D6 CRC64;
MPRLPSDDAR NIHSSFASGM RNFLSRGASN RAAQRARRGA DTGAHNQQTP NNAMNSPTSA
PEDEGIRNSH EDADQSSIAT GVATALFQRH QSQDSIFVPS KYRFPAPTAV SVPAVWSWQM
GQADWVPFDV QVMELLESLW AHMQSQQQQQ QQDEPPHELV ESLEEAQELL QTQEQQDQPQ
EGQSQHGTVR EIGESDDMTS PTAATSQARL EQSHKVYAHI SPWQYCLDLG KMTQQNLATR
RVRPIRRNVE SVGLWFAKGS DGHAERFPPE VEVHLEALWK ESLQGVRNPS AFVLTWENQR
TGHVHYTDII TMRESFNTGS QREIMRTELV AEAPLNDSAE AVKPGDSKEH SFSLPSLEVG
TEESGEAICK GHRKWLESDD FDASLVVVEG HEVPDDTCVI CLDNLAHEET APSTDAQQSK
KKKQRRRSNM DKDEKCCSSG GSSSRDTKDI SGTSSRNRRR SNSKIACSTI AASPNESEAD
PSSNADCDMN SPQDTGSKFP DSNKEEVVRL INCSHHFHTE CIRMYVQSCT KGGFYCPTCN
VLQLPGNGPC PPGKMKWRIC NRPLLAGHPD EAGTIIIDYI VSGGIQTERH ARPSIPFTGA
RRQAYLPDCL MGRRLLRLLI QAFVKGHIFT VGDSVTSGQS NVVVWNGIHH KTSVSGGVLH
YGYPDDTFLS RLAEELKARG FPLEADVPAA VSA
//
