ID A0A024TWJ4_9STRA Unreviewed; 626 AA.
AC A0A024TWJ4;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 08-NOV-2023, entry version 30.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN ORFNames=H310_08659 {ECO:0000313|EMBL:ETV98525.1};
OS Aphanomyces invadans.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC Aphanomyces.
OX NCBI_TaxID=157072 {ECO:0000313|EMBL:ETV98525.1};
RN [1] {ECO:0000313|EMBL:ETV98525.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NJM9701 {ECO:0000313|EMBL:ETV98525.1};
RG The Broad Institute Genomics Platform;
RA Russ C., Tyler B., van West P., Dieguez-Uribeondo J., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L., Chapman S.B.,
RA Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C., Pearson M.,
RA Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Aphanomyces invadans NJM9701.";
RL Submitted (DEC-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}.
CC -!- SIMILARITY: Belongs to the ZNF598/HEL2 family.
CC {ECO:0000256|ARBA:ARBA00035113}.
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DR EMBL; KI913969; ETV98525.1; -; Genomic_DNA.
DR RefSeq; XP_008872722.1; XM_008874500.1.
DR AlphaFoldDB; A0A024TWJ4; -.
DR EnsemblFungi; H310_08659-t26_2; H310_08659-t26_2-p1; H310_08659.
DR EnsemblProtists; ETV98525; ETV98525; H310_08659.
DR GeneID; 20085709; -.
DR VEuPathDB; FungiDB:H310_08659; -.
DR OrthoDB; 3059402at2759; -.
DR GO; GO:0005737; C:cytoplasm; 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:0072344; P:rescue of stalled ribosome; IEA:InterPro.
DR CDD; cd16615; RING-HC_ZNF598; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR041888; RING-HC_ZNF598/Hel2.
DR InterPro; IPR044288; ZNF598/Hel2.
DR InterPro; IPR013087; Znf_C2H2_type.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR22938:SF0; E3 UBIQUITIN-PROTEIN LIGASE ZNF598; 1.
DR PANTHER; PTHR22938; ZINC FINGER PROTEIN 598; 1.
DR Pfam; PF13920; zf-C3HC4_3; 1.
DR SMART; SM00355; ZnF_C2H2; 4.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 188..229
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 24..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 82..179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..44
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 82..141
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 626 AA; 69692 MW; 1841C765B1C48F53 CRC64;
MVRNFHFLVG SMATSRASTS VAVRGAAAPA QSQGTVNSNR SSTSKASHSR KKKPAQLVVP
SATVEQSGIL RPNAATFTPS LQHGASVIPT PDNAASKKQN PQQRSRRSRG TTEQPPIVVT
GAPANNSDRT KDTTATANPA TPLVHPSARG SRGGRNRKSR DAATLAKSTV VNEDDDERSE
SKEARELCLV CANPFRYHAI GECNHEGICS TCSMRMRLLM KDFNCPICKQ ANPRVIVTDV
IAPYASFGIW GDTGGPGVLL DDRSEMFFSR CDAHYESLVR RRDLYCRRCP TANRVKFRVL
EDLQLHMENE HATYFCDLCV QHQHFFVGEY PMYTMKELMH HQTSTVSATS RERHPLCEFC
HVRYYSDVEL HVHLERDHFK CHLCPEVQHR YYRNYKGLET HFRRQHLFCE DPSCIAKGFV
VFSNDIDFQA HMFSVHGNQD NRIRIAFTVR RGMEDEGGAS NVVSSGSNND SWEFVGPPPS
ASRQQEEFPA LPTAAPSATP WAKLAPVTPP AMIRPTAVAA PAPSSVPRAM LSRNALLASA
FGRGPKTEDA LEKELRPQYS QELKDWGRSK FRTLVAVEKK IEDMMADRAC FSTHLKAMPR
EQVCLVSSIP RRSLREFLVG STSSGV
//
