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Database: UniProt
Entry: A0A1Y1WEP5_9FUNG
LinkDB: A0A1Y1WEP5_9FUNG
Original site: A0A1Y1WEP5_9FUNG 
ID   A0A1Y1WEP5_9FUNG        Unreviewed;       744 AA.
AC   A0A1Y1WEP5;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   08-NOV-2023, entry version 19.
DE   RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE            EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN   ORFNames=DL89DRAFT_321142 {ECO:0000313|EMBL:ORX72001.1};
OS   Linderina pennispora.
OC   Eukaryota; Fungi; Fungi incertae sedis; Zoopagomycota; Kickxellomycotina;
OC   Kickxellomycetes; Kickxellales; Kickxellaceae; Linderina.
OX   NCBI_TaxID=61395 {ECO:0000313|EMBL:ORX72001.1, ECO:0000313|Proteomes:UP000193922};
RN   [1] {ECO:0000313|EMBL:ORX72001.1, ECO:0000313|Proteomes:UP000193922}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 12442 {ECO:0000313|EMBL:ORX72001.1,
RC   ECO:0000313|Proteomes:UP000193922};
RG   DOE Joint Genome Institute;
RA   Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA   Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA   Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA   Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA   Visel A., Grigoriev I.V.;
RT   "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL   Submitted (JUL-2016) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ORX72001.1}.
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DR   EMBL; MCFD01000003; ORX72001.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y1WEP5; -.
DR   STRING; 61395.A0A1Y1WEP5; -.
DR   OrthoDB; 3059402at2759; -.
DR   Proteomes; UP000193922; Unassembled WGS sequence.
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; 5.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 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   Reference proteome {ECO:0000313|Proteomes:UP000193922};
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          73..113
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          1..68
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          324..465
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          586..610
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          660..744
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..43
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        324..350
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        379..394
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        446..465
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        660..677
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        696..729
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   744 AA;  81717 MW;  21D649238328EE35 CRC64;
     MSNTPNANNA ADNQQQSTTT EQAVPPASTP ELKQQSKGKS SARGRNGRSA AHGKGSSEDK
     GDSEDDDDDE DVCFICADPV EFYAVGECDH RTCYLCNLRL RALFKSKACP YCKTDSEQLS
     THSFPYHDEK LSIKFDSKDA YDKAMYALQF NCPQRRCHYV DQTGWQGLKD HARQQHSLMF
     CDLCLKNKMS FAHEHKLFTK SQLRTHNSRG DNSGFPGHPM CEFCRTSFYD NDQLFDHCRK
     KHEQCFICVQ SGAGRQVYFK NYQTLEDHFN TDHFPCRQQT CIDRKFVVFG NELDLQAHEL
     ETHGSRIVGQ RARREARQVN INIHYSTNRA AGGSGSSNTG GSSSRGGRGT GSRRPETMMV
     NEPDSTGFSS AGRHRPAGFG QITEDDRRAT RSDTSSRDAP SSPEPEPERQ QPQTLWPELG
     AESSGSAHSA RAHPTMANSL GISMRERAPT DEKRPEVDSE TMSRHQELLQ RVSTYLSHRE
     QPVARFRKLT TQYKDNKVSA ADYVQNCWLL FLTVPGKNAK EMIQKTMKSV AELLPEQKQR
     DDLLKAWSNH RVKQQQFPAL APLTKTSTKA AGGSSNQARV LVIKQSTGSP GGRSGWASPK
     RGNVSPSQSV ANITKSLSSS SLSGFPSLSA SSSATSLHSM STAPRATPVV NAYSSKVSNS
     IGTASMSTSS SSGSRPRVTK AEFPGLPPST PARRKFAPVN PTTSSAWGSS SGTAPSTHLQ
     SGAGSRSNDK SKNAKGKNVL FRLG
//
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