ID A0A9Q8WJL5_9PEZI Unreviewed; 1588 AA.
AC A0A9Q8WJL5;
DT 13-SEP-2023, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2023, sequence version 1.
DT 28-JAN-2026, entry version 12.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN ORFNames=CLUP02_11563 {ECO:0000313|EMBL:UQC86063.1};
OS Colletotrichum lupini.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum acutatum species complex.
OX NCBI_TaxID=145971 {ECO:0000313|EMBL:UQC86063.1, ECO:0000313|Proteomes:UP000830671};
RN [1] {ECO:0000313|EMBL:UQC86063.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=IMI 504893 {ECO:0000313|EMBL:UQC86063.1};
RX PubMed=34402629;
RA Baroncelli R., Pensec F., Da Lio D., Boufleur T., Vicente I., Sarrocco S.,
RA Picot A., Baraldi E., Sukno S., Thon M., Le Floch G.;
RT "Complete Genome Sequence of the Plant-Pathogenic Fungus Colletotrichum
RT lupini.";
RL Mol. Plant Microbe Interact. 34:1461-1464(2021).
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the ZNF598/HEL2 family.
CC {ECO:0000256|ARBA:ARBA00035113}.
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DR EMBL; CP019478; UQC86063.1; -; Genomic_DNA.
DR RefSeq; XP_049147675.1; XM_049290530.1.
DR GeneID; 73345540; -.
DR KEGG; clup:CLUP02_11563; -.
DR Proteomes; UP000830671; Chromosome 6.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0043022; F:ribosome binding; IEA:TreeGrafter.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016567; P:protein ubiquitination; IEA:TreeGrafter.
DR GO; GO:0072344; P:rescue of stalled ribosome; IEA:InterPro.
DR CDD; cd16615; RING-HC_ZNF598; 1.
DR CDD; cd10567; SWIB-MDM2_like; 1.
DR Gene3D; 1.10.10.60; Homeodomain-like; 1.
DR Gene3D; 1.10.245.10; SWIB/MDM2 domain; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR014876; DEK_C.
DR InterPro; IPR057634; PAH_ZNF598/HEL2.
DR InterPro; IPR041888; RING-HC_ZNF598/HEL2.
DR InterPro; IPR019835; SWIB_domain.
DR InterPro; IPR036885; SWIB_MDM2_dom_sf.
DR InterPro; IPR003121; SWIB_MDM2_domain.
DR InterPro; IPR056437; Znf-C2H2_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; PF08766; DEK_C; 1.
DR Pfam; PF23202; PAH_ZNF598; 1.
DR Pfam; PF25447; RING_ZNF598; 1.
DR Pfam; PF02201; SWIB; 1.
DR Pfam; PF23230; zf-C2H2_13; 1.
DR SMART; SM00151; SWIB; 1.
DR SMART; SM00355; ZnF_C2H2; 4.
DR SUPFAM; SSF109715; DEK C-terminal domain; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR SUPFAM; SSF47592; SWIB/MDM2 domain; 1.
DR PROSITE; PS51998; DEK_C; 1.
DR PROSITE; PS51925; SWIB_MDM2; 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:UP000830671};
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 295..351
FT /note="DEK-C"
FT /evidence="ECO:0000259|PROSITE:PS51998"
FT DOMAIN 473..550
FT /note="DM2"
FT /evidence="ECO:0000259|PROSITE:PS51925"
FT DOMAIN 875..915
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 158..179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 216..275
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 355..476
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 780..852
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1149..1197
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1214..1263
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1393..1588
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 158..176
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 224..238
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 245..257
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 356..369
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 397..409
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 438..451
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 804..815
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 836..848
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1157..1171
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1214..1223
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1224..1263
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1393..1415
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1450..1501
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1505..1520
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1549..1558
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1588 AA; 172238 MW; BA65243B72DA665B CRC64;
MTEYDYLICL PRRPVWGGAA EGTSAGSQFG NVIGTASRSG TDGSTSQRLM HNCKTRKNPK
TTFFSVFPSF QPHITRTWAF YSSALFWLLR YLILPCCGYL TLPHLTEVPT EQEPNIGKCE
PHLFLPGPQI APHTAHCTHC THCTDTAHPS HLVVWDKTSP VHSHTPRSTS TSPSDTLYPS
GASALFRDSR LGSHAPPRDR PLFSLVRTER QRYALIRGQP NNPPTNSLLA DPSASSTIDR
PAASPSASQY SCATTPTDRA PATIGRSGSN IDTSTKHYSR NIIHSGSNMS LPLSSEDEDN
YTAIIDGILA TADLTTITRK KIRLGLEKAL GGKDLTAQKD AIKALIEERF DAISGSNDAA
PDSYSASPAP KREANGHDDD IDGEIEVSVA PVRKRQKRED SSEDADAKLA AKLQAQENQM
ARGRTTRGGN GASSKGTKAA KKKKAPRKKS DKKIDDSDVE DSGEAPKRKA GGGFQKPFNL
SEPLSELLGE PQLSRPQVVK KLWEHIKGND LQDPENKRQI ICDDKMHAIF KQSKVDMFQM
NKMIGAHLYP VEEQTFRAVW LDIRVQAANG WRIAKCLLVW LLEEDISRGW LWLQLQALRY
LSYSRETMIT DESFCMQLIL GYLRKTSNAS CTASMSRVQS HKCGLEPAGD SAKLSSWLLL
CYVSLEASSD GGMAVWRARR NPGRRSLTRM EVSTLSGSSC HLDEQWKGTF FAGPRHEFPP
PTNARANPTH SRFPWEPHII INFDSLHAIW NELFSCSYTN PQASSTDSTV SLSTRKTTVP
MADTHAAGGD SNPSRGNRNR GRGRGGGGGG GGGANAGTRG RGRGGRGRGG NNAAASTQPE
TSSASQAPVT KADNKVLTRT AAADDDTASS DGEVCFICAE PIKFHSIAPC NHKTCHICGL
RMRALYKTKD CPHCRTASPF VVFTDDANKR YEDYTDADIT SFDSNIGIRY TNEEIVGDTV
VLLRYNCPAE DCVFAGLGWP DLHRHVRSTH HMKMCDLCTR NKKVFTHEHE LFADKELEKH
MRHGDDRPGA IDQTGFKGHP LCGFCGSRFY DDDKLFDHCR EKHERCFICD RRDSRHPHYF
VNYNALEKHF EKDHFPCLDK ECLEKKFVVF ESEMDLKAHQ LEEHANSLSK DVRRDARVVN
MSGFDYRSTY ETERRGGGGG GRSGGGGGDG PSSGRQGRGR GRDPNAEPIP HSSAQPLRRD
ELAFQRQMAI HSAQSVSNRT FGGSLSQPAS TTPASSSRRG NGAPAPGGSS RQAPAAAAAP
APALPTAEME QLNVTDIASL PPQERAVMLR HQGVVERASN LLGHDQSKMK EFRDYISNFR
KGSLTAPQLV DAFFSLFADT SSNALGTLVR EVADLFEDKS KVAALHKAWQ DWRAINEDYP
SLPGLGGMHG ATTASSGWAS AASPSPTAPA AAPSSNQKHS NRVLRLKNST RAGASGPKPV
APAASANWVS TSGSSRPPAP SAFPALPAAS SSKSSAPQPS WIGPNNPSAS RSSGSAGPVR
STPAGRPPPS SAFPALPPAQ KPLTTIFGYG SGRGVRRDLG GAASNFSWGS APGSGAASEN
VSEREDEEAG QSTGGKKKKG KKVLVQWG
//
