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Database: UniProt
Entry: U4L5F5_PYROM
LinkDB: U4L5F5_PYROM
Original site: U4L5F5_PYROM 
ID   U4L5F5_PYROM            Unreviewed;       629 AA.
AC   U4L5F5;
DT   11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2013, sequence version 1.
DT   27-MAR-2024, entry version 57.
DE   SubName: Full=Similar to E3 ubiquitin-protein ligase itt1 acc. no. Q9US46 {ECO:0000313|EMBL:CCX07671.1};
GN   ORFNames=PCON_07260 {ECO:0000313|EMBL:CCX07671.1};
OS   Pyronema omphalodes (strain CBS 100304) (Pyronema confluens).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Pezizomycetes;
OC   Pezizales; Pyronemataceae; Pyronema.
OX   NCBI_TaxID=1076935 {ECO:0000313|EMBL:CCX07671.1};
RN   [1] {ECO:0000313|EMBL:CCX07671.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS100304 {ECO:0000313|EMBL:CCX07671.1};
RC   TISSUE=Vegetative mycelium {ECO:0000313|EMBL:CCX07671.1};
RX   PubMed=24068976; DOI=10.1371/journal.pgen.1003820;
RA   Traeger S., Altegoer F., Freitag M., Gabaldon T., Kempken F., Kumar A.,
RA   Marcet-Houben M., Poggeler S., Stajich J.E., Nowrousian M.;
RT   "The genome and development-dependent transcriptomes of Pyronema confluens:
RT   a window into fungal evolution.";
RL   PLoS Genet. 9:E1003820-E1003820(2013).
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DR   EMBL; HF935360; CCX07671.1; -; Genomic_DNA.
DR   AlphaFoldDB; U4L5F5; -.
DR   STRING; 1076935.U4L5F5; -.
DR   eggNOG; KOG1814; Eukaryota.
DR   OMA; PRSWCQG; -.
DR   OrthoDB; 4338126at2759; -.
DR   Proteomes; UP000018144; Unassembled WGS sequence.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:InterPro.
DR   CDD; cd20354; Rcat_RBR_RNF14; 1.
DR   Gene3D; 1.20.120.1750; -; 1.
DR   Gene3D; 3.10.110.10; Ubiquitin Conjugating Enzyme; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR031127; E3_UB_ligase_RBR.
DR   InterPro; IPR002867; IBR_dom.
DR   InterPro; IPR047548; Rcat_RBR_RNF14.
DR   InterPro; IPR006575; RWD_dom.
DR   InterPro; IPR044066; TRIAD_supradom.
DR   InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   PANTHER; PTHR11685; RBR FAMILY RING FINGER AND IBR DOMAIN-CONTAINING; 1.
DR   PANTHER; PTHR11685:SF457; TRANSLATION TERMINATION INHIBITOR PROTEIN ITT1; 1.
DR   Pfam; PF01485; IBR; 1.
DR   Pfam; PF05773; RWD; 1.
DR   SMART; SM00647; IBR; 2.
DR   SMART; SM00591; RWD; 1.
DR   SUPFAM; SSF57850; RING/U-box; 2.
DR   SUPFAM; SSF54495; UBC-like; 1.
DR   PROSITE; PS50908; RWD; 1.
DR   PROSITE; PS51873; TRIAD; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00175}.
FT   DOMAIN          18..133
FT                   /note="RWD"
FT                   /evidence="ECO:0000259|PROSITE:PS50908"
FT   DOMAIN          164..453
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51873"
FT   DOMAIN          168..213
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          227..258
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          557..629
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        230..258
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   629 AA;  68949 MW;  A7E6D73426200297 CRC64;
     MTSLSLETLS LSDDERSQEL FTIASIYPDE ITLLSPFSAS LVLPVIPLSP LTLQFASSPP
     LQLRYLPPIK AIFDLPESYP ASEPPRIEII TQPEWLPENI LQELKKECDE LWEEGMQTVY
     AVVDNIQQFT EGGFGGSKMV LPDELREEMV KFDQDAQREV FAKGTYDCGI CLEPKKGAQC
     HALRSCTHVF CKACLVDWYS GAITEGDVSA VRCSDPVCVK AATRQAAQLD APPTPPPEGV
     DAPAPPKPTI QPLPPTIPPE ELEEIGIPTD LVTRYVLLKK KKALEKDPHT IYCPRKWCQN
     PSKSSIERVE SNMKQNGGGY WLPDFNAVKE EPIKENNNGK EDTASVKLDK LQICSVCAFA
     FCRICRASWH GTLTICKPHD GTLTEEEIAN EKFLKENTTP CPTCNSPTLK SHGCNHMICA
     CTTHFCFLCS AYLDASNPYT HFNTRGTECY QRLWEGEEGD EENIRRIRAA EEQREQEMDN
     YEVVELAPAA AARPAQPAPV EPAPQQEEEI HEAQLIHPLG EEVVMDEDGI VWIDGQPFEV
     VWTDDEDSDA EPENQIAFED APDEELGPVA RRGGRGGAPA RGGGRGRGNA RGGQGGGRGG
     GRGGGQAARG GGRGGAQQAA ARGRGRGRP
//
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