ID U1HM85_ENDPU Unreviewed; 740 AA.
AC U1HM85;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=RING finger protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=EPUS_00296 {ECO:0000313|EMBL:ERF70109.1};
OS Endocarpon pusillum (strain Z07020 / HMAS-L-300199) (Lichen-forming
OS fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Verrucariales; Verrucariaceae; Endocarpon.
OX NCBI_TaxID=1263415 {ECO:0000313|EMBL:ERF70109.1, ECO:0000313|Proteomes:UP000019373};
RN [1] {ECO:0000313|Proteomes:UP000019373}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Z07020 / HMAS-L-300199 {ECO:0000313|Proteomes:UP000019373};
RX PubMed=24438332; DOI=10.1186/1471-2164-15-34;
RA Wang Y.-Y., Liu B., Zhang X.-Y., Zhou Q.-M., Zhang T., Li H., Yu Y.-F.,
RA Zhang X.-L., Hao X.-Y., Wang M., Wang L., Wei J.-C.;
RT "Genome characteristics reveal the impact of lichenization on lichen-
RT forming fungus Endocarpon pusillum Hedwig (Verrucariales, Ascomycota).";
RL BMC Genomics 15:34-34(2014).
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DR EMBL; KE721353; ERF70109.1; -; Genomic_DNA.
DR RefSeq; XP_007804144.1; XM_007805953.1.
DR AlphaFoldDB; U1HM85; -.
DR GeneID; 19235359; -.
DR eggNOG; KOG1814; Eukaryota.
DR HOGENOM; CLU_021364_3_0_1; -.
DR OMA; CFRCNTH; -.
DR OrthoDB; 3084186at2759; -.
DR Proteomes; UP000019373; 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 CDD; cd23134; RING-HC_ITT1-like; 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 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 Reference proteome {ECO:0000313|Proteomes:UP000019373};
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 14..170
FT /note="RWD"
FT /evidence="ECO:0000259|PROSITE:PS50908"
FT DOMAIN 206..487
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT DOMAIN 210..244
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 264..293
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 341..374
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 509..548
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 595..695
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 514..533
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 534..548
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 603..617
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 740 AA; 83326 MW; FAF63A796F51C225 CRC64;
MEDDPGAADD ERIIELSSIA AIFPEIVLDR NSPYQASLDI SVSPAAPLKI CFQHLTETSL
LNLPTPPTST EPDTEDLDAA LKDGPRQKNQ GTAAVHELVH LPSLNLKICL PEGYPAETAP
VFELSSCPAW IPETTLQRLT RDGVRLWEEL GRDQVIFTYI DHLQQAAEAG FDLAKDLGRE
FTLSGELEIA LLDYDLKSKR EVFEKETFDC GICLEPKKGA VCHRLLLCSH VFCVECLQEC
YKKCIAEGDV DNVKCLDPGC GKDTNPLPPN EQAHQGRTAA RRRRRQDPTL SPSELLQIPL
AEEVVQRYVH LKRKKKLESD KNTVYCPRQW CQGAARSKKY PKPIDPMHDA ADVTSDSDED
PQDTSNKGSK ESKTQEIPMS ERLCICEDCS YAFCSVCKKG WHGELTSYSL CNPRSEKELT
EEEKATAEYL ALHSTPCPTC SAPCQKTMGC NHMICFKCRT HFCYLCSSYL MESNPYQHFN
DKHNQCYMRL WELEDGDDEN AQVVAWDIPP DGLAFDSDSD DDDLSDDDDD ERDINWFERN
PLRRDDDDAA HFSDEEEIGQ EPVQRGRERL AAPADFPIKV RLHRHQLHHA LAAEHANRGG
QPLPQPRNRN PNQNQARGRG RGRGGGRAPP PPRAAAPEPA RERRFPIHPA PPSENESDSS
DTEDEVPIRF PRGAAPAPAP GQGNDGQQQP AMLRHMGIDR FLALAEQDQE DEWDSDELEE
EVLDVVEERR RRAANRRIWG
//
