ID M5FQU3_DACPD Unreviewed; 435 AA.
AC M5FQU3;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 44.
DE RecName: Full=RING-type domain-containing protein {ECO:0000259|PROSITE:PS51873};
DE Flags: Fragment;
GN ORFNames=DACRYDRAFT_72456 {ECO:0000313|EMBL:EJT97149.1};
OS Dacryopinax primogenitus (strain DJM 731) (Brown rot fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Dacrymycetes;
OC Dacrymycetales; Dacrymycetaceae; Dacryopinax.
OX NCBI_TaxID=1858805 {ECO:0000313|EMBL:EJT97149.1, ECO:0000313|Proteomes:UP000030653};
RN [1] {ECO:0000313|EMBL:EJT97149.1, ECO:0000313|Proteomes:UP000030653}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DJM-731 SS1 {ECO:0000313|EMBL:EJT97149.1,
RC ECO:0000313|Proteomes:UP000030653};
RX PubMed=22745431; DOI=10.1126/science.1221748;
RA Floudas D., Binder M., Riley R., Barry K., Blanchette R.A., Henrissat B.,
RA Martinez A.T., Otillar R., Spatafora J.W., Yadav J.S., Aerts A., Benoit I.,
RA Boyd A., Carlson A., Copeland A., Coutinho P.M., de Vries R.P.,
RA Ferreira P., Findley K., Foster B., Gaskell J., Glotzer D., Gorecki P.,
RA Heitman J., Hesse C., Hori C., Igarashi K., Jurgens J.A., Kallen N.,
RA Kersten P., Kohler A., Kuees U., Kumar T.K.A., Kuo A., LaButti K.,
RA Larrondo L.F., Lindquist E., Ling A., Lombard V., Lucas S., Lundell T.,
RA Martin R., McLaughlin D.J., Morgenstern I., Morin E., Murat C., Nagy L.G.,
RA Nolan M., Ohm R.A., Patyshakuliyeva A., Rokas A., Ruiz-Duenas F.J.,
RA Sabat G., Salamov A., Samejima M., Schmutz J., Slot J.C., St John F.,
RA Stenlid J., Sun H., Sun S., Syed K., Tsang A., Wiebenga A., Young D.,
RA Pisabarro A., Eastwood D.C., Martin F., Cullen D., Grigoriev I.V.,
RA Hibbett D.S.;
RT "The Paleozoic origin of enzymatic lignin decomposition reconstructed from
RT 31 fungal genomes.";
RL Science 336:1715-1719(2012).
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
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DR EMBL; JH795878; EJT97149.1; -; Genomic_DNA.
DR AlphaFoldDB; M5FQU3; -.
DR STRING; 1858805.M5FQU3; -.
DR HOGENOM; CLU_009961_0_0_1; -.
DR OMA; QCEREEC; -.
DR OrthoDB; 3354811at2759; -.
DR Proteomes; UP000030653; Unassembled WGS sequence.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd20339; BRcat_RBR_RNF216; 1.
DR CDD; cd20353; Rcat_RBR_RNF216; 1.
DR CDD; cd16630; RING-HC_RBR_RNF216; 1.
DR Gene3D; 1.20.120.1750; -; 1.
DR InterPro; IPR047545; BRcat_RBR_RNF216.
DR InterPro; IPR002867; IBR_dom.
DR InterPro; IPR047546; Rcat_RBR_RNF216.
DR InterPro; IPR047544; RING-HC_RBR_RNF216.
DR InterPro; IPR044066; TRIAD_supradom.
DR PANTHER; PTHR22770:SF47; E3 UBIQUITIN-PROTEIN LIGASE RNF216; 1.
DR PANTHER; PTHR22770; UBIQUITIN CONJUGATING ENZYME 7 INTERACTING PROTEIN-RELATED; 1.
DR Pfam; PF01485; IBR; 1.
DR SUPFAM; SSF57850; RING/U-box; 2.
DR PROSITE; PS51873; TRIAD; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000030653};
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}.
FT DOMAIN 85..297
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT REGION 23..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 350..371
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 351..366
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EJT97149.1"
SQ SEQUENCE 435 AA; 49151 MW; F08E6364CAFA5A07 CRC64;
MEQCNFFYAP THLRLLRESQ SEALPYTPKG RPTPSKIKGK GKATFDPDFE SEREWLLLKI
GADKLKADEE LAEKLNEEEY VANGEGLECG CCFGEYAFDK MVQCAEGHLF CRDCARRQAE
ERLGLRQTDL LCMDQSDCNA PFPETEIARF LTEKSLNLYH RIKQGKEIEK AGLVGLESCP
FCDYACVIEN DEEKLFRCEN EECLVISCRK CKKTDHLPKT CKEAEDDLRL NARHMVEEAM
SNALMRKCPK CHHPFVKEGG CNKMTCNQCR TLSCYRCRRV IQGYDHFSER PGQPRYGEAG
AVRDPSKCPL WDIDLEKLHA DEVTAAARKA QEEILSTDDN IQIVKQDLEV DLPKPPPPPP
GPGPGQPGYN GGVLPAEFME HVLPMPIPQA LPIVVPPPIH HAPFPAQHQY HYHAIVQYAP
MHAVAVIHQG IQPII
//
