ID A0A165I552_9APHY Unreviewed; 656 AA.
AC A0A165I552;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=RING-type domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=LAESUDRAFT_739975 {ECO:0000313|EMBL:KZT12603.1};
OS Laetiporus sulphureus 93-53.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Laetiporus.
OX NCBI_TaxID=1314785 {ECO:0000313|EMBL:KZT12603.1, ECO:0000313|Proteomes:UP000076871};
RN [1] {ECO:0000313|EMBL:KZT12603.1, ECO:0000313|Proteomes:UP000076871}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=93-53 {ECO:0000313|EMBL:KZT12603.1,
RC ECO:0000313|Proteomes:UP000076871};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
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DR EMBL; KV427605; KZT12603.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165I552; -.
DR STRING; 1314785.A0A165I552; -.
DR InParanoid; A0A165I552; -.
DR OrthoDB; 379257at2759; -.
DR Proteomes; UP000076871; 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; cd22584; Rcat_RBR_unk; 1.
DR CDD; cd16449; RING-HC; 1.
DR Gene3D; 1.20.120.1750; -; 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; IPR044066; TRIAD_supradom.
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; PF13639; zf-RING_2; 1.
DR SMART; SM00184; RING; 2.
DR SUPFAM; SSF57850; RING/U-box; 2.
DR PROSITE; PS51873; TRIAD; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000076871};
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 434..650
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT DOMAIN 438..485
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 327..379
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 265..292
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 358..377
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 656 AA; 73094 MW; 64F388FDCF9416D2 CRC64;
MARGDVVKTP DVPEMIMAGS MGEVVVSHAG RSQYSRIGGG VSACGLAALN CARVILDMER
TGLRNENIIR EIMKRETLEE VLRPCLSWSR PAHLDVEEIY KAPVFNKSLK LVMFAYEHSG
LGEFTQILSH LSNHTRDTRS STCAIITRPP EIVACVKLAT NKSDVFVIFD SHPRPQKHPN
GAAFIFQPSV VAAASYLAEL FSYDDRLLMD SSVQWQAQLL AHFSAHIFTA RDTMGTTAEL
AEAVLEASLE VLNLRARVLE LESHAGDLEV ENTQLSEDVT RLEDDIMELK AKNLRNDSRL
RKSEGAANGE LIPPAAHCTN NLSSISEKVR GKMPAIPTER ASQSSPRSYG LNDRSAKPWN
GGSRQASSRT GLNCSSSDEP MDMDDFTVAA ILLTQADQLK DADAMYAAEQ QRKFDEEDHY
LKRQMHDLKY TALDVFECGI CFDQFNRDVV AEVEPCGHRF CRECARNYAV SKVEGHRYPI
PCPLCMGDKA RKDPGAIDDS LIQQLGLSEK QYAIFVEMQM AAFSIILHCR KCENSVFVDK
QEYEAAKILV CPLQGCNYAW CKACSQKIEI GGPQHSCDGS AELKHLMDQK GWKYCPGCQT
PAEKIDGCNH MTCMSPGCNT HFCYGCGEAI TQSIRRQEIH SDLSAHYRRC RLFDYT
//
