ID A0A166TCB3_9AGAM Unreviewed; 545 AA.
AC A0A166TCB3;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=RING-type domain-containing protein {ECO:0000259|PROSITE:PS50089};
GN ORFNames=FIBSPDRAFT_814735 {ECO:0000313|EMBL:KZP30460.1};
OS Fibularhizoctonia sp. CBS 109695.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Atheliales; Atheliaceae; Fibularhizoctonia.
OX NCBI_TaxID=436010 {ECO:0000313|EMBL:KZP30460.1, ECO:0000313|Proteomes:UP000076532};
RN [1] {ECO:0000313|EMBL:KZP30460.1, ECO:0000313|Proteomes:UP000076532}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 109695 {ECO:0000313|EMBL:KZP30460.1,
RC ECO:0000313|Proteomes:UP000076532};
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; KV417493; KZP30460.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A166TCB3; -.
DR STRING; 436010.A0A166TCB3; -.
DR OrthoDB; 4593171at2759; -.
DR Proteomes; UP000076532; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR CDD; cd16449; RING-HC; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR047126; RNF141-like.
DR InterPro; IPR027370; Znf-RING_euk.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR12109:SF3; RING FINGER PROTEIN 141; 1.
DR PANTHER; PTHR12109; RING FINGER PROTEIN 141-RELATED; 1.
DR Pfam; PF13445; zf-RING_UBOX; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57850; RING/U-box; 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:UP000076532};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 254..313
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 340..391
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 175..202
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..35
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..91
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 97..114
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 115..136
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 137..167
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 359..391
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 545 AA; 61052 MW; 4CEFF111C6CC2629 CRC64;
MSFAPLPNTA RRNNTTRRAL IPQDNPTNTL VSTASGVPLP LPPGTSGGVR RKKSRSPSAR
PRADFSAITT ALGKKRKSTA PSSSGSGNFL FSARQDDMPV DRGRTPKLKS KTQSRHALEN
SSAMAVTSQQ QALGSRPSKK ERSKSRESKE RARKHTSEVD SDKEMVEPGG RNSQTVALSA
ELSKIKKELE VAKRQAHENK RTISKQSKVI DELRQKLTAG DKAMKENESQ LVKLKTKSKK
ADDTIASIEG HINCQICMEV LLKPFVLSPC GHVLCQGCLQ EWFRKAPASE DDMYESDDPD
YLVYRLKSCP CCRANVRERP LPLFILKGIA AAILKSKSVP HVSPPPEGDP WEGLFPPVGE
DFGEDDDEDG LEDDDDDEDE EDEEDEEDYN EWLTSVFAYG SDSDEEPYEG EYVSPQWEPP
SVTIDPAEYE YEDLSPGDLS VLRRGATLDM LDTFNMTYAH AEGLVAHLEE EKVHLGWNIR
LSADDETGED FIEYLYNDMN DRPERWDIME AENGTKICHR LIPEDELEEH DTTDSELWVD
NNDVD
//
