ID A0A165XN65_9AGAM Unreviewed; 411 AA.
AC A0A165XN65;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=CCHC-type domain-containing protein {ECO:0000259|PROSITE:PS50158};
GN ORFNames=FIBSPDRAFT_922625 {ECO:0000313|EMBL:KZP08723.1};
OS Fibularhizoctonia sp. CBS 109695.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Atheliales; Atheliaceae; Fibularhizoctonia.
OX NCBI_TaxID=436010 {ECO:0000313|EMBL:KZP08723.1, ECO:0000313|Proteomes:UP000076532};
RN [1] {ECO:0000313|EMBL:KZP08723.1, ECO:0000313|Proteomes:UP000076532}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 109695 {ECO:0000313|EMBL:KZP08723.1,
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; KV417715; KZP08723.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165XN65; -.
DR STRING; 436010.A0A165XN65; -.
DR OrthoDB; 7504at2759; -.
DR Proteomes; UP000076532; Unassembled WGS sequence.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR008554; Glutaredoxin-like.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR001878; Znf_CCHC.
DR PANTHER; PTHR13316:SF0; ZINC FINGER CCHC DOMAIN-CONTAINING PROTEIN 8; 1.
DR PANTHER; PTHR13316; ZINC FINGER, CCHC DOMAIN CONTAINING 8; 1.
DR Pfam; PF05768; Glrx-like; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS50158; ZF_CCHC; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00047};
KW Reference proteome {ECO:0000313|Proteomes:UP000076532};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00047};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00047}.
FT DOMAIN 131..147
FT /note="CCHC-type"
FT /evidence="ECO:0000259|PROSITE:PS50158"
FT REGION 268..296
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 319..411
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 268..289
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 345..386
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 411 AA; 45984 MW; B29C2AB410B9B618 CRC64;
MASGLARIAR LTLFSGPNCS LCDIAKAELA KVRQSRSFEL NTINIQDQGQ EKWKKKYVYW
IPALHLEGRE IAKGRWDAQT VIQALDEWES KKGQEETINP WDCSPLYERD VPDILGESPA
AGLQEAHQDP RRCFNCGDPS HAVSQCPTPA NHALIALSRQ MFVFSQSAHR QALGDLERVH
VVEGRRHQRL DWLDDFEPGE VRGDALREAL GTAGETEWLR NMALWGYPKG WTGTRDPRYE
VMKRIEEEPE YEDEDPFLIF GDKGEEEEIE LHPPRKQSPE REHATEEVPS SPKPTKLEAD
IHRWASYPTT YFSSALLPLY NGYALPPPPS ETFSRERQAL WEKITSVPPP PPPGAPPPPP
PTSSPPPLPP SGPPPPQPPP PSSPLAQAVP QLGSESLDSD SEADMDLSDE D
//
