ID A0A165JAY2_9BASI Unreviewed; 651 AA.
AC A0A165JAY2;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 28-JUN-2023, entry version 20.
DE RecName: Full=CCHC-type domain-containing protein {ECO:0000259|SMART:SM00343};
GN ORFNames=CALCODRAFT_491153 {ECO:0000313|EMBL:KZT61603.1};
OS Calocera cornea HHB12733.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Dacrymycetes;
OC Dacrymycetales; Dacrymycetaceae; Calocera.
OX NCBI_TaxID=1353952 {ECO:0000313|EMBL:KZT61603.1, ECO:0000313|Proteomes:UP000076842};
RN [1] {ECO:0000313|EMBL:KZT61603.1, ECO:0000313|Proteomes:UP000076842}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB12733 {ECO:0000313|EMBL:KZT61603.1,
RC ECO:0000313|Proteomes:UP000076842};
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).
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KV423922; KZT61603.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165JAY2; -.
DR STRING; 1353952.A0A165JAY2; -.
DR InParanoid; A0A165JAY2; -.
DR OrthoDB; 379273at2759; -.
DR Proteomes; UP000076842; 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; 4.10.60.10; Zinc finger, CCHC-type; 1.
DR InterPro; IPR040194; Cwf19-like.
DR InterPro; IPR006768; Cwf19-like_C_dom-1.
DR InterPro; IPR006767; Cwf19-like_C_dom-2.
DR InterPro; IPR036265; HIT-like_sf.
DR InterPro; IPR025829; Zn_knuckle_CX2CX3GHX4C.
DR InterPro; IPR001878; Znf_CCHC.
DR PANTHER; PTHR12072; CWF19, CELL CYCLE CONTROL PROTEIN; 1.
DR PANTHER; PTHR12072:SF4; CWF19-LIKE PROTEIN 1; 1.
DR Pfam; PF04677; CwfJ_C_1; 1.
DR Pfam; PF04676; CwfJ_C_2; 1.
DR Pfam; PF13696; zf-CCHC_2; 1.
DR SMART; SM00343; ZnF_C2HC; 3.
DR SUPFAM; SSF54197; HIT-like; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000076842};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 316..332
FT /note="CCHC-type"
FT /evidence="ECO:0000259|SMART:SM00343"
FT DOMAIN 354..371
FT /note="CCHC-type"
FT /evidence="ECO:0000259|SMART:SM00343"
FT DOMAIN 388..404
FT /note="CCHC-type"
FT /evidence="ECO:0000259|SMART:SM00343"
FT REGION 233..267
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 651 AA; 70633 MW; 75E762B7B9B1BFEB CRC64;
MADAAKILVL GSAHGALPSY LTKLRTFNAK HGPFDAVFCI GDFFSPPSFG VSVENEGLSD
LLEGKLEVTA PTFVLSSPNV EVPREVRERV DGEGGEICKN LALLEGIGRI DIPGKGVHVS
YDSSTTPLNI ADLEPHATTH ILLTHAHPSL VFPSLPTATS SENDADLLLK HRRPRYAFSG
ASGVWSEAQP FGWEEEGATE WTRCVSVGSV RGEGGKKQRF YYAFSLNPLQ VPPNPPNAVP
NPYLPTAAKA PLPSQEHNDQ PPQLKDLNGA ASANKRKFEA IAAAEAGNAD YRWGGEGKKA
RKERTDLSGK PPDGYRCRIC DSSDHYVQSC PDKLELDKSR AEARENDKPP EGYTCRRCGA
TADHFVKNCP KRAELGDTGG ALPSEGYVCR ACGSGKHYFK DCEVAAKGRN RGGGRGGKKE
IAPDECWFCL SNPNITKYLI TSIGSETYLT LPKGSLLPLS SQSPTHIPGG GHLLLIPITH
HPTLLSLPPD ISLPITAELE SYKSGLRALF KAHGCAAVSW EIARLSGRGG HAHMQVCAVP
LKLVEEGKVE EAFRREGEQG GVDWEEEMPG DAGREREGNY LRIELPGGKV LVHNIRPGPP
FNLQFPRMVL GRLLGLEDRI DWRTCPEGED EEREAAEAFK AAFAEYDPTL A
//
