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Database: UniProt
Entry: A0A167LR85_CALVF
LinkDB: A0A167LR85_CALVF
Original site: A0A167LR85_CALVF 
ID   A0A167LR85_CALVF        Unreviewed;       646 AA.
AC   A0A167LR85;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=C3H1-type domain-containing protein {ECO:0000259|PROSITE:PS50103};
GN   ORFNames=CALVIDRAFT_143294 {ECO:0000313|EMBL:KZO95948.1};
OS   Calocera viscosa (strain TUFC12733).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Dacrymycetes;
OC   Dacrymycetales; Dacrymycetaceae; Calocera.
OX   NCBI_TaxID=1330018 {ECO:0000313|EMBL:KZO95948.1, ECO:0000313|Proteomes:UP000076738};
RN   [1] {ECO:0000313|EMBL:KZO95948.1, ECO:0000313|Proteomes:UP000076738}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TUFC12733 {ECO:0000313|EMBL:KZO95948.1,
RC   ECO:0000313|Proteomes:UP000076738};
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; KV417286; KZO95948.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A167LR85; -.
DR   STRING; 1330018.A0A167LR85; -.
DR   OrthoDB; 179786at2759; -.
DR   Proteomes; UP000076738; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR   Gene3D; 4.10.1000.10; Zinc finger, CCCH-type; 1.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR041367; Znf-CCCH_4.
DR   InterPro; IPR000571; Znf_CCCH.
DR   PANTHER; PTHR24171; ANKYRIN REPEAT DOMAIN-CONTAINING PROTEIN 39-RELATED; 1.
DR   PANTHER; PTHR24171:SF8; ANKYRIN REPEAT DOMAIN-CONTAINING PROTEIN 39-RELATED; 1.
DR   Pfam; PF12796; Ank_2; 1.
DR   Pfam; PF14608; zf-CCCH_2; 1.
DR   Pfam; PF18044; zf-CCCH_4; 1.
DR   SMART; SM00248; ANK; 2.
DR   SMART; SM00356; ZnF_C3H1; 2.
DR   SUPFAM; SSF48403; Ankyrin repeat; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 1.
DR   PROSITE; PS50103; ZF_C3H1; 2.
PE   4: Predicted;
KW   ANK repeat {ECO:0000256|ARBA:ARBA00023043, ECO:0000256|PROSITE-
KW   ProRule:PRU00023}; Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076738};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00723};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00723}.
FT   REPEAT          35..67
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   DOMAIN          178..203
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50103"
FT   DOMAIN          430..457
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50103"
FT   ZN_FING         178..203
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT   ZN_FING         430..457
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT   REGION          141..176
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          260..285
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          327..378
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          408..431
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          455..608
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          626..646
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        141..155
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        346..365
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        500..516
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        527..547
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        585..603
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   646 AA;  67994 MW;  66037EDAA177B3CA CRC64;
     MVSPLWRAAS EGELEKVQEL LREASSVDVE IKDHTGATPL IQAIRNGHVE VVRVLVDHGA
     DPNNNSAQGR PDSYTEDATI LELLAAARGK LETSAPPAPV PSVPTNYMNY EQISYAAYPQ
     AYYPEGLVPA PYPPYPYMYR PDMMVPPPPP EQQQQQQPSQ SPVQRSENGS AGLPPPEIAK
     TIPCRFYPAC RYGSQCLFAH PDTAPAAQPA PAPAPGPNYG YPMPPVAYSY ASPPYDPSGM
     SYGPYYMTAP GMPGYPMGPM ASPPFPPQPG GPHQRSGSDV HSPLSATFSP VANPVMTGMW
     QVGVPPPISP YTHASVGQAV PMSPVEANHG LAGASPHPMA PPSPTTFYSP ANDVTIPTAP
     ASHRRSFSTP RALDFPGQPE MQDGMNGMNG MNGMNGMNGS ENHITNTYFR GSTRGRGGRR
     TSYLGGQRQP PSNVPCLFFP TGKCKNGDSC RFAHIMPGPD DPPPLHPRAA RPRASANDLD
     KQASFPTIHE PPNAPNGHVY PRNGSGNGSS PSSQGGGFDK LRAVGNGKQG AQTTGSSRSS
     SAAPINRQRI PNADDFPALG GAGAAPNGVK PIVGPTAAQV LQAPAPAPRS SSQARTSSEA
     GSDKAVRTID EVAEVTNKLE SVKIEGVPSS LPRAPTPARE SDAVFA
//
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