ID A0A167LBL7_CALVF Unreviewed; 483 AA.
AC A0A167LBL7;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=C2H2-type domain-containing protein {ECO:0000259|PROSITE:PS00028};
GN ORFNames=CALVIDRAFT_482625 {ECO:0000313|EMBL:KZO95522.1};
OS Calocera viscosa (strain TUFC12733).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Dacrymycetes;
OC Dacrymycetales; Dacrymycetaceae; Calocera.
OX NCBI_TaxID=1330018 {ECO:0000313|EMBL:KZO95522.1, ECO:0000313|Proteomes:UP000076738};
RN [1] {ECO:0000313|EMBL:KZO95522.1, ECO:0000313|Proteomes:UP000076738}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TUFC12733 {ECO:0000313|EMBL:KZO95522.1,
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).
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the REI1 family.
CC {ECO:0000256|ARBA:ARBA00034126}.
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DR EMBL; KV417288; KZO95522.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A167LBL7; -.
DR STRING; 1330018.A0A167LBL7; -.
DR OrthoDB; 180831at2759; -.
DR Proteomes; UP000076738; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0042254; P:ribosome biogenesis; IEA:UniProtKB-KW.
DR InterPro; IPR003604; Matrin/U1-like-C_Znf_C2H2.
DR InterPro; IPR041661; ZN622/Rei1/Reh1_Znf-C2H2.
DR InterPro; IPR040025; Znf622/Rei1/Reh1.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR13182; ZINC FINGER PROTEIN 622; 1.
DR PANTHER; PTHR13182:SF8; ZINC FINGER PROTEIN 622; 1.
DR Pfam; PF12756; zf-C2H2_2; 1.
DR Pfam; PF12874; zf-met; 1.
DR SMART; SM00355; ZnF_C2H2; 4.
DR SMART; SM00451; ZnF_U1; 2.
DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 2.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Reference proteome {ECO:0000313|Proteomes:UP000076738};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Ribosome biogenesis {ECO:0000256|ARBA:ARBA00022517}.
FT DOMAIN 86..108
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS00028"
FT REGION 122..173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 301..366
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 311..349
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 483 AA; 53385 MW; 56F3513261F54E04 CRC64;
MAATVAPDTY AIHGPSGEPL FTCLSCSIAF LTAEDQRAHY RSDHHRYNMK RRVANLPPVS
ATIFNQKVLD RRAETAVTVS IKDTTCEICK KVYGSEGAFR AHMGSKKHRD NELQAAIALS
LKPKEEEKEV PQEVQSYQAT DEVPSAPEAA VSSTPAEPST SAPADVEMHS DDEVEQTLEQ
KLAAARTHLT SSSCLFCPVD SGSVQANLAH MSTAHSFFLP DSDYLSDVPG LLAYLGEKVA
IGNVCLYCNG RGRAFHSLDA VRKHMLDRGH TKLAYDTEAD RSELGDWYDF AKSYPKKSKS
SRKRTLIVEE QGEDEEDGDE DGQVDGEWED VEDDGEADEI VELSGSEDSS EESDDGRPQI
TFGDTPYELV LPSGARIGHR SLKRYYDQSF SFRAPAKPSD PNSGAALVRR LLDDKNNQLV
PMKGGFGAFG EGTAVVKARN VGEAREAGRH VREFRDMKRR EEFKTKVGFR GNAQKHYRDP
LLQ
//
