ID A0A1Y2VD82_9PEZI Unreviewed; 661 AA.
AC A0A1Y2VD82;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 08-NOV-2023, entry version 19.
DE RecName: Full=C2H2-type domain-containing protein {ECO:0000259|PROSITE:PS00028};
DE Flags: Fragment;
GN ORFNames=M434DRAFT_47144 {ECO:0000313|EMBL:OTA95393.1};
OS Hypoxylon sp. CO27-5.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Hypoxylaceae; Hypoxylon.
OX NCBI_TaxID=1001938 {ECO:0000313|EMBL:OTA95393.1, ECO:0000313|Proteomes:UP000194361};
RN [1] {ECO:0000313|EMBL:OTA95393.1, ECO:0000313|Proteomes:UP000194361}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CO27-5 {ECO:0000313|EMBL:OTA95393.1,
RC ECO:0000313|Proteomes:UP000194361};
RX PubMed=28078400; DOI=10.1007/s00253-017-8091-1;
RA Wu W., Davis R.W., Tran-Gyamfi M.B., Kuo A., LaButti K., Mihaltcheva S.,
RA Hundley H., Chovatia M., Lindquist E., Barry K., Grigoriev I.V.,
RA Henrissat B., Gladden J.M.;
RT "Characterization of four endophytic fungi as potential consolidated
RT bioprocessing hosts for conversion of lignocellulose into advanced
RT biofuels.";
RL Appl. Microbiol. Biotechnol. 101:2603-2618(2017).
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the ANKZF1/VMS1 family.
CC {ECO:0000256|ARBA:ARBA00009262}.
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DR EMBL; KZ112443; OTA95393.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y2VD82; -.
DR STRING; 1001938.A0A1Y2VD82; -.
DR Proteomes; UP000194361; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR047139; ANKZ1/VMS1.
DR InterPro; IPR041175; VLRF1/Vms1.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR16036; ANKYRIN REPEAT AND ZINC FINGER DOMAIN-CONTAINING PROTEIN 1; 1.
DR PANTHER; PTHR16036:SF2; ANKYRIN REPEAT AND ZINC FINGER DOMAIN-CONTAINING PROTEIN 1; 1.
DR Pfam; PF13857; Ank_5; 1.
DR Pfam; PF18826; bVLRF1; 1.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
PE 3: Inferred from homology;
KW ANK repeat {ECO:0000256|ARBA:ARBA00023043, ECO:0000256|PROSITE-
KW ProRule:PRU00023}; Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Endonuclease {ECO:0000256|ARBA:ARBA00022759};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW Reference proteome {ECO:0000313|Proteomes:UP000194361};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 66..88
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS00028"
FT REPEAT 485..518
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REGION 29..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 116..177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 291..316
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 407..435
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 549..661
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 33..47
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 120..135
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 148..172
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 294..316
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 549..593
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 618..654
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 661
FT /evidence="ECO:0000313|EMBL:OTA95393.1"
SQ SEQUENCE 661 AA; 73778 MW; B96F42ACE88E6105 CRC64;
MEQKTEDLLR RPLYVYDLPD QVLNTLSLKQ DAVAEDQDPE KETAESITHT QDAPSSSPSV
VGSQSCSLCA LSFTSVQDQR SHLKSDLHHY NLKQKLRGRN PVSEIEFEKL IADLDESLSG
SESSESDEDE EDGDKESNLL TTLLRKQATL ADRKKNPDGN QEEHEEGNPR KRQRSGGAQP
LLWFSSPLLP PNNYFGIYRA IFSLEEAKDE STIVDTIKKK QLPPTPVPKP GPDGTFAAGA
YKGPHIFLCM IGGGHFAAMV VSLAPRQTKH GSVGPLNREA TVLAHKTFHR YTTRRKQGGS
QSANDNAKGN AHSAGSSIRR YNEQALTDEV RLLLQDWKGL LDTAELLFIR ATGSTNRRTL
FGPYEGQVLR ANDPRIRGFP FSTRRATQNE LMRSFIELTR LKVRVIDPSQ GTSKQEEAPT
EASTKPAKPA APKLTEEEET ALLHTSQLQA FIRRSKLPAL LSYLKNNNVS TDFLFQPPDV
AQNYHAPTPL HLAANQNSAP LVLGLLVKGG ADPTLKNREG KTAFELAGDR PTRDAFRVAR
DELGESKWDW EAAKVPPPLK KEEAEKRDER ERKENERKEA ERRRAEELRL GSEGPKVPDA
TGVNGKRGKS LLDAAGAKKT AQEKREEEVR GLTQEQRMKL ERERRARAAE ERFRRMQQAG
G
//
