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Database: UniProt
Entry: A0A0G2FYL4_9PEZI
LinkDB: A0A0G2FYL4_9PEZI
Original site: A0A0G2FYL4_9PEZI 
ID   A0A0G2FYL4_9PEZI        Unreviewed;       651 AA.
AC   A0A0G2FYL4;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   08-NOV-2023, entry version 25.
DE   SubName: Full=Putative ankyrin repeat-containing protein {ECO:0000313|EMBL:KKY39242.1};
GN   ORFNames=UCDDA912_g00720 {ECO:0000313|EMBL:KKY39242.1};
OS   Diaporthe ampelina.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Diaporthales; Diaporthaceae; Diaporthe.
OX   NCBI_TaxID=1214573 {ECO:0000313|EMBL:KKY39242.1, ECO:0000313|Proteomes:UP000034680};
RN   [1] {ECO:0000313|EMBL:KKY39242.1, ECO:0000313|Proteomes:UP000034680}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DA912 {ECO:0000313|EMBL:KKY39242.1};
RA   Lawrence D.P., Travadon R., Rolshausen P.E., Baumgartner K.;
RT   "Distinctive expansion of gene families associated with plant cell wall
RT   degradation and secondary metabolism in the genomes of grapevine trunk
RT   pathogens.";
RL   Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KKY39242.1, ECO:0000313|Proteomes:UP000034680}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DA912 {ECO:0000313|EMBL:KKY39242.1};
RA   Morales-Cruz A., Amrine K.C., Cantu D.;
RL   Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the ANKZF1/VMS1 family.
CC       {ECO:0000256|ARBA:ARBA00009262}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KKY39242.1}.
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DR   EMBL; LCUC01000024; KKY39242.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G2FYL4; -.
DR   STRING; 1214573.A0A0G2FYL4; -.
DR   OrthoDB; 8371at2759; -.
DR   Proteomes; UP000034680; 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; 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:UP000034680};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          67..89
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS00028"
FT   REPEAT          480..513
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REGION          32..59
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          114..177
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          287..312
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          410..433
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          544..651
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        119..133
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        150..171
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        290..307
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        412..426
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        550..593
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        608..645
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   651 AA;  72272 MW;  034FBC4C5966F0B4 CRC64;
     MATDPKRQDD LLRRPLYVYD LPPEVLATLN LKLDTEAQEQ PGPDTPSEPV PEQSQAPSEI
     AVGSLACSLC GLTFTTVLDQ RGHQKSDLHN YNLKQKLRGQ KPVSEVEFEK LVGDLDESLS
     GSDSEDSDED EDDSKKDSTL TALLKKQATL AEKRTGDNGD DESEWGRGKR KGTGKPPMMW
     FSSPVLPENN YFGIYRALFT SEELEKEDSI LEAVKKRQLQ PLAAPKASKD GSQLPAVYKG
     PHIFLCMIGG GHFAAMVVSL SPRQTKSGSG PMNREATVLA HKTFHRYTTR RKQGGSQSAN
     DNAKGAAHSA GSSLRRYNEQ ALVDDVRQLL TDWKGLLDTA DLLFIRATGV TNRRTLYGPY
     DGQILRANDP RVRGFPFSTR RATQNELMRS FIELTRLKVR ELLPVDPNAA TEAATKPQTA
     SKPSKQAPPK LTEEEETALL HTQQIQALIR RSKLPALLSY IKTNSLEANF RFQPADVNHH
     APTPLHMAAA QNAAALIVGL LTRGGADPTL PNGEGKTPFE LVGDRATRDS FRVARHELGE
     GAWDWEAAKV PPGMKKEEAD QRGERERKEA ERKEAERRRA EEERLKTQGP KVVDSAKRKG
     GGVLRGSVEK SAEEKRQEEA MGLTPEQRMR LDRERRARAA EERLRRMQAG S
//
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