ID B2WH31_PYRTR Unreviewed; 642 AA.
AC B2WH31;
DT 01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT 01-JUL-2008, sequence version 1.
DT 24-JAN-2024, entry version 65.
DE SubName: Full=Ankyrin repeat and zinc finger domain containing protein 1 {ECO:0000313|EMBL:EDU42341.1};
GN ORFNames=PTRG_09290 {ECO:0000313|EMBL:EDU42341.1};
OS Pyrenophora tritici-repentis (strain Pt-1C-BFP) (Wheat tan spot fungus)
OS (Drechslera tritici-repentis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC Pyrenophora.
OX NCBI_TaxID=426418 {ECO:0000313|EMBL:EDU42341.1, ECO:0000313|Proteomes:UP000001471};
RN [1] {ECO:0000313|Proteomes:UP000001471}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pt-1C-BFP {ECO:0000313|Proteomes:UP000001471};
RX PubMed=23316438; DOI=10.1534/g3.112.004044;
RA Manning V.A., Pandelova I., Dhillon B., Wilhelm L.J., Goodwin S.B.,
RA Berlin A.M., Figueroa M., Freitag M., Hane J.K., Henrissat B., Holman W.H.,
RA Kodira C.D., Martin J., Oliver R.P., Robbertse B., Schackwitz W.,
RA Schwartz D.C., Spatafora J.W., Turgeon B.G., Yandava C., Young S., Zhou S.,
RA Zeng Q., Grigoriev I.V., Ma L.-J., Ciuffetti L.M.;
RT "Comparative genomics of a plant-pathogenic fungus, Pyrenophora tritici-
RT repentis, reveals transduplication and the impact of repeat elements on
RT pathogenicity and population divergence.";
RL G3 (Bethesda) 3:41-63(2013).
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; DS231625; EDU42341.1; -; Genomic_DNA.
DR RefSeq; XP_001939622.1; XM_001939587.1.
DR AlphaFoldDB; B2WH31; -.
DR STRING; 426418.B2WH31; -.
DR EnsemblFungi; EDU42341; EDU42341; PTRG_09290.
DR GeneID; 6347580; -.
DR eggNOG; KOG2505; Eukaryota.
DR HOGENOM; CLU_014293_1_1_1; -.
DR InParanoid; B2WH31; -.
DR OMA; GPHIFMC; -.
DR OrthoDB; 8371at2759; -.
DR Proteomes; UP000001471; 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; PF00023; Ank; 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:UP000001471};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 61..83
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS00028"
FT REPEAT 471..504
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REGION 27..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 108..168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 280..306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 404..428
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 549..625
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..53
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 115..129
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 146..160
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 283..306
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 549..596
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 608..625
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 642 AA; 70533 MW; F42A2FD3F2FF3D37 CRC64;
MTEKGAHLLE RPLYVFDLPE ELLATLTLKD QAERPPQKEA PLESRKEVGD DDGAPAKATS
CNLCGLGFVT LADQRSHVRS DLHGYNLKQK IKGAKPVGEA EFEKLIGDLD ESISGSESSE
SDEEDEEDGS KPKDSTLSAL LKKQAKISDP EFDEFSSQKK QRGPGKPPLL WFTSPSIPEN
MSLGVYRAIF SNTEQEAESQ ILDTIRNKQL SPKQAPKIKA NEGGVPLPGT DIGPHYFLCM
IGGGHFAAMI VALAPKTGKK HTGVDERSTT VIAHKTFHRY TTRRKQGGSQ SANDNAKGNA
HSAGSSIRRY NESALVNEVR ELLSSWKSMI DTAELVFVRA TGATNRRTLF GPYEGQVLHQ
NDPRNRGFPF STRRATQKEL MRAFVELTRV KQSTIDEAAL AAMNNPEATR TTTTPAAKPK
PPKPTKEEEL ATLHTSQIIP LIKRSKVPAL LNYIKTNSVP STFTFLPANH HTPTPLHLAA
SLNSAPIVLA LLTKAGADPT LMNDDARTPF TLTGDRATRD AFRVARSELG ESAWDWEQAG
VPAAITKAEA DKRDAQEKSE KAAESKAEAD RRKAETERVR KESEAAEAKR NETRLGKGKT
LGAPVKTGAD LREEEMRGLT PEARARLERE RRALAAMRRM QQ
//
