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Database: UniProt
Entry: A0A0G2HZQ7_9PEZI
LinkDB: A0A0G2HZQ7_9PEZI
Original site: A0A0G2HZQ7_9PEZI 
ID   A0A0G2HZQ7_9PEZI        Unreviewed;       576 AA.
AC   A0A0G2HZQ7;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   SubName: Full=Putative pre-60s factor rei1 {ECO:0000313|EMBL:KKY33370.1};
GN   ORFNames=UCDDA912_g06593 {ECO:0000313|EMBL:KKY33370.1};
OS   Diaporthe ampelina.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Diaporthales; Diaporthaceae; Diaporthe.
OX   NCBI_TaxID=1214573 {ECO:0000313|EMBL:KKY33370.1, ECO:0000313|Proteomes:UP000034680};
RN   [1] {ECO:0000313|EMBL:KKY33370.1, ECO:0000313|Proteomes:UP000034680}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DA912 {ECO:0000313|EMBL:KKY33370.1};
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:KKY33370.1, ECO:0000313|Proteomes:UP000034680}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DA912 {ECO:0000313|EMBL:KKY33370.1};
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 REI1 family.
CC       {ECO:0000256|ARBA:ARBA00034126}.
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:KKY33370.1}.
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DR   EMBL; LCUC01000246; KKY33370.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G2HZQ7; -.
DR   STRING; 1214573.A0A0G2HZQ7; -.
DR   OrthoDB; 180831at2759; -.
DR   Proteomes; UP000034680; 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   Gene3D; 3.30.160.60; Classic Zinc Finger; 1.
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; 2.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022771};
KW   Reference proteome {ECO:0000313|Proteomes:UP000034680};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Ribosome biogenesis {ECO:0000256|ARBA:ARBA00022517};
KW   Zinc {ECO:0000256|ARBA:ARBA00022771};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT   DOMAIN          27..49
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS00028"
FT   DOMAIN          92..114
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS00028"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          172..225
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          334..389
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          409..434
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          520..553
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        183..225
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        530..553
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   576 AA;  64188 MW;  FB5F39099701D6C9 CRC64;
     MATVTGSRAA PPAPTAQDIS ASHPYTCNTC QVAFRNSDLQ KGHMRNDWHR YNLKRRVATL
     PPISSEVFTE KVLQARASTT AEAERAGFQT ECALCHKTYF SENSYQNHIG SQKHKAKAAA
     QLRKGRNDVA AADDASSMIS STFSLGEPVA SNTSEVDSDA EEEFSHIVEG MKKTGVSEQK
     RPSPVKRPSN PQILARTQNS EDDPVSEAST EQLSATPTPS KAADGAQATL SLNHCLFCNH
     ESPDVPLNVG HMEKTHGMFI PEKQYLVDIE GLLRSLQERI QEYHECLVCG KAKANAFAAQ
     THMRDTGHCK IPYTTEDEQL EIGEFYDFRS TYSDDEMEDD ESDDEESPQA GGVKLGGKRA
     AVTTNEDGEE IEEAEDAGWE TDSSASSLDS ADLTAVPAEN HYHQYERLEK HAHHSRSDSR
     PHRQRDGWHS HSHKPTRAVF YDEYELHLPS GRSVGHRSLN KYYRQNLRER PFLEGHQQHQ
     LALEDSDPDA MDVDGEEGNN GQQVVLSGLV RDQRRQLVGR GAEGGGGMLG VSDKKKKEVG
     KAAQRSRKVE HAHQKRNEWS VNKQANHQKH YHYSIL
//
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