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Database: UniProt
Entry: A0A094EGW9_9PEZI
LinkDB: A0A094EGW9_9PEZI
Original site: A0A094EGW9_9PEZI 
ID   A0A094EGW9_9PEZI        Unreviewed;       374 AA.
AC   A0A094EGW9;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=PinX1-related protein 1 {ECO:0000256|ARBA:ARBA00041961};
GN   ORFNames=V499_04324 {ECO:0000313|EMBL:KFY75698.1};
OS   Pseudogymnoascus sp. VKM F-103.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX   NCBI_TaxID=1420912 {ECO:0000313|EMBL:KFY75698.1, ECO:0000313|Proteomes:UP000029295};
RN   [1] {ECO:0000313|EMBL:KFY75698.1, ECO:0000313|Proteomes:UP000029295}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VKM F-103 {ECO:0000313|EMBL:KFY75698.1,
RC   ECO:0000313|Proteomes:UP000029295};
RA   Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA   Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA   Ozerskaya S.M.;
RT   "Population genomics of a fungus Geomyces pannorum provides evidence of
RT   horizontal gene transfer but not of sexual reproduction.";
RL   Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in rRNA-processing at A0, A1 and A2 sites and
CC       negatively regulates telomerase. {ECO:0000256|ARBA:ARBA00043878}.
CC   -!- SIMILARITY: Belongs to the PINX1 family.
CC       {ECO:0000256|ARBA:ARBA00038007}.
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:KFY75698.1}.
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DR   EMBL; JPKB01000644; KFY75698.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A094EGW9; -.
DR   HOGENOM; CLU_052839_0_0_1; -.
DR   Proteomes; UP000029295; Unassembled WGS sequence.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   InterPro; IPR000467; G_patch_dom.
DR   PANTHER; PTHR23149; G PATCH DOMAIN CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR23149:SF31; PROTEIN PXR1; 1.
DR   Pfam; PF01585; G-patch; 1.
DR   SMART; SM00443; G_patch; 1.
DR   PROSITE; PS50174; G_PATCH; 1.
PE   3: Inferred from homology;
FT   DOMAIN          25..79
FT                   /note="G-patch"
FT                   /evidence="ECO:0000259|PROSITE:PS50174"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          158..331
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        158..182
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        183..266
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        267..285
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   374 AA;  41107 MW;  06C58E848175E19D CRC64;
     MGLAEPRKRL KLSKDPNNTT WTKDTTGFGH KIMKSQGWTP GEYLGIKDAP HAEFHTEANA
     SHIRVVLKDD NLGIGAKKGS GLEQGECVGL DVFQNLLGRL NGRDEDEMER EQKSREDLKR
     AIYSERKWGS IRFVSGGFLI GDKIQDLIDG EADRLRQLAV DSSSSGSEDS SDSGSDSDSD
     TTPEPVVMKE KKSKKSKKSS KEIEVEVSEA SVDSENGKSK SKKKRKLADV EEDGGVSIVD
     KTKKSKKSKK SESEEDASES KDRKSKSKKD KKEKKDKKDK KDKKKKSKSK SSEDSLDSDS
     AVTSKSSKSK SKSKKSKSEK TASDSSDTTP VVVEISSRPI LLGGRHAVRS RNIAQKRLAA
     MNSASLNEIF MIKG
//
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