ID A0A093XGA8_TALMA Unreviewed; 318 AA.
AC A0A093XGA8;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Protein PXR1 {ECO:0000256|ARBA:ARBA00040376};
DE AltName: Full=PinX1-related protein 1 {ECO:0000256|ARBA:ARBA00041961};
DE AltName: Full=Protein pxr1 {ECO:0000256|ARBA:ARBA00040137};
GN ORFNames=GQ26_0290090 {ECO:0000313|EMBL:KFX44253.1};
OS Talaromyces marneffei PM1.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=1077442 {ECO:0000313|EMBL:KFX44253.1, ECO:0000313|Proteomes:UP000029285};
RN [1] {ECO:0000313|Proteomes:UP000029285}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PM1 {ECO:0000313|Proteomes:UP000029285};
RX PubMed=25330172; DOI=10.1371/journal.pgen.1004662;
RA Yang E., Wang G., Cai J., Woo P.C., Lau S.K., Yuen K.-Y., Chow W.-N.,
RA Lin X.;
RT "Signature Gene Expression Reveals Novel Clues to the Molecular Mechanisms
RT of Dimorphic Transition in Penicillium marneffei.";
RL PLoS Genet. 10:e1004662-e1004662(2014).
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:KFX44253.1}.
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DR EMBL; JPOX01000029; KFX44253.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093XGA8; -.
DR eggNOG; KOG2809; Eukaryota.
DR HOGENOM; CLU_052839_0_0_1; -.
DR Proteomes; UP000029285; 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 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..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 148..296
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 148..181
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 191..207
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 219..241
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 267..283
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 318 AA; 35534 MW; 0192B09983E2789B CRC64;
MGLAAPRKRV KISHDPNNTT WAQSTSGFGH KIMTSQGWTP GSYLGARNAN HSDTFTAASA
SHIRVTLKDD TLGLGARAPT LGNDNVAAID AFQGLLGRLN GKSDVQLEQE QRKRDDTRLA
VYASQKWQAV TFISGGFLVQ EKPDDALRSK SKKKHDSPND AIVADKTSSD ESRDESADEI
PPQIGDKASV SKTEKASKDA EAKGMKEKRK RKKEKSDKKA KKNKEENEKK EKKDKKEKKK
EKKDSSRKRR RAEKDVESES SDSFSSDEAD NKSSQQDTAR SQAPRPNWRH AIRGRHIQQK
RMAIMDERSL GEIFMIKA
//
