ID A0A093XM03_TALMA Unreviewed; 364 AA.
AC A0A093XM03;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 22-FEB-2023, entry version 27.
DE SubName: Full=Phosducin-like protein {ECO:0000313|EMBL:KFX46263.1};
DE Flags: Fragment;
GN ORFNames=GQ26_0190340 {ECO:0000313|EMBL:KFX46263.1};
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:KFX46263.1, ECO:0000313|Proteomes:UP000029285};
RN [1] {ECO:0000313|EMBL:KFX46263.1, ECO:0000313|Proteomes:UP000029285}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PM1 {ECO:0000313|EMBL:KFX46263.1,
RC 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 -!- SIMILARITY: Belongs to the phosducin family.
CC {ECO:0000256|ARBA:ARBA00009686}.
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:KFX46263.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JPOX01000019; KFX46263.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093XM03; -.
DR eggNOG; KOG3171; Eukaryota.
DR HOGENOM; CLU_053880_0_0_1; -.
DR Proteomes; UP000029285; Unassembled WGS sequence.
DR GO; GO:0008277; P:regulation of G protein-coupled receptor signaling pathway; IEA:InterPro.
DR CDD; cd02987; Phd_like_Phd; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR001200; Phosducin.
DR InterPro; IPR024253; Phosducin_thioredoxin-like_dom.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR46052; PHOSDUCIN-LIKE PROTEIN; 1.
DR PANTHER; PTHR46052:SF1; PHOSDUCIN-LIKE PROTEIN; 1.
DR Pfam; PF02114; Phosducin; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
PE 3: Inferred from homology;
FT DOMAIN 158..343
FT /note="Phosducin thioredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF02114"
FT REGION 91..139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 193..224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..105
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 106..120
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 195..218
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFX46263.1"
SQ SEQUENCE 364 AA; 40687 MW; 70662383C01C657F CRC64;
PTIHSLGGPQ QLVTPNSLSE SRSKFLLSFP LHSSQVTYLP DYVAHTLAAH SYKRILTPPP
PFSFDPEFLL FLLSFNMSSA QDEFDRLIRA NRDSSRTHPE DRDQSGSDSP ANNNDASADD
QYELSDADSD YGDHIKREDG NMVSRTGAYT VPSTVFEANT GPKGVIADAQ SFERARKKSF
RRTLLSAARL DSHSKFFGGN SSNNNITQHS QASSSPPSDE EDEFMRRWRE SRLQELQERG
QRRPSPSKRI YGRVDTVDAE GYLNAIERVA SDTVVVVCIY DPESSVSAQV EDAIEVVARK
YITTHFIKLH HEIAEMSHIE APALLAYKGG DIISTLIDIP RQIPRGGEIS SLTIEDLLKR
NRVF
//
