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Database: UniProt
Entry: A0A093Y1A3_TALMA
LinkDB: A0A093Y1A3_TALMA
Original site: A0A093Y1A3_TALMA 
ID   A0A093Y1A3_TALMA        Unreviewed;      1657 AA.
AC   A0A093Y1A3;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=Autophagy-related protein 14 {ECO:0000256|ARBA:ARBA00013807};
GN   ORFNames=GQ26_0051280 {ECO:0000313|EMBL:KFX51293.1};
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:KFX51293.1, ECO:0000313|Proteomes:UP000029285};
RN   [1] {ECO:0000313|EMBL:KFX51293.1, ECO:0000313|Proteomes:UP000029285}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PM1 {ECO:0000313|EMBL:KFX51293.1,
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 ATG14 family.
CC       {ECO:0000256|ARBA:ARBA00009574}.
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:KFX51293.1}.
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DR   EMBL; JPOX01000005; KFX51293.1; -; Genomic_DNA.
DR   Proteomes; UP000029285; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR   GO; GO:0032991; C:protein-containing complex; IEA:UniProt.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd12148; fungal_TF_MHR; 1.
DR   CDD; cd00067; GAL4; 1.
DR   Gene3D; 4.10.240.10; Zn(2)-C6 fungal-type DNA-binding domain; 1.
DR   InterPro; IPR018791; UV_resistance/autophagy_Atg14.
DR   InterPro; IPR036864; Zn2-C6_fun-type_DNA-bd_sf.
DR   InterPro; IPR001138; Zn2Cys6_DnaBD.
DR   PANTHER; PTHR31644:SF2; TRANSCRIPTIONAL ACTIVATOR ARO80; 1.
DR   PANTHER; PTHR31644; TRANSCRIPTIONAL ACTIVATOR ARO80-RELATED; 1.
DR   Pfam; PF10186; ATG14; 1.
DR   Pfam; PF00172; Zn_clus; 1.
DR   SMART; SM00066; GAL4; 1.
DR   SUPFAM; SSF57701; Zn2/Cys6 DNA-binding domain; 1.
DR   PROSITE; PS00463; ZN2_CY6_FUNGAL_1; 1.
DR   PROSITE; PS50048; ZN2_CY6_FUNGAL_2; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT   DOMAIN          682..718
FT                   /note="Zn(2)-C6 fungal-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50048"
FT   REGION          66..119
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          557..606
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          640..680
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          717..795
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          886..927
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1119..1138
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1449..1532
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1626..1657
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          274..319
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        66..90
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        91..108
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        558..573
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        640..662
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        717..747
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        886..907
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1485..1519
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1657 AA;  185927 MW;  843363154C6127F9 CRC64;
     MSDSNNNSRR ERPLLFSVNR KLRHLQGLSI RNLSITPPSR ARGKTIDDDD IPYSLKTPVK
     LAVQAQNRSV TQSRSYTDLK SISPKVQPLD GNQEQHDKQI RESRPNRRRS TLPWSGGDLE
     SRQTKLEDIA RSRMADVWFS IHCDGIDGPV YVSEVVEKTT NPDFRVLDLN VCGPHVSRMD
     QLCVKVWVKS ENMSDYTLLL ELHQSFRSLQ FVGKSLETFH HPLPPNCVLF HFADGIFTNL
     TDLPPTQTNL AGFTNGSPHM EPQSTSSYDA LMRLANLDDC IQDALATREK LESQINVILK
     KYQKSLELLN QVSQAEEKTA LIKRGIANEK KQVRLSAKRR DELIASINAR RESMTSGREN
     QNKTCTHLTD ARLKLTFSAS LLGHNREDAK GQIRRICEDL LAIYPIEPLS DKALAFTIAG
     LHLPNSKFDD IDREVVAAAL GYTGHLVYLL SFYLSVPLPY PIKPYMSSTF IQDPVSAGLS
     RRTFPLYPVN VQYRFEYGVF LLNKNIEVLM NRFGLRVLDI RHTLPNLKYL LYVLTARTNE
     LPARKAGGVR GLLLGRSTPM MSRQNSQDSF ASSEIMPPHR MPSELLRNDA NKSQTSPTTP
     PPFPLLSQAR FASGCLAHPR PLPERRRPSP RRLTTAIARM ESTHDGSMSQ DAVSLNNGSY
     DESNRELRSE TPPTQHRRGY QACDPCRKRK VKCDLGSVDN PRPPPCVRCR RESKRCEFSA
     TRRKRKTSDA EPEQETPLRR DKRMMVGEVL YGESSSSIGS NGKREPSYGP TAPAPFDNGN
     LHKYAWPENS PHTVSQASPI IQKDHHQHSP VSASHYHDGR GIQSSAYQAQ HSRGPPGSEI
     RQHVMNKTAA DLLFPTISNS HDALHLLSEA AGRTEDLNRQ RLENKARQSA GSYGAHMSAT
     SSTMPRNPHH PYPKRSHQMS ADGYSDTSAD YRKQNFETYN DPGYLDAVKA WSRLRFVRAG
     WLSVEEAMAY IAYYYKHLAP LSPIVIPDFS PPSTHRTLLT DEPVLAVTML TTASRYMKPK
     GDGAHTRGYY IHDRLWAYLR GMIERLFWGQ EKFTGNSVGM GTPRSLDIPL PAQGQASLRG
     HLRSLGTVEA LLILTDWHPR NLHFPPGDDE NTLLDADALL PSRNDGDSDS RGPSGGGVEG
     RFAFQKWLEP TWRSDRMSWM LLSTAQALAF ELGVFDRKAP SALESVAEQV RKRRVRRLII
     VYITQGSGRL GIPSMLPLDR WSDDIEPTTP ADATEAEIAI DRMQDLWVQI SKIMSLSNTD
     LFPSKEYTSE LIKTGRYKQQ IAEFLPHLQK FRAYYDSVSL SPQMQNILTI EYEYTRIYVN
     CLALQAVVER WTTINNEPSS KSSAASSLRV LMEIYRVNEK YIQEVVDASR KILHIVLDCL
     VPDEQLKHCP TFTLGATEDD VRVSLDLQDR TIEALRTCVV DDVHLSNTIS RLLELLTANI
     RTRFLRFAPT DRGADGDSHE RSSQPSSRVA SPRPTKDNNS TRRDSGAHWQ HQIPTPTHNK
     LGYQFNQGAG ESQQQHPVGS HHDPLAGIPA QPINSSNIGV SFMPPPPSVY YNYYGANGPS
     PPKLDDSNSI AQSVHEGGLP DWFALPLDQF FNSSATGVDQ GLGGTGPMLG EFDMLEVLLN
     EQLDKDGNVG GPSAGNGVEN MDGAPTPRNQ HQHHPFM
//
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