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Database: UniProt
Entry: M2QT50_CERS8
LinkDB: M2QT50_CERS8
Original site: M2QT50_CERS8 
ID   M2QT50_CERS8            Unreviewed;      1421 AA.
AC   M2QT50;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   RecName: Full=Autophagy-related protein 14 {ECO:0000256|ARBA:ARBA00013807};
GN   ORFNames=CERSUDRAFT_122278 {ECO:0000313|EMBL:EMD40218.1};
OS   Ceriporiopsis subvermispora (strain B) (White-rot fungus) (Gelatoporia
OS   subvermispora).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Polyporales; Gelatoporiaceae; Gelatoporia.
OX   NCBI_TaxID=914234 {ECO:0000313|EMBL:EMD40218.1, ECO:0000313|Proteomes:UP000016930};
RN   [1] {ECO:0000313|EMBL:EMD40218.1, ECO:0000313|Proteomes:UP000016930}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B {ECO:0000313|EMBL:EMD40218.1,
RC   ECO:0000313|Proteomes:UP000016930};
RX   PubMed=22434909; DOI=10.1073/pnas.1119912109;
RA   Fernandez-Fueyo E., Ruiz-Duenas F.J., Ferreira P., Floudas D.,
RA   Hibbett D.S., Canessa P., Larrondo L.F., James T.Y., Seelenfreund D.,
RA   Lobos S., Polanco R., Tello M., Honda Y., Watanabe T., Watanabe T.,
RA   Ryu J.S., Kubicek C.P., Schmoll M., Gaskell J., Hammel K.E., St John F.J.,
RA   Vanden Wymelenberg A., Sabat G., Splinter BonDurant S., Syed K.,
RA   Yadav J.S., Doddapaneni H., Subramanian V., Lavin J.L., Oguiza J.A.,
RA   Perez G., Pisabarro A.G., Ramirez L., Santoyo F., Master E., Coutinho P.M.,
RA   Henrissat B., Lombard V., Magnuson J.K., Kuees U., Hori C., Igarashi K.,
RA   Samejima M., Held B.W., Barry K.W., LaButti K.M., Lapidus A.,
RA   Lindquist E.A., Lucas S.M., Riley R., Salamov A.A., Hoffmeister D.,
RA   Schwenk D., Hadar Y., Yarden O., de Vries R.P., Wiebenga A., Stenlid J.,
RA   Eastwood D., Grigoriev I.V., Berka R.M., Blanchette R.A., Kersten P.,
RA   Martinez A.T., Vicuna R., Cullen D.;
RT   "Comparative genomics of Ceriporiopsis subvermispora and Phanerochaete
RT   chrysosporium provide insight into selective ligninolysis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:5458-5463(2012).
CC   -!- SIMILARITY: Belongs to the ATG14 family.
CC       {ECO:0000256|ARBA:ARBA00009574}.
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DR   EMBL; KB445793; EMD40218.1; -; Genomic_DNA.
DR   STRING; 914234.M2QT50; -.
DR   HOGENOM; CLU_253057_0_0_1; -.
DR   OrthoDB; 5488314at2759; -.
DR   Proteomes; UP000016930; Unassembled WGS sequence.
DR   GO; GO:0000148; C:1,3-beta-D-glucan synthase complex; IEA:InterPro.
DR   GO; GO:0003843; F:1,3-beta-D-glucan synthase activity; IEA:InterPro.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
DR   GO; GO:0006075; P:(1->3)-beta-D-glucan biosynthetic process; IEA:InterPro.
DR   CDD; cd08950; KR_fFAS_SDR_c_like; 1.
DR   Gene3D; 3.40.47.10; -; 1.
DR   Gene3D; 6.10.250.1930; -; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR041550; FASI_helical.
DR   InterPro; IPR003440; Glyco_trans_48.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR016039; Thiolase-like.
DR   InterPro; IPR018791; UV_resistance/autophagy_Atg14.
DR   PANTHER; PTHR10982:SF23; FATTY ACID SYNTHASE SUBUNIT ALPHA; 1.
DR   PANTHER; PTHR10982; MALONYL COA-ACYL CARRIER PROTEIN TRANSACYLASE; 1.
DR   Pfam; PF10186; ATG14; 1.
DR   Pfam; PF18314; FAS_I_H; 1.
DR   Pfam; PF02364; Glucan_synthase; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016930}.
FT   DOMAIN          495..690
FT                   /note="Fatty acid synthase type I helical"
FT                   /evidence="ECO:0000259|Pfam:PF18314"
FT   REGION          117..139
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1421 AA;  158247 MW;  A9D1C6A889806662 CRC64;
     MTRGRKYNSR SAPAQAVKSV FTRPSIVSHL RCRPRLDKLA STFSLFRFLR EQEQPRDRQH
     YLLDKRWTWV LIFVGTVYGA RTLQSEHTPQ HHIQPVLRKC EPSMFQLGLL TGRTRQITPR
     SPAASPPTPT SQSQCPTTVH PTHAEDALAF LEFLLTWEGQ IDRGCTMAEL MGGEERVREI
     WDGLERLQQA NEQTRERVRT LRSNLSARRR TLAIATSTFL HSHGSTATLV DLQLPHADTQ
     FPAVIPNTHI LSANHLYWTI YFSADTAPAR DVSGRCRIAF LLCSGPGVSP LPGDRGSDSF
     ARQIDNVAYQ LAALSDTIAH ARSELVQELV EVFSVVEVGG RPPLGGKAGT KGEWTIGGLV
     LPIPGDICRY PPDHINAVII HTLHFLSLLS FYLGIKLLFE VVWAGSRSAM DRGDDERGRW
     RMGQVRLMPS WLATTMELAK RLGSETEAKS WLDGVVASYA QRSGISLSAG GARGASGGAS
     GGPTINSEEF LKFKADQDQF AAQQIELYMR YLGRNSKAGE IKHDAEKANV AAFQVKLDAI
     SKEHGDTYVN GIQPVFDVLK ARHFDSSWNW VRQDALLMFY DIIFGRLNTI NHDMTARCIA
     IMNHVDPELV TYMQSYINRC DPNRGKTYRL AKQFGQQLIE NCREVIGQPP LYKDVTFPTA
     PHTEVTAKGN IVYSEVVREN VHKLEAYIQE DVLKLWNIVK TQPEISEEQK NRIKALYGGV
     IQSLHKCPEF HPRHSGPRKR RSSSQFLRPQ ISGVTTSITA DKVPLLHLKR KVGTNWECSS
     NLTSVYLDIL HEIATSGTTF KDKNALCTGV GKGSIGVEIV KGLLSGGAYV PCNCRILPGI
     FQQFGSKGSA LTVVPFNQGS KQDVEALIDY VYSTLGLDLD YILPFAAVPE NGCEIDGIDD
     KSELAHRIML VNLLRLLGAV KNKKASRQFV TRPTQVILPL SPNHGLFGND RLYSESKISL
     ETLFNRWNSE SWGEYLCLAG AVIRWTRGTS LMDATNMVTH EVEGYGVRTF SAKEMAFNIL
     GLMHPLLFSI TQVEPIWANL NRGMDHLPDL AEITTRIRTS LNKKSELRRA IARDNAADFK
     VVNGIEAEHV LQTVDVTPHA NLRFEYPQLE SVESLADVSK LRGMIDLEKV IVITGFAEVG
     PWGSSRTRWE MEARGEFTLH RSHHLHRSSP WMHRVPKIKL ACSSTPATVP LIPYPSGFVP
     GPSFIPPAQP LYDLAKRVDP HSGLPVPVAC LNFGPANALG SVKIHNGEHV LMGQYLTKLS
     SLGSSKNRRF VASDGQGYHW AHQAGQDDKW VCQNASNYHI MSYTLKAAGE PKYTGSSGCA
     LTIEEDYAYL TPGSSCAHLW DTKILAKEPA MYNGSNPFGV DEKGQSKLDD LPFYCIGFKS
     AALEFTLCTC IWASLRTQML YRTVSDMMNY MKAISTHCPI I
//
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