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Database: UniProt
Entry: A0A364L5L4_9EURO
LinkDB: A0A364L5L4_9EURO
Original site: A0A364L5L4_9EURO 
ID   A0A364L5L4_9EURO        Unreviewed;      1416 AA.
AC   A0A364L5L4;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=SEC7 domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=BHQ10_007117 {ECO:0000313|EMBL:RAO71105.1};
OS   Talaromyces amestolkiae.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC   Talaromyces sect. Talaromyces.
OX   NCBI_TaxID=1196081 {ECO:0000313|EMBL:RAO71105.1, ECO:0000313|Proteomes:UP000249363};
RN   [1] {ECO:0000313|EMBL:RAO71105.1, ECO:0000313|Proteomes:UP000249363}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CIB {ECO:0000313|EMBL:RAO71105.1,
RC   ECO:0000313|Proteomes:UP000249363};
RX   PubMed=28649280; DOI=10.1186/s13068-017-0844-7;
RA   de Eugenio L.I., Mendez-Liter J.A., Nieto-Dominguez M., Alonso L.,
RA   Gil-Munoz J., Barriuso J., Prieto A., Martinez M.J.;
RT   "Differential ?-glucosidase expression as a function of carbon source
RT   availability in Talaromyces amestolkiae: a genomic and proteomic
RT   approach.";
RL   Biotechnol. Biofuels 10:161-161(2017).
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:RAO71105.1}.
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DR   EMBL; MIKG01000014; RAO71105.1; -; Genomic_DNA.
DR   STRING; 1196081.A0A364L5L4; -.
DR   OrthoDB; 4248238at2759; -.
DR   Proteomes; UP000249363; Unassembled WGS sequence.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR   GO; GO:0032012; P:regulation of ARF protein signal transduction; IEA:InterPro.
DR   Gene3D; 1.10.1000.11; Arf Nucleotide-binding Site Opener,domain 2; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   InterPro; IPR023394; Sec7_C_sf.
DR   InterPro; IPR000904; Sec7_dom.
DR   InterPro; IPR035999; Sec7_dom_sf.
DR   PANTHER; PTHR10663:SF402; ARF GUANINE NUCLEOTIDE EXCHANGE FACTOR SYT1; 1.
DR   PANTHER; PTHR10663; GUANYL-NUCLEOTIDE EXCHANGE FACTOR; 1.
DR   Pfam; PF01369; Sec7; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00222; Sec7; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   SUPFAM; SSF48425; Sec7 domain; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS50190; SEC7; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW   Reference proteome {ECO:0000313|Proteomes:UP000249363};
KW   Transferase {ECO:0000256|ARBA:ARBA00022676}.
FT   DOMAIN          437..610
FT                   /note="SEC7"
FT                   /evidence="ECO:0000259|PROSITE:PS50190"
FT   DOMAIN          725..853
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   REGION          1..88
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          122..459
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1069..1245
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1266..1416
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          923..950
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        34..48
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        50..75
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        153..167
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        182..235
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        277..299
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        311..349
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        360..398
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        410..445
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1104..1136
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1167..1201
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1266..1283
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1286..1328
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1368..1386
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1416 AA;  155652 MW;  97D250E46425B2F6 CRC64;
     MHRIRARLAS SDGNDNKRYS LIFAPHARRS EHVPRPSPSS SQLDRRVSDS GPRPNVEDDT
     VVDGEKVERP SIYDRDNSNH GSGITGFSVA STSETSASMK RNRFSMLRFR HASDPQLSVT
     YSQSEKDVPP MPQIPPPPTI ITTAPTNSNL EKSARKSRLR NPLSRKSSRE VVKMGNASGP
     GLAKTPLSQT LGHTRLSHEE PGRLSTSTYQ SGTTNNPSEQ DMRFSESSRS DQGSIDRNPV
     KGDAPHPIKK LHMPRLMKSR ANLFPLPVKL PPPGAGNSHS GRTSPISNGG HSERTSMDPT
     TPDGADGDQI SPLPSPTQSS VKLASPKPSN QNPLLRKDST TSARSGHSAS SAKARLGRRG
     RSSTLNSFIE ASRNGEDLNN SSSNLPSGRN SISTNGRKSF GDLFGLGNRL RQNSEFSSQR
     DGRSSPRAPG TPTSVTKNGS ASASRTAVIA PDREEDDTPA TYLTKLQESV PKGSIGIILS
     KSDDDFYKVA LRKFMRTFAF FGEPIDMAIR KLLMEAELPK ETQQIDRFLQ GFADRYYECN
     PGVFATTDQT YFIAFSILIL HTDVFNKNNK RKMQKQDYVR NSRIDGVSEE ILECFYENIA
     YTPFIHVEDE LNLSTRQIPK RKGLLKVASS DHLARTSSQP VDPYAVILDG KLDTLRPGLK
     EVMNIDDPYS FPDSEGFKDI EPLHQAFFRS AVLQIVSARS RPDAFMTSTN MEDMADSHPG
     LVDIKVVKVG LLWRKDPRKK RARSPWQEWG ALLTSSQLYF FRDLYWTKSL MSQYENQRKR
     GSRLPVVFTP PVTDFKPDTI MSTSDAVGLI DSSYKKHKHA FLLVRHNGLE EVFLANSDAD
     MNDWLAKLNY AATFRTTGVP LKSTVGARYE GQKHQNMAXM DSTRSVSSQL QSDGTAPETK
     DYVDVRLAEE MSAAREQLMS RRIAEQDEKL TGYQNQLDDL LRNARHLQLL TPVNTRAREN
     VILAAGRIAA KLRWVRLDMW RTRCYNHFLS MDLGIDQKSS DAQKRSSLTT VKPVSPGLNT
     SLARLNSTHS LLTAPSISET TSVGPASPML PESTVISNEF LSPIIPDGYR LNSPSITSEP
     FDEKHAPVSP MSEAPPGGGS GSLNREPSIL SSGGRSEGPA SSILSSTTPM NTTNVDDSEE
     RVLREAGLLG VDGPADSPNP SPKLGNDAEI SEKHVDEKSD SNTDHRLSSH RRSLQRTLRD
     SHHKPNHQRS KKGRDSASSI PLVDSPAGGE GEGLSRKDAN FTLHGKKASV ITFGSEWQNI
     SAEERLKLRK PAASEEARAS DTNLIRDPRG SISSASVHSG RPQSMRSAST ATARSSRFVD
     SISVNNGIPE VPSMDVLLKE EEEEEEKQNQ QEAIPSNNGK DAEFAEPANA PTSTTSATTD
     EIPSENLASH DNGELVEPIS GQEQPRLNSH EQAVGA
//
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