ID A0A0A2IXK2_PENEN Unreviewed; 1401 AA.
AC A0A0A2IXK2;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=Transcription factor SipA3 {ECO:0008006|Google:ProtNLM};
GN ORFNames=PEX2_036440 {ECO:0000313|EMBL:KGO60032.1};
OS Penicillium expansum (Blue mold rot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=27334 {ECO:0000313|EMBL:KGO60032.1, ECO:0000313|Proteomes:UP000030143};
RN [1] {ECO:0000313|EMBL:KGO60032.1, ECO:0000313|Proteomes:UP000030143}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MD-8 {ECO:0000313|EMBL:KGO60032.1,
RC ECO:0000313|Proteomes:UP000030143};
RX PubMed=25338147; DOI=10.1094/MPMI-09-14-0261-FI;
RA Ballester A.R., Marcet-Houben M., Levin E., Sela N., Selma-Lazaro C.,
RA Carmona L., Wisniewski M., Droby S., Gonzalez-Candelas L., Gabaldon T.;
RT "Genome, transcriptome, and functional analyses of Penicillium expansum
RT provide new insights into secondary metabolism and pathogenicity.";
RL Mol. Plant Microbe Interact. 28:232-248(2015).
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:KGO60032.1}.
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DR EMBL; JQFZ01000083; KGO60032.1; -; Genomic_DNA.
DR RefSeq; XP_016601113.1; XM_016740919.1.
DR STRING; 27334.A0A0A2IXK2; -.
DR GeneID; 27676338; -.
DR HOGENOM; CLU_001720_0_0_1; -.
DR OrthoDB; 2027807at2759; -.
DR PhylomeDB; A0A0A2IXK2; -.
DR Proteomes; UP000030143; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR CDD; cd07609; BAR_SIP3_fungi; 1.
DR CDD; cd13280; PH_SIP3; 1.
DR Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR004148; BAR_dom.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR039463; Sip3/Lam1_BAR.
DR InterPro; IPR042067; Sip3_PH.
DR InterPro; IPR031968; VASt.
DR PANTHER; PTHR14248; CYCLIN Y, ISOFORM A; 1.
DR PANTHER; PTHR14248:SF18; CYCLIN Y, ISOFORM A; 1.
DR Pfam; PF16746; BAR_3; 1.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF16016; VASt; 1.
DR SMART; SM00233; PH; 1.
DR SUPFAM; SSF103657; BAR/IMD domain-like; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS51778; VAST; 1.
PE 4: Predicted;
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW Membrane {ECO:0000256|ARBA:ARBA00022989};
KW Reference proteome {ECO:0000313|Proteomes:UP000030143};
KW Transferase {ECO:0000256|ARBA:ARBA00022676};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 305..406
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 933..1104
FT /note="VASt"
FT /evidence="ECO:0000259|PROSITE:PS51778"
FT REGION 429..506
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 551..585
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 640..691
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 476..490
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 491..506
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 640..664
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1401 AA; 157157 MW; 62DBE77D7E119749 CRC64;
MSTQAQTPLP QVGKLVSVVP VGLKEAALDS PTFRATTLHF SDQVDFIEKW LDGYAKAATK
LSCELAALES VVNNFLSYST HPLVVSEAVV DHDYTLLAMR RCGEGSKDLW SGLVTTTRKL
ESLISEPIRD FIQEDLRHFK EIRRNLDQTQ KAYDYLQARY ASQSKSKEAS ALREEAFQLH
EAHKAYLKAA MDYSVQGPQV RNALDRLLVK VSCDQWREFR GFHNHNSGTF SKWSREMDRI
KGWLHEMEGS EKSSKRELLS TRKHIEEAAE FAARPSRELE DYNISTVPYL GSRPISTLNV
SKEMRPEKQG WLYLRTLSGK PTRTVWVKRW AFLKHGIFGC LVQGSRTGGV EESERIGVLL
CSIRPAFQEE RRFCFQVKTK NNTILLQADN QKELMEWIGA FEAAKQKALE NPASTDLSVS
GKVTVQDPAF SISQPPASEF AADPADSLTP HANDEPGAGD RSMTLPVPDR DGYSMRNSTD
IGSGRRPTGL DSESSAREHA REHTSRLIQK LDLHRKSNNA APMSPSIPGP AGGIASLISA
SHNILPYSNA GPLSVDDKRG RSLSNVDEPG SSLAPATLAN PPAPTSMSKA AVVVSNERGI
GLGLSDSTGG MPSGMMANLW GSSNWGFMNK HQLEQHQIDG VSNDAPEGRS SSTLSNTSTP
TIAAQPDAAG ALPEPRQQSG PRHRQTVSLD GDDVKLTQVS LGIGREYPSY YPQQLKIQDA
QFRLLFPDVK RDDALVLVFR ATWSPNDQQE FPGRAYVTTR NIYFYSHHFG LVLTTGVSLE
SIKEVTAAPG RDCDFLFLHT IPPLGSDTPG RVTIKTFLEP LRLLQKRLNF LIQGSIAVEQ
LNLESLIKAL IKMDTGSPAR NSSADSWEDL SSGLADIKHD GGKPTDLSNP KDIRLPIYID
KDLELDGGRT GRGRDIAKFR LPTQPVEYVP QGDLVLVTEK ILDISPKALF HILFGDKSAV
WQLLLHERQA REIKQGPWAS TELRHLRRDF HYNIGTTDIL GRTHENAISD YQIIDVLNDH
LCYVITDKKT PWHLPFRRSF RLVSKVVITF QAKSKSKLAI YTKVEWLWSP YGLKSIIDKK
ASDDLEQDSL DLVDLVSDQV RRLGVHSRTK KAITIFGHVG RQSHVSLFSG AGSNLKLEPR
KPRTQRAMHE LLLETFLSFL ETSVSFLMMW AFGVVRWSWK TVSAHKIILT MLATSAILNG
YYSSRDSWDW WHERHAGNFM ARLGVQPNLV MSKSIYMRDI DDAVANSTIW PGTGNASDCF
ATFHEQSMRY SEMPLSLSAS GPRDALTKSA IKRFQQTRER LGMYRHNLLV ALRVVNSIEK
EVIQTEWERW LREEVRRCRQ VEVLLGEETQ GDDSQTGQTA QAERVFAEHA DNVKQWYEEY
CSSCRMEQEK VIFNDRGDLI P
//