ID A0A094H010_9PEZI Unreviewed; 1705 AA.
AC A0A094H010;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=BZIP domain-containing protein {ECO:0000259|PROSITE:PS50217};
GN ORFNames=V501_09865 {ECO:0000313|EMBL:KFZ01686.1};
OS Pseudogymnoascus sp. VKM F-4519 (FW-2642).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420914 {ECO:0000313|EMBL:KFZ01686.1, ECO:0000313|Proteomes:UP000029315};
RN [1] {ECO:0000313|EMBL:KFZ01686.1, ECO:0000313|Proteomes:UP000029315}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4519 (FW-2642) {ECO:0000313|Proteomes:UP000029315};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor
CC biosynthesis. {ECO:0000256|ARBA:ARBA00004687}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the PIGC family.
CC {ECO:0000256|ARBA:ARBA00008321}.
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:KFZ01686.1}.
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DR EMBL; JPKD01003248; KFZ01686.1; -; Genomic_DNA.
DR STRING; 1420914.A0A094H010; -.
DR HOGENOM; CLU_001363_0_0_1; -.
DR UniPathway; UPA00196; -.
DR Proteomes; UP000029315; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005544; F:calcium-dependent phospholipid binding; IEA:InterPro.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR GO; GO:0006506; P:GPI anchor biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd14688; bZIP_YAP; 1.
DR Gene3D; 1.20.5.170; -; 1.
DR Gene3D; 1.10.220.10; Annexin; 3.
DR InterPro; IPR037104; Annexin_sf.
DR InterPro; IPR004827; bZIP.
DR InterPro; IPR046347; bZIP_sf.
DR InterPro; IPR009450; Plno_GlcNAc_GPI2.
DR PANTHER; PTHR12982; PHOSPHATIDYLINOSITOL GLYCAN, CLASS C; 1.
DR PANTHER; PTHR12982:SF0; PHOSPHATIDYLINOSITOL N-ACETYLGLUCOSAMINYLTRANSFERASE SUBUNIT C; 1.
DR Pfam; PF06432; GPI2; 1.
DR SMART; SM00338; BRLZ; 1.
DR SUPFAM; SSF47874; Annexin; 1.
DR SUPFAM; SSF57959; Leucine zipper domain; 1.
DR PROSITE; PS50217; BZIP; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000029315};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 135..163
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 296..315
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 327..344
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 378..395
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 407..427
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 433..455
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1389..1447
FT /note="BZIP"
FT /evidence="ECO:0000259|PROSITE:PS50217"
FT REGION 1..93
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 195..260
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 482..923
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1367..1405
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1493..1555
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..26
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 243..260
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 526..574
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 597..716
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 717..739
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 790..814
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 843..860
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 903..917
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1369..1384
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1385..1405
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1520..1555
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1705 AA; 189855 MW; 09ED013B7BC3E302 CRC64;
MMPHEPSPIS PTTPTKFPPP TRSATLPIPP RTWSAPTDRT LLAPEDAIYL GSPPHRRGAA
DKANLRMSNG DTTGDDSSRG HRRGRNKERM SSSRRRKVIW KKLLWVKQSY PDNYTDQETF
LEHLQRNPRL QPYDFWPLVA DSTVIVQQVC SVIIFIVCFV GIFQERVSPV TVVGTGTLST
VLGWVAWDRW VGQEQQSVSR PNHPPRPIDG PSMASSVSGA VKSDTKPQGA GPGLAALPLS
PRHSHSASAS SLHSQTSITS PIVGQPNGSS TFATYSPVAP YGSRSSFSPR NQQRLATAKS
AVLIYCALLG LSPILKSLTR STSSDSIWAL STWLMIINVF FFDYGGNVGV KFQASLSTNA
ALMASTVLAS RLPSTQHVFS LTLFSIEVFG LFPVFRRHLR HVSWRWHVAL TALLVMGAGG
GVGMVVTRGG WKAAVVGMTL GNLIAGLAMG GLSWLNLTNL HIQFRGWANS LIAPLIDDTD
VSDRVSSPTM SLNPEERRRR ISKSPGRAPS PPDDYSPPRS SRYAEPKSSR YYDDDDDDED
HRDRKRGDPY DYDDRSSARA PREPRDRDDG PRYAEAPYRP PASHKKTASF AMPGGFSDDE
EDPKINKYGK KEKDYYGDKG SSLSRRDDSP PPRDKPRYAD PEPESRYKRD VSPAYKPRYA
EPEPERKPRY AEPEPERKPK SRYKDESPPS KSKYDEPEAY KPRKYYDDDE SPPRRPKYAA
PDSPPQPKYA APVAPAAPAA PQQPKYSAPE RDAKPKYVTA DPSQRGGNPK YWDDKDKDSD
SDSDDSDEQD GPIGDRRIDI DFEIKHDHYD TTVRKREKHK HHHESPKYNE VALVTTTTDS
SRYAEPKRWE YAHPEEKITY TSKTESYTAN PEPNAYGRPA YDRPYAPPSS SRQPDPRAPV
NGPGQTQVVT VEPGRRNRAS SNFGPGGLGA GMLGVAAAAG VGASLANAPG SPMLEAYKGT
YQSMGPLTIT SKPYADNADV DILEIAPPAS PTSKRRHARF HDLENEASIL KKALRETKSK
AYPDPRPFIE ILPALTHEQI LDLRAEYKKQ VKTPDMKGVN IAKHIKVRLK EDKFFLKACY
ATALGRWESE AYWANSYYQG SQTSRELLIE SLMGRTNAEI RQIKDAFRDK KYSDSLTRCM
KQELKEDKFK KAVMMVLEEK RMDERPGRSL DRSLVEQDVR DLNRAIKSER GGESVMIGIV
VQRSDSHIRE ILRVYEASFR SNFAREMLKK SGNLVGEMLA HILNGIINRP VRDTLLLHHA
LTLTKSDSLR VDLLISRLVR YHWDRPHMEA IKREYRNRYG KELQEAVREG TKGAWGEFCE
ELCVKRVGDE VKRFDKVERI ERVERIEVHG GPNGGFNMKK FSFRTFRPSK DSGGEQGSSS
SDKQAVSSKR REQVRKAQRT HRERKEVYMK SLETEVLQLR TNEANLLQET RSLYAEIDQL
KSVLTELGVQ LPIVGASGLA EYGSTAFPTN SVVSIRQGSI GPQIHVGHSA ADTRHRNDGF
HLPANPPTGR SERVFHREDS QASNVTSSLQ SPASGGVLSS PNAYESGQSV TSPESTADLD
MESIGVEFVL TLESPCLGHM QGNPDDPEAP SGHVLTVSAP LLFRAPSIDT GPHICTTTPW
EAPASGLERL LNLSQGLVLD GEVTPVQAWN YIRQRVGPQG IEVERLQALT EKLLKEVSCH
GFGAVVEQGA FEGLVFDTLV VGQAS
//
