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Database: UniProt
Entry: A0A163JFF4_ABSGL
LinkDB: A0A163JFF4_ABSGL
Original site: A0A163JFF4_ABSGL 
ID   A0A163JFF4_ABSGL        Unreviewed;       540 AA.
AC   A0A163JFF4;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   RecName: Full=Phorbol-ester/DAG-type domain-containing protein {ECO:0000259|PROSITE:PS50081};
GN   Name=ABSGL_06777.1 scaffold 8673 {ECO:0000313|EMBL:SAM01041.1};
OS   Absidia glauca (Pin mould).
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Cunninghamellaceae; Absidia.
OX   NCBI_TaxID=4829 {ECO:0000313|EMBL:SAM01041.1};
RN   [1] {ECO:0000313|EMBL:SAM01041.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 101.48 {ECO:0000313|EMBL:SAM01041.1};
RA   Evans L.H., Alamgir A., Owens N., Weber N.D., Virtaneva K., Barbian K.,
RA   Babar A., Rosenke K.;
RL   Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; LT553500; SAM01041.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A163JFF4; -.
DR   STRING; 4829.A0A163JFF4; -.
DR   InParanoid; A0A163JFF4; -.
DR   OMA; VYTDHRW; -.
DR   OrthoDB; 1449562at2759; -.
DR   Proteomes; UP000078561; Unassembled WGS sequence.
DR   GO; GO:0005778; C:peroxisomal membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0007031; P:peroxisome organization; IEA:UniProt.
DR   Gene3D; 3.30.60.20; -; 1.
DR   InterPro; IPR046349; C1-like_sf.
DR   InterPro; IPR002219; PE/DAG-bd.
DR   InterPro; IPR010482; Peroxin.
DR   InterPro; IPR006614; Peroxin/Ferlin.
DR   PANTHER; PTHR31679; PEROXISOMAL MEMBRANE PROTEIN PEX30-RELATED; 1.
DR   PANTHER; PTHR31679:SF2; PEROXISOMAL MEMBRANE PROTEIN PEX30-RELATED; 1.
DR   Pfam; PF00130; C1_1; 1.
DR   Pfam; PF06398; Pex24p; 1.
DR   SMART; SM00109; C1; 1.
DR   SMART; SM00693; DysFN; 1.
DR   SUPFAM; SSF57889; Cysteine-rich domain; 1.
DR   PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR   PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000078561};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   TRANSMEM        259..285
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        347..375
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          7..56
FT                   /note="Phorbol-ester/DAG-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50081"
FT   REGION          60..156
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          169..209
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        65..146
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        193..209
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   540 AA;  62479 MW;  2DC793C23610B181 CRC64;
     MASPAKFHQF NVTTFHGLVY CDYCSKMLWG LARQGVQCSA CGYHCHVTCK DMALQCRPPK
     RVSPDSLSVT DSESESLSRY SLSTPRSSFD LPKSAQQQQQ QQQQQQQQQQ QQQKQKLYND
     DTLSGRSLNT RSKRLPSQQL SLDAGYNNPQ KDEALKTPPL YTSYIDLPQR QQQQQPQQQP
     PAPAKAFRRQ LKQQLDRSIQ SQGSDSNDKS MVMTLTMTPQ QMAKTFTRLI ARSRAFFHLV
     HYFHDVYNWK SPAKSLTYLG LWTLLCLYPT SVILLPPVLI VLLFFRSGLQ DRPANQILLP
     RYDEGTAEYY INLDHMQSCL IFFIRLYDNL SYHLQHASLN ENVYRLLFVM SLGLTLCLYW
     VGRWLVLALG VLVLVNKTRL GVALETILRL AMELLQTLID LAVFSRPSSK VSLEVSLYEN
     QRWWTGTGYT SQLLRSERTP WSNITGTEPL PSKDNMPPPS HYQWADDDWQ LDMTGPWSDD
     ILGLVSIIEC DEQGWVYTDH KWTNPKSRPD PLKDNNARSL TRRRRWYRKA RLVDSKETFD
//
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