ID   A0A0A2I2R1_PENEN        Unreviewed;       979 AA.
AC   A0A0A2I2R1;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   RecName: Full=SPX domain-containing protein {ECO:0000259|PROSITE:PS51382};
GN   ORFNames=PEX2_033680 {ECO:0000313|EMBL:KGO60379.1};
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:KGO60379.1, ECO:0000313|Proteomes:UP000030143};
RN   [1] {ECO:0000313|EMBL:KGO60379.1, ECO:0000313|Proteomes:UP000030143}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MD-8 {ECO:0000313|EMBL:KGO60379.1,
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   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Vacuole membrane
CC       {ECO:0000256|ARBA:ARBA00004128}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004128}.
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:KGO60379.1}.
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DR   EMBL; JQFZ01000074; KGO60379.1; -; Genomic_DNA.
DR   RefSeq; XP_016601445.1; XM_016740643.1.
DR   AlphaFoldDB; A0A0A2I2R1; -.
DR   STRING; 27334.A0A0A2I2R1; -.
DR   GeneID; 27676062; -.
DR   HOGENOM; CLU_009308_2_0_1; -.
DR   OrthoDB; 11387at2759; -.
DR   PhylomeDB; A0A0A2I2R1; -.
DR   Proteomes; UP000030143; Unassembled WGS sequence.
DR   GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   CDD; cd03024; DsbA_FrnE; 1.
DR   CDD; cd14480; SPX_VTC2_like; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   Gene3D; 3.20.100.30; VTC, catalytic tunnel domain; 1.
DR   InterPro; IPR001853; DSBA-like_thioredoxin_dom.
DR   InterPro; IPR003807; DUF202.
DR   InterPro; IPR004331; SPX_dom.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR018966; VTC_domain.
DR   InterPro; IPR042267; VTC_sf.
DR   PANTHER; PTHR46140; VACUOLAR TRANSPORTER CHAPERONE 1-RELATED; 1.
DR   PANTHER; PTHR46140:SF2; VACUOLAR TRANSPORTER CHAPERONE 2-RELATED; 1.
DR   Pfam; PF01323; DSBA; 1.
DR   Pfam; PF02656; DUF202; 1.
DR   Pfam; PF09359; VTC; 1.
DR   SUPFAM; SSF103481; Multidrug resistance efflux transporter EmrE; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS51382; SPX; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030143};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}; Vacuole {ECO:0000256|ARBA:ARBA00022554}.
FT   TRANSMEM        689..707
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        727..747
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          1..163
FT                   /note="SPX"
FT                   /evidence="ECO:0000259|PROSITE:PS51382"
FT   REGION          534..605
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        551..566
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        583..605
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   979 AA;  110831 MW;  226226AE1639ABA4 CRC64;
     MRFGKTLRAA VYPPWKGKYI DYNKLKTLLR ENDVTRDGED ASDSDDDQWT EQDEEAFVQE
     LLNVELDKVN SFQAETSQQL RERTTACEVK LRPLASTPEQ EPPVLDEQKK RAIASEVLQE
     LDNITKEVSA LEKYSRINFT GFLKAAKKHD RKRGARYRVK PLLQVRLSQL PFNSEDYSPL
     VHRLSVMYSF VRETLSHDIV QPREAEHGFG RETYSSYKFW VHSDNVLEVK THILRRLPVL
     IYRPGTSKDL DTITEDPTIT SLYFDSPQFD LYNQKVARAP EAGSLRLRWT GSLKDKPTIQ
     LEKKIVTDDD ESRQVKVQLK EKHIKEFLDG EYRFDKKLHR MEDSNNGESA AAEALKKDVD
     ELQSFIKDND LQPMLRANYT RTAFQIPGND RIRISLDTNL ALIREDTLDS ERPCRDPAEW
     HRTDLDGADM TYPFNAVRTG EITRFPHALL EIQLRGKAHN TEWVKDLMVS HLVKDAPRFS
     KFVHGVASLF EDYVNSFPFW LGELESDIRR DPETAFHEEQ ERLARRAEEN IAVGSFMGDA
     RSPGVRPQVG SPYHQYSNTG SPSAIRRSSA VIEPAARPSR PSIPEPQHRD TEPALEPEEE
     PEPPTRLESI FHSLGLSPQR WLGESVSLPP GVRHPGVWIK DAGPVRVESK VYLANQRTFI
     KWLHISILLS SLSLGLYNAA GKHNKVAQAL AVVYTFFAIF AAVWGWFIYE RRARLIRQRS
     GKDLDNMFGP IVVCIGLAVA LVLNFVFKYS SALSQGRNHP LPSVPVHSNS SAVFDSSSGA
     TYPADTFSLH WKAFYLNPAS AEYPGVNKAE MYARKFGPER AQAIFARLAA VGKGEGIQFS
     FGGNTGLTRD SHRLLWFAGQ REAEEVGKKE GADGVIGGLQ TRVAEKLFQA YFEDEKNITD
     LKVLLEAGVG AGLDRETVKK LLDEDVGAQE VDLEAKTAAR RLVSGVPYIS VQGKYHVEGA
     DEPEVFLDIF EKVKAEQKE
//