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
//