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Database: UniProt
Entry: A0A1V6QFG2_9EURO
LinkDB: A0A1V6QFG2_9EURO
Original site: A0A1V6QFG2_9EURO 
ID   A0A1V6QFG2_9EURO        Unreviewed;      1204 AA.
AC   A0A1V6QFG2;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:OQD87717.1};
GN   ORFNames=PENANT_c005G03594 {ECO:0000313|EMBL:OQD87717.1};
OS   Penicillium antarcticum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=416450 {ECO:0000313|EMBL:OQD87717.1, ECO:0000313|Proteomes:UP000191672};
RN   [1] {ECO:0000313|Proteomes:UP000191672}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBT 31811 {ECO:0000313|Proteomes:UP000191672};
RX   PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA   Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA   Frisvad J.C., Workman M., Nielsen J.;
RT   "Global analysis of biosynthetic gene clusters reveals vast potential of
RT   secondary metabolite production in Penicillium species.";
RL   Nat. Microbiol. 2:17044-17044(2017).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the GPN-loop GTPase family.
CC       {ECO:0000256|ARBA:ARBA00005290}.
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:OQD87717.1}.
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DR   EMBL; MDYN01000005; OQD87717.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V6QFG2; -.
DR   STRING; 416450.A0A1V6QFG2; -.
DR   OrthoDB; 767442at2759; -.
DR   Proteomes; UP000191672; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   CDD; cd17870; GPN1; 1.
DR   CDD; cd00299; GST_C_family; 1.
DR   CDD; cd00570; GST_N_family; 1.
DR   Gene3D; 1.20.1050.10; -; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR010987; Glutathione-S-Trfase_C-like.
DR   InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR   InterPro; IPR040079; Glutathione_S-Trfase.
DR   InterPro; IPR004045; Glutathione_S-Trfase_N.
DR   InterPro; IPR004130; Gpn.
DR   InterPro; IPR030230; Gpn1/Npa3/XAB1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   PANTHER; PTHR21231:SF8; GPN-LOOP GTPASE 1; 1.
DR   PANTHER; PTHR21231; XPA-BINDING PROTEIN 1-RELATED; 1.
DR   Pfam; PF03029; ATP_bind_1; 1.
DR   Pfam; PF13410; GST_C_2; 1.
DR   Pfam; PF13417; GST_N_3; 1.
DR   SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR   SFLD; SFLDG00358; Main_(cytGST); 1.
DR   SUPFAM; SSF47616; GST C-terminal domain-like; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS50405; GST_CTER; 1.
DR   PROSITE; PS50404; GST_NTER; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000191672};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        405..429
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        449..472
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        479..501
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          991..1069
FT                   /note="GST N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50404"
FT   DOMAIN          1074..1204
FT                   /note="GST C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50405"
FT   REGION          285..366
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          516..545
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          605..640
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          667..700
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          803..824
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          957..979
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        285..307
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        313..327
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        337..351
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        670..700
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        809..824
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1204 AA;  133504 MW;  2AAAC7F4E096A707 CRC64;
     MPSPVSVVCV GMAGSGKTTF MQRINSHLHE KNTVPYVLNL DPAVHSVPFD SNIDIRDSIN
     YKEVMKQYNL GPNGGILTSL NLFATKVDQI ISLLEKRTAP NPENPSAKPI EHILVDTPGQ
     IEVFVWSASG SILLETLASS FPTVIAYIID TPRASSTSTF MSNMLYACSI LYKTKLPMIL
     VFNKTDVKDA EFAKEWMTDF DIFQQALRQE EESGAFGTEG GAGGFGSGSG YMGSLLNSMS
     LMLEEFYRHL SVVGVSSMTG DGVDEFFEAV ETKRQEFERD YKPELERKKK EREEQKESQR
     ELELGKLMKD MSVSGSSART QKGPSHEPET VSEAEDDEDN IIKRGLADGE ADSDYEDYEG
     ADAGNDEGLS QRYKEALSGS QSAPSNQDNS FTRYLRASQM AMEIYFARCL GLSLFTITVL
     TVMLTGSIPL TSDIKDSVAA DEDDPKAPYA VPTLMVTSVY HAVCAFYAYT WYVGGGQGVF
     AIAVAGSSGL AAVGLWCMLF ASSNGKISRR TGADKRTTGF PFKNSEAAKK HAGKKGLNSA
     TPTLKSSMPL HLSRDEIVAR MAMSMNNSPL NNLFEPFQYR PDVDPNATRP HSFIRPQHGA
     VNHFLSTTPT HHQSHADRHG ASAGATPHLQ PQGQAPARMS LQQSRDFNNG IDDSAHLAQM
     REALQDSPAG QMMPPTTLSQ SVLGVGNPSP NGAHSTQNNN GLVMLESPSQ SFQPEFIALD
     VEPIGPVSFS TTSEEAGMKI VPDAPNLEYW RNKLFNVDEM ITLSEEEFQT YFPHVDNVYS
     HRSTQRYKSR PFVSHYWDCR LRGRPPGTPK SDNPEKKKRK RTARERDLCH VKIKVVEYFP
     QIESSADIMP VDSSPAPVSA PAPSAAPIAV PGIFTWALDT PESTRKSSGQ AFQMITPSHS
     LPPNHPGANG ARYYTIQRVN GNGANGKNDG VAGGHRHTLE ESDRVKKNSV QRYLNRETKD
     KRNKMEQTMS SGRSQKSYHT KATGLAAETV DKHAAESNLK LPFVQRVWIA LEMKGIPYQY
     IEVDPYQKPD SLLEVNPRGL VPALRHDDWG CYESNVLLEY LEDLNAGTAL LPRDAKLRAH
     CRLWADHINR HIVANFYRVL QEQNEQTQVQ KAQDLRSSIE QLLEAAHPKG PFFLGAQMSL
     VDVQAAPWII RLKRVLKPYR EWPDAEEGSR LAAWVDAIEN DQHVQATTST DELYLDSYQR
     YARE
//
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