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
//