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Database: UniProt
Entry: A0A1V6Z9M0_PENNA
LinkDB: A0A1V6Z9M0_PENNA
Original site: A0A1V6Z9M0_PENNA 
ID   A0A1V6Z9M0_PENNA        Unreviewed;      1079 AA.
AC   A0A1V6Z9M0;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   13-SEP-2023, entry version 21.
DE   RecName: Full=STAS domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=PENNAL_c0001G08520 {ECO:0000313|EMBL:OQE96152.1};
OS   Penicillium nalgiovense.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=60175 {ECO:0000313|EMBL:OQE96152.1, ECO:0000313|Proteomes:UP000191691};
RN   [1] {ECO:0000313|Proteomes:UP000191691}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBT 13039 {ECO:0000313|Proteomes:UP000191691};
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: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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:OQE96152.1}.
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DR   EMBL; MOOB01000001; OQE96152.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V6Z9M0; -.
DR   STRING; 60175.A0A1V6Z9M0; -.
DR   OMA; LEFCEND; -.
DR   OrthoDB; 204198at2759; -.
DR   Proteomes; UP000191691; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   CDD; cd00038; CAP_ED; 1.
DR   CDD; cd07042; STAS_SulP_like_sulfate_transporter; 1.
DR   Gene3D; 2.60.120.10; Jelly Rolls; 1.
DR   Gene3D; 3.30.750.24; STAS domain; 1.
DR   InterPro; IPR000595; cNMP-bd_dom.
DR   InterPro; IPR018490; cNMP-bd_dom_sf.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   InterPro; IPR011547; SLC26A/SulP_dom.
DR   InterPro; IPR002645; STAS_dom.
DR   InterPro; IPR036513; STAS_dom_sf.
DR   PANTHER; PTHR43310:SF4; SULFATE TRANSPORTER; 1.
DR   PANTHER; PTHR43310; SULFATE TRANSPORTER YBAR-RELATED; 1.
DR   Pfam; PF00027; cNMP_binding; 1.
DR   Pfam; PF01740; STAS; 1.
DR   Pfam; PF00916; Sulfate_transp; 1.
DR   SMART; SM00100; cNMP; 1.
DR   SUPFAM; SSF51206; cAMP-binding domain-like; 1.
DR   SUPFAM; SSF52091; SpoIIaa-like; 1.
DR   PROSITE; PS50042; CNMP_BINDING_3; 1.
DR   PROSITE; PS50801; STAS; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000191691};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        270..294
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        374..400
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        407..424
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        444..466
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        473..496
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        541..562
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        582..603
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        615..648
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        668..699
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          738..847
FT                   /note="STAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50801"
FT   DOMAIN          965..1036
FT                   /note="Cyclic nucleotide-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50042"
FT   REGION          175..234
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        210..225
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1079 AA;  117891 MW;  11D33153F39A4803 CRC64;
     MGVLQPRGRR DSRASALSRN LMFDRDIHGN APSETLVEHA NLGSPPGPMG AESSSYNGST
     MRTPNRSFYH RSFNSNMDPA HYASDGLRDQ TAELATYGLS LNKKSLLWDG PGLPPSLDIF
     HGSQNSASYS QDEATSSHAA GGALLEPEYA SVDPASASGS SALTEMIRRP SIDTVEDQVT
     QPGMDDISFP PPPTVYEEPE RDNEHTSLLS KPRSKSTQNY GTAGDAENQR PAVKRSPNLI
     TNGISSAALC TRILSSPKSW DRRMIWKEAV LYPASLVPAV LLGLLLNILD ALSYGMILFP
     LGEPLFAHLG TDGISMFYVS TIISQVVFSC GGSIFKGGIG SEMIEVVPFF HQMAFTIMNS
     IGKDNPKSVI ATTILAFSVS SILTGLVFFL MGVCGLGSLI GFFPRHILIG CIGGVGYFLL
     QTGMEVSARL PGSLEYNLPT IQKLFHLDTF PLWMIPLFLA IGLLVLKRFV RSNFLVGGYF
     IAVAVVFYIV ILSARISMGA LRHNGWVFDA PSSNNPWYHF YSLYDLSAVN WTAFGETIPA
     MFALTFFGVL HVPINVPALG ISTGEDNLNV DRELMAHGVT NALSGFVGSI QNYLVYTNSL
     LFIASGGSSR LAGLMLAAAT AGIMVIGPVI IGYIPIMVVG ALIFLLGIEL LQEALVDTWG
     KLTRLEYLTV AIIVVTMGAW DFVVGIFVGI ILACVNFVVQ TSRKSAIRAK FSGETSGSTV
     RRPPIQQQFL REAGQQTLII KLGGYLFFGT IVNVENTMRG LIEEEAFDRR PIRFIILDFS
     RVYGLDFSAA EAFTRINRVL RKRNVQIAIS GLDVEGDVGK SLQNVGLFES ESSVPIFEDL
     NSALEFCENN YLKVFYSRQE ALSTPTPTEP AANSELLQIP ASVPVPPGPK PPTLADNVVS
     SPRRQYLQRV ATSTIQAHET TMMASPAWSA MRQPLPLLLQ TFQGLSTENE DFWFPACAYF
     SRESYSAGTV LYHEGDSPRA FYLLESGMLR AGYDLPQGRY FELIVAGRPC GELPFFSDTR
     RTATVKAERD CVAWCLTGVQ WKALQDNEPR IARELLTVSL KLTTERMDSI TSYVLTMAA
//
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