ID A0A060SHB0_PYCCI Unreviewed; 1079 AA.
AC A0A060SHB0;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 13-SEP-2023, entry version 29.
DE RecName: Full=STAS domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=BN946_scf185016.g39 {ECO:0000313|EMBL:CDO73882.1};
OS Pycnoporus cinnabarinus (Cinnabar-red polypore) (Trametes cinnabarina).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Polyporaceae; Trametes.
OX NCBI_TaxID=5643 {ECO:0000313|EMBL:CDO73882.1, ECO:0000313|Proteomes:UP000029665};
RN [1] {ECO:0000313|EMBL:CDO73882.1, ECO:0000313|Proteomes:UP000029665}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BRFM137 {ECO:0000313|EMBL:CDO73882.1,
RC ECO:0000313|Proteomes:UP000029665};
RA Levasseur A., Lomascolo A., Ruiz-Duenas F.J., Uzan E., Piumi F., Kues U.,
RA Ram A.F.J., Murat C., Haon M., Benoit I., Arfi Y., Chevret D., Drula E.,
RA Kwon M.J., Gouret P., Lesage-Meessen L., Lombard V., Mariette J.,
RA Noirot C., Park J., Patyshakuliyeva A., Wieneger R.A.B., Wosten H.A.B.,
RA Martin F., Coutinho P.M., de Vries R., Martinez A.T., Klopp C.,
RA Pontarotti P., Henrissat B., Record E.;
RT "The genome of the white-rot fungus Pycnoporus cinnabarinus: a
RT basidiomycete model with a versatile arsenal for lignocellulosic biomass
RT breakdown.";
RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
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:CDO73882.1}.
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DR EMBL; CCBP010000124; CDO73882.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A060SHB0; -.
DR STRING; 5643.A0A060SHB0; -.
DR HOGENOM; CLU_003182_0_1_1; -.
DR OrthoDB; 204198at2759; -.
DR Proteomes; UP000029665; 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:UP000029665};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 325..347
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 354..373
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 393..413
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 425..449
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 461..483
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 495..517
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 537..556
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 563..582
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 602..623
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 635..668
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 688..719
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 759..866
FT /note="STAS"
FT /evidence="ECO:0000259|PROSITE:PS50801"
FT DOMAIN 943..1063
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 45..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 145..170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 182..241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..67
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 183..203
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 212..237
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1079 AA; 117222 MW; 0FAA3F7D9253A04B CRC64;
MSRNSSYGLS ETATALPVVA PGAANDASPG ERDLEALLRM QNGSPITRAG LLQPRSYVSS
SSKSSRPRHV PPAAHSQNTI RDSTMEISSI PLSTPSRLSV QSSDAFIFPD VGASSNEEDE
NGVMSASLTS DLSFKHVEDV TDLEASTSTL STQPGSGAVT PRALQGSSQP SGLSLLLARH
DQLSRSEATS PLDSETTTPT AERPNMMGAP LETIRENNSR SSSREVSTCS GERRRASSNE
SVPLLADLEA NHQIYQTNGD SRPEAVCKRN AKGVVKDLTF RISRGSGPVI KDALRSIPAV
ILGTLLNILD GISYGMIIFP AAGVFTGLGG VGVSMFFVTA IITQLIYSAG ASGFAGANGS
MMIEVVPFFH LIANQIAEDV GEHNPHAVIA TTMVAFAFSS ILTGVTFFLL GALRLGSLIG
FFPRHILVGC IGGVGVFLVI TGLTVSARIS DDEFSLSLET LKFFVLNVHI VMLWLPAFLL
AVLLRVITHF WEHQLIFPIY FCIIPAIFYV VVAAAHTDLG ALRDAGWLFE MSSTDEPWYY
FYSLFDFGAT DWAAFWATMP TQFALLFFNI LHPPLNVPAL AVSLNHDVDT DKELVAHGYS
NLLAGLIGTV PNYLVYVNTL LFYRVGGDTR IAGFMLAGAT TILLLVGTGP IAYIPVMVVG
ALIFVLGIDL VKEALWDTRH RVSTSEYITI ASIMICMTVW DFVTGVLFGI IVSCIFFVVQ
SSQRRSIRAL HTGDSVMSTV RRPGAHRAYL RDVTKQTTIV RLQGFMFFGT ITHVEEAIRA
VLEESAWCRT PIRFLVLDLA LVAGVDMSAA EAFMRVQRLL AGKKVVLVLC GFTIDSSVGR
ALSNVGLLDM DGVELFETFS DAIEWTENIY LRAWFKAQKV ETVPVALPGR QDDVIPFPGS
VVDSPRRAAL LDAGWRTIAR DHSPPGSHDA PEPFNTLVRA FSSYETIDRE TYAPLIAYLQ
RMSVPAGSVL WHQHDVPDGL YIVESGILRA TYRFADPTPP MVETMVPGTI AGELSALSGL
ERNATCVVER AAVVWKLNVE DLARLEEDHP DLARAFTRLV LKVAKLDYDI LITALATRQ
//