ID A0A1Y2X8P3_9PEZI Unreviewed; 1077 AA.
AC A0A1Y2X8P3;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 13-SEP-2023, entry version 21.
DE RecName: Full=Cyclic nucleotide-binding domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=K445DRAFT_315116 {ECO:0000313|EMBL:OTB18312.1};
OS Daldinia sp. EC12.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Hypoxylaceae; Daldinia.
OX NCBI_TaxID=1001832 {ECO:0000313|EMBL:OTB18312.1, ECO:0000313|Proteomes:UP000243732};
RN [1] {ECO:0000313|EMBL:OTB18312.1, ECO:0000313|Proteomes:UP000243732}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EC12 {ECO:0000313|EMBL:OTB18312.1,
RC ECO:0000313|Proteomes:UP000243732};
RX PubMed=28078400; DOI=10.1007/s00253-017-8091-1;
RA Wu W., Davis R.W., Tran-Gyamfi M.B., Kuo A., LaButti K., Mihaltcheva S.,
RA Hundley H., Chovatia M., Lindquist E., Barry K., Grigoriev I.V.,
RA Henrissat B., Gladden J.M.;
RT "Characterization of four endophytic fungi as potential consolidated
RT bioprocessing hosts for conversion of lignocellulose into advanced
RT biofuels.";
RL Appl. Microbiol. Biotechnol. 101:2603-2618(2017).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; KZ112931; OTB18312.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y2X8P3; -.
DR STRING; 1001832.A0A1Y2X8P3; -.
DR OrthoDB; 204198at2759; -.
DR Proteomes; UP000243732; 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:UP000243732};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 287..308
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 320..341
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 378..400
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 412..434
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 459..476
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 483..503
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 538..560
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 621..641
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 647..666
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 678..709
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 749..857
FT /note="STAS"
FT /evidence="ECO:0000259|PROSITE:PS50801"
FT DOMAIN 961..1060
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT REGION 1..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 107..195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..61
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 108..195
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1077 AA; 119910 MW; AD07F56D79F0A15A CRC64;
MATPSFGFTS WRRRSSSVTS QPDPVDVPGQ ILNPNQSSRL VPGDLRQLSS SLNSHNYREP
TRSFVPGSLR DHLPPVDSAS YARSVREDTA ELASYVLSDK KDRRSTSFLN RISSTSSHPS
RDQPVIQDES PSTGDLQASS TDTIDEVSEP SSLASGADDP MNSGPSALTS MFKRSPPQSL
HDLDAGDNSM SQNGQHLPSI DVLQAEHDDG LSETTPLLRR VSQIPEPEDS VTDVDIESQK
PKTAQWGPLS TGHGFRNKVR TIKGMMNPKT WDMRVIWQRT VVDPIHCLPA VIVGLLLNIL
DALSYGMILF PLGNPIFSNL GPAGISIFYV STIISQLTFS AGSIFRGGVG SELIEVVPFF
HNMATTITAI VGEDQPDAVI ATTITSFAIS SMLTGLVFYL MGRFRLGYVV GFIPRHILIG
CIGGVGWFLI ATGFEVSARL EEFRYDLDTG RKLIQSDTLP LWLIPLVLAI LLFGLQKKIT
SKYFLPVYIL SVPIFFYFFV FTIDSLNPEN LRKAGWIFEA PEAGQPWWYF WTLYKFNLVH
WGAILETVGA MFALTFFSVL HVPINVPALA QISGEDHLDL DHELKLHGYS NFLSGLAGSI
QNYLVFANTL FFMRSGGDSR LAGIMLAGLT FGVMTIGPVI IGYIPVMVVG TLIFVLGFEL
LLDALISPRR KLKLLEYLTI VVIVLTMGIY DFVVGIFVGI ILAFVSAIFH ASQVSAIRAT
YTGDQIGSMV RRNPSQHRYL REVGSQTYVI KLSGFLFFGT IVGVEEKIRH LISEDAFREH
PIKYLILDLW HVTGIDYSAA EGFKTINRLL AGKGVHLLLS GKDADSKIGR DLRAVGLGDD
GPSVMFMPDL NSALESCENE QLKTFYARQE ALRISRPAPS SNLDVPNKGQ FSQSLELLSQ
SPRRNHLDQA AKNVLNQQEM RRSTRWQNIS EPLRLMLQVF YDVSDKNEDF WFRARPYFVR
KEYTAGTVLY HCGEPANGFY LLERGELRAD YDTPQGRLYE PIVQGTTCGE LPFFSETNRT
ATVVAIKDCV VWVMDTENWE KLQREENDVA QELLRVSLKL TSERMEAMTK YISAVGN
//