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Database: UniProt
Entry: A0A2K3QDU1_9HYPO
LinkDB: A0A2K3QDU1_9HYPO
Original site: A0A2K3QDU1_9HYPO 
ID   A0A2K3QDU1_9HYPO        Unreviewed;       895 AA.
AC   A0A2K3QDU1;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   RecName: Full=Mechanosensitive ion channel protein {ECO:0000256|PIRNR:PIRNR017209};
GN   ORFNames=TCAP_04365 {ECO:0000313|EMBL:PNY25697.1};
OS   Tolypocladium capitatum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Tolypocladium.
OX   NCBI_TaxID=45235 {ECO:0000313|EMBL:PNY25697.1, ECO:0000313|Proteomes:UP000236621};
RN   [1] {ECO:0000313|EMBL:PNY25697.1, ECO:0000313|Proteomes:UP000236621}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 113982 {ECO:0000313|EMBL:PNY25697.1,
RC   ECO:0000313|Proteomes:UP000236621};
RA   Quandt C.A., Patterson W., Spatafora J.W.;
RT   "Harnessing the power of phylogenomics to disentangle the directionality
RT   and signatures of interkingdom host jumping in the parasitic fungal genus
RT   Tolypocladium.";
RL   Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000256|PIRNR:PIRNR017209}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the MscS (TC 1.A.23) family.
CC       {ECO:0000256|PIRNR:PIRNR017209}.
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:PNY25697.1}.
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DR   EMBL; NRSZ01000688; PNY25697.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2K3QDU1; -.
DR   STRING; 45235.A0A2K3QDU1; -.
DR   OrthoDB; 1362946at2759; -.
DR   Proteomes; UP000236621; Unassembled WGS sequence.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR002048; EF_hand_dom.
DR   InterPro; IPR010920; LSM_dom_sf.
DR   InterPro; IPR016688; MscS-like_plants/fungi.
DR   PANTHER; PTHR31323; MECHANOSENSITIVE ION CHANNEL PROTEIN MSY2; 1.
DR   PANTHER; PTHR31323:SF1; MECHANOSENSITIVE ION CHANNEL PROTEIN MSY2; 1.
DR   PIRSF; PIRSF017209; Memb_At2g17000_prd; 1.
DR   SUPFAM; SSF50182; Sm-like ribonucleoproteins; 1.
DR   PROSITE; PS00018; EF_HAND_1; 1.
DR   PROSITE; PS50222; EF_HAND_2; 1.
PE   3: Inferred from homology;
KW   Endoplasmic reticulum {ECO:0000256|PIRNR:PIRNR017209};
KW   Membrane {ECO:0000256|PIRNR:PIRNR017209, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000236621};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        121..141
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        162..180
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        186..205
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        212..232
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        481..507
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        513..536
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          425..460
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
FT   REGION          1..97
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          726..895
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        11..25
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        39..70
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        746..760
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        770..813
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        865..881
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   895 AA;  98510 MW;  CF1E82FDD198FE1E CRC64;
     MAPQLPDPMP SRHHSLTSRT SGFIPLSGGG RNDMDSGIPL TAVRSNSSTT GARKPIPGNS
     TSFESSQSVN EKGELHNRHA GRRRRVGSLG RRGTGDTDEV KVNAMGRLYA RVVGFSVVTR
     YMVYVVPIGL LLAVPLLVLP LTGHQNDIPV GSNNQDPKAP KMGPALFELF LWIEITWLTL
     WAAKTVAWFL PRVFMFFCGI VSVGVRKYAT ILSNLTITLS LFFWALASWL TFRSLFQQAS
     VNGIGWVQSL EQILGALFVS SGLLLGEKAI VQLISVSYHQ RSFANRIKAS KREVHLLGLL
     YDASRTLFPM YCREFADEDH IINDSIEMML RKKAGSRMTG AAVPMRLIGD VGRFGDKVTS
     AFGNIASEIT GKQVFNPNSA HSIVLEALEK RVSSEALGRR IWMSFVLEGK DALYVEDFRE
     VLGPAYTNEA EEAFNAMDGD SNGDISLDEM VRKVIEVGKE RRAIGEGMKD IGQALRVFDK
     VLLFVVFLLC IFVFFIFFRS SFVAVITSAG TTFLSLSFVF AVTTQEFLGS CIFLFVKHPY
     DVGDRVDIGD KKMVVDKISL LYTVFTRIDI MQVVQASSLR TLTLAVPNIQ LNNLWVENVS
     RSKAMVETFE LDVSYDTSFE DIELLRAEME KFVRSADNSR DFRPEFNISV GGVGHLDKMV
     LYMSIKHKSN WHNDSVRATR RSKFMCALAV ALKKVPIYGP SGGTETLGGP TNPAYSVAVS
     DQFASTARDE AAKKKEAGRM VPANGQTEEE GREAERHAIS EINTRSLAVD TADTRDDRSA
     TSRDPSEGPR RSRDADSPGT EPLKQDVTRG RRKAGEGLQN LAPTESGPGG LPAHAASPHL
     NAFDEEANTG MPSTFYSINR PAESRADGAL EEEKEALNPS ASHRGPHRGP SPGHR
//
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