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Database: UniProt
Entry: A0A395MQN0_9HYPO
LinkDB: A0A395MQN0_9HYPO
Original site: A0A395MQN0_9HYPO 
ID   A0A395MQN0_9HYPO        Unreviewed;      1274 AA.
AC   A0A395MQN0;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:RFN50120.1};
GN   ORFNames=FIE12Z_5648 {ECO:0000313|EMBL:RFN50120.1};
OS   Fusarium flagelliforme.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium incarnatum-equiseti species complex.
OX   NCBI_TaxID=2675880 {ECO:0000313|EMBL:RFN50120.1, ECO:0000313|Proteomes:UP000265631};
RN   [1] {ECO:0000313|EMBL:RFN50120.1, ECO:0000313|Proteomes:UP000265631}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL 13405 {ECO:0000313|EMBL:RFN50120.1,
RC   ECO:0000313|Proteomes:UP000265631};
RX   PubMed=29649280; DOI=10.1371/journal.ppat.1006946;
RA   Proctor R.H., McCormick S.P., Kim H.S., Cardoza R.E., Stanley A.M.,
RA   Lindo L., Kelly A., Brown D.W., Lee T., Vaughan M.M., Alexander N.J.,
RA   Busman M., Gutierrez S.;
RT   "Evolution of structural diversity of trichothecenes, a family of toxins
RT   produced by plant pathogenic and entomopathogenic fungi.";
RL   PLoS Pathog. 14:e1006946-e1006946(2018).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the CSC1 (TC 1.A.17) family.
CC       {ECO:0000256|ARBA:ARBA00007779}.
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:RFN50120.1}.
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DR   EMBL; PXXK01000150; RFN50120.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A395MQN0; -.
DR   OrthoDB; 54187at2759; -.
DR   Proteomes; UP000265631; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005227; F:calcium-activated cation channel activity; IEA:InterPro.
DR   InterPro; IPR045122; Csc1-like.
DR   InterPro; IPR003864; CSC1/OSCA1-like_7TM.
DR   InterPro; IPR027815; CSC1/OSCA1-like_cyt.
DR   InterPro; IPR032880; Csc1/OSCA1-like_N.
DR   InterPro; IPR022257; PHM7_ext.
DR   PANTHER; PTHR13018; PROBABLE MEMBRANE PROTEIN DUF221-RELATED; 1.
DR   PANTHER; PTHR13018:SF20; SPORULATION-SPECIFIC PROTEIN 75; 1.
DR   Pfam; PF14703; PHM7_cyt; 2.
DR   Pfam; PF12621; PHM7_ext; 1.
DR   Pfam; PF02714; RSN1_7TM; 1.
DR   Pfam; PF13967; RSN1_TM; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000265631};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   TRANSMEM        76..102
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        163..183
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        226..246
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        742..763
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        793..816
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        836..858
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        889..917
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        950..977
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        997..1022
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1034..1052
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          81..246
FT                   /note="CSC1/OSCA1-like N-terminal transmembrane"
FT                   /evidence="ECO:0000259|Pfam:PF13967"
FT   DOMAIN          271..348
FT                   /note="CSC1/OSCA1-like cytosolic"
FT                   /evidence="ECO:0000259|Pfam:PF14703"
FT   DOMAIN          621..728
FT                   /note="CSC1/OSCA1-like cytosolic"
FT                   /evidence="ECO:0000259|Pfam:PF14703"
FT   DOMAIN          741..1020
FT                   /note="CSC1/OSCA1-like 7TM region"
FT                   /evidence="ECO:0000259|Pfam:PF02714"
FT   DOMAIN          1192..1265
FT                   /note="10TM putative phosphate transporter extracellular
FT                   tail"
FT                   /evidence="ECO:0000259|Pfam:PF12621"
FT   REGION          37..70
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          343..425
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          456..530
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1090..1113
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        343..374
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        392..425
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        470..493
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        494..514
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1274 AA;  143796 MW;  50126C99C72425E3 CRC64;
     MSSADPSGTG TAESATDIAA ITSSIASSLL SSAISATTTG TPASTSSDGP TKTSSGGIGV
     TPPSETTSAA TSDRGIGIAT FFTALVVAVV VFSVQILAFL LLRNKLARIF KPKTYLVPER
     ERTDSPPTGL AGMLKTLWHY NDREIINKCG LDAYFFLRYL KTLLIIFIPI CCIVMPILIP
     INYVGGIGKE VNADEETRKQ ERDSNRPTGL DTLAWGNVSA KNVDRYGAHL LMGILVVIWV
     CWVFFIELKI YVKVRQDYLT SAEHRLKASA TTVLVNSIPA KWLSEEALTG LFDVFPGGIR
     NIWLNRDLSP LLEKVKERND IHQQLESAET DLIKSAKKAQ LKQAKAAEKK ERKEMKLKAV
     TKKERAERHA QLDAEAQEMA NSSGGQAAGD KHEVPHSVDQ GVRESEHDMD QQEGHDIDKE
     KSRGFKVPLL NPISKVGQGL LGVVSKAEKN VDNTLETTNG FMGLQQDEKR APSRGSERYR
     IRPSTDEDEL SSPSDTLRVQ NQSRNTNRHS GESTAAMNPE RREFGKPGNT VRKIDNIDEI
     YVKEDSKWWE FWKPPPGAYA SPVPQGDVAA AYRERKDAQS RPLWQRIKYA LPFVSPEIEE
     GPIEYETAFN PDYKEDAEPA EWEKYLKKKD RPTHRLPLFG KKWLFPIPLV TKKVDTIYWC
     REQLARLNVE IEEDQSHPER YPLMNSAFIQ FNHQVAAHMA CQSVIHHIPQ QMAPRMNEIS
     PRDVNWDNMA FSWWQEWLRS GLVFAAVVAM LFLWAIPVAW TAALSQLDNL IRNNSWLSFL
     RDNETVHKMA KSIAGVLPAV VLALLLFLVP VILGFFAEFK GVKTGSQKTE FVQRYYFVFL
     FIQVFLIVSI ASFFAASIDA LVENFKGLKT FEDVLDLLAK NLPTAANYFF SYMILQALST
     SSATLLQIGA LVMWYVIAKI LDSTARNKWS RNTKLNQVTW GRLFPIYTNF ACIGLVYCVI
     APLISIFAII TFGLLWMAQR YVMLYVNRFE HDTGGVLYPR AINQTFTGIY FMELCMAGLF
     FLAEDPTGKN VCTVHGVIMI VVLILTALYQ VLLNYSFGPL FRYLPITFED EAVLRDQAFQ
     RAQDQRLGLI DGDELQEEEE EEEDVKQPEK HGENGNAIEM RRFGSVRRPM KQVGTWARGG
     GQQLRKIAVV NKASDKNKRA SLYREKHRRK DIEAQRAIGE ALFGGFHDEI EDLTPEERDA
     LTRHAFQHEA LRARRPTVWI PRDDLGISDD EIRRTQAYSD HIWISNEGTA LDSKVRVVYG
     RAPPDFSEVD LINL
//
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