ID   A0A2H3T0N2_FUSOX        Unreviewed;       814 AA.
AC   A0A2H3T0N2;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=Related to DUF726 domain protein {ECO:0000313|EMBL:SCO79255.1};
GN   ORFNames=FRV6_03468 {ECO:0000313|EMBL:SCO79255.1};
OS   Fusarium oxysporum (Fusarium vascular wilt).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium oxysporum species complex.
OX   NCBI_TaxID=5507 {ECO:0000313|EMBL:SCO79255.1, ECO:0000313|Proteomes:UP000219369};
RN   [1] {ECO:0000313|Proteomes:UP000219369}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=V64-1 {ECO:0000313|Proteomes:UP000219369};
RA   Guldener U.;
RL   Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the TMCO4 family.
CC       {ECO:0000256|ARBA:ARBA00009824}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; FMJY01000002; SCO79255.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2H3T0N2; -.
DR   VEuPathDB; FungiDB:FOC1_g10016187; -.
DR   VEuPathDB; FungiDB:FOC4_g10014583; -.
DR   VEuPathDB; FungiDB:FOIG_01428; -.
DR   VEuPathDB; FungiDB:FOMG_01641; -.
DR   VEuPathDB; FungiDB:FOXG_00883; -.
DR   VEuPathDB; FungiDB:FOZG_01631; -.
DR   VEuPathDB; FungiDB:HZS61_001250; -.
DR   OrthoDB; 8526at2759; -.
DR   Proteomes; UP000219369; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR007941; DUF726.
DR   PANTHER; PTHR17920:SF3; TRANSMEMBRANE AND COILED-COIL DOMAIN-CONTAINING PROTEIN 4; 1.
DR   PANTHER; PTHR17920; TRANSMEMBRANE AND COILED-COIL DOMAIN-CONTAINING PROTEIN 4 TMCO4; 1.
DR   Pfam; PF05277; DUF726; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        268..294
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        300..330
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        442..460
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REGION          38..91
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          124..144
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          642..661
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          671..814
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        74..90
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        682..696
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        744..758
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   814 AA;  90013 MW;  A9D209BB8B202504 CRC64;
     MAPTCSDPRQ IVITLNPARR QALLKLVDEI TTYMSDQLQA SDDELGPVLS TPRNESGPST
     PRDENRSFTP RNDDSDRNAQ QQQPNKPSAQ ALRIQKAAIK HLKEWKKEFM PKLEEIVRVK
     DDHKIQEERR KHQQEAEKRK LDTPEEGENL ISFGENKIDK SEDIASLQAL YHPIPTRLTT
     IPAADRREAI SCILLLLLST GKYSAHTRAL ALYLASSLEI PQTFLIKEEM EIAKTLLESS
     KDQDKQQEVM SAEAEASKRR EENKFSRFWK VGLASVAGAA VIGVTGGLAA PLVAGAVGGI
     LGGVGLGGVA SFLGIFWMNG ALVGALFGAY GGKMTGEMMD KYAKEVEDFR FIPLRGEWGE
     VFNAEQDQAQ AQERRLRVTI GINGWLRDED DVTKPWRILG DDTEVFALRY EMKSLIALGH
     ALRSMVESFA WKKLKVEIIK RTAFATLLAA LWPIQVLAAA SNVDNPFGHA HNRSRKAGQL
     LADALINKVQ GERPVTLIGY SLGATAIHAC LQSLAERHAF GLIDSVVIIG APAPSAPPHW
     RTLRTVVSGK IFNVYSENDM ILGFVYRAHS LSMGVSGLQN IQEVEGIQNL DLSDSVSGHL
     RYPDLIGEIL NKCGFVGIKT TSEIEKDDVI LMKDRHAEGE LIDFEGTTVE GKESPQSPNQ
     EQIEKDLHGL NISPPALVSP SQPPDQGKSP QQSSNENPPL PQRPTPQDRK EEAPKLPRRP
     VASQAQPSSG PDDEAGPPLP RRPTEAQQED RPAIPRRPVG ADKEVNPPLP RRFESSHDTH
     QQQQRPWTPE SNLTDDEEYG HIAMVNYDSD HSTK
//