ID A0A395IBX6_ASPHC Unreviewed; 1249 AA.
AC A0A395IBX6;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=C2 domain protein {ECO:0000313|EMBL:RAL17546.1};
GN ORFNames=BO97DRAFT_359431 {ECO:0000313|EMBL:RAL17546.1};
OS Aspergillus homomorphus (strain CBS 101889).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1450537 {ECO:0000313|EMBL:RAL17546.1, ECO:0000313|Proteomes:UP000248961};
RN [1] {ECO:0000313|EMBL:RAL17546.1, ECO:0000313|Proteomes:UP000248961}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 101889 {ECO:0000313|EMBL:RAL17546.1,
RC ECO:0000313|Proteomes:UP000248961};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KZ824267; RAL17546.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A395IBX6; -.
DR STRING; 1450537.A0A395IBX6; -.
DR VEuPathDB; FungiDB:BO97DRAFT_359431; -.
DR OrthoDB; 1465207at2759; -.
DR Proteomes; UP000248961; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0061817; P:endoplasmic reticulum-plasma membrane tethering; IEA:InterPro.
DR GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR CDD; cd04041; C2A_fungal; 1.
DR CDD; cd04052; C2B_Tricalbin-like; 1.
DR CDD; cd21676; SMP_Mug190; 1.
DR Gene3D; 2.60.40.150; C2 domain; 2.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR037767; C2A_Mug190-like.
DR InterPro; IPR037765; C2B_Tricalbin.
DR InterPro; IPR031468; SMP_LBD.
DR PANTHER; PTHR47348; MEIOTICALLY UP-REGULATED GENE 190 PROTEIN; 1.
DR PANTHER; PTHR47348:SF3; MEIOTICALLY UP-REGULATED GENE 190 PROTEIN; 1.
DR Pfam; PF00168; C2; 2.
DR SMART; SM00239; C2; 2.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 2.
DR PROSITE; PS50004; C2; 2.
DR PROSITE; PS51847; SMP; 1.
PE 4: Predicted;
KW Lipid transport {ECO:0000256|ARBA:ARBA00023055};
KW Lipid-binding {ECO:0000256|ARBA:ARBA00023121};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000248961};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
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 180..198
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 204..220
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 443..465
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 247..474
FT /note="SMP-LTD"
FT /evidence="ECO:0000259|PROSITE:PS51847"
FT DOMAIN 472..601
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 661..805
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 1..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 107..126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 698..721
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1082..1212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..74
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 698..718
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1107..1124
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1139..1188
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1249 AA; 140633 MW; 7CF96A583DEC95AB CRC64;
MAQATGGRES PKTHRMGEHW SGGNPVPTIS HFMDRLEHDK QERKAHEETL AARKREQQAQ
NQEMPHKPRE TTGKTRMVTD PTTGKEIEVE DLDEDSMDAV KDPRLVVPNA NLGKPTEVKT
APDQSLSQYK ENQDITAPPD PIAEGTTSDV PIHGEKTNVL FHPTPTVTYK PMFDQLERRG
IGLCLGIVAG IVFLGRMFNG SLWGLLPLSF CIASGVWLWV QEVIRSGREM EWSSEQIRGQ
MATANLLPES VEWMNSFLGV FWGLINPEML SPVADTIEDI MQASAPGVVE NVRIAEIDQG
NNPIRILSLR ALPDDHVKQL KDQVHEENVK NKDPQEAAAA EEGGDYYNIE ASFAYHAKPS
GQTTSSKARN MHMQIVFYLG AKGLFGVPFP VFVELTELVG TVRARFQMMP EAPFVKDVTF
SLVGLPHVKA GCMPMVKGGV NILNLPLISN FVNYAIATAA GLFAAPKSMT MDLSMLLKGD
DIVKETQALG VMWVRIHRAI GLSKQDRRGS YGGGSDPYIN LSFSKYGKPM YCTRVITDDL
NPVWEETAAL LVTPELIKAD EALSVELWDS DRTTADDIVG KVELPIRKMI QHPGKMYAQV
SKLQGLNEGS EMPGELHWEV GFFGKPKLRA ELRTDGKKKD LPEQFRDVQE FQDEKGVISN
EEEDAITHTP PDPLWPSGIL SIVIHQIVNL EINNVKGSEG NRKGREYEPA KPYGDNTEEE
GSHLPTSYCK IILNDELIYR TRAKALSSKP IFNAGTERFI RDWRSAFVTI GVRDQRYRQH
DPILGVVPLK ISDLLQTSSQ VTRWYPLDGG IGFGRIRISI LFRSIETRLP PNMLGWDVGT
FEFVSEKLTT VNFNQRCKIK LRTGGSSGKI TKHVCSVDEN NNLTFDLSDE TYRRSLRLPI
KHRYRSPVVF EFHTHKKHHP SAYAVFWLQH LVDNETTEID IPIWHTKNGK RLTQNYITEQ
NWESKKSPGL EDLREIGRLR FSGRFSPGID DSHERFVVDS NSRETFETWE ACVAEGVRSQ
HMSASVPEEV EELHEKSLID GRDILKHADP RERKRWLDKQ GYDWSGAFGH DPSAYLDEHG
KQVAEPGRES PPHNPYNPPR TEATAYGTMH AEEKTKAHPD SSSSSESDDD DDHDHEINNS
LQPQQQRTLA DNDDFDVNSN LRRSSETGTN TTTTASASSG PSRSSTNEVQ KKAEQRSEQR
QQRGMMQWRP VRNAVFARDE TKYALRKMKM KFTGNLSGRE PDIETETGT
//
