ID A0A3A3A030_9EURO Unreviewed; 704 AA.
AC A0A3A3A030;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE SubName: Full=FHA domain protein {ECO:0000313|EMBL:RJE22671.1};
GN ORFNames=PHISCL_04974 {ECO:0000313|EMBL:RJE22671.1};
OS Aspergillus sclerotialis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Polypaecilum.
OX NCBI_TaxID=2070753 {ECO:0000313|EMBL:RJE22671.1, ECO:0000313|Proteomes:UP000266188};
RN [1] {ECO:0000313|Proteomes:UP000266188}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 366.77 {ECO:0000313|Proteomes:UP000266188};
RA Tafer H., Lopandic K.;
RL Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
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:RJE22671.1}.
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DR EMBL; MVGC01000156; RJE22671.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3A3A030; -.
DR STRING; 2070753.A0A3A3A030; -.
DR Proteomes; UP000266188; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR Gene3D; 2.60.200.20; -; 1.
DR InterPro; IPR000253; FHA_dom.
DR InterPro; IPR008984; SMAD_FHA_dom_sf.
DR PANTHER; PTHR23308:SF53; KANADAPTIN-RELATED; 1.
DR PANTHER; PTHR23308; NUCLEAR INHIBITOR OF PROTEIN PHOSPHATASE-1; 1.
DR Pfam; PF00498; FHA; 1.
DR SMART; SM00240; FHA; 1.
DR SUPFAM; SSF49879; SMAD/FHA domain; 1.
DR PROSITE; PS50006; FHA_DOMAIN; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000266188};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 673..698
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 33..94
FT /note="FHA"
FT /evidence="ECO:0000259|PROSITE:PS50006"
FT REGION 136..155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 173..239
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 255..325
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 493..536
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 557..672
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 193..211
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 212..231
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 307..325
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 493..511
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 512..536
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 557..579
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 599..645
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 650..668
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 704 AA; 77531 MW; BE7F6197A6CDC699 CRC64;
MPERQAVITL HPLFRPDVLP FRSLTFASDS DSVNIGRASK RETKNLAPAH HNAWFESRVM
SRDHAKLTVS LEKKDVYIRD NGSMHGTLLN DKKITPHCDV KISTGDVLTF GAEVVRASEI
FAPLRVRCEC QWFDTHEEKT PGSPSPQAPN SFCVPEEDDD VIDVAYDSMP AKDTAIHTSN
VDDSDVASDS ENHPPEDSTP LTSPSSNGKV SVESKPEDKP KADHESQNVP EDEQGSRQCP
IVLDSEQPAV ETAFSDLNSE GDPTKDDANN DPYESGNFSG SDGASHGVEL DSCDEDEQSA
VDEDDSSSDQ ISVHDSEKDD LSMESDHIPM KVNYKCPYVE ENDMEDGSIL SCVSEAGSLF
DSRRKELLEN IVGFETSHDD HRAKNRCKLR DQSPLEINDI TTSKSNAPPA LPMLNEKPGD
LLVNYHQRID RGQPFIDPCV PVPGNQYGIS YLPIYENSYI PYQDGPFMIG QPNTRNNGPG
ATDFTEVARS VNHAENSSDN QVQQSEKSAH GQSDNQEFEH GQGHTKQYEG SSVEENEHHT
MEDFDSMDDL IDWVEEKTSQ KEPLKRKADE MEKDSPSEIA ATSKSHSKSV ELSHIDQPAV
DSSEGSFSQD AQPRNPDGGL KCSPSQLSDL QPIKDTQPKQ NAASSRHKDQ PPRKRAKTGK
RSRVEKKSRK GSVARYATTA LVGALVGGLG TIAALASLPP EYFQ
//
